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Conserved domains on  [gi|1888712850|gb|QNB16883|]
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amino acid adenylation domain-containing protein [Paraburkholderia tropica]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05691 super family cl35369
peptide synthase; Validated
21-2297 0e+00

peptide synthase; Validated


The actual alignment was detected with superfamily member PRK05691:

Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1594.82  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   21 HGLAARLRALAQQRPEATALIVI--DADGDTRYDYAQLDRRARALAARFARDGAAAERALILMDSGVDYVSAFFGCLYAG 98
Cdd:PRK05691     9 LTLVQALQRRAAQTPDRLALRFLadDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGCLYAG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   99 VVAVPVYPPESKREQHLARLRGIARDAGVRYVLTTAALHERHADAWSMLAPGA-DVVAVDTLDArdTPSDAPLHP-VRAD 176
Cdd:PRK05691    89 VIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANApELLCVDTLDP--ALAEAWQEPaLQPD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  177 DLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLG--VRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQYF 254
Cdd:PRK05691   167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPAYF 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  255 LERPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAALYP 334
Cdd:PRK05691   247 LERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPDSFFA 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  335 CYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGRAEAARAdeaaTVLVGCGAVQAGHRvaivaraaaeshesheadVETE 414
Cdd:PRK05691   327 SYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGTG----SVLMSCGRSQPGHA------------------VLIV 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  415 TSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhaDGSgpaRWLRTGDLGFVHDGQLYIAGRVKDLVIVR 494
Cdd:PRK05691   385 DPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH----DGR---TWLRTGDLGFLRDGELFVTGRLKDMLIVR 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  495 GRNLYPQDVEQAVEAHAEFARKGRVIAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDACGETPAAIALLN 574
Cdd:PRK05691   458 GHNLYPQDIEKTVEREVEVVRKGRVAAFAVNHQGEEGIGIAAEISRSVQKILPPQALIKSIRQAVAEACQEAPSVVLLLN 537
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  575 PGALPKTSSGKLQRAATREGWRARTLDLYALWEQGAFVIGGDDDAARAPDapaaldarESALAALWCEALDARlALAPDA 654
Cdd:PRK05691   538 PGALPKTSSGKLQRSACRLRLADGSLDSYALFPALQAVEAAQTAASGDEL--------QARIAAIWCEQLKVE-QVAADD 608
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  655 HFFASGGSSLSAARLVALIGARLGRRVALAQIFETPTLAAMAAalaepeSVEEAQDDAQDEAQDNAPIEPAEEAVISHAQ 734
Cdd:PRK05691   609 HFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSA------AVARQLAGGGAAQAAIARLPRGQALPQSLAQ 682
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  735 QRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHlyaPRTEAAAPLAWAHVDLSD 814
Cdd:PRK05691   683 NRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVAL---QRIDAQGEFALQRIDLSD 759
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  815 LGdidEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAALDGAT 894
Cdd:PRK05691   760 LP---EAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQT 836
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  895 ThgeaqAKAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHtatdtASENADPRAAARVAFALPAP 974
Cdd:PRK05691   837 A-----ELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDH-----PRSARQAHSAARYSLRVDAS 906
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  975 LAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEAATPLASLFSQ 1054
Cdd:PRK05691   907 LSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQ 986
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1055 LRQRTLDAQANQALPFDVLVEHLRPARdaQHGpLFETSFNYLSDDYPALARWPGARAERVEIAETHVKVPLALDLRESRD 1134
Cdd:PRK05691   987 VRQATLGAQAHQDLPFEQLVEALPQAR--EQG-LFQVMFNHQQRDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEDRN 1063
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1135 GSMRAYFTYASARFDAASVERMAAQYLRAVEAFAhalgdrsadmtDAAAPTLATLDLLDADERARVSAASVARRTPPGEP 1214
Cdd:PRK05691  1064 GRLTLSFDYAAELFDAATIERLAEHFLALLEQVC-----------EDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQAW 1132
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1215 IHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLlaRDLQGGEP--VAIVAHRSARFVVAMLGVLKAGGAYVA 1292
Cdd:PRK05691  1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYL--RDKGVGPDvcVAIAAERSPQLLVGLLAILKAGGAYVP 1210
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1293 LDAGNPTQRLAQTLRDCGARLVLCEDdcSALDLMgvqhARIDAAQEEAQREQHLRA-PHALPAVD--PRSAAYVIYTSGS 1369
Cdd:PRK05691  1211 LDPDYPAERLAYMLADSGVELLLTQS--HLLERL----PQAEGVSAIALDSLHLDSwPSQAPGLHlhGDNLAYVIYTSGS 1284
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1370 SGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAAR 1449
Cdd:PRK05691  1285 TGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYG 1364
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1450 IDVLKIVPGHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRAAAt 1529
Cdd:PRK05691  1365 VTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGERS- 1443
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1530 lPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFA-AGARLYRSGDRARRLADGSLE 1608
Cdd:PRK05691  1444 -PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALE 1522
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1609 YLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIV---VAGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSV 1685
Cdd:PRK05691  1523 YLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVregAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQ 1602
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1686 LRVIDALPLNRNGKLDRQALSAlarPAAPHREaaRAAPQGETETALAQCWAALLdpsngtdnatdnatATPSltIARDDS 1765
Cdd:PRK05691  1603 LIRLDQMPLGPSGKLDRRALPE---PVWQQRE--HVEPRTELQQQIAAIWREVL--------------GLPR--VGLRDD 1661
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1766 FFALGGHSLAAMRLASRVRSRWSVELPLREIFASPTLAALAARIEAQRADSDRASNQvsnkaanaesatPLHALADRSAL 1845
Cdd:PRK05691  1662 FFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGERNSQG------------AIARVDRSQPV 1729
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIWVVDQLADRALAsYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDeGDPVLKIAPRMEVLMpv 1925
Cdd:PRK05691  1730 PLSYSQQRMWFLWQMEPDSPA-YNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVD-GVPVQQVAEDSGLRM-- 1805
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1926 ieplahpdndansHTNSHTNSDENARTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVHI 2005
Cdd:PRK05691  1806 -------------DWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDI 1872
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2006 LLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRaRFTPDAVREAQ-QFWRGYLADAPALLPLSTDRARPTRVSHAGAA 2084
Cdd:PRK05691  1873 FARELGALYEAFLDDRESPLEPLPVQYLDYSVWQR-QWLESGERQRQlDYWKAQLGNEHPLLELPADRPRPPVQSHRGEL 1951
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2085 RHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSRIaaDG 2164
Cdd:PRK05691  1952 YRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQL--DG 2029
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2165 AnlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRDLPRGNTR-VPGLAVELLRPPTTQSK 2243
Cdd:PRK05691  2030 Q--MSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSRqLAGMTVEYLVNDARATK 2107
                         2250      2260      2270      2280      2290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1888712850 2244 FDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADPRAPLAS 2297
Cdd:PRK05691  2108 FDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAE 2161
 
Name Accession Description Interval E-value
PRK05691 PRK05691
peptide synthase; Validated
21-2297 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1594.82  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   21 HGLAARLRALAQQRPEATALIVI--DADGDTRYDYAQLDRRARALAARFARDGAAAERALILMDSGVDYVSAFFGCLYAG 98
Cdd:PRK05691     9 LTLVQALQRRAAQTPDRLALRFLadDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGCLYAG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   99 VVAVPVYPPESKREQHLARLRGIARDAGVRYVLTTAALHERHADAWSMLAPGA-DVVAVDTLDArdTPSDAPLHP-VRAD 176
Cdd:PRK05691    89 VIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANApELLCVDTLDP--ALAEAWQEPaLQPD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  177 DLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLG--VRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQYF 254
Cdd:PRK05691   167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPAYF 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  255 LERPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAALYP 334
Cdd:PRK05691   247 LERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPDSFFA 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  335 CYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGRAEAARAdeaaTVLVGCGAVQAGHRvaivaraaaeshesheadVETE 414
Cdd:PRK05691   327 SYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGTG----SVLMSCGRSQPGHA------------------VLIV 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  415 TSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhaDGSgpaRWLRTGDLGFVHDGQLYIAGRVKDLVIVR 494
Cdd:PRK05691   385 DPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH----DGR---TWLRTGDLGFLRDGELFVTGRLKDMLIVR 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  495 GRNLYPQDVEQAVEAHAEFARKGRVIAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDACGETPAAIALLN 574
Cdd:PRK05691   458 GHNLYPQDIEKTVEREVEVVRKGRVAAFAVNHQGEEGIGIAAEISRSVQKILPPQALIKSIRQAVAEACQEAPSVVLLLN 537
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  575 PGALPKTSSGKLQRAATREGWRARTLDLYALWEQGAFVIGGDDDAARAPDapaaldarESALAALWCEALDARlALAPDA 654
Cdd:PRK05691   538 PGALPKTSSGKLQRSACRLRLADGSLDSYALFPALQAVEAAQTAASGDEL--------QARIAAIWCEQLKVE-QVAADD 608
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  655 HFFASGGSSLSAARLVALIGARLGRRVALAQIFETPTLAAMAAalaepeSVEEAQDDAQDEAQDNAPIEPAEEAVISHAQ 734
Cdd:PRK05691   609 HFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSA------AVARQLAGGGAAQAAIARLPRGQALPQSLAQ 682
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  735 QRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHlyaPRTEAAAPLAWAHVDLSD 814
Cdd:PRK05691   683 NRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVAL---QRIDAQGEFALQRIDLSD 759
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  815 LGdidEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAALDGAT 894
Cdd:PRK05691   760 LP---EAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQT 836
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  895 ThgeaqAKAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHtatdtASENADPRAAARVAFALPAP 974
Cdd:PRK05691   837 A-----ELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDH-----PRSARQAHSAARYSLRVDAS 906
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  975 LAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEAATPLASLFSQ 1054
Cdd:PRK05691   907 LSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQ 986
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1055 LRQRTLDAQANQALPFDVLVEHLRPARdaQHGpLFETSFNYLSDDYPALARWPGARAERVEIAETHVKVPLALDLRESRD 1134
Cdd:PRK05691   987 VRQATLGAQAHQDLPFEQLVEALPQAR--EQG-LFQVMFNHQQRDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEDRN 1063
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1135 GSMRAYFTYASARFDAASVERMAAQYLRAVEAFAhalgdrsadmtDAAAPTLATLDLLDADERARVSAASVARRTPPGEP 1214
Cdd:PRK05691  1064 GRLTLSFDYAAELFDAATIERLAEHFLALLEQVC-----------EDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQAW 1132
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1215 IHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLlaRDLQGGEP--VAIVAHRSARFVVAMLGVLKAGGAYVA 1292
Cdd:PRK05691  1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYL--RDKGVGPDvcVAIAAERSPQLLVGLLAILKAGGAYVP 1210
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1293 LDAGNPTQRLAQTLRDCGARLVLCEDdcSALDLMgvqhARIDAAQEEAQREQHLRA-PHALPAVD--PRSAAYVIYTSGS 1369
Cdd:PRK05691  1211 LDPDYPAERLAYMLADSGVELLLTQS--HLLERL----PQAEGVSAIALDSLHLDSwPSQAPGLHlhGDNLAYVIYTSGS 1284
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1370 SGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAAR 1449
Cdd:PRK05691  1285 TGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYG 1364
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1450 IDVLKIVPGHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRAAAt 1529
Cdd:PRK05691  1365 VTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGERS- 1443
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1530 lPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFA-AGARLYRSGDRARRLADGSLE 1608
Cdd:PRK05691  1444 -PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALE 1522
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1609 YLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIV---VAGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSV 1685
Cdd:PRK05691  1523 YLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVregAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQ 1602
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1686 LRVIDALPLNRNGKLDRQALSAlarPAAPHREaaRAAPQGETETALAQCWAALLdpsngtdnatdnatATPSltIARDDS 1765
Cdd:PRK05691  1603 LIRLDQMPLGPSGKLDRRALPE---PVWQQRE--HVEPRTELQQQIAAIWREVL--------------GLPR--VGLRDD 1661
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1766 FFALGGHSLAAMRLASRVRSRWSVELPLREIFASPTLAALAARIEAQRADSDRASNQvsnkaanaesatPLHALADRSAL 1845
Cdd:PRK05691  1662 FFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGERNSQG------------AIARVDRSQPV 1729
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIWVVDQLADRALAsYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDeGDPVLKIAPRMEVLMpv 1925
Cdd:PRK05691  1730 PLSYSQQRMWFLWQMEPDSPA-YNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVD-GVPVQQVAEDSGLRM-- 1805
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1926 ieplahpdndansHTNSHTNSDENARTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVHI 2005
Cdd:PRK05691  1806 -------------DWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDI 1872
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2006 LLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRaRFTPDAVREAQ-QFWRGYLADAPALLPLSTDRARPTRVSHAGAA 2084
Cdd:PRK05691  1873 FARELGALYEAFLDDRESPLEPLPVQYLDYSVWQR-QWLESGERQRQlDYWKAQLGNEHPLLELPADRPRPPVQSHRGEL 1951
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2085 RHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSRIaaDG 2164
Cdd:PRK05691  1952 YRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQL--DG 2029
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2165 AnlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRDLPRGNTR-VPGLAVELLRPPTTQSK 2243
Cdd:PRK05691  2030 Q--MSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSRqLAGMTVEYLVNDARATK 2107
                         2250      2260      2270      2280      2290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1888712850 2244 FDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADPRAPLAS 2297
Cdd:PRK05691  2108 FDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAE 2161
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
711-2117 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 819.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  711 DAQDEAQDNAPIEPAEEAVISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFvetgd 790
Cdd:COG1020      1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRL----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  791 aAHLYAPRTEAAAPLAWAHVDLSDLGDIDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIAT 870
Cdd:COG1020     76 -RTRAGRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIIS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  871 DGWSMQLLVEELVDGYRAALDGATTHGEAQAkaktrITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHT 950
Cdd:COG1020    155 DGLSDGLLLAELLRLYLAAYAGAPLPLPPLP-----IQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRP 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  951 ATDTASenadpRAAARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIG 1030
Cdd:COG1020    230 RPAVQS-----YRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVG 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1031 FFVNTLVLHSDCEAATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPALaRWPGAR 1110
Cdd:COG1020    305 FFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADEL-ELPGLT 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1111 AERVEIAETHVKVPLALDLRESRDGsMRAYFTYASARFDAASVERMAAQYLRAVEAFAHALGDRsadmtdaaaptLATLD 1190
Cdd:COG1020    384 LEPLELDSGTAKFDLTLTVVETGDG-LRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQP-----------LGDLP 451
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1191 LLDADERARVSAA--SVARRTPPGEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAI 1268
Cdd:COG1020    452 LLTAAERQQLLAEwnATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGV 531
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1269 VAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDDC-SALDLMGVQHARIDAAQEEAQREQHLR 1347
Cdd:COG1020    532 CLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALaARLPELGVPVLALDALALAAEPATNPP 611
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1348 APhalpaVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGAL 1427
Cdd:COG1020    612 VP-----VTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATL 686
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1428 HLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAErAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYG 1507
Cdd:COG1020    687 VLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAA-PEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYG 765
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1508 PTETTVGILTQPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPF- 1586
Cdd:COG1020    766 PTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFg 845
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1587 AAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGA----RLAAFATPQPGA 1662
Cdd:COG1020    846 FPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDApgdkRLVAYVVPEAGA 925
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1663 SLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQalsALARPAAPHREAARAAPQGETETALAQCWAALLDps 1742
Cdd:COG1020    926 AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL---ALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLV-- 1000
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1743 ngtdnatdnatatpsLTIARDDSFFALGGHSLAAMRLASRVRSRWSVELPLREIFASPTLAALAARIeaqradsdrasnq 1822
Cdd:COG1020   1001 ---------------VVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAA------------- 1052
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1823 vsnkAANAESATPLHALADRSALPLSLMQQRIWVVDQLADRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSA 1902
Cdd:COG1020   1053 ----AAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRAR 1128
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1903 FDADDEGDPVLKIAPRMEVLMPVIEPLAHPDNDanshtnshtnsdenARTQATAQALDDAARTPFDLSRAPLVRATLLRF 1982
Cdd:COG1020   1129 RAVRQEGPRLRLLVALAAALALAALLALLLAAA--------------AAAAELLAAAALLLLLALLLLALLLLLLLLLLL 1194
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1983 DAAHHVLIVSLHHIVADGGSVHILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADA 2062
Cdd:COG1020   1195 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLL 1274
                         1370      1380      1390      1400      1410
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850 2063 PALLPLSTDRARPTRVSHAGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQ 2117
Cdd:COG1020   1275 ALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
30-597 0e+00

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 599.61  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   30 LAQQRPEATALIVIDADGDT--RYDYAQLDRRARALAARFARDGAAAERALILMDSGVDYVSAFFGCLYAGVVAVPVYPP 107
Cdd:cd05931      2 RAAARPDRPAYTFLDDEGGReeTLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  108 EskREQHLARLRGIARDAGVRYVLTTAALHER-HADAWSMLAPGADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSG 186
Cdd:cd05931     82 T--PGRHAERLAAILADAGPRVVLTTAAALAAvRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  187 STGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQYFLERPLRWLDAIA 266
Cdd:cd05931    160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRWLRLIS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  267 RHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAALYPCYGLAEATLFVT 346
Cdd:cd05931    240 RYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEATLFVS 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  347 GGVRGAGLVSHAFSSAALSAGRAEAARADEAATVLVGCGAVQAGHRVAIvaraaaeshesheadVETETSRageRLADGR 426
Cdd:cd05931    320 GGPPGTGPVVLRVDRDALAGRAVAVAADDPAARELVSCGRPLPDQEVRI---------------VDPETGR---ELPDGE 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  427 IGEIHVSGPSVAHGYWQRADASAQAFvdAPRHADGSGParWLRTGDLGFVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQA 506
Cdd:cd05931    382 VGEIWVRGPSVASGYWGRPEATAETF--GALAATDEGG--WLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEAT 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  507 VEAHAEFARKGRVIAFGATLGGGETLGLALEIAPRmKKRFAAAQIVETLRRIAFDACGETPAAIALLNPGALPKTSSGKL 586
Cdd:cd05931    458 AEEAHPALRPGCVAAFSVPDDGEERLVVVAEVERG-ADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKI 536
                          570
                   ....*....|.
gi 1888712850  587 QRAATREGWRA 597
Cdd:cd05931    537 QRRACRAAYLD 547
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1240-1644 5.53e-129

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 412.04  E-value: 5.53e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLLARD-LQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCED 1318
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGgVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1319 DCSALDLMGVQHARIDAAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPP 1398
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1399 RARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAAR-IDVLKIVPGHLHALLQA-ERAADALpaH 1476
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAAlPPALASL--R 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1477 TLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVG-ILTQPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGG 1555
Cdd:TIGR01733  239 LVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWsTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1556 TGELYLGGAGVALGYLHQPALTAARFVPHPFA--AGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARL 1633
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 398
                          410
                   ....*....|.
gi 1888712850 1634 KALDGVRDAAV 1644
Cdd:TIGR01733  399 LRHPGVREAVV 409
AMP-binding pfam00501
AMP-binding enzyme;
1219-1620 1.02e-90

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 302.31  E-value: 1.02e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAV-IDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGN 1297
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 PTQRLAQTLRDCGARLVLCEDDCSALDLMGVQHAR--------IDAAQEEAQREQHLRA------PHALPAVDPRSAAYV 1363
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLevvklvlvLDRDPVLKEEPLPEEAkpadvpPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1364 IYTSGSSGAPKGVVIAHGALTNYVDAV----LARLDPPPRARFAMVSTIGADLGHTV-LFGALASGGALHLIDRDTTLDA 1438
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1439 DRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAH--TLVLGGEATSWELLDTIAALRPdCRVHNHYGPTETTvGIL 1516
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSlrLVLSGGAPLPPELARRFRELFG-GALVNGYGLTETT-GVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1517 TQPAAQACRAAATLPLGRPLDNNETWLLD-EHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPhpfaagARLYRS 1595
Cdd:pfam00501  319 TTPLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRT 392
                          410       420
                   ....*....|....*....|....*
gi 1888712850 1596 GDRARRLADGSLEYLGRIDDQVKIR 1620
Cdd:pfam00501  393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
75-588 9.35e-90

FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.


Pssm-ID: 468603 [Multi-domain]  Cd Length: 613  Bit Score: 306.58  E-value: 9.35e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPP-ESKREQHLarlRGIARDAGVRYVLTT----AALHERHADAwsmlaP 149
Cdd:NF040633    87 DRVAILANNSPEYIFGFLGALYAGMVPVPLYDPnEPGHADHL---RAVLADSGPTVVLTNktsaPAVRAHFADL-----P 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  150 GAD---VVAVDTL-------------DARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLG 213
Cdd:NF040633   159 AAErprILSVDSLpdslaeswvnpmaTIEGQPLLAPAGTDPSDDTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQ 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  214 VRPDDVFVSWLPLYHDMGLIGSLLQPVFsGIPLVLMSPQYFLERPLRWLDAIARHRG---TISGAPDFAYRLCAERINDE 290
Cdd:NF040633   239 LKTPLRLVSWLPLHHDMGIILAAFVTIL-GLEFELMSPRDFIQQPKRWVDQLSRREDdvnVYTVVPNFALELAARYANPE 317
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  291 TRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGRAE 370
Cdd:NF040633   318 EGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERPLFTYFDREALAEGRAV 397
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  371 AARADEAATV-LVGCGAVQAGHrvaivaraaaeshesHEADVETETsraGERLADGRIGEIHVSGPSVAHGYWQRADASA 449
Cdd:NF040633   398 EVAEDSENAVpFASNGQVVRPQ---------------VLAIVDPET---GQELPDGTVGEIWVHGDNMAAGYLDREEETA 459
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  450 QAF-------VDAPRHADGSGPARWLRTGDLGFVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAF 522
Cdd:NF040633   460 ETFrntlgerLAENSRAEGAPEDNWMATGDLGVIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAF 539
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1888712850  523 GATLGGGETLGLaleIAPRMKKRFAA--AQIVETLRRIAFDACGETPAAIALLNPGALPKTSSGKLQR 588
Cdd:NF040633   540 AVPGDDVEKLVI---LAERDDEADESgdAEAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIAR 604
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
75-592 3.46e-89

long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.


Pssm-ID: 468483 [Multi-domain]  Cd Length: 625  Bit Score: 305.11  E-value: 3.46e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKreQHLARLRGIARDAGVRYVLTTAALHERHADAWSMLaPGAD-- 152
Cdd:NF038339    77 DRVAILAPQGLDYVVSFFAAIYAGNIAVPLFDPDEP--GHTDRLHAVLGDCKPSAILTATSSAEGVRKFFRSL-PAKErp 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  153 -VVAVDTLDarDTPSDAPLHP-VRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDM 230
Cdd:NF038339   154 rVIAVDAVP--DSVGSTWVRPdADLDDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDENSRGVTWLPLFHDM 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  231 GLIGSLLQPVFsGIPLVLMSPQYFLERPLRWLDAIAR---HRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGS 307
Cdd:NF038339   232 GLLTVILPALG-GKYITIMSPAAFVRRPGRWIRELAAvsdGAGTFAAAPNFAFEHAAARGLPKEGEPLDLSNVIGLINGS 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  308 EPVRRDTLDDFVARFAPAGFDAAALYPCYGLAEATLFVTGGVRG-AGLVSHAfSSAALSAGRAEAARADEAATVL-VGCG 385
Cdd:NF038339   311 EPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREdEAKVIYV-DREELNAGRIVEVDPDAPNAVAqVSCG 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  386 AVqaghrvaivaraaaeSHESHEADVETETsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAF-------VDAPRH 458
Cdd:NF038339   390 YV---------------ARSQWAVIVDPET---GTELPDGQVGEIWLHGNNIGTGYWGRPEETEETFhnklksrLEEGSH 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  459 ADGSGP-ARWLRTGDLGFVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAF--------------- 522
Cdd:NF038339   452 AEGAPEdANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFsvpanqlpaevfens 531
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850  523 --GATLGGG---ETLGLALEIAPRMKKrFAAAQIVETLRRIAFDACGETPAAIALLNPGALPKTSSGKLQRAATR 592
Cdd:NF038339   532 hsGLKYDADdssEQLVIVAERAPGAGK-ADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACK 605
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
27-598 7.93e-87

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 296.79  E-value: 7.93e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   27 LRALAQQRPEATALIVIDADGD-----TRYDYAQLDRRARALAARFARDGAAAERALILMDSGVDYVSAFFGCLYAGVVA 101
Cdd:NF038337    10 LRERAGLQPDDVAFRYTDYEQDwagvtETLTWAQLYRRTLNVAHEVRRHGTTGDRAVILAPQGLPYIVAFLGAMQAGLIA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  102 VPVYPPESKreQHLARLRGIARDAGVRYVLTTAAL------HERHADAwsmlAPGADVVAVDTLDArDTPSDAPLHPVRA 175
Cdd:NF038337    90 VPLSVPQPG--SHDERVSAVLADTSPSVVLTTSAAaaavaeYLHRPDT----GAVPAVIEIDSLDL-DGPNSPSIRISDA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  176 DDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGL-----GVRP-DDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLM 249
Cdd:NF038337   163 PSIAYLQYTSGSTRLPAGVMVSHRNLQVNFQQLMAAYfpdtnGVAPrDTTIVSWLPFYHDMGLVLGVIAPILGGYRSELT 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  250 SPQYFLERPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDA 329
Cdd:NF038337   243 SPVAFLQRPARWIHAMANGSPVFSAAPNFAFELAVRKTTDADLAGLDLGNVIGIVSGAERIHPATLDRFCKRFAPYNFRE 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  330 AALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGrAEAARADEAATVLVGCGAVQaghrvaivaraaaeSHESHEA 409
Cdd:NF038337   323 DMMQPSYGLAEATVYVASRAEGGAPEVVHFEPEKLSEG-SAQRCEARTGSPLLSYGTPT--------------SPTVRIV 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  410 DVETETSRagerlADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHADGSGPAR-WLRTGDLGFVHDGQLYIAGRVK 488
Cdd:NF038337   388 DPDTCIEC-----PAGTVGEIWVHGDNVAEGYWQKPEETRRTFGGVLANPSPGTPEGpWLRTGDLGFISEDEMFIVGRMK 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  489 DLVIVRGRNLYPQDVEQAVEAhaefARKGRVIAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRR----IAFDACG 564
Cdd:NF038337   463 DLLIVYGRNHYPEDIESTVQE----ITGGRVAAISVPVDETEKLVTIIELKKRGDSDEEAMRKLDAVKNnvtaAISRSHG 538
                          570       580       590
                   ....*....|....*....|....*....|....
gi 1888712850  565 ETPAAIALLNPGALPKTSSGKLQRAATREGWRAR 598
Cdd:NF038337   539 LNVADLVLVPPGSIPTTTSGKIRRAACVEQYRRQ 572
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1716-1812 4.03e-05

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 44.16  E-value: 4.03e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  1716 REAARAAPQGETETALAQCWAALLDpsngtdnatdnatATPSLTIARDDSFFALGGHSLAAMRLASRVRSRWSVELPLRE 1795
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLG-------------HAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATL 68
                            90
                    ....*....|....*..
gi 1888712850  1796 IFASPTLAALAARIEAQ 1812
Cdd:smart00823   69 VFDHPTPAALAEHLAAE 85
 
Name Accession Description Interval E-value
PRK05691 PRK05691
peptide synthase; Validated
21-2297 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1594.82  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   21 HGLAARLRALAQQRPEATALIVI--DADGDTRYDYAQLDRRARALAARFARDGAAAERALILMDSGVDYVSAFFGCLYAG 98
Cdd:PRK05691     9 LTLVQALQRRAAQTPDRLALRFLadDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGCLYAG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   99 VVAVPVYPPESKREQHLARLRGIARDAGVRYVLTTAALHERHADAWSMLAPGA-DVVAVDTLDArdTPSDAPLHP-VRAD 176
Cdd:PRK05691    89 VIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANApELLCVDTLDP--ALAEAWQEPaLQPD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  177 DLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLG--VRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQYF 254
Cdd:PRK05691   167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPAYF 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  255 LERPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAALYP 334
Cdd:PRK05691   247 LERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPDSFFA 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  335 CYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGRAEAARAdeaaTVLVGCGAVQAGHRvaivaraaaeshesheadVETE 414
Cdd:PRK05691   327 SYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGTG----SVLMSCGRSQPGHA------------------VLIV 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  415 TSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhaDGSgpaRWLRTGDLGFVHDGQLYIAGRVKDLVIVR 494
Cdd:PRK05691   385 DPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH----DGR---TWLRTGDLGFLRDGELFVTGRLKDMLIVR 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  495 GRNLYPQDVEQAVEAHAEFARKGRVIAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDACGETPAAIALLN 574
Cdd:PRK05691   458 GHNLYPQDIEKTVEREVEVVRKGRVAAFAVNHQGEEGIGIAAEISRSVQKILPPQALIKSIRQAVAEACQEAPSVVLLLN 537
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  575 PGALPKTSSGKLQRAATREGWRARTLDLYALWEQGAFVIGGDDDAARAPDapaaldarESALAALWCEALDARlALAPDA 654
Cdd:PRK05691   538 PGALPKTSSGKLQRSACRLRLADGSLDSYALFPALQAVEAAQTAASGDEL--------QARIAAIWCEQLKVE-QVAADD 608
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  655 HFFASGGSSLSAARLVALIGARLGRRVALAQIFETPTLAAMAAalaepeSVEEAQDDAQDEAQDNAPIEPAEEAVISHAQ 734
Cdd:PRK05691   609 HFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSA------AVARQLAGGGAAQAAIARLPRGQALPQSLAQ 682
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  735 QRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHlyaPRTEAAAPLAWAHVDLSD 814
Cdd:PRK05691   683 NRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVAL---QRIDAQGEFALQRIDLSD 759
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  815 LGdidEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAALDGAT 894
Cdd:PRK05691   760 LP---EAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQT 836
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  895 ThgeaqAKAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHtatdtASENADPRAAARVAFALPAP 974
Cdd:PRK05691   837 A-----ELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDH-----PRSARQAHSAARYSLRVDAS 906
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  975 LAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEAATPLASLFSQ 1054
Cdd:PRK05691   907 LSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQ 986
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1055 LRQRTLDAQANQALPFDVLVEHLRPARdaQHGpLFETSFNYLSDDYPALARWPGARAERVEIAETHVKVPLALDLRESRD 1134
Cdd:PRK05691   987 VRQATLGAQAHQDLPFEQLVEALPQAR--EQG-LFQVMFNHQQRDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEDRN 1063
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1135 GSMRAYFTYASARFDAASVERMAAQYLRAVEAFAhalgdrsadmtDAAAPTLATLDLLDADERARVSAASVARRTPPGEP 1214
Cdd:PRK05691  1064 GRLTLSFDYAAELFDAATIERLAEHFLALLEQVC-----------EDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQAW 1132
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1215 IHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLlaRDLQGGEP--VAIVAHRSARFVVAMLGVLKAGGAYVA 1292
Cdd:PRK05691  1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYL--RDKGVGPDvcVAIAAERSPQLLVGLLAILKAGGAYVP 1210
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1293 LDAGNPTQRLAQTLRDCGARLVLCEDdcSALDLMgvqhARIDAAQEEAQREQHLRA-PHALPAVD--PRSAAYVIYTSGS 1369
Cdd:PRK05691  1211 LDPDYPAERLAYMLADSGVELLLTQS--HLLERL----PQAEGVSAIALDSLHLDSwPSQAPGLHlhGDNLAYVIYTSGS 1284
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1370 SGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAAR 1449
Cdd:PRK05691  1285 TGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYG 1364
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1450 IDVLKIVPGHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRAAAt 1529
Cdd:PRK05691  1365 VTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGERS- 1443
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1530 lPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFA-AGARLYRSGDRARRLADGSLE 1608
Cdd:PRK05691  1444 -PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALE 1522
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1609 YLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIV---VAGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSV 1685
Cdd:PRK05691  1523 YLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVregAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQ 1602
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1686 LRVIDALPLNRNGKLDRQALSAlarPAAPHREaaRAAPQGETETALAQCWAALLdpsngtdnatdnatATPSltIARDDS 1765
Cdd:PRK05691  1603 LIRLDQMPLGPSGKLDRRALPE---PVWQQRE--HVEPRTELQQQIAAIWREVL--------------GLPR--VGLRDD 1661
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1766 FFALGGHSLAAMRLASRVRSRWSVELPLREIFASPTLAALAARIEAQRADSDRASNQvsnkaanaesatPLHALADRSAL 1845
Cdd:PRK05691  1662 FFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGERNSQG------------AIARVDRSQPV 1729
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIWVVDQLADRALAsYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDeGDPVLKIAPRMEVLMpv 1925
Cdd:PRK05691  1730 PLSYSQQRMWFLWQMEPDSPA-YNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVD-GVPVQQVAEDSGLRM-- 1805
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1926 ieplahpdndansHTNSHTNSDENARTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVHI 2005
Cdd:PRK05691  1806 -------------DWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDI 1872
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2006 LLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRaRFTPDAVREAQ-QFWRGYLADAPALLPLSTDRARPTRVSHAGAA 2084
Cdd:PRK05691  1873 FARELGALYEAFLDDRESPLEPLPVQYLDYSVWQR-QWLESGERQRQlDYWKAQLGNEHPLLELPADRPRPPVQSHRGEL 1951
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2085 RHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSRIaaDG 2164
Cdd:PRK05691  1952 YRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQL--DG 2029
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2165 AnlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRDLPRGNTR-VPGLAVELLRPPTTQSK 2243
Cdd:PRK05691  2030 Q--MSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSRqLAGMTVEYLVNDARATK 2107
                         2250      2260      2270      2280      2290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1888712850 2244 FDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADPRAPLAS 2297
Cdd:PRK05691  2108 FDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAE 2161
PRK12467 PRK12467
peptide synthase; Provisional
713-2296 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1189.58  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  713 QDEAQD--NAPIEPAEEAV----ISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFV 786
Cdd:PRK12467    29 QEEGVSfaNLPIPQVRSAFeripLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFV 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  787 ETGDAAhlyapRTEAAAPLAwAHVDLSDLGDIDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALH 866
Cdd:PRK12467   109 QDEEGF-----RQVIDASLS-LTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLH 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  867 HIATDGWSMQLLVEELVDGYRAALDGAtthgEAQAkAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALP 946
Cdd:PRK12467   183 HIISDGWSMRVLVEELVQLYSAYSQGR----EPSL-PALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELP 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  947 YDHtatdtasenadPRAA------ARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANR 1020
Cdd:PRK12467   258 TDR-----------PRPAvpsyrgARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1021 TRPETHDVIGFFVNTLVLHSDCEAATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSD-- 1098
Cdd:PRK12467   327 NRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTat 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1099 --DYPALARWPGARAERVEIAETHVKVPLALDLRESRDGsMRAYFTYASARFDAASVERMAAQYLRAVEAFAHALGDRsa 1176
Cdd:PRK12467   407 ggRDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQG-LWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRR-- 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1177 dmtdaaaptLATLDLLDADERAR-VSAASVARRTPPGEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWL 1255
Cdd:PRK12467   484 ---------LGELPLLDAEERAReLVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVL 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1256 LARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDDCSALDLMGVQHARIDA 1335
Cdd:PRK12467   555 IAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCL 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1336 AQEEAQReQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHT 1415
Cdd:PRK12467   635 DEPADLL-CGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVT 713
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1416 VLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAA 1495
Cdd:PRK12467   714 ELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRA 793
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1496 LRPDCRVHNHYGPTETTVGILTQPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPA 1575
Cdd:PRK12467   794 LGPGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPA 873
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1576 LTAARFVPHPFAA-GARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV---AGAR 1651
Cdd:PRK12467   874 LTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQpgdAGLQ 953
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1652 LAAFATPQPGASLDAAALKRAL-----AALLPDYMVPSVLRVIDALPLNRNGKLDRQALSalaRPAAPHREAARAAPQGE 1726
Cdd:PRK12467   954 LVAYLVPAAVADGAEHQATRDElkaqlRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALP---KPDASAVQATFVAPQTE 1030
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1727 TETALAQCWAALLDPSNgtdnatdnatatpsltIARDDSFFALGGHSLAAMRLASRVRSRWSVELPLREIFASPTLAALA 1806
Cdd:PRK12467  1031 LEKRLAAIWADVLKVER----------------VGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFA 1094
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1807 ARIEAQradsdrasnqvsnkaanAESATPLHALADRSA-LPLSLMQQRIWVVDQLaDRALASYNMTAGLDLRGPLDAARL 1885
Cdd:PRK12467  1095 QAVAAQ-----------------QQGAQPALPDVDRDQpLPLSYAQERQWFLWQL-EPGSAAYHIPQALRLKGPLDIEAL 1156
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1886 QRSLAALIARHEVLRSAFdADDEGDPVLKIAPRMEVlmpviePLAHPDNDANshtnshTNSDENARTQATAQalddaART 1965
Cdd:PRK12467  1157 ERSFDALVARHESLRTTF-VQEDGRTRQVIHPVGSL------TLEEPLLLAA------DKDEAQLKVYVEAE-----ARQ 1218
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1966 PFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVHILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFtp 2045
Cdd:PRK12467  1219 PFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWM-- 1296
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2046 DAVREAQQ--FWRGYLADAPALLPLSTDRARPTRVSHAGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRH 2123
Cdd:PRK12467  1297 DAGERARQlaYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRY 1376
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2124 TGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSRIaaDGAnlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKR 2203
Cdd:PRK12467  1377 SGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEV--DGQ--ASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPER 1452
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2204 RRDANPLVQVLFV-LRDLPRGNTRVPGLAVELLRPPTTQSKFDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRA 2282
Cdd:PRK12467  1453 SLSHSPLFQVMFNhQRDDHQAQAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLN 1532
                         1610
                   ....*....|....
gi 1888712850 2283 TLDAVSADPRAPLA 2296
Cdd:PRK12467  1533 LLQGLVADPERRLG 1546
PRK12467 PRK12467
peptide synthase; Provisional
21-2286 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 927.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   21 HGLAARLRALAQQRPEATALIVidadGDTRYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFFGCLYAGV 99
Cdd:PRK12467   512 DCVHQLIEAQARQHPERPALVF----GEQVLSYAELNRQANRLAHVLIAAGVGPDvLVGIAVERSIEMVVGLLAVLKAGG 587
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  100 VAVPVYPpeskrEQHLARLRGIARDAGVRYVLTTAALHERhadawsmLAPGADVVAVDTLDARDTPSDAPLH----PVRA 175
Cdd:PRK12467   588 AYVPLDP-----EYPQDRLAYMLDDSGVRLLLTQSHLLAQ-------LPVPAGLRSLCLDEPADLLCGYSGHnpevALDP 655
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  176 DDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGlIGSLLQPVFSGIPLVLMSPQYFL 255
Cdd:PRK12467   656 DNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLG-VTELFGALASGATLHLLPPDCAR 734
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  256 ErPLRWLDAIARHRGTISGAPDFAYRLcaerINDETRAKLDLSSWRLAFSGSE-PVrrdtldDFVARFAPAGfDAAALYP 334
Cdd:PRK12467   735 D-AEAFAALMADQGVTVLKIVPSHLQA----LLQASRVALPRPQRALVCGGEAlQV------DLLARVRALG-PGARLIN 802
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  335 CYGLAEATLFVT-GGVRGAGLVSHAFSSAALSAGRAEAARADEAATVLVGCgavqaghrvaivaraaaeshesheadvet 413
Cdd:PRK12467   803 HYGPTETTVGVStYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGV----------------------------- 853
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  414 etsragerladgrIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHADGSgpaRWLRTGDLG-FVHDGQLYIAGRVKDLVI 492
Cdd:PRK12467   854 -------------VGELYIGGAGLARGYHRRPALTAERFVPDPFGADGG---RLYRTGDLArYRADGVIEYLGRMDHQVK 917
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  493 VRGRNLYPQDVEQAVEAHAEfARKGRVIAfgatLGGGETLGLALEIAPRMKKRFAAAQIV-ETLRRIAFDACGE--TPAA 569
Cdd:PRK12467   918 IRGFRIELGEIEARLLAQPG-VREAVVLA----QPGDAGLQLVAYLVPAAVADGAEHQATrDELKAQLRQVLPDymVPAH 992
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  570 IALLNpgALPKTSSGKLQRAA--------TREGWRARTLDLyalweqgafviggdddaarapdapaaldarESALAALWC 641
Cdd:PRK12467   993 LLLLD--SLPLTPNGKLDRKAlpkpdasaVQATFVAPQTEL------------------------------EKRLAAIWA 1040
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  642 EALDA-RLALapDAHFFASGGSSLSAARLVALIGARLGRRVALAQIFETPTLaamaaalaepESVEEAQDDAQDEAQDNA 720
Cdd:PRK12467  1041 DVLKVeRVGL--TDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTL----------AGFAQAVAAQQQGAQPAL 1108
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  721 PIEPAEEA-VISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYaprT 799
Cdd:PRK12467  1109 PDVDRDQPlPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQV---I 1185
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  800 EAAAPLAWAHvDLSDLGDIDEhdreRALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLV 879
Cdd:PRK12467  1186 HPVGSLTLEE-PLLLAADKDE----AQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLV 1260
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  880 EELVDGYRAaldgaTTHGEAQAKAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHtatdtasena 959
Cdd:PRK12467  1261 DELVALYAA-----YSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDR---------- 1325
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  960 dPRAA------ARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFV 1033
Cdd:PRK12467  1326 -PRPAvqshrgARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFV 1404
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1034 NTLVLHSDCEAATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPALARWPGARAER 1113
Cdd:PRK12467  1405 NTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAQLPGLSVES 1484
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1114 VEIAETHVKVPLALDLRESRDGsMRAYFTYASARFDAASVERMAAQYLRAVEAFAhalgdrsadmTDAAAPtLATLDLLD 1193
Cdd:PRK12467  1485 LSWESQTAQFDLTLDTYESSEG-LQASLTYATDLFEASTIERLAGHWLNLLQGLV----------ADPERR-LGELDLLD 1552
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1194 ADERARVSAA--SVARRTPPGEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAH 1271
Cdd:PRK12467  1553 EAERRQILEGwnATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVE 1632
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1272 RSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDD-CSALDLM-GVQHARIDaaQEEAQREQHLRAP 1349
Cdd:PRK12467  1633 RSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHlQARLPLPdGLRSLVLD--QEDDWLEGYSDSN 1710
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1350 HALpAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHL 1429
Cdd:PRK12467  1711 PAV-NLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVI 1789
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1430 IDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQ-AERAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGP 1508
Cdd:PRK12467  1790 APPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQmDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGP 1869
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1509 TETTVGILTQPAAQACRA-AATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFA 1587
Cdd:PRK12467  1870 TETAVDVTHWTCRRKDLEgRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFG 1949
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1588 -AGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGA---RLAAFATPQPGAS 1663
Cdd:PRK12467  1950 tVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGAngkQLVAYVVPTDPGL 2029
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1664 LDAAALKRAL--------AALLPDYMVPSVLRVIDALPLNRNGKLDRQALSalaRPAAPHREAARAAPQGETETALAQCW 1735
Cdd:PRK12467  2030 VDDDEAQVALrailknhlKASLPEYMVPAHLVFLARMPLTPNGKLDRKALP---APDASELQQAYVAPQSELEQRLAAIW 2106
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1736 AALLDPSNgtdnatdnatatpsltIARDDSFFALGGHSLAAMRLASRVRSRwSVELPLREIFASPTLAALAARIEAQRAd 1815
Cdd:PRK12467  2107 QDVLGLEQ----------------VGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAVAQEGDG- 2168
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1816 sdrasnQVSNKAANAESATPLhaladrsaLPLslmqQRIWVVDQLADRalASYNMTAGLDLRGPLDAARLQRSLAALIAR 1895
Cdd:PRK12467  2169 ------TVSIDQGPVTGDLPL--------LPI----QQMFFADDIPER--HHWNQSVLLEPREALDAELLEAALQALLVH 2228
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1896 HEVLRSAFDADDEGDPVLKIAPRmEVLMPVIEPLAHPDNDANshtnshtnsdenartqataQALDDAARTPFDLSRAPLV 1975
Cdd:PRK12467  2229 HDALRLGFVQEDGGWSAMHRAPE-QERRPLLWQVVVADKEEL-------------------EALCEQAQRSLDLEEGPLL 2288
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1976 RATLLRFDAAHHVLIVSLHHIVADGGSVHILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFTPDAVREAQQFW 2055
Cdd:PRK12467  2289 RAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYW 2368
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2056 RGYLADAPALLPLSTDRARPTRVSHAGAARHFRLDATLgarvRTLAQAhgmtPFA-------VLLASFQWFLHRHTGADD 2128
Cdd:PRK12467  2369 QAQLQGASTELPCDHPQGGLQRRHAASVTTHLDSEWTR----RLLQEA----PAAyrtqvndLLLTALARVIARWTGQAS 2440
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2129 LVIGTDVDGRE----RAELEALIGFFVNVVPLRsriaadganlASFDAWLDAARQSTWDALdhRALPfDRIVDALALkrR 2204
Cdd:PRK12467  2441 TLIQLEGHGREdlfdEIDLTRTVGWFTSLYPVK----------LSPTASLATSIKTIKEQL--RAVP-NKGLGFGVL--R 2505
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2205 RDANPLVQVlfVLRDLPRGNTRVPGLAvellrppttqsKFD-------MALFVEAVD----------------------- 2254
Cdd:PRK12467  2506 YLGSEAARQ--TLQALPVPRITFNYLG-----------QFDgsfdaekQALFVPSGEfsgaeqseeaplgnwlsingqvy 2572
                         2330      2340      2350
                   ....*....|....*....|....*....|...
gi 1888712850 2255 -GGYDIEWVYASALFDAATIERAFDAWRATLDA 2286
Cdd:PRK12467  2573 gGELNLGWTFSQEMFDEATIQRLADAYAEELRA 2605
PRK12316 PRK12316
peptide synthase; Provisional
21-2289 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 886.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   21 HGLAARLRALAQQRPEATALIVidadGDTRYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFFGCLYAGV 99
Cdd:PRK12316  2003 PGVHQRIAEQAARAPEAIAVVF----GDQHLSYAELDSRANRLAHRLRARGVGPEvRVAIAAERSFELVVALLAVLKAGG 2078
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  100 VAVPV---YPPEskreqhlaRLRGIARDAGVRYVLTTAALHERhadawSMLAPGADVVAVDTLDA-RDTPSDAPLHPVRA 175
Cdd:PRK12316  2079 AYVPLdpnYPAE--------RLAYMLEDSGAALLLTQRHLLER-----LPLPAGVARLPLDRDAEwADYPDTAPAVQLAG 2145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  176 DDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDmGLIGSLLQPVFSGIPLVLMSPQYFL 255
Cdd:PRK12316  2146 ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFD-GAHEQWFHPLLNGARVLIRDDELWD 2224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  256 erPLRWLDAIARHRGTISGAPDFAYRLCAErinDETRAKLDLSSWRLAFSGsepvrrDTLDDFVARFAPAGFDAAALYPC 335
Cdd:PRK12316  2225 --PEQLYDEMERHGVTILDFPPVYLQQLAE---HAERDGRPPAVRVYCFGG------EAVPAASLRLAWEALRPVYLFNG 2293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  336 YGLAEATLFVTggvrgaglvshafssaalsagraeaaradeaatvLVGCGAVQAGHRVAIVARAAAESHESHEADVETET 415
Cdd:PRK12316  2294 YGPTEAVVTPL----------------------------------LWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNL 2339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  416 sragerLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHADGsgpARWLRTGDLG-FVHDGQLYIAGRVKDLVIVR 494
Cdd:PRK12316  2340 ------LAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASG---ERLYRTGDLArYRADGVVEYLGRIDHQVKIR 2410
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  495 GRNLYPQDVEQAVEAHaEFARKGRVIAfgatLGGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDACgeTPAAIALLN 574
Cdd:PRK12316  2411 GFRIELGEIEARLQAH-PAVREAVVVA----QDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYM--VPAHWVVLE 2483
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  575 pgALPKTSSGKLQRAATREgwrartLDLYALweQGAFViggdddaarapdapAALDARESALAALWCEALDARlALAPDA 654
Cdd:PRK12316  2484 --RLPLNPNGKLDRKALPK------PDVSQL--RQAYV--------------APQEGLEQRLAAIWQAVLKVE-QVGLDD 2538
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  655 HFFASGGSSLSAARLVALIGARLGRRVALAQIFETPTLAAMAAAlaepesveeAQDDAQDEAQDNAPIEPAEEAVISHAQ 734
Cdd:PRK12316  2539 HFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAAS---------LESGQTSRAPVLQKVTRVQPLPLSHAQ 2609
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  735 QRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYAPRTEAAAPLAWAHVDLSD 814
Cdd:PRK12316  2610 QRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVAD 2689
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  815 lgdidehdreRALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAAldgat 894
Cdd:PRK12316  2690 ----------AAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGA----- 2754
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  895 THGEAQAKAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHTATDTASenadpRAAARVAFALPAP 974
Cdd:PRK12316  2755 RRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQS-----HRGARLDVALDVA 2829
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  975 LAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEAATPLASLFSQ 1054
Cdd:PRK12316  2830 LSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQ 2909
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1055 LRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYlSDDYPALARWPGARAERVEIAETHVKVPLALDLRESRD 1134
Cdd:PRK12316  2910 VKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNH-QSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAE 2988
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1135 GsMRAYFTYASARFDAASVERMAAQYLRAVEAFAHAlgdrsadmtdaAAPTLATLDLLDADERARVSAA--SVARRTPPG 1212
Cdd:PRK12316  2989 G-LGASLTYATDLFDARTVERLARHWQNLLRGMVEN-----------PQRSVDELAMLDAEERGQLLEAwnATAAEYPLE 3056
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1213 EPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVA 1292
Cdd:PRK12316  3057 RGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVP 3136
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1293 LDAGNPTQRLAQTLRDCGARLVLCEDDCSALDLMGVQHARIDAAQEEAQREqhlrapHALPAVDPRSAAYVIYTSGSSGA 1372
Cdd:PRK12316  3137 LDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEA------NPAIRTMPENLAYVIYTSGSTGK 3210
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1373 PKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDV 1452
Cdd:PRK12316  3211 PKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDV 3290
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1453 LKIVPGHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAALRPdcrVHNHYGPTETTVGILTqpAAQACRAAATLPL 1532
Cdd:PRK12316  3291 LHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTH--WQCVEEGKDAVPI 3365
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1533 GRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGR 1612
Cdd:PRK12316  3366 GRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGR 3445
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1613 IDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDAL 1692
Cdd:PRK12316  3446 VDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERM 3525
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1693 PLNRNGKLDRQalsALARPAAPHREAARAAPQGETETALAQCWAALLDPSNgtdnatdnatatpsltIARDDSFFALGGH 1772
Cdd:PRK12316  3526 PLTPNGKLDRK---ALPRPDAALLQQDYVAPVNELERRLAAIWADVLKLEQ----------------VGLTDNFFELGGD 3586
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1773 SLAAMRLASRVRSRwSVELPLREIFASPTLAALAariEAQRADSDRASNQvsnkaANAESATPLHAlADRSALPLSLMQQ 1852
Cdd:PRK12316  3587 SIISLQVVSRARQA-GIRFTPKDLFQHQTIQGLA---RVARVGGGVAVDQ-----GPVSGETLLLP-IQQQFFEEPVPER 3656
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1853 RIWVVDQLadralasynmtagLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDEGDPV--LKIAPRMEVLMpviepla 1930
Cdd:PRK12316  3657 HHWNQSLL-------------LKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAehLPVELGGALLW------- 3716
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1931 hpdndanshtnshtnsDENARTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVHILLDEL 2010
Cdd:PRK12316  3717 ----------------RAELDDAEELERLGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDL 3780
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2011 CELYRAQRDGAPPALAPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADAPALLPlsTDRARPTRVSHAGAARHFRLD 2090
Cdd:PRK12316  3781 QQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSSELP--CDHPQGALQNRHAASVQTRLD 3858
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2091 ATLGARVRTLAQAHGMTPFA-VLLASFQWFLHRHTGADDLVIGTDVDGRER----AELEALIGFFVNVVPLRSRIAAD-G 2164
Cdd:PRK12316  3859 RELTRRLLQQAPAAYRTQVNdLLLTALARVVCRWTGEASALVQLEGHGREDlfadIDLSRTVGWFTSLFPVRLSPVEDlG 3938
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2165 ANLASFDAWL-----------------DAARQSTWDALDHRALPFDRivdalaLKRRRDANPLVQVLFVLRDLPRGNTRV 2227
Cdd:PRK12316  3939 ASIKAIKEQLraipnkgigfgllrylgDEESRRTLAGLPVPRITFNY------LGQFDGSFDEEMALFVPAGESAGAEQS 4012
                         2250      2260      2270      2280      2290      2300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850 2228 PGLAVELLrppttqskfdMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSA 2289
Cdd:PRK12316  4013 PDAPLDNW----------LSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVE 4064
PRK12316 PRK12316
peptide synthase; Provisional
720-2163 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 877.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  720 APIEPAEEAVISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYAPrt 799
Cdd:PRK12316    42 AGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVP-- 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  800 eAAAPLAWAHVDLSDLgdiDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLV 879
Cdd:PRK12316   120 -LDRPLEVEFEDCSGL---PEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLI 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  880 EELVDGYRAALDGATTHGEAQAkaktrITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHtatdtasena 959
Cdd:PRK12316   196 EEFSRFYSAYATGAEPGLPALP-----IQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDH---------- 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  960 dPRAA------ARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFV 1033
Cdd:PRK12316   261 -PRPAvpsyrgSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFV 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1034 NTLVLHSDCEAATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNY--LSDDYPALARWPGARA 1111
Cdd:PRK12316   340 NTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHqpLVADIEALDTVAGLEF 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1112 ERVEIAETHVKVPLALDLRESrDGSMRAYFTYASARFDAASVERMAAQYLRAVEAfahalgdrsadMTDAAAPTLATLDL 1191
Cdd:PRK12316   420 GQLEWKSRTTQFDLTLDTYEK-GGRLHAALTYATDLFEARTVERMARHWQNLLRG-----------MVENPQARVDELPM 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1192 LDADERARVSAA--SVARRTPPGEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIV 1269
Cdd:PRK12316   488 LDAEERGQLVEGwnATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVA 567
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1270 AHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDDCSALDLMGVQHARIDAAQEEAQREQHLRAP 1349
Cdd:PRK12316   568 MERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEEN 647
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1350 HALpAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHL 1429
Cdd:PRK12316   648 PGT-ELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVV 726
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1430 IDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPT 1509
Cdd:PRK12316   727 AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPT 806
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1510 ETTVGILTQpaAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAG 1589
Cdd:PRK12316   807 EAAIDVTHW--TCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAG 884
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1590 ARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGARLAAFATPQPGASLDAAAL 1669
Cdd:PRK12316   885 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDWREAL 964
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1670 KRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSAlarPAAPHREAARAAPQGETETALAQCWAALLDPSNgtdnat 1749
Cdd:PRK12316   965 KAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPA---PEASVAQQGYVAPRNALERTLAAIWQDVLGVER------ 1035
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1750 dnatatpsltIARDDSFFALGGHSLAAMRLASRVRsRWSVELPLREIFASPTLAALAarieaqradsdrasnqvsnKAAN 1829
Cdd:PRK12316  1036 ----------VGLDDNFFELGGDSIVSIQVVSRAR-QAGIQLSPRDLFQHQTIRSLA-------------------LVAK 1085
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1830 AESATPLHALADRSALPLSLMQQRIWvvdQLADRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDEG 1909
Cdd:PRK12316  1086 AGQATAADQGPASGEVALAPVQRWFF---EQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGG 1162
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1910 DPVLKIAPRMEvlmpviEPLAHPDndanshtnshtnsdenARTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVL 1989
Cdd:PRK12316  1163 WQQAYAAPQAG------EVLWQRQ----------------AASEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQRL 1220
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1990 IVSLHHIVADGGSVHILLDELCELYRAqrdgappALAPLAVQYADYAHW-QRARFTPDAVREAQQFWRGYLADAPALLPl 2068
Cdd:PRK12316  1221 LLVIHHLVVDGVSWRILLEDLQRAYAD-------LDADLPARTSSYQAWaRRLHEHAGARAEELDYWQAQLEDAPHELP- 1292
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2069 sTDRARPTRVSHAGAARHFRLDATLGARVRTLAQAHGMTPFA-VLLASFQWFLHRHTGADDLVIGTDVDGRE----RAEL 2143
Cdd:PRK12316  1293 -CENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNdLLLTALARVTCRWSGQASVLVQLEGHGREdlfeDIDL 1371
                         1450      1460
                   ....*....|....*....|
gi 1888712850 2144 EALIGFFVNVVPLRSRIAAD 2163
Cdd:PRK12316  1372 SRTVGWFTSLFPVRLTPAAD 1391
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
711-2117 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 819.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  711 DAQDEAQDNAPIEPAEEAVISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFvetgd 790
Cdd:COG1020      1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRL----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  791 aAHLYAPRTEAAAPLAWAHVDLSDLGDIDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIAT 870
Cdd:COG1020     76 -RTRAGRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIIS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  871 DGWSMQLLVEELVDGYRAALDGATTHGEAQAkaktrITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHT 950
Cdd:COG1020    155 DGLSDGLLLAELLRLYLAAYAGAPLPLPPLP-----IQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRP 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  951 ATDTASenadpRAAARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIG 1030
Cdd:COG1020    230 RPAVQS-----YRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVG 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1031 FFVNTLVLHSDCEAATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPALaRWPGAR 1110
Cdd:COG1020    305 FFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADEL-ELPGLT 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1111 AERVEIAETHVKVPLALDLRESRDGsMRAYFTYASARFDAASVERMAAQYLRAVEAFAHALGDRsadmtdaaaptLATLD 1190
Cdd:COG1020    384 LEPLELDSGTAKFDLTLTVVETGDG-LRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQP-----------LGDLP 451
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1191 LLDADERARVSAA--SVARRTPPGEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAI 1268
Cdd:COG1020    452 LLTAAERQQLLAEwnATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGV 531
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1269 VAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDDC-SALDLMGVQHARIDAAQEEAQREQHLR 1347
Cdd:COG1020    532 CLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALaARLPELGVPVLALDALALAAEPATNPP 611
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1348 APhalpaVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGAL 1427
Cdd:COG1020    612 VP-----VTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATL 686
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1428 HLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAErAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYG 1507
Cdd:COG1020    687 VLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAA-PEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYG 765
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1508 PTETTVGILTQPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPF- 1586
Cdd:COG1020    766 PTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFg 845
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1587 AAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGA----RLAAFATPQPGA 1662
Cdd:COG1020    846 FPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDApgdkRLVAYVVPEAGA 925
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1663 SLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQalsALARPAAPHREAARAAPQGETETALAQCWAALLDps 1742
Cdd:COG1020    926 AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL---ALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLV-- 1000
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1743 ngtdnatdnatatpsLTIARDDSFFALGGHSLAAMRLASRVRSRWSVELPLREIFASPTLAALAARIeaqradsdrasnq 1822
Cdd:COG1020   1001 ---------------VVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAA------------- 1052
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1823 vsnkAANAESATPLHALADRSALPLSLMQQRIWVVDQLADRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSA 1902
Cdd:COG1020   1053 ----AAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRAR 1128
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1903 FDADDEGDPVLKIAPRMEVLMPVIEPLAHPDNDanshtnshtnsdenARTQATAQALDDAARTPFDLSRAPLVRATLLRF 1982
Cdd:COG1020   1129 RAVRQEGPRLRLLVALAAALALAALLALLLAAA--------------AAAAELLAAAALLLLLALLLLALLLLLLLLLLL 1194
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1983 DAAHHVLIVSLHHIVADGGSVHILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADA 2062
Cdd:COG1020   1195 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLL 1274
                         1370      1380      1390      1400      1410
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850 2063 PALLPLSTDRARPTRVSHAGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQ 2117
Cdd:COG1020   1275 ALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
PRK12316 PRK12316
peptide synthase; Provisional
718-2297 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 791.08  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  718 DNAPIEPAEEAVI---SHAQQRQLFAWRLDPASRAYhvAAGIRLD-GALDREALRQSLDRLCERHAALRTHFVETGDAAH 793
Cdd:PRK12316  1544 DALPLPAGEIADIyplSPMQQGMLFHSLYEQEAGDY--INQLRVDvQGLDPDRFRAAWQATVDRHEILRSGFLWQDGLEQ 1621
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  794 -LYAPRTEAAAPLAwaHVDLSDLGDIDEhdrerALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDG 872
Cdd:PRK12316  1622 pLQVIHKQVELPFA--ELDWRGREDLGQ-----ALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDG 1694
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  873 WSMQLLVEELVDGYRaaldgatthGEAQAKAKTRitYADYAAWQRRwlaSDAAARQlAYWRAALADDAPPLALpydhtaT 952
Cdd:PRK12316  1695 WSNAQLLGEVLQRYA---------GQPVAAPGGR--YRDYIAWLQR---QDAAASE-AFWKEQLAALEEPTRL------A 1753
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  953 DTASENADPRAAARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTR--PETHDVIG 1030
Cdd:PRK12316  1754 QAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAelPGIEQQIG 1833
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1031 FFVNTLVLHSDCEAATPLASLFSQLRQRTLdaqanqALpfdvlvehlrpaRDAQHGPLFETS----------FNYL--SD 1098
Cdd:PRK12316  1834 LFINTLPVIAAPRPDQSVADWLQEVQALNL------AL------------REHEHTPLYDIQrwagqggealFDSLlvFE 1895
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1099 DYP---ALARWP--GARAERVEIAE-THVKVPLALDLRESrdgsMRAYFTYASARFDAASVERMAAQYLRAVEAFAhalg 1172
Cdd:PRK12316  1896 NYPvaeALKQGApaGLVFGRVSNHEqTNYPLTLAVTLGET----LSLQYSYDRGHFDAAAIERLDRHLLHLLEQMA---- 1967
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1173 drsadmtDAAAPTLATLDLLDADERARVSAAsvARRTPPGEP----IHLRVARHADTQPDAPAVIDGALRMSYAELDARA 1248
Cdd:PRK12316  1968 -------EDAQAALGELALLDAGERQRILAD--WDRTPEAYPrgpgVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRA 2038
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1249 AHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDDCSALDLM-- 1326
Cdd:PRK12316  2039 NRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLpa 2118
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1327 GVQHARIDAAQEEAQREQHlrapHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVS 1406
Cdd:PRK12316  2119 GVARLPLDRDAEWADYPDT----APAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFM 2194
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1407 TIGADLGHTVLFGALASGGALhLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQ-AERAADALPAHTLVLGGEAT 1485
Cdd:PRK12316  2195 SFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEhAERDGRPPAVRVYCFGGEAV 2273
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1486 SWELLD-TIAALRPDcRVHNHYGPTETTVGILT-QPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGG 1563
Cdd:PRK12316  2274 PAASLRlAWEALRPV-YLFNGYGPTEAVVTPLLwKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGG 2352
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1564 AGVALGYLHQPALTAARFVPHPFAA-GARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDA 1642
Cdd:PRK12316  2353 EGLARGYLNRPGLTAERFVPDPFSAsGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREA 2432
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1643 AVIVVAGA---RLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSalaRPAAPHREAA 1719
Cdd:PRK12316  2433 VVVAQDGAsgkQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALP---KPDVSQLRQA 2509
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1720 RAAPQGETETALAQCWAALLDPSNgtdnatdnatatpsltIARDDSFFALGGHSLAAMRLASRVRSRWSVELPLREIFAS 1799
Cdd:PRK12316  2510 YVAPQEGLEQRLAAIWQAVLKVEQ----------------VGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFER 2573
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1800 PTLAALAARIEAQRAdsdrasnqvsnkaanaESATPLHALADRSALPLSLMQQRIWVVDQLaDRALASYNMTAGLDLRGP 1879
Cdd:PRK12316  2574 PTLAAFAASLESGQT----------------SRAPVLQKVTRVQPLPLSHAQQRQWFLWQL-EPESAAYHLPSALHLRGV 2636
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1880 LDAARLQRSLAALIARHEVLRSAFDADDEGdPVLKIAPRMEVLMPVIEPLAHPDndanshtnshtnsdenartQATAQAL 1959
Cdd:PRK12316  2637 LDQAALEQAFDALVLRHETLRTRFVEVGEQ-TRQVILPNMSLRIVLEDCAGVAD-------------------AAIRQRV 2696
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1960 DDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVHILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQ 2039
Cdd:PRK12316  2697 AEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQ 2776
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2040 RARFTPDAVREAQQFWRGYLADAPALLPLSTDRARPTRVSHAGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWF 2119
Cdd:PRK12316  2777 RAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVL 2856
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2120 LHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRsriaADGANLASFDAWLDAARQSTWDALDHRALPFDRIVDAL 2199
Cdd:PRK12316  2857 LHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLR----AQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEAL 2932
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2200 ALKRRRDANPLVQVLFVLRDLPRGNTRVPGLAVELLRPPTTQSKFDMALFVEAVDGGYDIEWVYASALFDAATIERAFDA 2279
Cdd:PRK12316  2933 QPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARH 3012
                         1610
                   ....*....|....*...
gi 1888712850 2280 WRATLDAVSADPRAPLAS 2297
Cdd:PRK12316  3013 WQNLLRGMVENPQRSVDE 3030
PRK05691 PRK05691
peptide synthase; Validated
19-2302 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 773.57  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   19 PAHGLAARLRALAQQRPEATALIvidADGDTrYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFFGCLYA 97
Cdd:PRK05691  1129 AQAWLPELLNEQARQTPERIALV---WDGGS-LDYAELHAQANRLAHYLRDKGVGPDvCVAIAAERSPQLLVGLLAILKA 1204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   98 GVVAVPV---YPPEskreqhlaRLRGIARDAGVRYVLTTAALHERHADAwsmlaPGADVVAVDTLDARDTPSDAPLHPVR 174
Cdd:PRK05691  1205 GGAYVPLdpdYPAE--------RLAYMLADSGVELLLTQSHLLERLPQA-----EGVSAIALDSLHLDSWPSQAPGLHLH 1271
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  175 ADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGlIGSLLQPVFSGIPLVLMSPQYF 254
Cdd:PRK05691  1272 GDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVS-VWECFWPLITGCRLVLAGPGEH 1350
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  255 LErPLRWLDAIARHRGTISgapDFAYRLCAERInDETRAKlDLSSWRLAFSGSEPVRRDTLDDFVARFApagfdAAALYP 334
Cdd:PRK05691  1351 RD-PQRIAELVQQYGVTTL---HFVPPLLQLFI-DEPLAA-ACTSLRRLFSGGEALPAELRNRVLQRLP-----QVQLHN 1419
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  335 CYGLAEATLFVTggvrgaglvsHAFSSAalSAGRAEAARADEAATVlvgCGAVqaghrvaivaraaaeshesheaDVETE 414
Cdd:PRK05691  1420 RYGPTETAINVT----------HWQCQA--EDGERSPIGRPLGNVL---CRVL----------------------DAELN 1462
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  415 TsragerLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHADGsgpARWLRTGDLG-FVHDGQLYIAGRVKDLVIV 493
Cdd:PRK05691  1463 L------LPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDG---ARLYRTGDRArWNADGALEYLGRLDQQVKL 1533
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  494 RGRNLYPQDVEQAVEAHAEFARKGRVI---AFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLrriafdacgeTPAAI 570
Cdd:PRK05691  1534 RGFRVEPEEIQARLLAQPGVAQAAVLVregAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYM----------VPAQL 1603
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  571 ALLNpgALPKTSSGKLQRAATREgwrartldlyALWEQGAFViggdddaarapdapAALDARESALAALWCEALD-ARLA 649
Cdd:PRK05691  1604 IRLD--QMPLGPSGKLDRRALPE----------PVWQQREHV--------------EPRTELQQQIAAIWREVLGlPRVG 1657
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  650 LAPDahFFASGGSSLSAARLVALIGARLGRRVALAQIFETPTLAAMAaalaepESVEEAQDD-AQDEAQDNAPIEPAEEA 728
Cdd:PRK05691  1658 LRDD--FFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFA------EQVARIQAAgERNSQGAIARVDRSQPV 1729
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  729 VISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHlyaprtEAAAPLAWA 808
Cdd:PRK05691  1730 PLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPV------QQVAEDSGL 1803
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  809 HVDLSDLGDIDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRA 888
Cdd:PRK05691  1804 RMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEA 1883
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  889 ALDGATTHGEAQAkaktrITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHtatdtasenadPRAAAR-- 966
Cdd:PRK05691  1884 FLDDRESPLEPLP-----VQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADR-----------PRPPVQsh 1947
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  967 ----VAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDC 1042
Cdd:PRK05691  1948 rgelYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQL 2027
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1043 EAATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPALARWPGARAERVEIAETHVK 1122
Cdd:PRK05691  2028 DGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSRQLAGMTVEYLVNDARATK 2107
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1123 VPLALDLREsRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAfahalgdrsadMTDAAAPTLATLDLLDADERARV-- 1200
Cdd:PRK05691  2108 FDLNLEVTD-LDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEA-----------LLGDPQQRLAELPLLAAAEQQQLld 2175
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1201 SAASVARRTPPGEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAM 1280
Cdd:PRK05691  2176 SLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGL 2255
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1281 LGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLceDDCSALDLMGVQHARI-------DAAQEEAQreqhlrAPHALP 1353
Cdd:PRK05691  2256 LAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL--SDRALFEALGELPAGVarwcledDAAALAAY------SDAPLP 2327
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1354 AVD-PRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLiDR 1432
Cdd:PRK05691  2328 FLSlPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVL-RA 2406
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1433 DTTLDADRFAQTLAAARIDVLKIVPGHLHALLQ-AERAADALPAHTLVLGGEATSWELLDTI-AALRPDcRVHNHYGPTE 1510
Cdd:PRK05691  2407 QGQWGAEEICQLIREQQVSILGFTPSYGSQLAQwLAGQGEQLPVRMCITGGEALTGEHLQRIrQAFAPQ-LFFNAYGPTE 2485
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1511 TTVGILTQPA-AQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAA- 1588
Cdd:PRK05691  2486 TVVMPLACLApEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAd 2565
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1589 GARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV---AGARLAAF-ATPQPGASL 1664
Cdd:PRK05691  2566 GGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALdtpSGKQLAGYlVSAVAGQDD 2645
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1665 DAAAL-----KRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALsalarpAAPHREAAR---AAPQGETETALAQCWA 1736
Cdd:PRK05691  2646 EAQAAlrealKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL------PAPDPELNRqayQAPRSELEQQLAQIWR 2719
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1737 ALLDPSNgtdnatdnatatpsltIARDDSFFALGGHSLAAMRLASRVRSRwSVELPLREIFASPTLAALAArieaqRADS 1816
Cdd:PRK05691  2720 EVLNVER----------------VGLGDNFFELGGDSILSIQVVSRARQL-GIHFSPRDLFQHQTVQTLAA-----VATH 2777
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1817 DRASNQVSNKAANAESATPLHALADRSALPlslmQQRIWvvdqladralasyNMTAGLDLRGPLDAARLQRSLAALIARH 1896
Cdd:PRK05691  2778 SEAAQAEQGPLQGASGLTPIQHWFFDSPVP----QPQHW-------------NQALLLEPRQALDPALLEQALQALVEHH 2840
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1897 EVLRSAFDADDEGDPVLKIAPRMEVLMPVIEPlahpdndanshtnshtnsdenaRTQATAQALDDAARTPFDLSRAPLVR 1976
Cdd:PRK05691  2841 DALRLRFSQADGRWQAEYRAVTAQELLWQVTV----------------------ADFAECAALFADAQRSLDLQQGPLLR 2898
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1977 ATLLRFDAAHHVLIVSLHHIVADGGSVHILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFTPDAVREAQQFWR 2056
Cdd:PRK05691  2899 ALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQ 2978
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2057 GYLADAPALLPlsTDRARPTRVSHAGAARHFRLDATlgaRVRTLAQ----AHGMTPFAVLLASFQWFLHRHTGADDLVIG 2132
Cdd:PRK05691  2979 AQLGGPRAELP--CDRPQGGNLNRHAQTVSVRLDAE---RTRQLLQqapaAYRTQVNDLLLTALARVLCRWSGQPSVLVQ 3053
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2133 TDVDGRER----AELEALIGFFVNVVPLRSR--IAADGANLASFDAWLDAARQSTWDALDHRALpfdRIVDALALKRRRD 2206
Cdd:PRK05691  3054 LEGHGREAlfddIDLTRSVGWFTSAYPLRLTpaPGDDAARGESIKAIKEQLRAVPHKGLGYGVL---RYLADAAVREAMA 3130
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2207 ANPLVQVLF----------VLRDLPRGNTRVPGLAVELLRPPTTQSKFDMALFveavDGGYDIEWVYASALFDAATIERA 2276
Cdd:PRK05691  3131 ALPQAPITFnylgqfdqsfASDALFRPLDEPAGPAHDPDAPLPNELSVDGQVY----GGELVLRWTYSAERYDEQTIAEL 3206
                         2330      2340
                   ....*....|....*....|....*.
gi 1888712850 2277 FDAWRATLDAVSADPRAPLASSLSTS 2302
Cdd:PRK05691  3207 AEAYLAELQALIAHCLADGAGGLTPS 3232
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
30-597 0e+00

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 599.61  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   30 LAQQRPEATALIVIDADGDT--RYDYAQLDRRARALAARFARDGAAAERALILMDSGVDYVSAFFGCLYAGVVAVPVYPP 107
Cdd:cd05931      2 RAAARPDRPAYTFLDDEGGReeTLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  108 EskREQHLARLRGIARDAGVRYVLTTAALHER-HADAWSMLAPGADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSG 186
Cdd:cd05931     82 T--PGRHAERLAAILADAGPRVVLTTAAALAAvRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  187 STGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQYFLERPLRWLDAIA 266
Cdd:cd05931    160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRWLRLIS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  267 RHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAALYPCYGLAEATLFVT 346
Cdd:cd05931    240 RYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEATLFVS 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  347 GGVRGAGLVSHAFSSAALSAGRAEAARADEAATVLVGCGAVQAGHRVAIvaraaaeshesheadVETETSRageRLADGR 426
Cdd:cd05931    320 GGPPGTGPVVLRVDRDALAGRAVAVAADDPAARELVSCGRPLPDQEVRI---------------VDPETGR---ELPDGE 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  427 IGEIHVSGPSVAHGYWQRADASAQAFvdAPRHADGSGParWLRTGDLGFVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQA 506
Cdd:cd05931    382 VGEIWVRGPSVASGYWGRPEATAETF--GALAATDEGG--WLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEAT 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  507 VEAHAEFARKGRVIAFGATLGGGETLGLALEIAPRmKKRFAAAQIVETLRRIAFDACGETPAAIALLNPGALPKTSSGKL 586
Cdd:cd05931    458 AEEAHPALRPGCVAAFSVPDDGEERLVVVAEVERG-ADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKI 536
                          570
                   ....*....|.
gi 1888712850  587 QRAATREGWRA 597
Cdd:cd05931    537 QRRACRAAYLD 547
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
1227-1705 2.35e-167

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 521.70  E-value: 2.35e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLceddcsaldlmgvqharidaaqeeaqreqhlraphalpaVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNY 1386
Cdd:cd05930     81 EDSGAKLVL---------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1387 VDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQA 1466
Cdd:cd05930    122 LLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQE 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1467 ERAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRAAATLPLGRPLDNNETWLLDE 1546
Cdd:cd05930    202 LELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDE 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1547 HLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEP 1626
Cdd:cd05930    282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1627 GEIAARLKALDGVRDAAVIVVAGA----RLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDR 1702
Cdd:cd05930    362 GEIEAALLAHPGVREAAVVAREDGdgekRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDR 441

                   ...
gi 1888712850 1703 QAL 1705
Cdd:cd05930    442 KAL 444
PRK12316 PRK12316
peptide synthase; Provisional
710-1823 7.59e-160

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 554.57  E-value: 7.59e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  710 DDAQDEAQDNAPIEPAEEAVISHAQQRQLFAWRLDPASRAYHVAAGIRLDGaLDREALRQSLDRLCERHAALRTHFVETG 789
Cdd:PRK12316  4085 DQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQG 4163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  790 daahlyaprtEAAAPLAWAH----VDLSDLGDIDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLAL 865
Cdd:PRK12316  4164 ----------ELGRPLQVVHkqvsLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTN 4233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  866 HHIATDGWSMQLLVEELVDGYRaaldgatthGEAQAKAKTRitYADYAAWQRRwlaSDAAARQlAYWRAALADDAPPlal 945
Cdd:PRK12316  4234 HHILMDGWSNSQLLGEVLERYS---------GRPPAQPGGR--YRDYIAWLQR---QDAAASE-AFWREQLAALDEP--- 4295
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  946 pydhTATDTASENADPRAAARVA---FALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRT- 1021
Cdd:PRK12316  4296 ----TRLAQAIARADLRSANGYGehvRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPa 4371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1022 -RPETHDVIGFFVNTLVLHSDCEAATPLASLFSQLRQRTLDAQANQALPFdvlvEHLRPARDAQHGPLFETSFNYlsDDY 1100
Cdd:PRK12316  4372 eLPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPL----YEIQRWAGQGGEALFDSLLVF--ENY 4445
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1101 P---ALARWP--GARAERVEIAE-THVKVPLALDLRESrdgsMRAYFTYASARFDAASVERMAAQYLRAVEAfahalgdr 1174
Cdd:PRK12316  4446 PvseALQQGApgGLRFGEVTNHEqTNYPLTLAVGLGET----LSLQFSYDRGHFDAATIERLARHLTNLLEA-------- 4513
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1175 sadMTDAAAPTLATLDLLDADERARVSAasVARRTPPGEP----IHLRVARHADTQPDAPAVIDGALRMSYAELDARAAH 1250
Cdd:PRK12316  4514 ---MAEDPQRRLGELQLLEKAEQQRIVA--LWNRTDAGYPatrcVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANR 4588
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1251 VAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDdcSALDLM---- 1326
Cdd:PRK12316  4589 LAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS--HLLQRLpipd 4666
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1327 GVQHARIDAAQEEAQREQHlrAPhaLPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVS 1406
Cdd:PRK12316  4667 GLASLALDRDEDWEGFPAH--DP--AVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFM 4742
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1407 TIGADLGHTVLFGALASGGALHLIDrDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQ-AERAADALPAHTLVLGGEAT 1485
Cdd:PRK12316  4743 SFSFDGSHEGLYHPLINGASVVIRD-DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEhAERDGEPPSLRVYCFGGEAV 4821
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1486 SWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRA-AATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGA 1564
Cdd:PRK12316  4822 AQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACgAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGE 4901
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1565 GVALGYLHQPALTAARFVPHPF-AAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAA 1643
Cdd:PRK12316  4902 GVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4981
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1644 VIVV---AGARLAAFATPQPGASLDAAALKR--------ALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSAlarPA 1712
Cdd:PRK12316  4982 VIAQegaVGKQLVGYVVPQDPALADADEAQAelrdelkaALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQ---PD 5058
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1713 APHREAARAAPQGETETALAQCWAALLDPSNgtdnatdnatatpsltIARDDSFFALGGHSLAAMRLASRVRSRWSVELP 1792
Cdd:PRK12316  5059 ASLLQQAYVAPRSELEQQVAAIWAEVLQLER----------------VGLDDNFFELGGHSLLAIQVTSRIQLELGLELP 5122
                         1130      1140      1150
                   ....*....|....*....|....*....|.
gi 1888712850 1793 LREIFASPTLAALAARIEAQRADSDRASNQV 1823
Cdd:PRK12316  5123 LRELFQTPTLAAFVELAAAAGSGDDEKFDDL 5153
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
1844-2291 1.97e-158

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 496.11  E-value: 1.97e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1844 ALPLSLMQQRIWVVDQLaDRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDeGDPVLKIAPRMEVLM 1923
Cdd:cd19531      1 PLPLSFAQQRLWFLDQL-EPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVD-GEPVQVILPPLPLPL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1924 PVIEplahpdndanshtnsHTNSDENARTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSV 2003
Cdd:cd19531     79 PVVD---------------LSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSM 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2004 HILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADAPALLPLSTDRARPTRVSHAGA 2083
Cdd:cd19531    144 GVLLRELAALYAAFLAGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGA 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2084 ARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSRIAAD 2163
Cdd:cd19531    224 RVRFTLPAELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGD 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2164 ganlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRDLPRGNTRVPGLAVELLRPPTTQSK 2243
Cdd:cd19531    304 ----PTFRELLARVRETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAK 379
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1888712850 2244 FDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19531    380 FDLTLSLTETDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
731-1170 4.85e-152

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 478.39  E-value: 4.85e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  731 SHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHlyaPRTEAAAPLAWAHV 810
Cdd:cd19531      5 SFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPV---QVILPPLPLPLPVV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  811 DLSDLgdiDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAAL 890
Cdd:cd19531     82 DLSGL---PEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  891 dgattHGEAQAKAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHtatdtasenadPR------AA 964
Cdd:cd19531    159 -----AGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDR-----------PRpavqsfRG 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  965 ARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEA 1044
Cdd:cd19531    223 ARVRFTLPAELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSG 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1045 ATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPALaRWPGARAERVEIAETHVKVP 1124
Cdd:cd19531    303 DPTFRELLARVRETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAAL-ELPGLTVEPLEVDSGTAKFD 381
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1888712850 1125 LALDLREsRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAFAHA 1170
Cdd:cd19531    382 LTLSLTE-TDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVAD 426
PRK12467 PRK12467
peptide synthase; Provisional
730-2210 3.25e-151

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 527.04  E-value: 3.25e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  730 ISHAQQRQLFAWRLDPASRAYHVAAGIRLDGaLDREALRQSLDRLCERHAALRTHFVETGdaahlyaprtEAAAPLAWAH 809
Cdd:PRK12467  2649 LSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDG----------ELEEPLQVVY 2717
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  810 ----VDLSDLGDIDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDG 885
Cdd:PRK12467  2718 kqarLPFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQR 2797
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  886 YRaaldgatthGEAQAKAKTRitYADYAAWqrrwLASDAAARQLAYWRAALADDAPP--LALPYDHTATDTASENADPRa 963
Cdd:PRK12467  2798 YF---------GQPPPAREGR--YRDYIAW----LQAQDAEASEAFWKEQLAALEEPtrLARALYPAPAEAVAGHGAHY- 2861
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  964 aarvaFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTrPETHDV---IGFFVNTLVLhs 1040
Cdd:PRK12467  2862 -----LHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRP-AQLRGAeqqLGLFINTLPV-- 2933
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1041 dceAATPLAslfsqlRQRTLD-AQANQAlpfdvlvEHLRpARDAQHGPLFETS----------FNYL--SDDYPALARWP 1107
Cdd:PRK12467  2934 ---IASPRA------EQTVSDwLQQVQA-------QNLA-LREFEHTPLADIQrwagqggealFDSIlvFENYPISEALK 2996
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1108 GARAERVEIAETHVK--VPLALDLRESRDGSMRAYFTYASARFDAASVERMAAQylraveaFAHALgdrsADMTDAAAPT 1185
Cdd:PRK12467  2997 QGAPSGLRFGAVSSReqTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAES-------FDRLL----QAMLNNPAAR 3065
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1186 LATLDLLDADERARVSAASVARRT--PPGEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGG 1263
Cdd:PRK12467  3066 LGELPTLAAHERRQVLHAWNATAAayPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPD 3145
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1264 EPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDdcSALD----LMGVQHARIDAAQEE 1339
Cdd:PRK12467  3146 VLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQA--HLLEqlpaPAGDTALTLDRLDLN 3223
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1340 AQREQHLRaphalPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFG 1419
Cdd:PRK12467  3224 GYSENNPS-----TRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLW 3298
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1420 ALASGGALHLIDRDTtLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAALRPD 1499
Cdd:PRK12467  3299 TLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKP 3377
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1500 CRVHNHYGPTETTVG-ILTQPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTA 1578
Cdd:PRK12467  3378 RGLTNGYGPTEAVVTvTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTA 3457
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1579 ARFVPHPFA-AGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV---AGARLAA 1654
Cdd:PRK12467  3458 ERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARdgaGGKQLVA 3537
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1655 FATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSalarpaAPHREAARA--APQGETETALA 1732
Cdd:PRK12467  3538 YVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALP------DPDAKGSREyvAPRSEVEQQLA 3611
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1733 QCWAALLDPSNgtdnatdnatatpsltIARDDSFFALGGHSLAAMRLASRVRSRWSVELPLREIFASPTLAALAARIEAq 1812
Cdd:PRK12467  3612 AIWADVLGVEQ----------------VGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPL- 3674
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1813 radsdrasnqvsnkaanaesatplhaladrSALPLSLMqqriwvvdqladralasynmtagldlrgpLDAARLQRSLAAL 1892
Cdd:PRK12467  3675 ------------------------------GDVPVNLL-----------------------------LDLNRLETGFPAL 3695
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1893 IARHEVLRSAFDAddegdpvlkiaprmevlmpviEPLahpdndanshtnshtnsdenartqatAQALDDaartpfdlsra 1972
Cdd:PRK12467  3696 FCRHEGLGTVFDY---------------------EPL--------------------------AVILEG----------- 3717
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1973 plvratllrfdaAHHVLIVSLHHIVADGgsvhilldelcelyraqrdGAPPALAPLAVQYADYAHWQRARftpdavreAQ 2052
Cdd:PRK12467  3718 ------------DRHVLGLTCRHLLDDG-------------------WQDTSLQAMAVQYADYILWQQAK--------GP 3758
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2053 QFWRGyladapallplstdrarptrvshagaarhFRLDATLGARVRTLAQAHGmtpfavllasfqwflhrhtgaddlvig 2132
Cdd:PRK12467  3759 YGLLG-----------------------------WSLGGTLARLVAELLEREG--------------------------- 3782
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2133 tdvdgreraELEALIGFFVNVVPLRSRIAAD---GANLASFDAwLDAARQSTWDALDHRALPFDRIVdALALKRRRDANP 2209
Cdd:PRK12467  3783 ---------ESEAFLGLFDNTLPLPDEFVPQaefLELLRQLGE-LIGRANRLLRGLEEGGVGPDVLV-GIAIQRCFDIAP 3851

                   .
gi 1888712850 2210 L 2210
Cdd:PRK12467  3852 L 3852
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
723-1819 7.85e-136

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 461.44  E-value: 7.85e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  723 EPAEEAV-ISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAahlyaPRTEA 801
Cdd:PRK10252     2 EPMSQHLpLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGE-----VWQWV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  802 AAPLAWAHVDLSDLGDidEHDRERALRECAQRFADAPFDLLRG-PLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVE 880
Cdd:PRK10252    77 DPALTFPLPEIIDLRT--QPDPHAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  881 ELVDGYRAALDGAtthgeaQAKAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALpydhTATDTASENAD 960
Cdd:PRK10252   155 RIAAIYCAWLRGE------PTPASPFTPFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASL----SPAPLPGRSAS 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  961 PRAAARvafALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHS 1040
Cdd:PRK10252   225 ADILRL---KLEFTDGAFRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRV 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1041 DCEAATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQhgPLFETSFNYLSDDYPAlaRWPGARAERVEIAETH 1120
Cdd:PRK10252   302 HIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDE--PLFGPVLNIKVFDYQL--DFPGVQAQTHTLATGP 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1121 VKvPLALDLRESRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAFAhalgdrsadmtdaAAPTL--ATLDLLDADERA 1198
Cdd:PRK10252   378 VN-DLELALFPDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFA-------------ADPALlcGDVDILLPGEYA 443
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1199 RVSAASVARRTPPGEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVV 1278
Cdd:PRK10252   444 QLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTL 523
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1279 AMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDDCSAL--DLMGVQHARIDAAQEEAQReqhlrAPHALPAvd 1356
Cdd:PRK10252   524 ALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRfaDVPDLTSLCYNAPLAPQGA-----APLQLSQ-- 596
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1357 PRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTL 1436
Cdd:PRK10252   597 PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHR 676
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1437 DADRFAQTLAAARIDVLKIVPGHLHALLQA---ERAADALPAHTLVL-GGEATSWELLDTIAALRpDCRVHNHYGPTETT 1512
Cdd:PRK10252   677 DPLAMQQFFAEYGVTTTHFVPSMLAAFVASltpEGARQSCASLRQVFcSGEALPADLCREWQQLT-GAPLHNLYGPTEAA 755
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1513 VGILTQPAAQACRAAAT---LPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAG 1589
Cdd:PRK10252   756 VDVSWYPAFGEELAAVRgssVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPG 835
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1590 ARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDA---AVIVVAGA-------RLAAFATPQ 1659
Cdd:PRK10252   836 ERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthACVINQAAatggdarQLVGYLVSQ 915
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1660 PGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALsalarPAAPH-REAARAAPQGETETALAQCWAAL 1738
Cdd:PRK10252   916 SGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL-----PLPELkAQVPGRAPKTGTETIIAAAFSSL 990
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1739 LDPSngtdnatdnatatpslTIARDDSFFALGGHSLAAMRLASRVRSRWSVELPLREIFASPTLAALAARIEAQRADSDR 1818
Cdd:PRK10252   991 LGCD----------------VVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRR 1054

                   .
gi 1888712850 1819 A 1819
Cdd:PRK10252  1055 L 1055
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1240-1644 5.53e-129

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 412.04  E-value: 5.53e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLLARD-LQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCED 1318
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGgVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1319 DCSALDLMGVQHARIDAAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPP 1398
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1399 RARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAAR-IDVLKIVPGHLHALLQA-ERAADALpaH 1476
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAAlPPALASL--R 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1477 TLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVG-ILTQPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGG 1555
Cdd:TIGR01733  239 LVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWsTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1556 TGELYLGGAGVALGYLHQPALTAARFVPHPFA--AGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARL 1633
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 398
                          410
                   ....*....|.
gi 1888712850 1634 KALDGVRDAAV 1644
Cdd:TIGR01733  399 LRHPGVREAVV 409
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
1219-1705 3.07e-128

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 413.28  E-value: 3.07e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNP 1298
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1299 TQRLAQTLRDCGARLVLCEDDcSALDLMGVQHARIDAAQEEAqrEQHLRAPHAlPAVDPRSAAYVIYTSGSSGAPKGVVI 1378
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPA-LAGELAVELVAVTLLDQPGA--AAGADAEPD-PALDADDLAYVIYTSGSTGRPKGVVM 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1379 AHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPG 1458
Cdd:cd17651    157 PHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTV 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1459 HLHALLQAERAADALPA--HTLVLGGEA-TSWELLDTIAALRPDCRVHNHYGPTETTV---GILTQPAAQACRaaaTLPL 1532
Cdd:cd17651    237 ALRALAEHGRPLGVRLAalRYLLTGGEQlVLTEDLREFCAGLPGLRLHNHYGPTETHVvtaLSLPGDPAAWPA---PPPI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1533 GRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGR 1612
Cdd:cd17651    314 GRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGR 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1613 IDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRV 1688
Cdd:cd17651    394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLARedrpGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVL 473
                          490
                   ....*....|....*..
gi 1888712850 1689 IDALPLNRNGKLDRQAL 1705
Cdd:cd17651    474 LDALPLTPNGKLDRRAL 490
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
1218-1705 1.95e-126

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 407.74  E-value: 1.95e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1218 RVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGN 1297
Cdd:cd12117      2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 PTQRLAQTLRDCGARLVLceDDCSALDLMGVQHARIDAAQEEAQREqhlrAPHALPAVDPRSAAYVIYTSGSSGAPKGVV 1377
Cdd:cd12117     82 PAERLAFMLADAGAKVLL--TDRSLAGRAGGLEVAVVIDEALDAGP----AGNPAVPVSPDDLAYVMYTSGSTGRPKGVA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1378 IAHGALTNYV-DAVLARLDPppRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIV 1456
Cdd:cd12117    156 VTHRGVVRLVkNTNYVTLGP--DDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLT 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1457 PGHLHALlqAERAADALP-AHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRAAATLPLGRP 1535
Cdd:cd12117    234 AALFNQL--ADEDPECFAgLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRP 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1536 LDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDD 1615
Cdd:cd12117    312 IANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDD 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1616 QVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGA----RLAAFATPQPGASldAAALKRALAALLPDYMVPSVLRVIDA 1691
Cdd:cd12117    392 QVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAggdkRLVAYVVAEGALD--AAELRAFLRERLPAYMVPAAFVVLDE 469
                          490
                   ....*....|....
gi 1888712850 1692 LPLNRNGKLDRQAL 1705
Cdd:cd12117    470 LPLTANGKVDRRAL 483
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
1216-1705 1.19e-125

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 405.51  E-value: 1.19e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1216 HLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDA 1295
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1296 GNPTQRLAQTLRDCGARLVLCEDDCSAldlmgvqHARIDAAQEEAQREQHLRAPHALPAVDPR--SAAYVIYTSGSSGAP 1373
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAA-------RLPAGGDVALLGDEALAAPPATPPLVPPRpdNLAYVIYTSGSTGRP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1374 KGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVL 1453
Cdd:cd17646    154 KGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTC 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1454 KIVPGHLHALLQaERAADALPAHTLVL-GGEATSWELLDTIAALrPDCRVHNHYGPTETTVGIlTQPAAQACRAAATLPL 1532
Cdd:cd17646    234 HFVPSMLRVFLA-EPAAGSCASLRRVFcSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDV-THWPVRGPAETPSVPI 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1533 GRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGR 1612
Cdd:cd17646    311 GRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGR 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1613 IDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALL-PDYMVPSVLR 1687
Cdd:cd17646    391 SDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAapagAARLVGYVVPAAGAAGPDTAALRAHLAERlPEYMVPAAFV 470
                          490
                   ....*....|....*...
gi 1888712850 1688 VIDALPLNRNGKLDRQAL 1705
Cdd:cd17646    471 VLDALPLTANGKLDRAAL 488
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
1223-1707 2.32e-125

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 404.79  E-value: 2.32e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1223 ADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRL 1302
Cdd:cd17655      7 AEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1303 AQTLRDCGARLVLCEDDcSALDLMGVQHA-RIDAAQEEAQREQHLRaphalPAVDPRSAAYVIYTSGSSGAPKGVVIAHG 1381
Cdd:cd17655     87 QYILEDSGADILLTQSH-LQPPIAFIGLIdLLDEDTIYHEESENLE-----PVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1382 ALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLH 1461
Cdd:cd17655    161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1462 aLLQAERAADALPAHTLVLGGEATSWELLDTIAAL-RPDCRVHNHYGPTETTVGILTQPAAQACRAAATLPLGRPLDNNE 1540
Cdd:cd17655    241 -LLDAADDSEGLSLKHLIVGGEALSTELAKKIIELfGTNPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTR 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1541 TWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIR 1620
Cdd:cd17655    320 IYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1621 GYRVEPGEIAARLKALDGVRDAAVIVVAGAR----LAAFATPQPgaSLDAAALKRALAALLPDYMVPSVLRVIDALPLNR 1696
Cdd:cd17655    400 GYRIELGEIEARLLQHPDIKEAVVIARKDEQgqnyLCAYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTP 477
                          490
                   ....*....|.
gi 1888712850 1697 NGKLDRQALSA 1707
Cdd:cd17655    478 NGKVDRKALPE 488
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
1227-1705 1.98e-123

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 398.59  E-value: 1.98e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLCEDDCSA---LDLMGVQHARIDAAqeeaqreqhlRAPHAL-PAVDPRSAAYVIYTSGSSGAPKGVVIAHGA 1382
Cdd:cd12116     81 EDAEPALVLTDDALPDrlpAGLPVLLLALAAAA----------AAPAAPrTPVSPDDLAYVIYTSGSTGRPKGVVVSHRN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1383 LTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHA 1462
Cdd:cd12116    151 LVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRM 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1463 LLQAEraADALPAHTLVLGGEATSWELLDTIaaLRPDCRVHNHYGPTETTVGILTQPAAQACRAaatLPLGRPLDNNETW 1542
Cdd:cd12116    231 LLDAG--WQGRAGLTALCGGEALPPDLAARL--LSRVGSLWNLYGPTETTIWSTAARVTAAAGP---IPIGRPLANTQVY 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1543 LLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFA-AGARLYRSGDRARRLADGSLEYLGRIDDQVKIRG 1621
Cdd:cd12116    304 VLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRG 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1622 YRVEPGEIAARLKALDGVRDAAVIVV---AGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNG 1698
Cdd:cd12116    384 HRIELGEIEAALAAHPGVAQAAVVVRedgGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANG 463

                   ....*..
gi 1888712850 1699 KLDRQAL 1705
Cdd:cd12116    464 KLDRKAL 470
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
1227-1705 9.73e-122

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 392.39  E-value: 9.73e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLceddcsaldlmgvqharidaaqeeaqreqhlraphalpaVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNY 1386
Cdd:cd17652     81 ADARPALLL---------------------------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANL 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1387 VDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALlqa 1466
Cdd:cd17652    122 AAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL--- 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1467 erAADALPA-HTLVLGGEATSWELLDTIAalrPDCRVHNHYGPTETTVG-ILTQPAAQACraaaTLPLGRPLDNNETWLL 1544
Cdd:cd17652    199 --PPDDLPDlRTLVVAGEACPAELVDRWA---PGRRMINAYGPTETTVCaTMAGPLPGGG----VPPIGRPVPGTRVYVL 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1545 DEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAA-GARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYR 1623
Cdd:cd17652    270 DARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGApGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFR 349
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1624 VEPGEIAARLKALDGVRDAAVIV----VAGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGK 1699
Cdd:cd17652    350 IELGEVEAALTEHPGVAEAVVVVrddrPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGK 429

                   ....*.
gi 1888712850 1700 LDRQAL 1705
Cdd:cd17652    430 LDRRAL 435
PRK09192 PRK09192
fatty acyl-AMP ligase;
75-605 1.86e-117

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 385.51  E-value: 1.86e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPES--KREQHLARLRGIARDAGVRYVLTTAALHERHADAWSMLAPGAD 152
Cdd:PRK09192    75 DRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfgGRESYIAQLRGMLASAQPAAIITPDELLPWVNEATHGNPLLHV 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  153 VVAVDtLDARDTPsDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAI-QAGLGVRPDDVFVSWLPLYHDMG 231
Cdd:PRK09192   155 LSHAW-FKALPEA-DVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIsHDGLKVRPGDRCVSWLPFYHDMG 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  232 LIGSLLQPVFSGIPLVLMSPQYFLERPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVR 311
Cdd:PRK09192   233 LVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLISRNRGTISYSPPFGYELCARRVNSKDLAELDLSCWRVAGIGADMIR 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  312 RDTLDDFVARFAPAGFDAAALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGRAEAARADEAATV--LVGCGAVQA 389
Cdd:PRK09192   313 PDVLHQFAEAFAPAGFDDKAFMPSYGLAEATLAVSFSPLGSGIVVEEVDRDRLEYQGKAVAPGAETRRVrtFVNCGKALP 392
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  390 GhrvaivaraaaeshesHEADVETEtsrAGERLADGRIGEIHVSGPSVAHGYWqRADASAQAFVdaprhADGsgparWLR 469
Cdd:PRK09192   393 G----------------HEIEIRNE---AGMPLPERVVGHICVRGPSLMSGYF-RDEESQDVLA-----ADG-----WLD 442
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  470 TGDLGFVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFaRKGRVIAFGATLGGGETlgLALEIAPRMKKRFAAA 549
Cdd:PRK09192   443 TGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPEL-RSGDAAAFSIAQENGEK--IVLLVQCRISDEERRG 519
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1888712850  550 QIVETLRRIAFDACGeTPAAIALLNPGALPKTSSGKLQRAATREGWRARTLDLYAL 605
Cdd:PRK09192   520 QLIHALAALVRSEFG-VEAAVELVPPHSLPRTSSGKLSRAKAKKRYLSGAFASLDV 574
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
1227-1705 2.32e-115

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 374.40  E-value: 2.32e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLCEDdcsaldlmgvqharidaaqeeaqreqhlraphalpavdPRSAAYVIYTSGSSGAPKGVVIAHGALTNY 1386
Cdd:cd17649     81 EDSGAGLLLTHH--------------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAH 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1387 VDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQ- 1465
Cdd:cd17649    123 CQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEe 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1466 --AERAADALPAHTLVLGGEATSWELLDtiAALRPDCRVHNHYGPTETTV-GILTQPAAQACRAAATLPLGRPLDNNETW 1542
Cdd:cd17649    203 adRTGDGRPPSLRLYIFGGEALSPELLR--RWLKAPVRLFNAYGPTEATVtPLVWKCEAGAARAGASMPIGRPLGGRSAY 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1543 LLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAA-GARLYRSGDRARRLADGSLEYLGRIDDQVKIRG 1621
Cdd:cd17649    281 ILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRG 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1622 YRVEPGEIAARLKALDGVRDAAVIVVAGA---RLAAFATPQPGASLDAAALKRALAALL--PDYMVPSVLRVIDALPLNR 1696
Cdd:cd17649    361 FRIELGEIEAALLEHPGVREAAVVALDGAggkQLVAYVVLRAAAAQPELRAQLRTALRAslPDYMVPAHLVFLARLPLTP 440

                   ....*....
gi 1888712850 1697 NGKLDRQAL 1705
Cdd:cd17649    441 NGKLDRKAL 449
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
1227-1705 4.35e-115

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 373.57  E-value: 4.35e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLceddcsaldlmgvqharidaaqeeaqreqhlraphalpaVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNY 1386
Cdd:cd17643     81 ADSGPSLLL---------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVLAL 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1387 VDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQA 1466
Cdd:cd17643    122 FAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEA 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1467 ERAA--DALPAHTLVLGGEATSWELLDTIAALRPDCRVH--NHYGPTETTVGILTQPAAQACRAAATL-PLGRPLDNNET 1541
Cdd:cd17643    202 ADRDgrDPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQlvNMYGITETTVHVTFRPLDAADLPAAAAsPIGRPLPGLRV 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1542 WLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPF-AAGARLYRSGDRARRLADGSLEYLGRIDDQVKIR 1620
Cdd:cd17643    282 YVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIR 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1621 GYRVEPGEIAARLKALDGVRDAAVIVVAGA----RLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNR 1696
Cdd:cd17643    362 GFRIELGEIEAALATHPSVRDAAVIVREDEpgdtRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTV 441

                   ....*....
gi 1888712850 1697 NGKLDRQAL 1705
Cdd:cd17643    442 NGKLDRAAL 450
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
1215-1705 3.87e-113

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 368.18  E-value: 3.87e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1215 IHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALD 1294
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1295 AGNPTQRLAQTLRDCGARLVLceddcsaldlmgvqharidaaqeeaqreqhlraphalpaVDPRSAAYVIYTSGSSGAPK 1374
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVL---------------------------------------TDPDDLAYVIYTSGSTGRPK 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1375 GVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDrdTTLDADRFAqtlAAARIDVLK 1454
Cdd:cd12115    122 GVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD--NVLALPDLP---AAAEVTLIN 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1455 IVPGHLHALLQAeraaDALPA--HTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVgiLTQPAAQACRAAATLPL 1532
Cdd:cd12115    197 TVPSAAAELLRH----DALPAsvRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTT--YSTVAPVPPGASGEVSI 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1533 GRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGR 1612
Cdd:cd12115    271 GRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGR 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1613 IDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGA----RLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRV 1688
Cdd:cd12115    351 ADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAagerRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVR 430
                          490
                   ....*....|....*..
gi 1888712850 1689 IDALPLNRNGKLDRQAL 1705
Cdd:cd12115    431 LDALPLTPNGKIDRSAL 447
PRK05850 PRK05850
acyl-CoA synthetase; Validated
23-596 1.40e-112

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 371.58  E-value: 1.40e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIVIDADGDT-----RYDYAQLDRRARALAARFARDGAAAERALILMDSGVDYVSAFFGCLYA 97
Cdd:PRK05850     3 VPSLLRERASLQPDDAAFTFIDYEQDPagvaeTLTWSQLYRRTLNVAEELRRHGSTGDRAVILAPQGLEYIVAFLGALQA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   98 GVVAVPVYPPEskREQHLARLRGIARDAGVRYVLTTAALHE---RHADAWSmLAPGADVVAVDTLDArDTPSDAPLHPVR 174
Cdd:PRK05850    83 GLIAVPLSVPQ--GGAHDERVSAVLRDTSPSVVLTTSAVVDdvtEYVAPQP-GQSAPPVIEVDLLDL-DSPRGSDARPRD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  175 ADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQA------GLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVL 248
Cdd:PRK05850   159 LPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSdyfgdtGGVPPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  249 MSPQYFLERPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFD 328
Cdd:PRK05850   239 TSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTSDDDMAGLDLGGVLGIISGSERVHPATLKRFADRFAPFNLR 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  329 AAALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGrAEAARADEAATVLVGCGAVQaghrvaivaraaaeSHESHE 408
Cdd:PRK05850   319 ETAIRPSYGLAEATVYVATREPGQPPESVRFDYEKLSAG-HAKRCETGGGTPLVSYGSPR--------------SPTVRI 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  409 ADVETETsrageRLADGRIGEIHVSGPSVAHGYWQRADASAQAF---VDAPRHADGSGParWLRTGDLGFVHDGQLYIAG 485
Cdd:PRK05850   384 VDPDTCI-----ECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPGTPEGP--WLRTGDLGFISEGELFIVG 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  486 RVKDLVIVRGRNLYPQDVEQAVEahaEFARkGRVIAFGATLGGGETLGLALEiaprMKKRFAAAQivETLRRIAF----- 560
Cdd:PRK05850   457 RIKDLLIVDGRNHYPDDIEATIQ---EITG-GRVAAISVPDDGTEKLVAIIE----LKKRGDSDE--EAMDRLRTvkrev 526
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1888712850  561 -----DACGETPAAIALLNPGALPKTSSGKLQRAATREGWR 596
Cdd:PRK05850   527 tsaisKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQYR 567
PRK05691 PRK05691
peptide synthase; Validated
715-1810 1.23e-111

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 399.93  E-value: 1.23e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  715 EAQDNAPIEPAEEAVISHAQqrqlfawrLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHL 794
Cdd:PRK05691  3253 EIEDVYPLTPMQEGLLLHTL--------LEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETML 3324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  795 YAPRTEAAAPlawahVDLSDLGDIDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWS 874
Cdd:PRK05691  3325 QVIHKPGRTP-----IDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWC 3399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  875 MQLLVEELVDGYRAALDGAtthgEAQAKAKTRitYADYAAW-QRRWLAsdaAARQlaYWRAALADDAPPLALPYDHTATD 953
Cdd:PRK05691  3400 RSLLMNDFFEIYTALGEGR----EAQLPVPPR--YRDYIGWlQRQDLA---QARQ--WWQDNLRGFERPTPIPSDRPFLR 3468
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  954 TASENADPRAAARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANR--TRPETHDVIGF 1031
Cdd:PRK05691  3469 EHAGDSGGMVVGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGL 3548
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1032 FVNTLVLHSDCEAATPLASL---FSQLRQRTLDAQANQALPFDVLVEHlrpARDAQHGPLFETSFNYLSD--DYPALARW 1106
Cdd:PRK05691  3549 FINSIALRVQLPAAGQRCSVrqwLQGLLDSNMELREYEYLPLVAIQEC---SELPKGQPLFDSLFVFENApvEVSVLDRA 3625
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1107 PGARAeRVEIAETHVKVPLALDLRESRDgsMRAYFTYASARFDAASVERMAAQYLRAVEAFAHAL-GDrsadmtdaaapt 1185
Cdd:PRK05691  3626 QSLNA-SSDSGRTHTNFPLTAVCYPGDD--LGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFhGD------------ 3690
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1186 LATLDLLDADERA-RVSAASVARRTPPGEPIHLR-----VARHAdtQPDAPAVIDGalRMSYAELDARAAHVAQWLLARD 1259
Cdd:PRK05691  3691 LSELPLLGEQERDfLLDGCNRSERDYPLEQSYVRlfeaqVAAHP--QRIAASCLDQ--QWSYAELNRAANRLGHALRAAG 3766
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1260 LQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDDCSA-----LDLMGVQHARID 1334
Cdd:PRK05691  3767 VGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREqaralLDELGCANRPRL 3846
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1335 AAQEEAQREQHlraPHALPAV--DPRSAAYVIYTSGSSGAPKGVVIA-HGALTNYVDAVlARLDPPPRARFAMVSTIGAD 1411
Cdd:PRK05691  3847 LVWEEVQAGEV---ASHNPGIysGPDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKV-PYLALSEADVIAQTASQSFD 3922
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1412 LGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAA-DALpaHTLVLGGEATSWELL 1490
Cdd:PRK05691  3923 ISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQAlDGL--RWMLPTGEAMPPELA 4000
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1491 DTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGY 1570
Cdd:PRK05691  4001 RQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGY 4080
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1571 LHQPALTAARFVPHPFAA-GARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAG 1649
Cdd:PRK05691  4081 VGDPLRTALAFVPHPFGApGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEG 4160
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1650 AR---LAAFATPQPGA---SLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSALARPAAphREAARAAP 1723
Cdd:PRK05691  4161 VNgkhLVGYLVPHQTVlaqGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQL--QSQAYLAP 4238
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1724 QGETETALAQCWAALLDPSNgtdnatdnatatpsltIARDDSFFALGGHSLAAMRLASRVRSRWSVELPLREIFASPTLA 1803
Cdd:PRK05691  4239 RNELEQTLATIWADVLKVER----------------VGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVE 4302

                   ....*..
gi 1888712850 1804 ALAARIE 1810
Cdd:PRK05691  4303 ELAEYIE 4309
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
1227-1705 4.56e-111

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 363.13  E-value: 4.56e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLCEDDCSALDlmgvqhARIDAAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNY 1386
Cdd:cd12114     81 ADAGARLVLTDGPDAQLD------VAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1387 VDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQA 1466
Cdd:cd12114    155 ILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDV 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1467 ERAADALPAH--TLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRAAATLPLGRPLDNNETWLL 1544
Cdd:cd12114    235 LEAAQALLPSlrLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLANQRYRVL 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1545 DEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPfaAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRV 1624
Cdd:cd12114    315 DPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRI 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1625 EPGEIAARLKALDGVRDAAVIVV---AGARLAAFATPQPGASLDAAALKRALAALL-PDYMVPSVLRVIDALPLNRNGKL 1700
Cdd:cd12114    393 ELGEIEAALQAHPGVARAVVVVLgdpGGKRLAAFVVPDNDGTPIAPDALRAFLAQTlPAYMIPSRVIALEALPLTANGKV 472

                   ....*
gi 1888712850 1701 DRQAL 1705
Cdd:cd12114    473 DRAAL 477
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
1845-2291 5.30e-111

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 361.36  E-value: 5.30e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1845 LPLSLMQQRIWVVDQLaDRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFdADDEGDPVLKIAPRMEVLmP 1924
Cdd:cd19540      2 IPLSFAQQRLWFLNRL-DGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVF-PEDDGGPYQVVLPAAEAR-P 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1925 VIEPLAHPDNDAnshtnshtnsdenartqatAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVH 2004
Cdd:cd19540     79 DLTVVDVTEDEL-------------------AARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMA 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2005 ILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFT----PDAVREAQ-QFWRGYLADAPALLPLSTDRARPTRVS 2079
Cdd:cd19540    140 PLARDLATAYAARRAGRAPDWAPLPVQYADYALWQRELLGdeddPDSLAARQlAYWRETLAGLPEELELPTDRPRPAVAS 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2080 HAGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSR 2159
Cdd:cd19540    220 YRGGTVEFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTD 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2160 IAADganlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRDLPRGNTRVPGLAVELLRPPT 2239
Cdd:cd19540    300 VSGD----PTFAELLARVRETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDT 375
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1888712850 2240 TQSKFDMAL-FVEAVD-----GGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19540    376 GVAKFDLSFtLTERRDadgapAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
1221-1706 1.03e-104

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 343.14  E-value: 1.03e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1221 RHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQ 1300
Cdd:cd17653      5 RIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1301 RLAQTLRDCGARLVLCEDdcsaldlmgvqharidaaqeeaqreqhlrAPHALpavdprsaAYVIYTSGSSGAPKGVVIAH 1380
Cdd:cd17653     85 RIQAILRTSGATLLLTTD-----------------------------SPDDL--------AYIIFTSGSTGIPKGVMVPH 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1381 GALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDrdttlDADRFAQTlaAARIDVLKIVPghl 1460
Cdd:cd17653    128 RGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD-----PSDPFAHV--ARTVDALMSTP--- 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1461 hALLQAERAADALPAHTLVLGGEATSWELLDTIAALRpdcRVHNHYGPTETTVGILTQpaaqACRAAATLPLGRPLDNNE 1540
Cdd:cd17653    198 -SILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGR---RLYNAYGPTECTISSTMT----ELLPGQPVTIGKPIPNST 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1541 TWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIR 1620
Cdd:cd17653    270 CYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVR 349
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1621 GYRVEPGEIAARLKALDG-VRDAAVIVVAGaRLAAFATPqpgASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGK 1699
Cdd:cd17653    350 GFRINLEEIEEVVLQSQPeVTQAAAIVVNG-RLVAFVTP---ETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGK 425

                   ....*..
gi 1888712850 1700 LDRQALS 1706
Cdd:cd17653    426 VDRKALR 432
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
1223-1705 5.62e-103

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 338.84  E-value: 5.62e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1223 ADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRL 1302
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1303 AQTLRDCGARLVLceddcsaldlmgvqharidaaqeeaqreqhlraphalpaVDPRSAAYVIYTSGSSGAPKGVVIAHGA 1382
Cdd:cd05945     81 REILDAAKPALLI---------------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDN 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1383 LTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLH- 1461
Cdd:cd05945    122 LVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAm 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1462 ALLQAERAADALPAHTLVL-GGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILT-QPAAQACRAAATLPLGRPLDNN 1539
Cdd:cd05945    202 CLLSPTFTPESLPSLRHFLfCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYiEVTPEVLDGYDRLPIGYAKPGA 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1540 ETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPfaaGARLYRSGDRARRLADGSLEYLGRIDDQVKI 1619
Cdd:cd05945    282 KLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVKL 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1620 RGYRVEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQPGASLDAAALKRAL-AALLPDYMVPSVLRVIDALPL 1694
Cdd:cd05945    359 NGYRIELEEIEAALRQVPGVKEAVVVPKykgeKVTELIAFVVPKPGAEAGLTKAIKAElAERLPPYMIPRRFVYLDELPL 438
                          490
                   ....*....|.
gi 1888712850 1695 NRNGKLDRQAL 1705
Cdd:cd05945    439 NANGKIDRKAL 449
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
731-1168 2.30e-100

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 330.54  E-value: 2.30e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  731 SHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAH-LYAPRTEAAAPLAWAH 809
Cdd:cd19540      5 SFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYqVVLPAAEARPDLTVVD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  810 VDlsdlgdidehdrERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAA 889
Cdd:cd19540     85 VT------------EDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAAR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  890 LDGAtthgeAQAKAKTRITYADYAAWQRRWLASDA-----AARQLAYWRAALADDAPPLALPYDHTATDTASenadpRAA 964
Cdd:cd19540    153 RAGR-----APDWAPLPVQYADYALWQRELLGDEDdpdslAARQLAYWRETLAGLPEELELPTDRPRPAVAS-----YRG 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  965 ARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEA 1044
Cdd:cd19540    223 GTVEFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSG 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1045 ATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPALaRWPGARAERVEIAETHVKVP 1124
Cdd:cd19540    303 DPTFAELLARVRETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATL-ELPGLTVEPVPVDTGVAKFD 381
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1888712850 1125 LALDLRESRD-----GSMRAYFTYASARFDAASVERMAAQYLRAVEAFA 1168
Cdd:cd19540    382 LSFTLTERRDadgapAGLTGELEYATDLFDRSTAERLADRFVRVLEAVV 430
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
1227-1705 9.86e-98

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 323.65  E-value: 9.86e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLceddcsaldlmgvqharidaaqeeaqreqhlraphalpaVDPRSAAYVIYTSGSSGAPKGVVIAHgalTNY 1386
Cdd:cd17650     81 EDSGAKLLL---------------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEH---RNV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1387 VDAVLA-----RLDPPPRARFAMVStIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLH 1461
Cdd:cd17650    119 AHAAHAwrreyELDSFPVRLLQMAS-FSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIR 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1462 ALLQ--AERAADALPAHTLVLGGEATSWELLDTIAA-LRPDCRVHNHYGPTETTV-GILTQPAAQACRAAATLPLGRPLD 1537
Cdd:cd17650    198 PVMAyvYRNGLDLSAMRLLIVGSDGCKAQDFKTLAArFGQGMRIINSYGVTEATIdSTYYEEGRDPLGDSANVPIGRPLP 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1538 NNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQV 1617
Cdd:cd17650    278 NTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQV 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1618 KIRGYRVEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQpgASLDAAALKRALAALLPDYMVPSVLRVIDALP 1693
Cdd:cd17650    358 KIRGFRIELGEIESQLARHPAIDEAVVAVRedkgGEARLCAYVVAA--ATLNTAELRAFLAKELPSYMIPSYYVQLDALP 435
                          490
                   ....*....|..
gi 1888712850 1694 LNRNGKLDRQAL 1705
Cdd:cd17650    436 LTPNGKVDRRAL 447
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1215-1709 6.15e-97

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 322.57  E-value: 6.15e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1215 IHLRVARHADTQPDAPAVI--DGalRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVA 1292
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCawDG--SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1293 LDAGNPTQRLAQTLRDCGARLVLCEDdcsaldlmgvqharidaaqeeaqreqhlraphalpavdPRSAAYVIYTSGSSGA 1372
Cdd:cd05918     79 LDPSHPLQRLQEILQDTGAKVVLTSS--------------------------------------PSDAAYVIFTSGSTGK 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1373 PKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDadRFAQTLAAARIDV 1452
Cdd:cd05918    121 PKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTW 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1453 LKIVPGhLHALLQAEraadALPA-HTLVLGGEATSWELLDTIAalrPDCRVHNHYGPTETTVGILTQPAAQACRAAAtlp 1531
Cdd:cd05918    199 AFLTPS-VARLLDPE----DVPSlRTLVLGGEALTQSDVDTWA---DRVRLINAYGPAECTIAATVSPVVPSTDPRN--- 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1532 LGRPLDNNeTWLLDE--HLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHP-------FAAGARLYRSGDRARRL 1602
Cdd:cd05918    268 IGRPLGAT-CWVVDPdnHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYN 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1603 ADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKA-LDGVRDAAVIVV------AGARLAAFATPQPGASLDAAALKRALAA 1675
Cdd:cd05918    347 PDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVVkpkdgsSSPQLVAFVVLDGSSSGSGDGDSLFLEP 426
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1888712850 1676 LL-----------------PDYMVPSVLRVIDALPLNRNGKLDRQALSALA 1709
Cdd:cd05918    427 SDefralvaelrsklrqrlPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
23-601 6.39e-96

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 318.68  E-value: 6.39e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAA-ERALILMDSGVDYVSAFFGCLYAGVVA 101
Cdd:COG0318      1 LADLLRRAAARHPDRPALV----FGGRRLTYAELDARARRLAAALRALGVGPgDRVALLLPNSPEFVVAFLAALRAGAVV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  102 VPVYPPESKREqhlarLRGIARDAGVRYVLTtaalherhadawsmlapgadvvavdtldardtpsdaplhpvraddlAFL 181
Cdd:COG0318     77 VPLNPRLTAEE-----LAYILEDSGARALVT----------------------------------------------ALI 105
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  182 QYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSpqYFleRPLRW 261
Cdd:COG0318    106 LYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP--RF--DPERV 181
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  262 LDAIARHRGT-ISGAPDFAYRLCaeriNDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFapagfdAAALYPCYGLAE 340
Cdd:COG0318    182 LELIERERVTvLFGVPTMLARLL----RHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF------GVRIVEGYGLTE 251
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  341 ATLFVTGGVRGAGLvshafssaalsagraeaaradeaaTVLVGCGAVQAGhrvaivaraaaeshesHEADVETETsraGE 420
Cdd:COG0318    252 TSPVVTVNPEDPGE------------------------RRPGSVGRPLPG----------------VEVRIVDED---GR 288
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  421 RLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDaprhadgsgpaRWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLY 499
Cdd:COG0318    289 ELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-----------GWLRTGDLGRLdEDGYLYIVGRKKDMIISGGENVY 357
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  500 PQDVEQAVEAHAEfarkgrvIAFGATLG-----GGETLGLALEIAPRMkkRFAAAQIVETLR-RIA-FdacgETPAAIAL 572
Cdd:COG0318    358 PAEVEEVLAAHPG-------VAEAAVVGvpdekWGERVVAFVVLRPGA--ELDAEELRAFLReRLArY----KVPRRVEF 424
                          570       580
                   ....*....|....*....|....*....
gi 1888712850  573 LnpGALPKTSSGKLQRAATREGWRARTLD 601
Cdd:COG0318    425 V--DELPRTASGKIDRRALRERYAAGALE 451
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
1215-1705 1.49e-94

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 315.14  E-value: 1.49e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1215 IHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALD 1294
Cdd:cd17644      2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1295 AGNPTQRLAQTLRDCGARLVLCEddcsaldlmgvqharidaaqeeaqreqhlraPHALpavdprsaAYVIYTSGSSGAPK 1374
Cdd:cd17644     82 PNYPQERLTYILEDAQISVLLTQ-------------------------------PENL--------AYVIYTSGSTGKPK 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1375 GVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLK 1454
Cdd:cd17644    123 GVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLS 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1455 IVPGHLHALLQA--ERAADALPAHTLVL-GGEATSWELLDTIA-ALRPDCRVHNHYGPTETTV-GILTQPAAQACRAAAT 1529
Cdd:cd17644    203 LPPAYWHLLVLEllLSTIDLPSSLRLVIvGGEAVQPELVRQWQkNVGNFIQLINVYGPTEATIaATVCRLTQLTERNITS 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1530 LPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAA--GARLYRSGDRARRLADGSL 1607
Cdd:cd17644    283 VPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNI 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1608 EYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIV----VAGARLAAFATPQPGASLDAAALKRALAALLPDYMVP 1683
Cdd:cd17644    363 EYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVredqPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIP 442
                          490       500
                   ....*....|....*....|..
gi 1888712850 1684 SVLRVIDALPLNRNGKLDRQAL 1705
Cdd:cd17644    443 SAFVVLEELPLTPNGKIDRRAL 464
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1215-1713 5.67e-93

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 310.20  E-value: 5.67e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1215 IHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALD 1294
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1295 AGNPTQRLAQTLRDCGARLVLCeddcsaldlmgvqharidaaqeeaqreqhlraphalpavdprsaAYVIYTSGSSGAPK 1374
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT--------------------------------------------ALILYTSGTTGRPK 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1375 GVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTV-LFGALASGGALHLIDRdttLDADRFAQTLAAARIDVL 1453
Cdd:COG0318    117 GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLLPR---FDPERVLELIERERVTVL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1454 KIVPGHLHALLQAERAADALPAH--TLVLGGEATSWELLDTIAAlRPDCRVHNHYGPTETTVGILTQPAAQACRAAATLp 1531
Cdd:COG0318    194 FGVPTMLARLLRHPEFARYDLSSlrLVVSGGAPLPPELLERFEE-RFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSV- 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1532 lGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPhpfaagaRLYRSGDRARRLADGSLEYLG 1611
Cdd:COG0318    272 -GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-------GWLRTGDLGRLDEDGYLYIVG 343
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1612 RIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLR 1687
Cdd:COG0318    344 RKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPdekwGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVE 423
                          490       500
                   ....*....|....*....|....*.
gi 1888712850 1688 VIDALPLNRNGKLDRQALSALARPAA 1713
Cdd:COG0318    424 FVDELPRTASGKIDRRALRERYAAGA 449
AMP-binding pfam00501
AMP-binding enzyme;
1219-1620 1.02e-90

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 302.31  E-value: 1.02e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAV-IDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGN 1297
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 PTQRLAQTLRDCGARLVLCEDDCSALDLMGVQHAR--------IDAAQEEAQREQHLRA------PHALPAVDPRSAAYV 1363
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLevvklvlvLDRDPVLKEEPLPEEAkpadvpPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1364 IYTSGSSGAPKGVVIAHGALTNYVDAV----LARLDPPPRARFAMVSTIGADLGHTV-LFGALASGGALHLIDRDTTLDA 1438
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1439 DRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAH--TLVLGGEATSWELLDTIAALRPdCRVHNHYGPTETTvGIL 1516
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSlrLVLSGGAPLPPELARRFRELFG-GALVNGYGLTETT-GVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1517 TQPAAQACRAAATLPLGRPLDNNETWLLD-EHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPhpfaagARLYRS 1595
Cdd:pfam00501  319 TTPLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRT 392
                          410       420
                   ....*....|....*....|....*
gi 1888712850 1596 GDRARRLADGSLEYLGRIDDQVKIR 1620
Cdd:pfam00501  393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
1227-1705 2.04e-90

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 303.63  E-value: 2.04e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLCEDDC-SALDLMGVQHARID--AAQEEAQREQHLRAPHALpavdprsaAYVIYTSGSSGAPKGVVIAHGAL 1383
Cdd:cd17656     82 LDSGVRVVLTQRHLkSKLSFNKSTILLEDpsISQEDTSNIDYINNSDDL--------LYIIYTSGTTGKPKGVQLEHKNM 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1384 TNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLkIVPGHLHAL 1463
Cdd:cd17656    154 VNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1464 LQAER-AADALPAHT--LVLGGEA--TSWELLDTIaaLRPDCRVHNHYGPTETTVgILTQPAAQACRAAATLPLGRPLDN 1538
Cdd:cd17656    233 IFSEReFINRFPTCVkhIITAGEQlvITNEFKEML--HEHNVHLHNHYGPSETHV-VTTYTINPEAEIPELPPIGKPISN 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1539 NETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVK 1618
Cdd:cd17656    310 TWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVK 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1619 IRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQpgASLDAAALKRALAALLPDYMVPSVLRVIDALPL 1694
Cdd:cd17656    390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKAddkgEKYLCAYFVME--QELNISQLREYLAKQLPEYMIPSFFVPLDQLPL 467
                          490
                   ....*....|.
gi 1888712850 1695 NRNGKLDRQAL 1705
Cdd:cd17656    468 TPNGKVDRKAL 478
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
75-600 2.37e-90

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 308.97  E-value: 2.37e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKreQHLARLRGIARDAGVRYVLTTAALHERHADAWSMLaPGAD-- 152
Cdd:PRK07769    80 DRVAILAPQNLDYLIAFFGALYAGRIAVPLFDPAEP--GHVGRLHAVLDDCTPSAILTTTDSAEGVRKFFRAR-PAKErp 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  153 -VVAVDTLDARDTPSDAPLHPVRaDDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMG 231
Cdd:PRK07769   157 rVIAVDAVPDEVGATWVPPEANE-DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMG 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  232 LIGSLLQPVFsGIPLVLMSPQYFLERPLRWLDAIARH----RGTISGAPDFAYRLCAER-INDETRAKLDLSSWRLAFSG 306
Cdd:PRK07769   236 LITVLLPALL-GHYITFMSPAAFVRRPGRWIRELARKpggtGGTFSAAPNFAFEHAAARgLPKDGEPPLDLSNVKGLLNG 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  307 SEPVRRDTLDDFVARFAPAGFDAAALYPCYGLAEATLFV-TGGVRGAGLVSHAfSSAALSAGRAEAARADEAATVL-VGC 384
Cdd:PRK07769   315 SEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVsTTPMDEEPTVIYV-DRDELNAGRFVEVPADAPNAVAqVSA 393
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  385 GAVQAGHRVaivaraaaeshesheADVETETsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVD------APRH 458
Cdd:PRK07769   394 GKVGVSEWA---------------VIVDPET---ASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNilksrlSESH 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  459 ADGSGP-ARWLRTGDLGFVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAFG-------------A 524
Cdd:PRK07769   456 AEGAPDdALWVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSvpanqlpqvvfddS 535
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  525 TLG-------GGETLGLALEIAPRMKKRFAAAqIVETLRRIAFDACGETPAAIALLNPGALPKTSSGKLQRAATREGWRA 597
Cdd:PRK07769   536 HAGlkfdpedTSEQLVIVAERAPGAHKLDPQP-IADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLD 614

                   ...
gi 1888712850  598 RTL 600
Cdd:PRK07769   615 GSL 617
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
75-588 9.35e-90

FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.


Pssm-ID: 468603 [Multi-domain]  Cd Length: 613  Bit Score: 306.58  E-value: 9.35e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPP-ESKREQHLarlRGIARDAGVRYVLTT----AALHERHADAwsmlaP 149
Cdd:NF040633    87 DRVAILANNSPEYIFGFLGALYAGMVPVPLYDPnEPGHADHL---RAVLADSGPTVVLTNktsaPAVRAHFADL-----P 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  150 GAD---VVAVDTL-------------DARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLG 213
Cdd:NF040633   159 AAErprILSVDSLpdslaeswvnpmaTIEGQPLLAPAGTDPSDDTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQ 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  214 VRPDDVFVSWLPLYHDMGLIGSLLQPVFsGIPLVLMSPQYFLERPLRWLDAIARHRG---TISGAPDFAYRLCAERINDE 290
Cdd:NF040633   239 LKTPLRLVSWLPLHHDMGIILAAFVTIL-GLEFELMSPRDFIQQPKRWVDQLSRREDdvnVYTVVPNFALELAARYANPE 317
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  291 TRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGRAE 370
Cdd:NF040633   318 EGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERPLFTYFDREALAEGRAV 397
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  371 AARADEAATV-LVGCGAVQAGHrvaivaraaaeshesHEADVETETsraGERLADGRIGEIHVSGPSVAHGYWQRADASA 449
Cdd:NF040633   398 EVAEDSENAVpFASNGQVVRPQ---------------VLAIVDPET---GQELPDGTVGEIWVHGDNMAAGYLDREEETA 459
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  450 QAF-------VDAPRHADGSGPARWLRTGDLGFVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAF 522
Cdd:NF040633   460 ETFrntlgerLAENSRAEGAPEDNWMATGDLGVIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAF 539
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1888712850  523 GATLGGGETLGLaleIAPRMKKRFAA--AQIVETLRRIAFDACGETPAAIALLNPGALPKTSSGKLQR 588
Cdd:NF040633   540 AVPGDDVEKLVI---LAERDDEADESgdAEAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIAR 604
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
75-592 3.46e-89

long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.


Pssm-ID: 468483 [Multi-domain]  Cd Length: 625  Bit Score: 305.11  E-value: 3.46e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKreQHLARLRGIARDAGVRYVLTTAALHERHADAWSMLaPGAD-- 152
Cdd:NF038339    77 DRVAILAPQGLDYVVSFFAAIYAGNIAVPLFDPDEP--GHTDRLHAVLGDCKPSAILTATSSAEGVRKFFRSL-PAKErp 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  153 -VVAVDTLDarDTPSDAPLHP-VRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDM 230
Cdd:NF038339   154 rVIAVDAVP--DSVGSTWVRPdADLDDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDENSRGVTWLPLFHDM 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  231 GLIGSLLQPVFsGIPLVLMSPQYFLERPLRWLDAIAR---HRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGS 307
Cdd:NF038339   232 GLLTVILPALG-GKYITIMSPAAFVRRPGRWIRELAAvsdGAGTFAAAPNFAFEHAAARGLPKEGEPLDLSNVIGLINGS 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  308 EPVRRDTLDDFVARFAPAGFDAAALYPCYGLAEATLFVTGGVRG-AGLVSHAfSSAALSAGRAEAARADEAATVL-VGCG 385
Cdd:NF038339   311 EPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREdEAKVIYV-DREELNAGRIVEVDPDAPNAVAqVSCG 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  386 AVqaghrvaivaraaaeSHESHEADVETETsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAF-------VDAPRH 458
Cdd:NF038339   390 YV---------------ARSQWAVIVDPET---GTELPDGQVGEIWLHGNNIGTGYWGRPEETEETFhnklksrLEEGSH 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  459 ADGSGP-ARWLRTGDLGFVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAF--------------- 522
Cdd:NF038339   452 AEGAPEdANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFsvpanqlpaevfens 531
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850  523 --GATLGGG---ETLGLALEIAPRMKKrFAAAQIVETLRRIAFDACGETPAAIALLNPGALPKTSSGKLQRAATR 592
Cdd:NF038339   532 hsGLKYDADdssEQLVIVAERAPGAGK-ADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACK 605
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
75-601 5.83e-88

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 301.27  E-value: 5.83e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPEskREQHLARLRGIARDAGVRYVLTTAALHERHADAWSMLaPGAD-- 152
Cdd:PRK12476    93 DRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPE--LPGHAERLDTALRDAEPTVVLTTTAAAEAVEGFLRNL-PRLRrp 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  153 -VVAVDTLDARDTPSDAPLhPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIA-IQAGLGVRPDDVFVSWLPLYHDM 230
Cdd:PRK12476   170 rVIAIDAIPDSAGESFVPV-ELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQmILSIDLLDRNTHGVSWLPLYHDM 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  231 GLIgSLLQPVFSGIPLVLMSPQYFLERPLRWLDAI---ARHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLaFSGS 307
Cdd:PRK12476   249 GLS-MIGFPAVYGGHSTLMSPTAFVRRPQRWIKALsegSRTGRVVTAAPNFAYEWAAQRGLPAEGDDIDLSNVVL-IIGS 326
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  308 EPVRRDTLDDFVARFAPAGFDAAALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGRAEAARADEAATVL-VGCGA 386
Cdd:PRK12476   327 EPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADAPNAVAhVSCGQ 406
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  387 VqaghrvaivaraaaeSHESHEADVETETsraGERLADGRIGEIHVSGPSVAHGYWQRAD-------ASAQAFVDAPRHA 459
Cdd:PRK12476   407 V---------------ARSQWAVIVDPDT---GAELPDGEVGEIWLHGDNIGRGYWGRPEetertfgAKLQSRLAEGSHA 468
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  460 DGSGP-ARWLRTGDLGFVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAFGATLGGGETLGLALEI 538
Cdd:PRK12476   469 DGAADdGTWLRTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGYVTAFTVPAEDNERLVIVAER 548
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1888712850  539 APRmKKRFAAAQIVETLRRIAFDACGETPAAIALLNPGALPKTSSGKLQRAATREGWRARTLD 601
Cdd:PRK12476   549 AAG-TSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLG 610
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
725-1198 1.26e-87

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 294.63  E-value: 1.26e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  725 AEEAVISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAhlyaPR--TEAA 802
Cdd:pfam00668    2 QDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGE----PVqvILEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  803 APLAWAHVDLSDLGDIDEhdrERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEEL 882
Cdd:pfam00668   78 RPFELEIIDISDLSESEE---EEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  883 VDGYRAALDGATThgeaQAKAKTriTYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHTatdtasENADPR 962
Cdd:pfam00668  155 ADLYQQLLKGEPL----PLPPKT--PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYA------RPADRS 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  963 AAA-RVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSD 1041
Cdd:pfam00668  223 FKGdRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRID 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1042 CEAATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSF---NYLSDDYPALARWPGARAERVEIAE 1118
Cdd:pfam00668  303 PKGGKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFsfqNYLGQDSQEEEFQLSELDLSVSSVI 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1119 THV-KVPLALDLREsRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAFAhalgdrsadmTDAAAPtLATLDLLDADER 1197
Cdd:pfam00668  383 EEEaKYDLSLTASE-RGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAI----------AHPSQP-LSELDLLSDAEK 450

                   .
gi 1888712850 1198 A 1198
Cdd:pfam00668  451 Q 451
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
27-598 7.93e-87

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 296.79  E-value: 7.93e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   27 LRALAQQRPEATALIVIDADGD-----TRYDYAQLDRRARALAARFARDGAAAERALILMDSGVDYVSAFFGCLYAGVVA 101
Cdd:NF038337    10 LRERAGLQPDDVAFRYTDYEQDwagvtETLTWAQLYRRTLNVAHEVRRHGTTGDRAVILAPQGLPYIVAFLGAMQAGLIA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  102 VPVYPPESKreQHLARLRGIARDAGVRYVLTTAAL------HERHADAwsmlAPGADVVAVDTLDArDTPSDAPLHPVRA 175
Cdd:NF038337    90 VPLSVPQPG--SHDERVSAVLADTSPSVVLTTSAAaaavaeYLHRPDT----GAVPAVIEIDSLDL-DGPNSPSIRISDA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  176 DDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGL-----GVRP-DDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLM 249
Cdd:NF038337   163 PSIAYLQYTSGSTRLPAGVMVSHRNLQVNFQQLMAAYfpdtnGVAPrDTTIVSWLPFYHDMGLVLGVIAPILGGYRSELT 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  250 SPQYFLERPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDA 329
Cdd:NF038337   243 SPVAFLQRPARWIHAMANGSPVFSAAPNFAFELAVRKTTDADLAGLDLGNVIGIVSGAERIHPATLDRFCKRFAPYNFRE 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  330 AALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGrAEAARADEAATVLVGCGAVQaghrvaivaraaaeSHESHEA 409
Cdd:NF038337   323 DMMQPSYGLAEATVYVASRAEGGAPEVVHFEPEKLSEG-SAQRCEARTGSPLLSYGTPT--------------SPTVRIV 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  410 DVETETSRagerlADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHADGSGPAR-WLRTGDLGFVHDGQLYIAGRVK 488
Cdd:NF038337   388 DPDTCIEC-----PAGTVGEIWVHGDNVAEGYWQKPEETRRTFGGVLANPSPGTPEGpWLRTGDLGFISEDEMFIVGRMK 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  489 DLVIVRGRNLYPQDVEQAVEAhaefARKGRVIAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRR----IAFDACG 564
Cdd:NF038337   463 DLLIVYGRNHYPEDIESTVQE----ITGGRVAAISVPVDETEKLVTIIELKKRGDSDEEAMRKLDAVKNnvtaAISRSHG 538
                          570       580       590
                   ....*....|....*....|....*....|....
gi 1888712850  565 ETPAAIALLNPGALPKTSSGKLQRAATREGWRAR 598
Cdd:NF038337   539 LNVADLVLVPPGSIPTTTSGKIRRAACVEQYRRQ 572
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
1845-2291 1.10e-86

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 291.09  E-value: 1.10e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1845 LPLSLMQQRIWVVDQLADRAlASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDeGDPVLKIAPRMEVLmP 1924
Cdd:cd19538      2 IPLSFAQRRLWFLHQLEGPS-ATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEED-GVPYQLILEEDEAT-P 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1925 VIEplahpdndanshtnsHTNSDENArtqaTAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVH 2004
Cdd:cd19538     79 KLE---------------IKEVDEEE----LESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLA 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2005 ILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARF---TPDAVREAQQ--FWRGYLADAPALLPLSTDRARPTRVS 2079
Cdd:cd19538    140 PLTRDLSKAYRARCKGEAPELAPLPVQYADYALWQQELLgdeSDPDSLIARQlaYWKKQLAGLPDEIELPTDYPRPAESS 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2080 HAGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSr 2159
Cdd:cd19538    220 YEGGTLTFEIDSELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRT- 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2160 iaaDGANLASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRDLPRGNTRVPGLAVELLRPPT 2239
Cdd:cd19538    299 ---DTSGNPSFRELLERVKETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTV 375
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850 2240 TQSKFDMA--LFVEAVDGGYD-----IEwvYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19538    376 GSAKFDLTfeLREQYNDGTPNgiegfIE--YRTDLFDHETIEALAQRYLLLLESAVENP 432
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
142-593 1.79e-86

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 294.60  E-value: 1.79e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  142 DAWSMLAP--GADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPD-D 218
Cdd:PRK07768   116 EPFLAAAPvlEEKGIRVLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtD 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  219 VFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQYFLERPLRWLDAIARHRGTISGAPDFAYRLCAERI-NDETRAKLDL 297
Cdd:PRK07768   196 VMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLrRQAKPGAFDL 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  298 SSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGRAEAARADEA 377
Cdd:PRK07768   276 SSLRFALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEATLAVSFSPCGAGLVVDEVDADLLAALRRAVPATKGN 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  378 ATVLVGCGAVQAGhrvaivaraaaeshesHEADVeteTSRAGERLADGRIGEIHVSGPSVAHGYwqradasaqafvdapR 457
Cdd:PRK07768   356 TRRLATLGPPLPG----------------LEVRV---VDEDGQVLPPRGVGVIELRGESVTPGY---------------L 401
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  458 HADGSGPAR----WLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVeAHAEFARKGRVIAFGATLG-GGET 531
Cdd:PRK07768   402 TMDGFIPAQdadgWLDTGDLGyLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAA-ARVEGVRPGNAVAVRLDAGhSREG 480
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850  532 LGLALEIaprmkkrfAAAQIVETLRRIA-------FDACGETPAAIALLNPGALPKTSSGKLQRAATRE 593
Cdd:PRK07768   481 FAVAVES--------NAFEDPAEVRRIRhqvahevVAEVGVRPRNVVVLGPGSIPKTPSGKLRRANAAE 541
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
17-597 2.97e-86

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 293.80  E-value: 2.97e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   17 AVPAHGLAARLRALAQQRPEATALI---VIDADG-DTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAF 91
Cdd:cd05906      2 LHRPEGAPRTLLELLLRAAERGPTKgitYIDADGsEEFQSYQDLLEDARRLAAGLRQLGlRPGDSVILQFDDNEDFIPAF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   92 FGCLYAGVVAVPVYPPESKREQH--LARLRGIARDAGVRYVLTTAALHE--RHADAWSMLaPGADVVAVDtlDARDTPSD 167
Cdd:cd05906     82 WACVLAGFVPAPLTVPPTYDEPNarLRKLRHIWQLLGSPVVLTDAELVAefAGLETLSGL-PGIRVLSIE--ELLDTAAD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  168 APLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLV 247
Cdd:cd05906    159 HDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  248 LMSPQYFLERPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGF 327
Cdd:cd05906    239 HVPTEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGL 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  328 DAAALYPCYGLAEATLFVTggvrgaglVSHAFSSAALSAGraeaaradeaaTVLVGCGAVQAGhrvaivaraaaeshesh 407
Cdd:cd05906    319 PPDAIRPAFGMTETCSGVI--------YSRSFPTYDHSQA-----------LEFVSLGRPIPG----------------- 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  408 eADVETeTSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDaprhaDGsgparWLRTGDLGFVHDGQLYIAGRV 487
Cdd:cd05906    363 -VSMRI-VDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTE-----DG-----WFRTGDLGFLDNGNLTITGRT 430
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  488 KDLVIVRGRNLYPQDVEQAVEAhAEFARKGRVIAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDACGETP 567
Cdd:cd05906    431 KDTIIVNGVNYYSHEIEAAVEE-VPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSREVGVSP 509
                          570       580       590
                   ....*....|....*....|....*....|
gi 1888712850  568 AAIALLNPGALPKTSSGKLQRAATREGWRA 597
Cdd:cd05906    510 AYLIPLPKEEIPKTSLGKIQRSKLKAAFEA 539
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
730-1170 2.07e-85

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 287.35  E-value: 2.07e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  730 ISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYAPRTEAAAPLAwaH 809
Cdd:cd19539      4 LSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLE--V 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  810 VDLSDLGDidehDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAA 889
Cdd:cd19539     82 RDLSDPDS----DRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAAR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  890 LDGATTHGEAqakakTRITYADYAAWQRRWLASDAAARQLAYWRAALaDDAPPLALPYDHTATDTAsenadPRAAARVAF 969
Cdd:cd19539    158 RKGPAAPLPE-----LRQQYKEYAAWQREALAAPRAAELLDFWRRRL-RGAEPTALPTDRPRPAGF-----PYPGADLRF 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  970 ALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEAATPLA 1049
Cdd:cd19539    227 ELDAELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFR 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1050 SLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPALARWPGARAERVEIAETHVKVPLALDL 1129
Cdd:cd19539    307 DLIARVRKALVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTV 386
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1888712850 1130 RESrDGSMRAYFTYASARFDAASVERMAAQYLRAVEAFAHA 1170
Cdd:cd19539    387 TEE-GTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLAN 426
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
1846-2291 2.32e-85

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 286.97  E-value: 2.32e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIWVVDQLADRALAsYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDEGDPVLKIAPRME-VLMP 1924
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGPA-YNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPaPLEV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1925 VIEPLAHPDndanshtnshtnsdenaRTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVH 2004
Cdd:cd19539     82 RDLSDPDSD-----------------RERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLD 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2005 ILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADApALLPLSTDRARPTRVSHAGAA 2084
Cdd:cd19539    145 VFARDLAALYAARRKGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGA-EPTALPTDRPRPAGFPYPGAD 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2085 RHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSRIAADg 2164
Cdd:cd19539    224 LRFELDAELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDC- 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2165 anlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRDLPRGNTRVPG-LAVELLRPPTTQSK 2243
Cdd:cd19539    303 ---ATFRDLIARVRKALVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGgLSYTEGSDIPDGAK 379
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1888712850 2244 FDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19539    380 FDLNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1846-2290 7.86e-85

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 285.69  E-value: 7.86e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIWVVDQ-LADRAlaSYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDEgdpvlkiaprmevlmp 1924
Cdd:cd20483      3 PMSTFQRRLWFLHNfLEDKT--FLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDD---------------- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1925 viEPLAHPDNDANSHTNSHTNSDENARTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVH 2004
Cdd:cd20483     65 --FGEQQVLDDPSFHLIVIDLSEAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2005 ILLDELCELYRAQRDGAPPA-LAPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADAPA---LLPLSTdRARPTRVSH 2080
Cdd:cd20483    143 SIFEQFTALYDALRAGRDLAtVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDaskLLPFAK-AERPPVKDY 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2081 AGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTdVDG-RERAELEALIGFFVNVVPLRSR 2159
Cdd:cd20483    222 ERSTVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGM-VDGdRPHPDFDDLVGFFVNMLPIRCR 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2160 IAADGanlaSFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFvlrdlprgNTRVPG---------- 2229
Cdd:cd20483    301 MDCDM----SFDDLLESTKTTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAV--------NYQVHGkfpeydtgdf 368
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1888712850 2230 --LAVELLRPPTtqsKFDMAL-FVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSAD 2290
Cdd:cd20483    369 kfTDYDHYDIPT---ACDIALeAEEDPDGGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
1846-2303 7.87e-85

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 286.54  E-value: 7.87e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIWVVDQLADRAlASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDEGDPVLKIAPRMEVLMPV 1925
Cdd:pfam00668    6 PLSPAQKRMWFLEKLEPHS-SAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1926 IEpLAHpdndanshtnshtnSDENARTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVHI 2005
Cdd:pfam00668   85 ID-ISD--------------LSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGI 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2006 LLDELCELYRAQRDGAPPALAPLaVQYADYAHWQRARFTPDAVREAQQFWRGYLADAPALLPLSTDRARPTRVSHAGAAR 2085
Cdd:pfam00668  150 LLRDLADLYQQLLKGEPLPLPPK-TPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2086 HFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSRIaADGA 2165
Cdd:pfam00668  229 SFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDP-KGGK 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2166 NLASFdawLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRDLPRGNTRVPGLAVELLRP-----PTT 2240
Cdd:pfam00668  308 TFSEL---IKRVQEDLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEEFQLSELDLsvssvIEE 384
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1888712850 2241 QSKFDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADPRAPLASSLSTSP 2303
Cdd:pfam00668  385 EAKYDLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSD 447
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1828-2297 8.68e-85

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 307.17  E-value: 8.68e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1828 ANAESATPLHALADRSALPLSLMQQRIWVVDQLAdRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADD 1907
Cdd:COG1020      1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLL-LGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1908 EGDPVLKIAPRMEVLMPVIEPLAHPDndanshtnshtnsdenARTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHH 1987
Cdd:COG1020     80 GRPVQVIQPVVAAPLPVVVLLVDLEA----------------LAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLL 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1988 VLIVSLHHIVADGGSVHILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADAPALLP 2067
Cdd:COG1020    144 LLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLE 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2068 LSTDRARPTRVSHAGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALI 2147
Cdd:COG1020    224 LPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLV 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2148 GFFVNVVPLRSRIAADganlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRDLPRGNTRV 2227
Cdd:COG1020    304 GFFVNTLPLRVDLSGD----PSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELEL 379
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2228 PGLAVELLRPPTTQSKFDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADPRAPLAS 2297
Cdd:COG1020    380 PGLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGD 449
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
1227-1706 6.22e-83

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 281.21  E-value: 6.22e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLAR-DLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQT 1305
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVaEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1306 LRDCGARLVLceddcsaldlmgvqharidaaqeeaqreqhlraphalpaVDPRSAAYVIYTSGSSGAPKGVVIAHGALTN 1385
Cdd:cd17648     81 LEDTGARVVI---------------------------------------TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVN 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1386 YVDAVLARLDPPPRARFAMVSTIGADLGHTV--LFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPghlhAL 1463
Cdd:cd17648    122 LRTSLSERYFGRDNGDEAVLFFSNYVFDFFVeqMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTP----SV 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1464 LQAERAADALPAHTLVLGGEATSWELLDTIAALRPDcRVHNHYGPTETTVGILTQPAAQACRAAATLplGRPLDNNETWL 1543
Cdd:cd17648    198 LQQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAG-LIINAYGPTETTVTNHKRFFPGDQRFDKSL--GRPVRNTKCYV 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1544 LDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAA--------GARLYRSGDRARRLADGSLEYLGRIDD 1615
Cdd:cd17648    275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDF 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1616 QVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGA---------RLAAFATPQPGAsLDAAALKRALAALLPDYMVPSVL 1686
Cdd:cd17648    355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAsqaqsriqkYLVGYYLPEPGH-VPESDLLSFLRAKLPRYMVPARL 433
                          490       500
                   ....*....|....*....|
gi 1888712850 1687 RVIDALPLNRNGKLDRQALS 1706
Cdd:cd17648    434 VRLEGIPVTINGKLDVRALP 453
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
1227-1705 7.82e-82

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 277.51  E-value: 7.82e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:cd17645     12 PDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYML 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLceddcsaldlmgvqharidaaqeeaqreqhlraphalpaVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNY 1386
Cdd:cd17645     92 ADSSAKILL---------------------------------------TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNL 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1387 VDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQA 1466
Cdd:cd17645    133 CEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQFMQL 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1467 ERAAdalpAHTLVLGGEATSwelldtiAALRPDCRVHNHYGPTETTVGILTQPAAQACRaaaTLPLGRPLDNNETWLLDE 1546
Cdd:cd17645    213 DNQS----LRVLLTGGDKLK-------KIERKGYKLVNNYGPTENTVVATSFEIDKPYA---NIPIGKPIDNTRVYILDE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1547 HLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEP 1626
Cdd:cd17645    279 ALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEP 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1627 GEIAARLKALDGVRDAAVIVV--AGAR--LAAFATPQPGASldAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDR 1702
Cdd:cd17645    359 GEIEPFLMNHPLIELAAVLAKedADGRkyLVAYVTAPEEIP--HEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDR 436

                   ...
gi 1888712850 1703 QAL 1705
Cdd:cd17645    437 KAL 439
PRK12316 PRK12316
peptide synthase; Provisional
1845-2297 2.44e-78

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 291.09  E-value: 2.44e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1845 LPLSLMQQRIWVVDQLaDRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDAddEGDPVLKIAPRMEVLMP 1924
Cdd:PRK12316    50 DRLSYAQQRMWFLWQL-EPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPR--GADDSLAQVPLDRPLEV 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1925 VIEPLAHpdndanshtnshtnSDENARTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVH 2004
Cdd:PRK12316   127 EFEDCSG--------------LPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMN 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2005 ILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFtpDAVREAQQ--FWRGYLADAPALLPLSTDRARPTRVSHAG 2082
Cdd:PRK12316   193 VLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWL--EAGEQERQleYWRAQLGEEHPVLELPTDHPRPAVPSYRG 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2083 AARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSRIaa 2162
Cdd:PRK12316   271 SRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVF-- 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2163 DGAnlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRDLP---RGNTRVPGLAVELLRPPT 2239
Cdd:PRK12316   349 DGR--TRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLVadiEALDTVAGLEFGQLEWKS 426
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1888712850 2240 TQSKFDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADPRAPLAS 2297
Cdd:PRK12316   427 RTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDE 484
AMP-binding pfam00501
AMP-binding enzyme;
27-494 4.58e-73

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 251.08  E-value: 4.58e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   27 LRALAQQRPEATALIVidaDGDTRYDYAQLDRRARALAARFARDGA-AAERALILMDSGVDYVSAFFGCLYAGVVAVPVY 105
Cdd:pfam00501    1 LERQAARTPDKTALEV---GEGRRLTYRELDERANRLAAGLRALGVgKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  106 PpeskrEQHLARLRGIARDAGVRYVLTTAALH-ERHADAWSMLAPGADVVAVDTLDARDT-----------PSDAPLHPV 173
Cdd:pfam00501   78 P-----RLPAEELAYILEDSGAKVLITDDALKlEELLEALGKLEVVKLVLVLDRDPVLKEeplpeeakpadVPPPPPPPP 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  174 RADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAI----QAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLM 249
Cdd:pfam00501  153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLP 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  250 SPQYFLeRPLRWLDAIARHRGTI-SGAPDFAYRLcaerINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPagfd 328
Cdd:pfam00501  233 PGFPAL-DPAALLELIERYKVTVlYGVPTLLNML----LEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG---- 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  329 aaALYPCYGLAEATLFVTGGVRGAGLVshafsSAALSAGraeaaradeaaTVLVGCGAVQaghrvaivaraaaesheshe 408
Cdd:pfam00501  304 --ALVNGYGLTETTGVVTTPLPLDEDL-----RSLGSVG-----------RPLPGTEVKI-------------------- 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  409 ADVETetsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVdaprhadgsgPARWLRTGDLGFVH-DGQLYIAGRV 487
Cdd:pfam00501  346 VDDET-----GEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD----------EDGWYRTGDLGRRDeDGYLEIVGRK 410

                   ....*..
gi 1888712850  488 KDLVIVR 494
Cdd:pfam00501  411 KDQIKLG 417
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1846-2291 9.94e-72

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 247.37  E-value: 9.94e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIWVVDQ-LADRAlaSYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDEGDpvlkiAPRMEVLM- 1923
Cdd:cd19532      3 PMSFGQSRFWFLQQyLEDPT--TFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDG-----EPMQGVLAs 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1924 PVIEpLAHpdndanshtnsHTNSDEnartQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSV 2003
Cdd:cd19532     76 SPLR-LEH-----------VQISDE----AEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSF 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2004 HILLDELCELYRAQRdgappaLAPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADAPA---LLPLSTDRARPTRVSH 2080
Cdd:cd19532    140 QIFLRDLERAYNGQP------LLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEplpLLPFAKVKSRPPLTRY 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2081 AGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSRI 2160
Cdd:cd19532    214 DTHTAERRLDAALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRR 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2161 AADganlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLF-----VLRDLPRGNTRVPGLAVELL 2235
Cdd:cd19532    294 DPS----QTFADVLKETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFInyrqgVAESRPFGDCELEGEEFEDA 369
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1888712850 2236 RPPttqskFDMAL-FVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19532    370 RTP-----YDLSLdIIDNPDGDCLLTLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
727-1169 8.12e-71

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 245.25  E-value: 8.12e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  727 EAVISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHlyaprtEAAAPLA 806
Cdd:cd19538      1 EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPY------QLILEED 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  807 WAHVDLsDLGDIDEHDRERALRECAQRfadaPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGY 886
Cdd:cd19538     75 EATPKL-EIKEVDEEELESEINEAVRY----PFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAY 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  887 RAALdgattHGEAQAKAKTRITYADYAAWQRRWLASDAA-----ARQLAYWRAALADDAPPLALPYDHtatdtasenadP 961
Cdd:cd19538    150 RARC-----KGEAPELAPLPVQYADYALWQQELLGDESDpdsliARQLAYWKKQLAGLPDEIELPTDY-----------P 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  962 RAAAR------VAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNT 1035
Cdd:cd19538    214 RPAESsyeggtLTFEIDSELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNT 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1036 LVLHSDCEAATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPALaRWPGARAErVE 1115
Cdd:cd19538    294 LVLRTDTSGNPSFRELLERVKETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSL-DLPGLEAK-LE 371
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850 1116 IAET-HVKVPLALDLRESRD----GSMRAYFTYASARFDAASVERMAAQYLRAVEAFAH 1169
Cdd:cd19538    372 LRTVgSAKFDLTFELREQYNdgtpNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVE 430
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
932-1831 9.14e-71

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 263.46  E-value: 9.14e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  932 WRAALadDAPPL-ALPYDHTatdtasenaDPRAAARVAFALPAPLAQAVRAsaARHRATPFVVLLAAYHAWLYRVTGQRA 1010
Cdd:TIGR03443    2 WSERL--DNPTLsVLPHDYL---------RPANNRLVEATYSLQLPSAEVT--AGGGSTPFIILLAAFAALVYRLTGDED 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1011 IRTGVPVANRTRPethdvigffvntLVLHSDCEAATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPA-RDAQHGPLF 1089
Cdd:TIGR03443   69 IVLGTSSNKSGRP------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAkKLERTPPLF 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1090 ETSFnylsddYPAlarwPGARAERVEiaeTHVKVPLALDL-RESRDGSMRAYFT---YASARFdAASVERMAaQYLRAVE 1165
Cdd:TIGR03443  137 RLAF------QDA----PDNQQTTYS---TGSTTDLTVFLtPSSPELELSIYYNsllFSSDRI-TIVADQLA-QLLSAAS 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1166 A-FAHALGDRSAdMTDAAAPTLA--TLDLLDADERArvsaasvarrtppgePIHLRVARHADTQPDAPAVIDGALRM--- 1239
Cdd:TIGR03443  202 SnPDEPIGKVSL-ITPSQKSLLPdpTKDLDWSGFRG---------------AIHDIFADNAEKHPDRTCVVETPSFLdps 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 ------SYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRlaQT-------- 1305
Cdd:TIGR03443  266 sktrsfTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPAR--QTiylsvakp 343
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1306 -----LRDCGARLVLCEDDCS-ALDLM------------GVQHARIDAAQEEA-QREQHLRAPHALPAVDPRSAAYVIYT 1366
Cdd:TIGR03443  344 ralivIEKAGTLDQLVRDYIDkELELRteipalalqddgSLVGGSLEGGETDVlAPYQALKDTPTGVVVGPDSNPTLSFT 423
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1367 SGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLA 1446
Cdd:TIGR03443  424 SGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMA 503
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1447 AARIDVLKIVPGhLHALLQAErAADALPA--HTLVLGGEATSWELLdTIAALRPDCRVHNHYGPTET--TVGILTQPAAQ 1522
Cdd:TIGR03443  504 KYGATVTHLTPA-MGQLLSAQ-ATTPIPSlhHAFFVGDILTKRDCL-RLQTLAENVCIVNMYGTTETqrAVSYFEIPSRS 580
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1523 A-----CRAAATLPLGRPLDNNETWLLDEH--LNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFA-------- 1587
Cdd:TIGR03443  581 SdstflKNLKDVMPAGKGMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVdpshwidl 660
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1588 -----AGA---------RLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVvagaR-- 1651
Cdd:TIGR03443  661 dkennKPErefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLV----Rrd 736
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1652 ------LAAFATPQPGASLDAAALKRALAALL--------------------------PDYMVPSVLRVIDALPLNRNGK 1699
Cdd:TIGR03443  737 kdeeptLVSYIVPQDKSDELEEFKSEVDDEESsdpvvkglikyrklikdireylkkklPSYAIPTVIVPLKKLPLNPNGK 816
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1700 LDRQAL-----SALARPAAPHREAARAAPQGETETALAQCWAALLdpsngtdnatdnatATPSLTIARDDSFFALGGHSL 1774
Cdd:TIGR03443  817 VDKPALpfpdtAQLAAVAKNRSASAADEEFTETEREIRDLWLELL--------------PNRPATISPDDSFFDLGGHSI 882
                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1888712850 1775 AAMRLASRVRSRWSVELPLREIFASPTLAALAARIEAQRADSDRASNQVSNKAANAE 1831
Cdd:TIGR03443  883 LATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDRLKKGEELADEGDSEIEEEET 939
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
87-611 6.56e-68

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 238.93  E-value: 6.56e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   87 YVSAFFGCLYAGVVAVPVYPPESkrEQHLARLRGIARDAGVRYVLTTAALHERHADawsmlapgadvvavdtldardtps 166
Cdd:cd05908     53 FLYLFWACLLGGMIAVPVSIGSN--EEHKLKLNKVWNTLKNPYLITEEEVLCELAD------------------------ 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  167 daplhpvradDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPL 246
Cdd:cd05908    107 ----------ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQ 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  247 VLMSPQYFLERPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAG 326
Cdd:cd05908    177 YLMPTRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYG 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  327 FDAAALYPCYGLAEATLfvtgGVRGAGLVSHAFSSAALSAGraeaaradeaatVLVGCGAVQAGHRVAIVARAAAESHES 406
Cdd:cd05908    257 LKRNAILPVYGLAEASV----GASLPKAQSPFKTITLGRRH------------VTHGEPEPEVDKKDSECLTFVEVGKPI 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  407 HEADVETeTSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDaprhaDGsgparWLRTGDLGFVHDGQLYIAGR 486
Cdd:cd05908    321 DETDIRI-CDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTD-----DG-----WLKTGDLGFIRNGRLVITGR 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  487 VKDLVIVRGRNLYPQDVEQAVEaHAEFARKGRVIAFG---ATLGGGETLGLAL------EIAPRMKK------RFAAAQI 551
Cdd:cd05908    390 EKDIIFVNGQNVYPHDIERIAE-ELEGVELGRVVACGvnnSNTRNEEIFCFIEhrksedDFYPLGKKikkhlnKRGGWQI 468
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850  552 VETL--RRIafdacgetpaaiallnpgalPKTSSGKLQRAATREGwrartldlyalWEQGAF 611
Cdd:cd05908    469 NEVLpiRRI--------------------PKTTSGKVKRYELAQR-----------YQSGEF 499
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
1845-2291 7.28e-68

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 236.54  E-value: 7.28e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1845 LPLSLMQQRIWVVDQLADRAlASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDeGDPVLKIAPRMEVLMP 1924
Cdd:cd19066      2 IPLSPMQRGMWFLKKLATDP-SAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEA-GRYEQVVLDKTVRFRI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1925 VIEPLAHpdndansHTNSHtnsdenartqATAQALDDAA-RTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSV 2003
Cdd:cd19066     80 EIIDLRN-------LADPE----------ARLLELIDQIqQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSF 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2004 HILLDELCELYRAQRDGAPpALAPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADAPALLPLSTDRARPTRVSHAGA 2083
Cdd:cd19066    143 QILFEDISSVYDAAERQKP-TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVL 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2084 ARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSRIAAD 2163
Cdd:cd19066    222 TLEFFLRSEETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPD 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2164 ganlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRDLPRGNTRVPGLAV-ELLRPPTTQS 2242
Cdd:cd19066    302 ----ATFPELLKRTKEQSREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFtTPVYTSSEGT 377
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2243 KFDMAL-FVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19066    378 VFDLDLeASEDPDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
730-1168 1.19e-67

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 235.77  E-value: 1.19e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  730 ISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVE-TGDAAHLYAPRTEAAAPlawA 808
Cdd:cd19066      4 LSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEeAGRYEQVVLDKTVRFRI---E 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  809 HVDLSDLgdIDEHDRERALRECAQRfadAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRA 888
Cdd:cd19066     81 IIDLRNL--ADPEARLLELIDQIQQ---TIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  889 ALDGATThgeaqaKAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHTATDTASENAdpraaARVA 968
Cdd:cd19066    156 AERQKPT------LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEV-----LTLE 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  969 FALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEAATPL 1048
Cdd:cd19066    225 FFLRSEETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATF 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1049 ASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPaLARWPGARAERVEIA-ETHVKVPLAL 1127
Cdd:cd19066    305 PELLKRTKEQSREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQ-LGKTGGFIFTTPVYTsSEGTVFDLDL 383
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1888712850 1128 DLRESRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAFA 1168
Cdd:cd19066    384 EASEDPDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLI 424
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
1847-2109 1.73e-67

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 228.38  E-value: 1.73e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1847 LSLMQQRIWVvdqlADRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDeGDPVLKIAPRMEVLMPVI 1926
Cdd:COG4908      1 LSPAQKRFLF----LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIDPDADLPLEVV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1927 EPLAHPDNDanshtnshtnsdenaRTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVHIL 2006
Cdd:COG4908     76 DLSALPEPE---------------REAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGIL 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2007 LDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADAPALLPLSTDRARPTRVSHAGAARH 2086
Cdd:COG4908    141 LRELAALYAALLEGEPPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLS 220
                          250       260
                   ....*....|....*....|...
gi 1888712850 2087 FRLDATLGARVRTLAQAHGMTPF 2109
Cdd:COG4908    221 FTLPAELTEALKALAKAHGATVN 243
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
731-991 3.05e-66

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 224.92  E-value: 3.05e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  731 SHAQQRQlfaWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHlyaPRTEAAAPLAWAHV 810
Cdd:COG4908      2 SPAQKRF---LFLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPV---QRIDPDADLPLEVV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  811 DLSDLgdiDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAAL 890
Cdd:COG4908     76 DLSAL---PEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  891 DGATTHGEAQAkaktrITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHTATDTASENadpraAARVAFA 970
Cdd:COG4908    153 EGEPPPLPELP-----IQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFR-----GATLSFT 222
                          250       260
                   ....*....|....*....|.
gi 1888712850  971 LPAPLAQAVRASAARHRATPF 991
Cdd:COG4908    223 LPAELTEALKALAKAHGATVN 243
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
85-592 1.02e-65

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 233.50  E-value: 1.02e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   85 VDYVSAFFGCLYAGVvAVPVYP-------PESKREQHLARLRGIardaGVRYVLTtaalHERHADAwsMLAPGADVVAVD 157
Cdd:PRK05851    65 VELVAAIQGAWLAGA-AVSILPgpvrgadDGRWADATLTRFAGI----GVRTVLS----HGSHLER--LRAVDSSVTVHD 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  158 TLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGV-RPDDVFVSWLPLYHDMGLIgSL 236
Cdd:PRK05851   134 LATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLdAATDVGCSWLPLYHDMGLA-FL 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  237 LQPVFSGIPLVLMSPQYFLERPLRWLDAIARHRGTISGAPDFAYRLC---AERINDetrakLDLSSWRLAFSGSEPVRRD 313
Cdd:PRK05851   213 LTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAAPNFAYNLIgkyARRVSD-----VDLGALRVALNGGEPVDCD 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  314 TLDDFVARFAPAGFDAAALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAALSAgraeaaraDEAATVLvgcGAVQAGhrv 393
Cdd:PRK05851   288 GFERFATAMAPFGFDAGAAAPSYGLAESTCAVTVPVPGIGLRVDEVTTDDGSG--------ARRHAVL---GNPIPG--- 353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  394 aivaraaaeshesheADVETETSRAGERLADGRIGEIHVSGPSVAHGYwqradasaqaFVDAPRHADGsgparWLRTGDL 473
Cdd:PRK05851   354 ---------------MEVRISPGDGAAGVAGREIGEIEIRGASMMSGY----------LGQAPIDPDD-----WFPTGDL 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  474 GFVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQaVEAHAEFARKGRVIAFGaTLGGGETLGLAleIAPRMKKRFAAAQIVE 553
Cdd:PRK05851   404 GYLVDGGLVVCGRAKELITVAGRNIFPTEIER-VAAQVRGVREGAVVAVG-TGEGSARPGLV--IAAEFRGPDEAGARSE 479
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1888712850  554 TLRRIAFDaCGETPAAIALLNPGALPKTSSGKLQRAATR 592
Cdd:PRK05851   480 VVQRVASE-CGVVPSDVVFVAPGSLPRTSSGKLRRLAVK 517
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1222-1705 1.61e-64

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 229.40  E-value: 1.61e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1222 HADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQR 1301
Cdd:PRK04813    11 FAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAER 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1302 LAQTLRDCGARLVLCEDDcsaLDLMGVQHARIDAAQEEAQREQHlRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHG 1381
Cdd:PRK04813    91 IEMIIEVAKPSLIIATEE---LPLEILGIPVITLDELKDIFATG-NPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1382 ALTNYVDAVLARLDPPPRARF---AMVSTigaDLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPG 1458
Cdd:PRK04813   167 NLVSFTNWMLEDFALPEGPQFlnqAPYSF---DLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPS 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1459 HLH-ALLQAERAADALPA--HTLVLGGEATSwellDTIAALR---PDCRVHNHYGPTETTVG---------ILTQpaaqa 1523
Cdd:PRK04813   244 FADmCLLDPSFNEEHLPNltHFLFCGEELPH----KTAKKLLerfPSATIYNTYGPTEATVAvtsieitdeMLDQ----- 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1524 craAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHpfaAGARLYRSGDRARrLA 1603
Cdd:PRK04813   315 ---YKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF---DGQPAYHTGDAGY-LE 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1604 DGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVI-------VVAgarLAAFATPQPGASLDAAALKRA---- 1672
Cdd:PRK04813   388 DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVpynkdhkVQY---LIAYVVPKEEDFEREFELTKAikke 464
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1888712850 1673 LAALLPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:PRK04813   465 LKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
730-1169 3.37e-64

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 225.80  E-value: 3.37e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  730 ISHAQQRQLFAWRL--DPAsrAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYApRTEAAAPLAW 807
Cdd:cd19532      4 MSFGQSRFWFLQQYleDPT--TFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPMQ-GVLASSPLRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  808 AHVDLSDLGDIDEHdreralrecAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYR 887
Cdd:cd19532     81 EHVQISDEAEVEEE---------FERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  888 aalDGATTHGEAQakaktritYADYAAWQRRWLASDAAARQLAYWRAALADDAPPL-ALPYDHTATDTASENADpraAAR 966
Cdd:cd19532    152 ---GQPLLPPPLQ--------YLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLpLLPFAKVKSRPPLTRYD---THT 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  967 VAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEAAT 1046
Cdd:cd19532    218 AERRLDAALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQ 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1047 PLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDyPALARWPGARAERVEIaeTHVKVP-- 1124
Cdd:cd19532    298 TFADVLKETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGV-AESRPFGDCELEGEEF--EDARTPyd 374
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1888712850 1125 LALDLRESRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAFAH 1169
Cdd:cd19532    375 LSLDIIDNPDGDCLLTLKVQSSLYSEEDAELLLDSYVNLLEAFAR 419
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
730-1161 8.50e-64

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 224.83  E-value: 8.50e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  730 ISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVEtGDAAHLYAPRTEAAAPLAWah 809
Cdd:cd20483      4 MSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFE-GDDFGEQQVLDDPSFHLIV-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  810 VDLSDlgdidEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAA 889
Cdd:cd20483     81 IDLSE-----AADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDAL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  890 LDGATTHGEAQAkaktRITYADYAAWQRRWLASDAAARQLAYWRAALAD--DAPPLaLPYdhtATDTASENADPrAAARV 967
Cdd:cd20483    156 RAGRDLATVPPP----PVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGipDASKL-LPF---AKAERPPVKDY-ERSTV 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  968 AFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEAATP 1047
Cdd:cd20483    227 EATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMS 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1048 LASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDdypalARWPGARAERVEIAET-HVKVP-- 1124
Cdd:cd20483    307 FDDLLESTKTTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQVH-----GKFPEYDTGDFKFTDYdHYDIPta 381
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1888712850 1125 --LALDLRESRDGSMRAYFTYASARFDAASVERMAAQYL 1161
Cdd:cd20483    382 cdIALEAEEDPDGGLDLRLEFSTTLYDSADMERFLDNFV 420
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
23-588 4.95e-60

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 215.12  E-value: 4.95e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAA-ERALILMDSGVDYVSAFFGCLYAGVVA 101
Cdd:cd05936      1 LADLLEEAARRFPDKTALI----FMGRKLTYRELDALAEAFAAGLQNLGVQPgDRVALMLPNCPQFPIAYFGALKAGAVV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  102 VPVYPPESKREqhlarLRGIARDAGVRYVlttaalherhadawsmlapgadVVAVDTLDARDTPSDAPLHPVR-ADDLAF 180
Cdd:cd05936     77 VPLNPLYTPRE-----LEHILNDSGAKAL----------------------IVAVSFTDLLAAGAPLGERVALtPEDVAV 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  181 LQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGV--RPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMsPQYfleRP 258
Cdd:cd05936    130 LQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDllEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLI-PRF---RP 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  259 LRWLDAIARHRGTI-SGAPDfayrLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFapagfdAAALYPCYG 337
Cdd:cd05936    206 IGVLKEIRKHRVTIfPGVPT----MYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT------GVPIVEGYG 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  338 LAEATLFVTG----GVRGAGLVSHAFSsaalsagraeaaradeaatvlvgcgavqaghrvaivaraaaeSHESHEADVET 413
Cdd:cd05936    276 LTETSPVVAVnpldGPRKPGSIGIPLP------------------------------------------GTEVKIVDDDG 313
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  414 ETsragerLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFV-HDGQLYIAGRVKDLVI 492
Cdd:cd05936    314 EE------LPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG-----------WLRTGDIGYMdEDGYFFIVDRKKDMII 376
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  493 VRGRNLYPQDVEQAVEAH---AEFA-------RKG-RVIAFgATLGGGETLGLAlEIAPRMKKRFAAAQIvetlrriafd 561
Cdd:cd05936    377 VGGFNVYPREVEEVLYEHpavAEAAvvgvpdpYSGeAVKAF-VVLKEGASLTEE-EIIAFCREQLAGYKV---------- 444
                          570       580
                   ....*....|....*....|....*..
gi 1888712850  562 acgetPAAIALLNpgALPKTSSGKLQR 588
Cdd:cd05936    445 -----PRQVEFRD--ELPKSAVGKILR 464
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
1845-2291 2.95e-59

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 211.29  E-value: 2.95e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1845 LPLSLMQQRIwVVDQLADRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDEGDPVLKIAPRMEVLMP 1924
Cdd:cd19543      2 YPLSPMQEGM-LFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1925 VIEPlahpdndanshtnSHTNSDEnaRTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVH 2004
Cdd:cd19543     81 ELDL-------------SHLSEAE--QEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLP 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2005 ILLDELCELYRAQRDGAPPALAPlAVQYADYAHWQRARftpDAvREAQQFWRGYLADAPALLPLSTDRARPTRVSHAGAA 2084
Cdd:cd19543    146 ILLKELFAIYAALGEGQPPSLPP-VRPYRDYIAWLQRQ---DK-EAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGE 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2085 RHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRErAEL---EALIGFFVNVVPLRSRIA 2161
Cdd:cd19543    221 VSFELSAELTARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRP-AELpgiETMVGLFINTLPVRVRLD 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2162 ADganlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRrrdanPLVQVLFVLRDLPRGNTRVP-----GLAVELLR 2236
Cdd:cd19543    300 PD----QTVLELLKDLQAQQLELREHEYVPLYEIQAWSEGKQ-----ALFDHLLVFENYPVDESLEEeqdedGLRITDVS 370
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850 2237 pPTTQSKFDMALFVeAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19543    371 -AEEQTNYPLTVVA-IPGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
177-587 8.05e-59

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 207.14  E-value: 8.05e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  177 DLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHdMGLIGSLLQPVFSGIPLVLMSPQyfle 256
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFH-IGGLFGLLGALLAGGTVVLLPKF---- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  257 RPLRWLDAIARHRGTISGAPDFAYRLCAERINdetRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPagfdaaALYPCY 336
Cdd:cd04433     76 DPEAALELIEREKVTILLGVPTLLARLLKAPE---SAGYDLSSLRALVSGGAPLPPELLERFEEAPGI------KLVNGY 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  337 GLAEATLFVTGGVRGAGlvshafSSAALSAGRAEaaradeaatvlvgcgavqaghrvaivaraaaeshesheADVETE-T 415
Cdd:cd04433    147 GLTETGGTVATGPPDDD------ARKPGSVGRPV--------------------------------------PGVEVRiV 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  416 SRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDaprhadgsgpaRWLRTGDLGFVH-DGQLYIAGRVKDLVIVR 494
Cdd:cd04433    183 DPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-----------GWYRTGDLGRLDeDGYLYIVGRLKDMIKSG 251
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  495 GRNLYPQDVEQAVEAHAEFArkgRVIAFGATLG-GGETLGLAleIAPRMKKRFAAAQIVETLR-RIAFDAcgeTPAAIAL 572
Cdd:cd04433    252 GENVYPAEVEAVLLGHPGVA---EAAVVGVPDPeWGERVVAV--VVLRPGADLDAEELRAHVReRLAPYK---VPRRVVF 323
                          410
                   ....*....|....*
gi 1888712850  573 LNpgALPKTSSGKLQ 587
Cdd:cd04433    324 VD--ALPRTASGKID 336
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
1361-1701 1.01e-58

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 206.75  E-value: 1.01e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1361 AYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDttlDADR 1440
Cdd:cd04433      3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DPEA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1441 FAQTLAAARIDVLKIVPGHLHALLQAERAADA-LPA-HTLVLGGEATSWELLDTIAAlRPDCRVHNHYGPTETTVGILTQ 1518
Cdd:cd04433     80 ALELIEREKVTILLGVPTLLARLLKAPESAGYdLSSlRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTETGGTVATG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1519 PAAQACRAAATLplGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFvphpfaaGARLYRSGDR 1598
Cdd:cd04433    159 PPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDL 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1599 ARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQPGASLDAAALKRALA 1674
Cdd:cd04433    230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVpdpeWGERVVAVVVLRPGADLDAEELRAHVR 309
                          330       340
                   ....*....|....*....|....*..
gi 1888712850 1675 ALLPDYMVPSVLRVIDALPLNRNGKLD 1701
Cdd:cd04433    310 ERLAPYKVPRRVVFVDALPRTASGKID 336
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
731-1168 1.42e-58

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 209.37  E-value: 1.42e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  731 SHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYAPRTEAaaPLAWAHV 810
Cdd:cd19543      5 SPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDR--KLPWREL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  811 DLSDLgdiDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAAL 890
Cdd:cd19543     83 DLSHL---SEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  891 DGATTHGEAQAkaktriTYADYAAW-QRRwlasDAAArQLAYWRAALA--DDAPPLalpydhtATDTASENADPRAAARV 967
Cdd:cd19543    160 EGQPPSLPPVR------PYRDYIAWlQRQ----DKEA-AEAYWREYLAgfEEPTPL-------PKELPADADGSYEPGEV 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  968 AFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANR--TRPETHDVIGFFVNTLVLHSDCEAA 1045
Cdd:cd19543    222 SFELSAELTARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRpaELPGIETMVGLFINTLPVRVRLDPD 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1046 TPLASLFSQLRQRTLDAQANQALPfdvLVEhLRpARDAQHGPLFETSF---NYLSDDYPALARWPGARAERVEIAETHVK 1122
Cdd:cd19543    302 QTVLELLKDLQAQQLELREHEYVP---LYE-IQ-AWSEGKQALFDHLLvfeNYPVDESLEEEQDEDGLRITDVSAEEQTN 376
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1888712850 1123 VPLAldLRESRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAFA 1168
Cdd:cd19543    377 YPLT--VVAIPGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVA 420
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
742-1166 2.37e-58

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 209.09  E-value: 2.37e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  742 RLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLyapRTEAAAPLAWAHVDLSDL--GDID 819
Cdd:cd20484     16 KMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQ---KIEPSKPLSFQEEDISSLkeSEII 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  820 EHDRERAlREcaqrfadaPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAALDGAT-THGE 898
Cdd:cd20484     93 AYLREKA-KE--------PFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQpTLAS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  899 AQAkaktriTYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHtatdtasenadPRAAARvAFA-------L 971
Cdd:cd20484    164 SPA------SYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADR-----------PRSSAP-SFEgqtytrrL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  972 PAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVAnrTRPETH--DVIGFFVNTLVLHSDCEAATPLA 1049
Cdd:cd20484    226 PSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTM--GRPEERfdSLIGYFINMLPIRSRILGEETFS 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1050 SLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSF---NYL-SDDYPA-LARWPGARA-ERVEIAETHVKV 1123
Cdd:cd20484    304 DFIRKLQLTVLDGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFfyqNFLqSTSLQQfLAEYQDVLSiEFVEGIHQEGEY 383
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1888712850 1124 PLALDLRESRDGsMRAYFTYASARFDAASVERMAAQYLRAVEA 1166
Cdd:cd20484    384 ELVLEVYEQEDR-FTLNIKYNPDLFDASTIERMMEHYVKLAEE 425
PRK12316 PRK12316
peptide synthase; Provisional
31-1190 6.00e-56

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 217.13  E-value: 6.00e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALividADGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVPVYPpes 109
Cdd:PRK12316  3067 VERTPDAVAL----AFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVgVAVERSLEMVVGLLAILKAGGAYVPLDP--- 3139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  110 krEQHLARLRGIARDAGVRYVLTTAALHERHADawsmlapGADVVAVDTlDARDTPSDAPLHPVRADDLAFLQYTSGSTG 189
Cdd:PRK12316  3140 --EYPEERLAYMLEDSGAQLLLSQSHLRLPLAQ-------GVQVLDLDR-GDENYAEANPAIRTMPENLAYVIYTSGSTG 3209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  190 SPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDmGLIGSLLQPVFSGIPLVLMSPQYFLERPLrwldAIARHR 269
Cdd:PRK12316  3210 KPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFD-VFVEELFWPLMSGARVVLAGPEDWRDPAL----LVELIN 3284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  270 GTISGAPDFAYRLCAERINDETRAklDLSSWRLAFSGSEPVRRDTLDDFVARfapagfdaAALYPCYGLAEATLFVTGGV 349
Cdd:PRK12316  3285 SEGVDVLHAYPSMLQAFLEEEDAH--RCTSLKRIVCGGEALPADLQQQVFAG--------LPLYNLYGPTEATITVTHWQ 3354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  350 RGAGLVSHAFSSAALSAGRAEAARAdeaatvlvgcgavqaghrvaivaraaaeshesheadvetetsrAGERLADGRIGE 429
Cdd:PRK12316  3355 CVEEGKDAVPIGRPIANRACYILDG-------------------------------------------SLEPVPVGALGE 3391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  430 IHVSGPSVAHGYWQRADASAQAFVDAPRHADGsgpaRWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVE 508
Cdd:PRK12316  3392 LYLGGEGLARGYHNRPGLTAERFVPDPFVPGE----RLYRTGDLArYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLL 3467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  509 AHAEFARKGRVIAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLrriafdacgeTPAAIALLNpgALPKTSSGKLQR 588
Cdd:PRK12316  3468 EHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYM----------VPAHLLFLE--RMPLTPNGKLDR 3535
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  589 AAtregwrartldlyalweqgafvIGGDDDAARAPDAPAALDARESALAALWCEALD-ARLALAPdaHFFASGGSSLSAA 667
Cdd:PRK12316  3536 KA----------------------LPRPDAALLQQDYVAPVNELERRLAAIWADVLKlEQVGLTD--NFFELGGDSIISL 3591
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  668 RLVALigAR-LGRRVALAQIFETPTLAAMAAALAepesVEEAQDDAQDEAQDNAPIEPA-----EEAVishAQQRQLFAW 741
Cdd:PRK12316  3592 QVVSR--ARqAGIRFTPKDLFQHQTIQGLARVAR----VGGGVAVDQGPVSGETLLLPIqqqffEEPV---PERHHWNQS 3662
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  742 RLdpasrayhvaagIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYAPRTEAAAPLAWAhvdlsdlGDIDEH 821
Cdd:PRK12316  3663 LL------------LKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWR-------AELDDA 3723
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  822 DRERALRECAQRfadaPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAALDGATTHgeaqA 901
Cdd:PRK12316  3724 EELERLGEEAQR----SLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPR----L 3795
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  902 KAKTrITYADYAAWQRRWLASDAAARQLAYWRAALADdaPPLALPYDHTATDTASenadpRAAARVAFALPAPLA-QAVR 980
Cdd:PRK12316  3796 PAKT-SSFKAWAERLQEHARGEALKAELAYWQEQLQG--VSSELPCDHPQGALQN-----RHAASVQTRLDRELTrRLLQ 3867
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  981 ASAARHRATPFVVLLAAYHAWLYRVTGQRAirTGVPVANRTRPETHDVI------GFFVNTLVLHSdCEAATPLASLFSQ 1054
Cdd:PRK12316  3868 QAPAAYRTQVNDLLLTALARVVCRWTGEAS--ALVQLEGHGREDLFADIdlsrtvGWFTSLFPVRL-SPVEDLGASIKAI 3944
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1055 LRQrtLDAQANQALPFDVL-VEHLRPARDAQHG-PLFETSFNYLS------DDYPALARWPGARAERVEIAETHVKVPLA 1126
Cdd:PRK12316  3945 KEQ--LRAIPNKGIGFGLLrYLGDEESRRTLAGlPVPRITFNYLGqfdgsfDEEMALFVPAGESAGAEQSPDAPLDNWLS 4022
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850 1127 LDLReSRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAF-AHALGDRSADMTDAAAPtLATLD 1190
Cdd:PRK12316  4023 LNGR-VYGGELSLDWTFSREMFEEATIQRLADDYAAELTALvEHCCDAERHGVTPSDFP-LAGLD 4085
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
23-985 1.36e-54

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 211.25  E-value: 1.36e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFFGCLYAGVVA 101
Cdd:COG1020    478 LHELFEAQAARTPDAVAVV----FGDQSLTYAELNARANRLAHHLRALGVGPGdLVGVCLERSLEMVVALLAVLKAGAAY 553
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  102 VPV---YPPEskreqhlaRLRGIARDAGVRYVLTTAALHERHADAwsmlapGADVVAVDTLDARDTPSDAPLHPVRADDL 178
Cdd:COG1020    554 VPLdpaYPAE--------RLAYMLEDAGARLVLTQSALAARLPEL------GVPVLALDALALAAEPATNPPVPVTPDDL 619
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  179 AFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGlIGSLLQPVFSGIPLVLMSPQYFLErP 258
Cdd:COG1020    620 AYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDAS-VWEIFGALLSGATLVLAPPEARRD-P 697
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  259 LRWLDAIARHRGTISGAPDFAYRLCAERINDetraklDLSSWRLAFSGSEPVRRDTLDDFVARFApagfdAAALYPCYGL 338
Cdd:COG1020    698 AALAELLARHRVTVLNLTPSLLRALLDAAPE------ALPSLRLVLVGGEALPPELVRRWRARLP-----GARLVNLYGP 766
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  339 AEATLFVTggvrgaglvshafssaalsagraeaaradeaatvlvgcgavqaghrvaivaraaaeSHESHEADVETETS-- 416
Cdd:COG1020    767 TETTVDST--------------------------------------------------------YYEVTPPDADGGSVpi 790
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  417 -------------RAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHADGsgpARWLRTGDLG-FVHDGQLY 482
Cdd:COG1020    791 grpiantrvyvldAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPG---ARLYRTGDLArWLPDGNLE 867
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  483 IAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFArkgRVIAFGATLGGGETLGLALEIAPRmkkrfAAAQIVETLRRIAFDA 562
Cdd:COG1020    868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVR---EAVVVAREDAPGDKRLVAYVVPEA-----GAAAAAALLRLALALL 939
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  563 CGETPAAIALLNPGALPKTSSGKLQRAATREGWRARTLDLYAlweqgafviggdddaarapdapaALDARESALAALWCE 642
Cdd:COG1020    940 LPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAA-----------------------PPAEEEEEEAALALL 996
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  643 ALDARLALAPDAHFFASGGSSLSAARLVALIGARLGRRVALAQIFETPTlaamaaalaePESVEEAQDDAQDEAQDNAPI 722
Cdd:COG1020    997 LLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAA----------AAAAAAAAAAAAAAAAPLAAA 1066
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  723 EPAEEAVISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYAPRTEAA 802
Cdd:COG1020   1067 AAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAA 1146
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  803 APLAWAHVDLSDLGDIDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEEL 882
Cdd:COG1020   1147 ALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAA 1226
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  883 VDGYRAALDGATTHGEAQAKAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHTATDTASENADPR 962
Cdd:COG1020   1227 AAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLL 1306
                          970       980
                   ....*....|....*....|...
gi 1888712850  963 AAARVAFALPAPLAQAVRASAAR 985
Cdd:COG1020   1307 LALALALLLLLLLLLALLLLALL 1329
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1846-2291 1.43e-54

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 197.92  E-value: 1.43e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIWVVdQLADRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDeGDPVLKIAPRmevlmpv 1925
Cdd:cd20484      3 PLSEGQKGLWML-QKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEED-GVPFQKIEPS------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1926 iEPLAHPDNDAnshtnSHTNSDEnartqaTAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVHI 2005
Cdd:cd20484     74 -KPLSFQEEDI-----SSLKESE------IIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLT 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2006 LLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADAPALLPLSTDRARPTRVSHAGAAR 2085
Cdd:cd20484    142 LIHSLLDAYQALLQGKQPTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTY 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2086 HFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNVVPLRSRIAADga 2165
Cdd:cd20484    222 TRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGE-- 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2166 nlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFV---------LRDLPRGNTrvPGLAVELLR 2236
Cdd:cd20484    300 --ETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFyqnflqstsLQQFLAEYQ--DVLSIEFVE 375
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850 2237 PPTTQSKFDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd20484    376 GIHQEGEYELVLEVYEQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
1215-1707 3.92e-54

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 199.24  E-value: 3.92e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1215 IHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALD 1294
Cdd:TIGR03098    2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1295 AGNPTQRLAQTLRDCGARLVL---------------CEDDCSALDLMGVQHARIDAAQEEAQR-EQHLRAPHALPAVD-- 1356
Cdd:TIGR03098   82 PLLKAEQVAHILADCNVRLLVtsserldllhpalpgCHDLRTLIIVGDPAHASEGHPGEEPASwPKLLALGDADPPHPvi 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1357 PRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTL 1436
Cdd:TIGR03098  162 DSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLPR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1437 DADRfaqTLAAARIDVLKIVP---GHLHALLQAERAADALpaHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTV 1513
Cdd:TIGR03098  242 DVLK---ALEKHGITGLAAVPplwAQLAQLDWPESAAPSL--RYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEAFR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1514 GILTQPAAQACRAAAtlpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHP-FAAGARL 1592
Cdd:TIGR03098  317 STYLPPEEVDRRPDS---IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpFPGELHL 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1593 YR----SGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASL 1664
Cdd:TIGR03098  394 PElavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPdptlGQAIVLVVTPPGGEEL 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1888712850 1665 DAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSA 1707
Cdd:TIGR03098  474 DRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1219-1729 5.91e-54

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 199.95  E-value: 5.91e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVI----DGALR-MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVAL 1293
Cdd:COG0365     15 LDRHAEGRGDKVALIwegeDGEERtLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1294 DAGNPTQRLAQTLRDCGARLVLCEDDCSALDLMGVQHARIDAAQEEAQREQHL-----------------------RAPH 1350
Cdd:COG0365     95 FPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVivvgrtgadvpmegdldwdellaAASA 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1351 ALPAV-----DPrsaAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLAR-LDPPPRARFAMVSTIGADLGHT-VLFGALAS 1423
Cdd:COG0365    175 EFEPEptdadDP---LFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTADIGWATGHSyIVYGPLLN 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1424 GGALHLID-RDTTLDADRFAQTLAAARIDVLKIVPGHLHALLqaeRAADALPAH-------TLVLGGEA---TSWE-LLD 1491
Cdd:COG0365    252 GATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALM---KAGDEPLKKydlsslrLLGSAGEPlnpEVWEwWYE 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1492 TIaalrpDCRVHNHYGPTETTVGILTQPaaqacraaATLPL-----GRPLDNNETWLLDEHLNPVGTGGTGELYLGGA-- 1564
Cdd:COG0365    329 AV-----GVPIVDGWGQTETGGIFISNL--------PGLPVkpgsmGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwp 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1565 GVALGYLHQPALTAARFvphpFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAV 1644
Cdd:COG0365    396 GMFRGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1645 IVVA----GARLAAFATPQPGASldaaalkralaallPD-----------------YMVPSVLRVIDALPLNRNGKLDRQ 1703
Cdd:COG0365    472 VGVPdeirGQVVKAFVVLKPGVE--------------PSdelakelqahvreelgpYAYPREIEFVDELPKTRSGKIMRR 537
                          570       580
                   ....*....|....*....|....*.
gi 1888712850 1704 ALsalarpaaphREAARAAPQGETET 1729
Cdd:COG0365    538 LL----------RKIAEGRPLGDTST 553
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
1219-1702 4.03e-52

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 190.90  E-value: 4.03e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNP 1298
Cdd:cd17631      1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1299 TQRLAQTLRDCGARLVLceDDcsaldlmgvqharidaaqeeaqreqhlraphalpavdprsAAYVIYTSGSSGAPKGVVI 1378
Cdd:cd17631     81 PPEVAYILADSGAKVLF--DD----------------------------------------LALLMYTSGTTGRPKGAML 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1379 AHGALTNYVDAVLARLDPPPRARFAMVstigADLGHTV-----LFGALASGGALHLIDRdttLDADRFAQTLAAARIDVL 1453
Cdd:cd17631    119 THRNLLWNAVNALAALDLGPDDVLLVV----APLFHIGglgvfTLPTLLRGGTVVILRK---FDPETVLDLIERHRVTSF 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1454 KIVPGHLHALLQAERAA--DALPAHTLVLGGEATSWELLDTIAALrpDCRVHNHYGPTETTVGILTQPAAQACRAAATLp 1531
Cdd:cd17631    192 FLVPTMIQALLQHPRFAttDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFLSPEDHRRKLGSA- 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1532 lGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlyRSGDRARRLADGSLEYLG 1611
Cdd:cd17631    269 -GRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVD 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1612 RIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLR 1687
Cdd:cd17631    341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPdekwGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVE 420
                          490
                   ....*....|....*
gi 1888712850 1688 VIDALPLNRNGKLDR 1702
Cdd:cd17631    421 FVDALPRNATGKILK 435
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
27-593 5.92e-50

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 186.93  E-value: 5.92e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   27 LRALAQQRPEATALividADGDTRYDYAQLDRRARALAARFARDGAAA-ER-ALILMDSGVdYVSAFFGCLYAGVVAVPV 104
Cdd:PRK06187    12 LRHGARKHPDKEAV----YFDGRRTTYAELDERVNRLANALRALGVKKgDRvAVFDWNSHE-YLEAYFAVPKIGAVLHPI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  105 ---YPPEskreqhlaRLRGIARDAGVRYVLTTAAL------------HERH---ADAWSMLAPGADVVAVDTLDArDTPS 166
Cdd:PRK06187    87 nirLKPE--------EIAYILNDAEDRVVLVDSEFvpllaailpqlpTVRTvivEGDGPAAPLAPEVGEYEELLA-AASD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  167 DAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLiGSLLQPVFSGIPL 246
Cdd:PRK06187   158 TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAW-GLPYLALMAGAKQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  247 VLmsPQYFLERPLrwLDAIARHRGTISGA-PDFAYRLcaerINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFApA 325
Cdd:PRK06187   237 VI--PRRFDPENL--LDLIETERVTFFFAvPTIWQML----LKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFG-I 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  326 GFDAAalypcYGLAEATLFVTGGVRGAGLVSHAfsSAALSAGraeaaradeaatvLVGCGavqaghrvaivaraaaeshe 405
Cdd:PRK06187   308 DLVQG-----YGMTETSPVVSVLPPEDQLPGQW--TKRRSAG-------------RPLPG-------------------- 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  406 sHEADVETEtsrAGERLA--DGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFVH-DGQLY 482
Cdd:PRK06187   348 -VEARIVDD---DGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG-----------WLHTGDVGYIDeDGYLY 412
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  483 IAGRVKDLVIVRGRNLYPQDVEQAVEAH---AEFARKG--------RVIAFgATLGGGETLGlALEIAPRMKKRFAAAQI 551
Cdd:PRK06187   413 ITDRIKDVIISGGENIYPRELEDALYGHpavAEVAVIGvpdekwgeRPVAV-VVLKPGATLD-AKELRAFLRGRLAKFKL 490
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1888712850  552 vetLRRIAF-DacgetpaaiallnpgALPKTSSGKLQRAATRE 593
Cdd:PRK06187   491 ---PKRIAFvD---------------ELPRTSVGKILKRVLRE 515
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
1845-2291 3.18e-49

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 182.68  E-value: 3.18e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1845 LPLSLMQQRIWVVDQLADRAlASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDAD-----------DEGDPVL 1913
Cdd:cd19546      5 VPATAGQLRTWLLARLDEET-RGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDggdvhqrildaDAARPEL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1914 KIAPRMEVLMPVIeplahpdndanshtnshtnsdenartqataqaLDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSL 1993
Cdd:cd19546     84 PVVPATEEELPAL--------------------------------LADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVV 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1994 HHIVADGGSVHILLDELCELYRAQRDGAPPALAPLAVQYADYAHWQRARF----TPDAVREAQ-QFWRGYLADAPALLPL 2068
Cdd:cd19546    132 HRIAADDESLDVLVRDLAAAYGARREGRAPERAPLPLQFADYALWERELLagedDRDSLIGDQiAYWRDALAGAPDELEL 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2069 STDRARPTRVSHAGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGR-ERAELEALI 2147
Cdd:cd19546    212 PTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDdEEGDLEGMV 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2148 GFFVNVVPLRSRIAADganlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLVQVLFVLRD---LPRGN 2224
Cdd:cd19546    292 GPFARPLALRTDLSGD----PTFRELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDddnDPWDA 367
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1888712850 2225 TRVPGLAVELLRPPTTQSKFDMALFV------EAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19546    368 PELPGLRTSPVPLGTEAMELDLSLALterrndDGDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
1845-2291 2.89e-48

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 179.10  E-value: 2.89e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1845 LPLSLMQQRIWVVDQLaDRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDaDDEGDPVLKIAPRMEVLMP 1924
Cdd:cd19533      2 LPLTSAQRGVWFAEQL-DPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFT-EEEGEPYQWIDPYTPVPIR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1925 VIEPLAHPDNDAnshtnshtnsdenartqATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVH 2004
Cdd:cd19533     80 HIDLSGDPDPEG-----------------AAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFA 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2005 ILLDELCELYRAQRDGAPPALAPLA---------VQYADYAHWQRARftpdavreaqQFWRGYLADAPALLPLSTdraRP 2075
Cdd:cd19533    143 LFGQRVAEIYTALLKGRPAPPAPFGsfldlveeeQAYRQSERFERDR----------AFWTEQFEDLPEPVSLAR---RA 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2076 TRVSHAGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGR-ERAELEALiGFFVNVV 2154
Cdd:cd19533    210 PGRSLAFLRRTAELPPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlGAAARQTP-GMVANTL 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2155 PLRSRIAADganlASFDAWLDAARQSTWDALDHRALPFDRIVDALAL--KRRRDANPLVQVLFVLRDLPRGNTRvpGLAV 2232
Cdd:cd19533    289 PLRLTVDPQ----QTFAELVAQVSRELRSLLRHQRYRYEDLRRDLGLtgELHPLFGPTVNYMPFDYGLDFGGVV--GLTH 362
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1888712850 2233 ELLRPPTTqskfDMALFVEAVD--GGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19533    363 NLSSGPTN----DLSIFVYDRDdeSGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
27-588 2.21e-47

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 177.03  E-value: 2.21e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   27 LRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVY 105
Cdd:cd17631      1 LRRRARRHPDRTALV----FGGRSLTYAELDERVNRLAHALRALGvAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  106 PpeskreqhlaRLRGiardAGVRYVLTTAalherhadawsmlapGADVVAvdtldardtpsdaplhpvraDDLAFLQYTS 185
Cdd:cd17631     77 F----------RLTP----PEVAYILADS---------------GAKVLF--------------------DDLALLMYTS 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  186 GSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMsPQYfleRPLRWLDAI 265
Cdd:cd17631    108 GTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVIL-RKF---DPETVLDLI 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  266 ARHRGT-ISGAPDFAYRLCAErindETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARfapagfdAAALYPCYGLAEATLF 344
Cdd:cd17631    184 ERHRVTsFFLVPTMIQALLQH----PRFATTDLSSLRAVIYGGAPMPERLLRALQAR-------GVKFVQGYGMTETSPG 252
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  345 VTggvrgaGLVSHAFSSAALSAGRAeaaradeaatvlvgcgavqaghrvaivaraaaesHESHEADVETEtsrAGERLAD 424
Cdd:cd17631    253 VT------FLSPEDHRRKLGSAGRP----------------------------------VFFVEVRIVDP---DGREVPP 289
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  425 GRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDV 503
Cdd:cd17631    290 GEVGEIVVRGPHVMAGYWNRPEATAAAFRDG-----------WFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEV 358
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  504 EQAVEAH---AEFARKG--------RVIAFgatlgggetlglaleIAPRMKKRFAAAQIVETLR-RIAFDACgetPAAIA 571
Cdd:cd17631    359 EDVLYEHpavAEVAVIGvpdekwgeAVVAV---------------VVPRPGAELDEDELIAHCReRLARYKI---PKSVE 420
                          570
                   ....*....|....*..
gi 1888712850  572 LLNpgALPKTSSGKLQR 588
Cdd:cd17631    421 FVD--ALPRNATGKILK 435
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
1844-2291 7.63e-47

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 174.94  E-value: 7.63e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1844 ALPLSLMQQRI---WVVDQLADRALASYNMTAGLDLRGPLdaarLQRSLAALIARHEVLRSAFDADDEGDPVLKIAPRME 1920
Cdd:cd19536      1 MYPLSSLQEGMlfhSLLNPGGSVYLHNYTYTVGRRLNLDL----LLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1921 VlmPVIEPLAHPDNDANSHTNSHTNSDEnartqataqalddaaRTPFDLSRAPLVRATLLRFDAAHH-VLIVSLHHIVAD 1999
Cdd:cd19536     77 V--PVTELDLTPLEEQLDPLRAYKEETK---------------IRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILD 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2000 GGSVHILLDELCELYRAQRDGAPPALAPlAVQYADYAHWQRARFTPDAvreAQQFWRGYLADA--PALLPLstdraRPTR 2077
Cdd:cd19536    140 GWSLYLLVKEILAVYNQLLEYKPLSLPP-AQPYRDFVAHERASIQQAA---SERYWREYLAGAtlATLPAL-----SEAV 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2078 VSHAGAARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGR--ERAELEALIGFFVNVVP 2155
Cdd:cd19536    211 GGGPEQDSELLVSVPLPVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRseETTGAERLLGLFLNTLP 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2156 LRSRiaadgANLASFDAWLDAARQSTWDALDHRALPfdrivdaLALKRRR-DANPLVQVLFVLRDLPRGNTRVPGLAVEL 2234
Cdd:cd19536    291 LRVT-----LSEETVEDLLKRAQEQELESLSHEQVP-------LADIQRCsEGEPLFDSIVNFRHFDLDFGLPEWGSDEG 358
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1888712850 2235 LRPPTTQSKF----DMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19536    359 MRRGLLFSEFksnyDVNLSVLPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
1218-1705 1.41e-46

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 176.63  E-value: 1.41e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1218 RVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALdagN 1297
Cdd:PRK07656    10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL---N 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 PT---QRLAQTLRDCGARLVLCEDDCSALD------LMGVQHARI------DAAQEEAQREQHLRAPHAL----PAVDPR 1358
Cdd:PRK07656    87 TRytaDEAAYILARGDAKALFVLGLFLGVDysattrLPALEHVVIceteedDPHTEKMKTFTDFLAAGDPaeraPEVDPD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1359 SAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTV-LFGALASGGALhLIDRdtTLD 1437
Cdd:PRK07656   167 DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAgVNAPLMRGATI-LPLP--VFD 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1438 ADRFAQTLAAARIDVLKIVPGHLHALLQAE-RAADALpaHTL---VLGGEATSWELLDTIAALRPDCRVHNHYGPTETT- 1512
Cdd:PRK07656   244 PDEVFRLIETERITVLPGPPTMYNSLLQHPdRSAEDL--SSLrlaVTGAASMPVALLERFESELGVDIVLTGYGLSEASg 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1513 VGILTQPAAQACRAAATlpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAarfvpHPFAAGARL 1592
Cdd:PRK07656   322 VTTFNRLDDDRKTVAGT--IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATA-----AAIDADGWL 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1593 YrSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGARLA----AFATPQPGASLDAAA 1668
Cdd:PRK07656   395 H-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGevgkAYVVLKPGAELTEEE 473
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1888712850 1669 LKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:PRK07656   474 LIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
PRK12467 PRK12467
peptide synthase; Provisional
14-1190 1.99e-46

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 185.75  E-value: 1.99e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   14 DTDAVPAHGLAARLRALAQQRPEATALIVidadGDTRYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFF 92
Cdd:PRK12467  1567 HTGYPLARLVHQLIEDQAAATPEAVALVF----GEQELTYGELNRRANRLAHRLIALGVGPEvLVGIAVERSLEMVVGLL 1642
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   93 GCLYAGVVAVPV---YPPEskreqhlaRLRGIARDAGVRYVLTTAALHERHAdawsmLAPGADVVAVDTLDA--RDTPSD 167
Cdd:PRK12467  1643 AILKAGGAYVPLdpeYPRE--------RLAYMIEDSGIELLLTQSHLQARLP-----LPDGLRSLVLDQEDDwlEGYSDS 1709
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  168 APLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGsLLQPVFSGIPLV 247
Cdd:PRK12467  1710 NPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWE-LFWPLINGARLV 1788
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  248 LMSPQYFLErPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAkldLSSWRLAFSGsEPVRRDTLDDFVARFAPAGf 327
Cdd:PRK12467  1789 IAPPGAHRD-PEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHP---LSLRRVVCGG-EALEVEALRPWLERLPDTG- 1862
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  328 daaaLYPCYGLAEATLFVTggvrgaglvshafssaalsagraeaaRADEAATVLVGCGAVQAGHRVaivaraaaeshesh 407
Cdd:PRK12467  1863 ----LFNLYGPTETAVDVT--------------------------HWTCRRKDLEGRDSVPIGQPI-------------- 1898
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  408 eADVETETSRAGERLAD-GRIGEIHVSGPSVAHGYWQRADASAQAFVDAPrhaDGSGPARWLRTGDLG-FVHDGQLYIAG 485
Cdd:PRK12467  1899 -ANLSTYILDASLNPVPiGVAGELYLGGVGLARGYLNRPALTAERFVADP---FGTVGSRLYRTGDLArYRADGVIEYLG 1974
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  486 RVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAFGAtlGGGETLGLALEIAPRMkkrFAAAQIVETLRRIAFDACGE 565
Cdd:PRK12467  1975 RIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGA--NGKQLVAYVVPTDPGL---VDDDEAQVALRAILKNHLKA 2049
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  566 T------PAAIALLnpGALPKTSSGKLQRAATREgwrartLDLYALweQGAFViggdddaarapdapAALDARESALAAL 639
Cdd:PRK12467  2050 SlpeymvPAHLVFL--ARMPLTPNGKLDRKALPA------PDASEL--QQAYV--------------APQSELEQRLAAI 2105
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  640 WCEALD-ARLALapDAHFFASGGSSLSAARLVAligarlgrRVALAQIFETPTLAAMAAALAEPESVEEAQDDA----QD 714
Cdd:PRK12467  2106 WQDVLGlEQVGL--HDNFFELGGDSIISIQVVS--------RARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTvsidQG 2175
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  715 EAQDNAPIEPAeeavishaqQRQLFAwrlDPASRAYHVAAGIRLD--GALDREALRQSLDRLCERHAALRTHFVETGDAA 792
Cdd:PRK12467  2176 PVTGDLPLLPI---------QQMFFA---DDIPERHHWNQSVLLEprEALDAELLEAALQALLVHHDALRLGFVQEDGGW 2243
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  793 H-LYAPRTEAAAPLAWAHVdlsdLGDIDEHdreRALRECAQRfadaPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATD 871
Cdd:PRK12467  2244 SaMHRAPEQERRPLLWQVV----VADKEEL---EALCEQAQR----SLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVD 2312
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  872 GWSMQLLVEELVDGYRAALDGATTHGEAQAKAktrityadYAAWQRR---WLASDAAARQLAYWRAALADdaPPLALPYD 948
Cdd:PRK12467  2313 GVSWRILLEDLQTAYRQLQGGQPVKLPAKTSA--------FKAWAERlqtYAASAALADELGYWQAQLQG--ASTELPCD 2382
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  949 HtatdtASENADPRAAARVAFALPAPLA-QAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAirTGVPVANRTRPETHD 1027
Cdd:PRK12467  2383 H-----PQGGLQRRHAASVTTHLDSEWTrRLLQEAPAAYRTQVNDLLLTALARVIARWTGQAS--TLIQLEGHGREDLFD 2455
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1028 VI------GFFVN--TLVLHSDCEAATPLASLFSQLRqrtldAQANQALPFDVLvEHLRPARDAQ---HGPLFETSFNYL 1096
Cdd:PRK12467  2456 EIdltrtvGWFTSlyPVKLSPTASLATSIKTIKEQLR-----AVPNKGLGFGVL-RYLGSEAARQtlqALPVPRITFNYL 2529
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1097 -------SDDYPALARWPGARAERVEIAETHVKVPLALDlRESRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAF-A 1168
Cdd:PRK12467  2530 gqfdgsfDAEKQALFVPSGEFSGAEQSEEAPLGNWLSIN-GQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALiE 2608
                         1210      1220
                   ....*....|....*....|..
gi 1888712850 1169 HALGDRSADMTDAAAPtLATLD 1190
Cdd:PRK12467  2609 HCCSNDQRGVTPSDFP-LAGLS 2629
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
730-1168 1.38e-44

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 168.32  E-value: 1.38e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  730 ISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVET-GDAAHLYAPRTEAAAPlawa 808
Cdd:cd19533      4 LTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEeGEPYQWIDPYTPVPIR---- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  809 HVDLSDlgdidEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRA 888
Cdd:cd19533     80 HIDLSG-----DPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  889 ALDGAtthgeaQAKAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALpydhtatdTASENADPRAAARVA 968
Cdd:cd19533    155 LLKGR------PAPPAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSL--------ARRAPGRSLAFLRRT 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  969 FALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEAATPL 1048
Cdd:cd19533    221 AELPPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTF 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1049 ASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQhgPLFETSFNYLSDDYPalARWPGARAerveIAETHVKVP---L 1125
Cdd:cd19533    301 AELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGELH--PLFGPTVNYMPFDYG--LDFGGVVG----LTHNLSSGPtndL 372
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1888712850 1126 ALDLRESRDGS-MRAYFTYASARFDAASVERMAAQYLRAVEAFA 1168
Cdd:cd19533    373 SIFVYDRDDESgLRIDFDANPALYSGEDLARHQERLLRLLEEAA 416
PRK12316 PRK12316
peptide synthase; Provisional
31-1190 1.41e-43

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 176.30  E-value: 1.41e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALividADGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVPVYPpes 109
Cdd:PRK12316   521 VERTPEAPAL----AFGEETLDYAELNRRANRLAHALIERGVGPDVLVgVAMERSIEMVVALLAILKAGGAYVPLDP--- 593
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  110 krEQHLARLRGIARDAGVRYVLttaalHERHADAWSMLAPGADVVAVDTLDA--RDTPSDAPLHPVRADDLAFLQYTSGS 187
Cdd:PRK12316   594 --EYPAERLAYMLEDSGVQLLL-----SQSHLGRKLPLAAGVQVLDLDRPAAwlEGYSEENPGTELNPENLAYVIYTSGS 666
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  188 TGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGlIGSLLQPVFSGIPLVLMSPQYFLErPLRWLDAIAR 267
Cdd:PRK12316   667 TGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGDHRD-PAKLVELINR 744
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  268 HR-GTISGAPDFAYRLcaerINDETRAklDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGfdaaaLYPCYGLAEATLFVT 346
Cdd:PRK12316   745 EGvDTLHFVPSMLQAF----LQDEDVA--SCTSLRRIVCSGEALPADAQEQVFAKLPQAG-----LYNLYGPTEAAIDVT 813
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  347 ggvrgaglvshafSSAALSAGRaeaaradeaatvlvgcGAVQAGHRVAIVARAAAEShesheadvetetsrAGERLADGR 426
Cdd:PRK12316   814 -------------HWTCVEEGG----------------DSVPIGRPIANLACYILDA--------------NLEPVPVGV 850
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  427 IGEIHVSGPSVAHGYWQRADASAQAFVDAPrHADGsgpARWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQ 505
Cdd:PRK12316   851 LGELYLAGRGLARGYHGRPGLTAERFVPSP-FVAG---ERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 926
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  506 AVEAHaEFARKGRVIAfgatLGGGETLGLALEIAPrmkkrfaAAQIVETLRRIAFDACGE--TPAAIALLNpgALPKTSS 583
Cdd:PRK12316   927 RLLEH-PWVREAAVLA----VDGKQLVGYVVLESE-------GGDWREALKAHLAASLPEymVPAQWLALE--RLPLTPN 992
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  584 GKLQRAATREgwrartldLYALWEQGAFViggdddaarapdapAALDARESALAALWCEALDA-RLALapDAHFFASGGS 662
Cdd:PRK12316   993 GKLDRKALPA--------PEASVAQQGYV--------------APRNALERTLAAIWQDVLGVeRVGL--DDNFFELGGD 1048
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  663 SLSAARLVAligarlgrRVALAQIFETPtlaamaAALAEPESVEEAQDDAQDEAQDNAPIEPAEEAVISHAQQRQLFAWR 742
Cdd:PRK12316  1049 SIVSIQVVS--------RARQAGIQLSP------RDLFQHQTIRSLALVAKAGQATAADQGPASGEVALAPVQRWFFEQA 1114
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  743 LdPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAH-LYAPRtEAAAPLaWAhvdlSDLGDIDEh 821
Cdd:PRK12316  1115 I-PQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQqAYAAP-QAGEVL-WQ----RQAASEEE- 1186
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  822 drERALRECAQRfadaPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAALdgatthgeAQA 901
Cdd:PRK12316  1187 --LLALCEEAQR----SLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLD--------ADL 1252
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  902 KAKTrityADYAAWQRRWLA-SDAAARQLAYWRAALADdaPPLALPYDHtaTDTASENadpRAAARVAFALPAPLA-QAV 979
Cdd:PRK12316  1253 PART----SSYQAWARRLHEhAGARAEELDYWQAQLED--APHELPCEN--PDGALEN---RHERKLELRLDAERTrQLL 1321
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  980 RASAARHRATPFVVLLAAYHAWLYRVTGQRAIRtgVPVANRTRPETHDVI------GFFVN--TLVLHSDCEAATPLASL 1051
Cdd:PRK12316  1322 QEAPAAYRTQVNDLLLTALARVTCRWSGQASVL--VQLEGHGREDLFEDIdlsrtvGWFTSlfPVRLTPAADLGESIKAI 1399
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1052 FSQLRqrtldAQANQALPFDVL----VEHLRPARDAQHGPlfETSFNYL-----SDDYPAL---ARWPGARAERVEiaet 1119
Cdd:PRK12316  1400 KEQLR-----AVPDKGIGYGLLrylaGEEAAARLAALPQP--RITFNYLgqfdrQFDEAALfvpATESAGAAQDPC---- 1468
                         1130      1140      1150      1160      1170      1180      1190
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850 1120 hvkVPLALDLR---ESRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAF-AHALGDRSADMTDAAAPtLATLD 1190
Cdd:PRK12316  1469 ---APLANWLSiegQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALiEHCCDERNRGVTPSDFP-LAGLS 1539
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
31-514 1.52e-43

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 167.80  E-value: 1.52e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIviDADGDTRYDYAQLDRRARALAarfardGAAAER-------ALILMDSGVDYVSAFFGCLYAGVVAVP 103
Cdd:cd05904     15 ASAHPSRPALI--DAATGRALTYAELERRVRRLA------AGLAKRggrkgdvVLLLSPNSIEFPVAFLAVLSLGAVVTT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  104 VYPPESKREqhLARLrgiARDAGVRYVLTTAALHERHADAWS--MLAPGADVV--AVDTLDARDTPSDAPLHPVRADDLA 179
Cdd:cd05904     87 ANPLSTPAE--IAKQ---VKDSGAKLAFTTAELAEKLASLALpvVLLDSAEFDslSFSDLLFEADEAEPPVVVIKQDDVA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  180 FLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLG--VRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMsPQYFLEr 257
Cdd:cd05904    162 ALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVM-PRFDLE- 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  258 plRWLDAIARHRGTI-SGAPDFAYRLCAERINDetraKLDLSSWRLAFSGSEPVRRDTLDDFVARFApagfdAAALYPCY 336
Cdd:cd05904    240 --ELLAAIERYKVTHlPVVPPIVLALVKSPIVD----KYDLSSLRQIMSGAAPLGKELIEAFRAKFP-----NVDLGQGY 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  337 GLAEATLFVTGGVRGAGLVSHAFSSAALSAGRaeaaradeaatvlvgcgavqaghrvaivaraaaesheshEAD-VETET 415
Cdd:cd05904    309 GMTESTGVVAMCFAPEKDRAKYGSVGRLVPNV---------------------------------------EAKiVDPET 349
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  416 sraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDaprhaDGsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVR 494
Cdd:cd05904    350 ---GESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK-----EG-----WLHTGDLCYIdEDGYLFIVDRLKELIKYK 416
                          490       500
                   ....*....|....*....|
gi 1888712850  495 GRNLYPQDVEQAVEAHAEFA 514
Cdd:cd05904    417 GFQVAPAELEALLLSHPEIL 436
PRK05691 PRK05691
peptide synthase; Validated
21-1190 1.53e-43

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 176.13  E-value: 1.53e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   21 HGLAArlrALAQQRPEATALIVidaDGDTrYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFFGCLYAGV 99
Cdd:PRK05691  2191 HGLFA---AQAARTPQAPALTF---AGQT-LSYAELDARANRLARALRERGVGPQvRVGLALERSLEMVVGLLAILKAGG 2263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  100 VAVPVYPpeskrEQHLARLRGIARDAGVRYVLTTAALHErhadAWSMLAPG-ADVVAVDTLDARDTPSDAPLHPVR-ADD 177
Cdd:PRK05691  2264 AYVPLDP-----EYPLERLHYMIEDSGIGLLLSDRALFE----ALGELPAGvARWCLEDDAAALAAYSDAPLPFLSlPQH 2334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  178 LAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGlIGSLLQPVFSGIPLVLMSPQYFLER 257
Cdd:PRK05691  2335 QAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAA-SERLLVPLLCGARVVLRAQGQWGAE 2413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  258 PLRWLdaIARHRGTISG-APDFAYRLCAERINDETRakldlSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAalypcY 336
Cdd:PRK05691  2414 EICQL--IREQQVSILGfTPSYGSQLAQWLAGQGEQ-----LPVRMCITGGEALTGEHLQRIRQAFAPQLFFNA-----Y 2481
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  337 GLAEATLFvtggvrgaglvshafSSAALSAgraeaaradeaATVLVGCGAVQAGHRVAIVARAAAEshesheADVETets 416
Cdd:PRK05691  2482 GPTETVVM---------------PLACLAP-----------EQLEEGAASVPIGRVVGARVAYILD------ADLAL--- 2526
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  417 ragerLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHADGsgpARWLRTGDLGFVH-DGQLYIAGRVKDLVIVRG 495
Cdd:PRK05691  2527 -----VPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADG---GRLYRTGDLVRLRaDGLVEYVGRIDHQVKIRG 2598
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  496 RNLYPQDVEQAVEAHAEfARKGRVIAFGATlGGGETLG-LALEIAPRMKKrfAAAQIVETLRRIAFDACGE--TPAAIAL 572
Cdd:PRK05691  2599 FRIELGEIESRLLEHPA-VREAVVLALDTP-SGKQLAGyLVSAVAGQDDE--AQAALREALKAHLKQQLPDymVPAHLIL 2674
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  573 LnpGALPKTSSGKLQR--------AATREGWRARTLDLyalweqgafviggdddaarapdapaaldarESALAALWCEAL 644
Cdd:PRK05691  2675 L--DSLPLTANGKLDRralpapdpELNRQAYQAPRSEL------------------------------EQQLAQIWREVL 2722
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  645 D-ARLALapDAHFFASGGSSLSAARLVALigAR-LGRRVALAQIFETPTLAAMAAALAEPESVEeaqdDAQDEAQDNAPI 722
Cdd:PRK05691  2723 NvERVGL--GDNFFELGGDSILSIQVVSR--ARqLGIHFSPRDLFQHQTVQTLAAVATHSEAAQ----AEQGPLQGASGL 2794
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  723 EPaeeavISHaqqrqlfaWRLD-PASRAYHVAAGIRLD--GALDREALRQSLDRLCERHAALRTHFVETgDAAHLYAPRT 799
Cdd:PRK05691  2795 TP-----IQH--------WFFDsPVPQPQHWNQALLLEprQALDPALLEQALQALVEHHDALRLRFSQA-DGRWQAEYRA 2860
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  800 EAAAPLAWaHVDLSDLGDidehdreralreCAQRFADA--PFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQL 877
Cdd:PRK05691  2861 VTAQELLW-QVTVADFAE------------CAALFADAqrSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRV 2927
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  878 LVEELVDGYRAALDGATTHGEAQAKAktritYADYAAWQRRWLASDAAARQLAYWRAALAddAPPLALPYDHTATDTASe 957
Cdd:PRK05691  2928 LLEDLQALYRQLSAGAEPALPAKTSA-----FRDWAARLQAYAGSESLREELGWWQAQLG--GPRAELPCDRPQGGNLN- 2999
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  958 nadpRAAARVAFALPAPLAQAV--RASAArHRATPFVVLLAAYHAWLYRVTGQRAirTGVPVANRTRPETHDVI------ 1029
Cdd:PRK05691  3000 ----RHAQTVSVRLDAERTRQLlqQAPAA-YRTQVNDLLLTALARVLCRWSGQPS--VLVQLEGHGREALFDDIdltrsv 3072
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1030 GFFVNTLVLH------SDCEAATPLASLFSQLRQrtldaQANQALPFDVLVEHLRPARDAQHG--PLFETSFNYL----- 1096
Cdd:PRK05691  3073 GWFTSAYPLRltpapgDDAARGESIKAIKEQLRA-----VPHKGLGYGVLRYLADAAVREAMAalPQAPITFNYLgqfdq 3147
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1097 SDDYPALARWPGARAERVEIAETHVKVPLALDlRESRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAF-AHALGDRS 1175
Cdd:PRK05691  3148 SFASDALFRPLDEPAGPAHDPDAPLPNELSVD-GQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALiAHCLADGA 3226
                         1210
                   ....*....|....*
gi 1888712850 1176 ADMTDAAAPtLATLD 1190
Cdd:PRK05691  3227 GGLTPSDFP-LAQLT 3240
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
1239-1700 7.51e-42

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 162.00  E-value: 7.51e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1239 MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCED 1318
Cdd:cd05911     11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1319 DC-----SALDLMGVQhARI---DAAQEEAQREQHLRAP------HALPAVDPRSA---AYVIYTSGSSGAPKGVVIAHG 1381
Cdd:cd05911     91 DGlekvkEAAKELGPK-DKIivlDDKPDGVLSIEDLLSPtlgeedEDLPPPLKDGKddtAAILYSSGTTGLPKGVCLSHR 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1382 ALTNYVDAVLARLDP--PPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDttlDADRFAQTLAAARIDVLKIVPGH 1459
Cdd:cd05911    170 NLIANLSQVQTFLYGndGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKF---DSELFLDLIEKYKITFLYLVPPI 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1460 LHALLQAER--AADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRAAatlpLGRPLD 1537
Cdd:cd05911    247 AAALAKSPLldKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGS----VGRLLP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1538 NNETWLLDEHLNP-VGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlYRSGDRARRLADGSLEYLGRIDDQ 1616
Cdd:cd05911    323 NVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYLYIVDRKKEL 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1617 VKIRGYRVEPGEIAARLKALDGVRDAAVI----VVAGARLAAFATPQPGASLDAAALKralaallpDYMVPSV-----LR 1687
Cdd:cd05911    397 IKYKGFQVAPAELEAVLLEHPGVADAAVIgipdEVSGELPRAYVVRKPGEKLTEKEVK--------DYVAKKVasykqLR 468
                          490
                   ....*....|....*..
gi 1888712850 1688 ----VIDALPLNRNGKL 1700
Cdd:cd05911    469 ggvvFVDEIPKSASGKI 485
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1246-1705 1.21e-41

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 160.68  E-value: 1.21e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1246 ARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGA----YVALDAGNPTQRLAQTLRDCGARLVLCEDDCS 1321
Cdd:cd05922      1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1322 ALDLMGVQHARIDAAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRAR 1401
Cdd:cd05922     81 DRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1402 FAMVSTIGADLGHTVLFGALASGGALhLIDRDTTLDADrFAQTLAAARIDVLKIVPGHLHALLQAERAADALPA-HTLVL 1480
Cdd:cd05922    161 ALTVLPLSYDYGLSVLNTHLLRGATL-VLTNDGVLDDA-FWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSlRYLTQ 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1481 GGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRAAATLplGRPLDNNETWLLDEHLNPVGTGGTGELY 1560
Cdd:cd05922    239 AGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSI--GLAIPGGEFEILDDDGTPTPPGEPGEIV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1561 LGGAGVALGYLHQPAltaarFVPHPFAAGARLYrSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVR 1640
Cdd:cd05922    317 HRGPNVMKGYWNDPP-----YRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLII 390
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1888712850 1641 DAAVIVV---AGARLAAFATPQPGASldAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:cd05922    391 EAAAVGLpdpLGEKLALFVTAPDKID--PKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
1230-1705 1.29e-41

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 162.30  E-value: 1.29e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1230 PAVIDGALR-MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRlaQTLRD 1308
Cdd:cd17647     11 PSLNSSKTRsFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR--QNIYL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1309 CGARlvlceddcsALDLMGVQHARIdaaqeeaqreqhlraphalpAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVD 1388
Cdd:cd17647     89 GVAK---------PRGLIVIRAAGV--------------------VVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFP 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1389 AVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGhLHALLQAER 1468
Cdd:cd17647    140 WMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPA-MGQLLTAQA 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1469 AADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETT-------VGILTQPAAQACRAAATLPLGRPLDNNET 1541
Cdd:cd17647    219 TTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQravsyfeVPSRSSDPTFLKNLKDVMPAGRGMLNVQL 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1542 WLLDEH--LNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPH--------------------PFAAGAR--LYRSGD 1597
Cdd:cd17647    299 LVVNRNdrTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnepwrQFWLGPRdrLYRTGD 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1598 RARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGAR----LAAFATPQPGASLDAAALKRAL 1673
Cdd:cd17647    379 LGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDeeptLVSYIVPRFDKPDDESFAQEDV 458
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850 1674 AALL---------------------------PDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:cd17647    459 PKEVstdpivkgligyrklikdireflkkrlASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
1219-1705 3.37e-41

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 161.12  E-value: 3.37e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNP 1298
Cdd:PRK06187    12 LRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLK 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1299 TQRLAQTLRDCGARLVLCEDD-----CSALDLMGVQHARI-------DAAQEEAQREQHLRAPHA----LPAVDPRSAAY 1362
Cdd:PRK06187    92 PEEIAYILNDAEDRVVLVDSEfvpllAAILPQLPTVRTVIvegdgpaAPLAPEVGEYEELLAAASdtfdFPDIDENDAAA 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1363 VIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFaMVST----IGAdLGHTVLfgALASGGALHLIDRdttLDA 1438
Cdd:PRK06187   172 MLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVY-LVIVpmfhVHA-WGLPYL--ALMAGAKQVIPRR---FDP 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1439 DRFAQTLAAARIDVLKIVPGHLHALLQAERA--ADALPAHTLVLGGEATSWELLDTIAAlRPDCRVHNHYGPTETTvGIL 1516
Cdd:PRK06187   245 ENLLDLIETERVTFFFAVPTIWQMLLKAPRAyfVDFSSLRLVIYGGAALPPALLREFKE-KFGIDLVQGYGMTETS-PVV 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1517 T-QPAAQACRAAATLPL--GRPLDNNETWLLDEHLN--PVGTGGTGELYLGGAGVALGYLHQPALTAARFVphpfaAGar 1591
Cdd:PRK06187   323 SvLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGDelPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID-----GG-- 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1592 LYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAA 1667
Cdd:PRK06187   396 WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPdekwGERPVAVVVLKPGATLDAK 475
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1888712850 1668 ALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:PRK06187   476 ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
75-510 5.03e-41

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 157.81  E-value: 5.03e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPV---YPPEskreqhlaRLRGIARDAGVRYVLTTAALheRHADAWSMLAPGA 151
Cdd:TIGR01733   26 DRVAVLLERSAELVVAILAVLKAGAAYVPLdpaYPAE--------RLAFILEDAGARLLLTDSAL--ASRLAGLVLPVIL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  152 DVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMG 231
Cdd:TIGR01733   96 LDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDAS 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  232 LIgSLLQPVFSGIPLVLMSPQYFLERPLRWLDAIARHRGT-ISGAPDFAYRLCAERIndetrakLDLSSWRLAFSGSEPV 310
Cdd:TIGR01733  176 VE-EIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTvLNLTPSLLALLAAALP-------PALASLRLVILGGEAL 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  311 RRDTLDDFVARfapagFDAAALYPCYGLAEATLFVTggvrgaglvshafsSAALSAGRAEAARADEAATVLVGCGAVqag 390
Cdd:TIGR01733  248 TPALVDRWRAR-----GPGARLINLYGPTETTVWST--------------ATLVDPDDAPRESPVPIGRPLANTRLY--- 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  391 hrvaivaraaaeshesheadVETEtsrAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVdaPRHADGSGPARWLRT 470
Cdd:TIGR01733  306 --------------------VLDD---DLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFV--PDPFAGGDGARLYRT 360
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1888712850  471 GDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:TIGR01733  361 GDLVrYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRH 401
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
43-505 6.49e-41

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 159.30  E-value: 6.49e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   43 IDADGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKREqhLARLrgi 121
Cdd:cd05911      3 IDADTGKELTYAQLRTLSRRLAAGLRKLGlKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADE--LAHQ--- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  122 ARDAGVRYVLTTAALHERHADAWSMLAPGADVVAVDTLDARDTPSDAPLHPV--------------RADDLAFLQYTSGS 187
Cdd:cd05911     78 LKISKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTlgeededlppplkdGKDDTAAILYSSGT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  188 TGSPKGVMVSHGNLLANEIAIQAGLG--VRPDDVFVSWLPLYHDMGLIGSLLQPVFsGIPLVLMsPQYFLErplRWLDAI 265
Cdd:cd05911    158 TGLPKGVCLSHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIM-PKFDSE---LFLDLI 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  266 ARHRGTISG-APDFAYRLcaerINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAalypcYGLAEATLF 344
Cdd:cd05911    233 EKYKITFLYlVPPIAAAL----AKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQG-----YGMTETGGI 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  345 VT---GGVRGAGlvshafssaalSAGraeaaradeaaTVLVGCgavqaghrvaivaraaaesheshEADVETETSraGER 421
Cdd:cd05911    304 LTvnpDGDDKPG-----------SVG-----------RLLPNV-----------------------EAKIVDDDG--KDS 336
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  422 LADGRIGEIHVSGPSVAHGYWQRADASAQAFVDaprhaDGsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYP 500
Cdd:cd05911    337 LGPNEPGEICVRGPQVMKGYYNNPEATKETFDE-----DG-----WLHTGDIGYFdEDGYLYIVDRKKELIKYKGFQVAP 406

                   ....*
gi 1888712850  501 QDVEQ 505
Cdd:cd05911    407 AELEA 411
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
1227-1705 7.21e-41

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 158.88  E-value: 7.21e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALdagNPT---QRLA 1303
Cdd:cd05936     13 PDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL---NPLytpRELE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1304 QTLRDCGARLVLCeddcsaldLMGVQHARIDAAqeeaqreqhlrAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGAL 1383
Cdd:cd05936     90 HILNDSGAKALIV--------AVSFTDLLAAGA-----------PLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1384 TNYVDAVLARLDPPPRARFAMVSTIgaDLGHT-----VLFGALASGGALHLIDRdttLDADRFAQTLAAARIDVLKIVPG 1458
Cdd:cd05936    151 VANALQIKAWLEDLLEGDDVVLAAL--PLFHVfgltvALLLPLALGATIVLIPR---FRPIGVLKEIRKHRVTIFPGVPT 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1459 HLHALLQA-ERAADALPAHTLVL-GGEATSWELLDTIAAlRPDCRVHNHYGPTETT-VGILTQPAAQACRAAatlpLGRP 1535
Cdd:cd05936    226 MYIALLNApEFKKRDFSSLRLCIsGGAPLPVEVAERFEE-LTGVPIVEGYGLTETSpVVAVNPLDGPRKPGS----IGIP 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1536 LDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlyRSGDRARRLADGSLEYLGRIDD 1615
Cdd:cd05936    301 LPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVDRKKD 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1616 QVKIRGYRVEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDA 1691
Cdd:cd05936    374 MIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdpySGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDE 453
                          490
                   ....*....|....
gi 1888712850 1692 LPLNRNGKLDRQAL 1705
Cdd:cd05936    454 LPKSAVGKILRREL 467
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
15-510 2.59e-40

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 159.88  E-value: 2.59e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   15 TDAVPAHGLAARLRALAQQRPEATALIVIDADGDTRYDYAQLDRRARALaarfardgAAA---------ERALILMDSGV 85
Cdd:COG1022      5 SDVPPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRAL--------AAGllalgvkpgDRVAILSDNRP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   86 DYVSAFFGCLYAGVVAVPVYPPESKREqhlarLRGIARDAGVRYVLT-TAALHERHADAWSMLAPGADVVAVDTLDARDT 164
Cdd:COG1022     77 EWVIADLAILAAGAVTVPIYPTSSAEE-----VAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLRHIVVLDPRGLRDD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  165 PS--------------------DAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWL 224
Cdd:COG1022    152 PRllsldellalgrevadpaelEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  225 PLYHDMGLIGSLLQpVFSGIPLvlmspqYFLERPlrwlDAIARHRGTIsgAPDFayrLCA-----ERINDETRAKLDLSS 299
Cdd:COG1022    232 PLAHVFERTVSYYA-LAAGATV------AFAESP----DTLAEDLREV--KPTF---MLAvprvwEKVYAGIQAKAEEAG 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  300 WrlafsgsepVRRDTLDDFVA---RFAPAGFD----AAALYPCYGLAEATLF-----VTGG-VR-----GAGL---VSHA 358
Cdd:COG1022    296 G---------LKRKLFRWALAvgrRYARARLAgkspSLLLRLKHALADKLVFsklreALGGrLRfavsgGAALgpeLARF 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  359 FSSAALsagraeaaradeaaTVLVGCGAvqaghrvaivaraaaeshesheadveTETS------RAGE-------RLADG 425
Cdd:COG1022    367 FRALGI--------------PVLEGYGL--------------------------TETSpvitvnRPGDnrigtvgPPLPG 406
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  426 ---RI---GEIHVSGPSVAHGYWQRADASAQAFVdaprhADGsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVR-GRN 497
Cdd:COG1022    407 vevKIaedGEILVRGPNVMKGYYKNPEATAEAFD-----ADG-----WLHTGDIGELdEDGFLRITGRKKDLIVTSgGKN 476
                          570
                   ....*....|...
gi 1888712850  498 LYPQDVEQAVEAH 510
Cdd:COG1022    477 VAPQPIENALKAS 489
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
1227-1705 6.20e-40

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 155.71  E-value: 6.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALR----MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRL 1302
Cdd:cd17654      1 PDRPALIIDQTTsdttVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1303 AQTLRDCGARLVL--CEDDCSALDLMgvqharidaaqeEAQREQHLRAPHALpavdprsaAYVIYTSGSSGAPKGVVIAH 1380
Cdd:cd17654     81 LTVMKKCHVSYLLqnKELDNAPLSFT------------PEHRHFNIRTDECL--------AYVIHTSGTTGTPKIVAVPH 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1381 GALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAA-RIDVLKIVPGH 1459
Cdd:cd17654    141 KCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRhRITVLQATPTL 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1460 LHALLQAERAADALPAHT----LVLGGEAT-SWELLDTIAALRPDCRVHNHYGPTETTVGILTQpaaQACRAAATLPLGR 1534
Cdd:cd17654    221 FRRFGSQSIKSTVLSATSslrvLALGGEPFpSLVILSSWRGKGNRTRIFNIYGITEVSCWALAY---KVPEEDSPVQLGS 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1535 PLDNNETWLLDEHlnpvGTGGTGELYLGGagVALGYLHQPALTAARfvphpfaagARLYRSGDRARRlADGSLEYLGRID 1614
Cdd:cd17654    298 PLLGTVIEVRDQN----GSEGTGQVFLGG--LNRVCILDDEVTVPK---------GTMRATGDFVTV-KDGELFFLGRKD 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1615 DQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGARLAAFATPQPGASLD--AAALKRALAALLPDYMVpsvlrVIDAL 1692
Cdd:cd17654    362 SQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGESSSSRIhkELQLTLLSSHAIPDTFV-----QIDKL 436
                          490
                   ....*....|...
gi 1888712850 1693 PLNRNGKLDRQAL 1705
Cdd:cd17654    437 PLTSHGKVDKSEL 449
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
31-593 9.95e-40

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 157.58  E-value: 9.95e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIVIDADGDTR-YDYAQLDRRARALaarfardgAAA---------ERALILMDSGVDYVSAFFGCLYAGVV 100
Cdd:COG0365     19 AEGRGDKVALIWEGEDGEERtLTYAELRREVNRF--------ANAlralgvkkgDRVAIYLPNIPEAVIAMLACARIGAV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  101 AVPVYP---PESkreqhlarLRGIARDAGVRYVLTTAALHERH---------ADAWSMLAPGADVVAVDTLDA------- 161
Cdd:COG0365     91 HSPVFPgfgAEA--------LADRIEDAEAKVLITADGGLRGGkvidlkekvDEALEELPSLEHVIVVGRTGAdvpmegd 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  162 -------RDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLAN-EIAIQAGLGVRPDDVF-----VSWLplyh 228
Cdd:COG0365    163 ldwdellAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHaATTAKYVLDLKPGDVFwctadIGWA---- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  229 dMGLIGSLLQPVFSGIPLVLMSPQYFLERPLRWLDAIARHRGTISGAPDFAYRLCAeRINDETRAKLDLSSWRLAFSGSE 308
Cdd:COG0365    239 -TGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALM-KAGDEPLKKYDLSSLRLLGSAGE 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  309 PVRRDTLDDFVARFapagfdAAALYPCYGLAEATLFVTGGVRG----AGlvshafssaalSAGRaeaaradeaatVLVGc 384
Cdd:COG0365    317 PLNPEVWEWWYEAV------GVPIVDGWGQTETGGIFISNLPGlpvkPG-----------SMGK-----------PVPG- 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  385 gavqaghrvaivaraaaeshesHEADVETETsraGERLADGRIGEIHVSG--PSVAHGYWQRADASAQAFVDaprHADGs 462
Cdd:COG0365    368 ----------------------YDVAVVDED---GNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYFG---RFPG- 418
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  463 gparWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFA-----------RKGRVIAFgATLGGGE 530
Cdd:COG0365    419 ----WYRTGDGARRDeDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAeaavvgvpdeiRGQVVKAF-VVLKPGV 493
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850  531 TLG--LALEIAPRMKKRFAAaqiVETLRRIAFdacgeTPaaiallnpgALPKTSSGKLQRAATRE 593
Cdd:COG0365    494 EPSdeLAKELQAHVREELGP---YAYPREIEF-----VD---------ELPKTRSGKIMRRLLRK 541
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
1845-2291 7.81e-39

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 150.92  E-value: 7.81e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1845 LPLSLMQQRIwVVDQLadRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAF-DADDEGDpvlkiaprmevLM 1923
Cdd:cd19542      2 YPCTPMQEGM-LLSQL--RSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGT-----------FL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1924 PVIepLAHPDNDANSHTNShtnsdenarTQATAQALDDAARTPFDLSRaPLVRATLLRFDAAHHVLIVSLHHIVADGGSV 2003
Cdd:cd19542     68 QVV--LKSLDPPIEEVETD---------EDSLDALTRDLLDDPTLFGQ-PPHRLTLLETSSGEVYLVLRISHALYDGVSL 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2004 HILLDELCELYRAQRDGAPPalaplavQYADYAHWQRARFTPdavrEAQQFWRGYLADA-PALLPLSTDRARPTRVSHAG 2082
Cdd:cd19542    136 PIILRDLAAAYNGQLLPPAP-------PFSDYISYLQSQSQE----ESLQYWRKYLQGAsPCAFPSLSPKRPAERSLSST 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2083 AARHFRLD---ATLGARVRTLAQAhgmtPFAVLLAsfqwflhRHTGADDLVIGTDVDGRE--RAELEALIGFFVNVVPLR 2157
Cdd:cd19542    205 RRSLAKLEafcASLGVTLASLFQA----AWALVLA-------RYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVR 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2158 SRIAADgANLASFdawLDAARQSTWDALDHRALPFDRIVDALALKRRRDANPLvqVLFVLRDLPRGNTRVPGLAVELLRP 2237
Cdd:cd19542    274 VKLDPD-WTVLDL---LRQLQQQYLRSLPHQHLSLREIQRALGLWPSGTLFNT--LVSYQNFEASPESELSGSSVFELSA 347
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1888712850 2238 PTTQSKFDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19542    348 AEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
35-590 1.04e-38

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 151.91  E-value: 1.04e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   35 PEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVPV---YPPEsk 110
Cdd:cd05930      1 PDAVAVV----DGDQSLTYAELDARANRLARYLRERGVGPGDLVaVLLERSLEMVVAILAVLKAGAAYVPLdpsYPAE-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  111 reqhlaRLRGIARDAGVRYVLTTAalherhadawsmlapgadvvavdtldardtpsdaplhpvraDDLAFLQYTSGSTGS 190
Cdd:cd05930     75 ------RLAYILEDSGAKLVLTDP-----------------------------------------DDLAYVIYTSGSTGK 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  191 PKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGlIGSLLQPVFSGIPLVLMSPQYFLErPLRWLDAIARHRG 270
Cdd:cd05930    108 PKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVS-VWEIFGALLAGATLVVLPEEVRKD-PEALADLLAEEGI 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  271 TISGAPDFAYRLCAerindETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARfapagFDAAALYPCYGLAEATLFVTggvr 350
Cdd:cd05930    186 TVLHLTPSLLRLLL-----QELELAALPSLRLVLVGGEALPPDLVRRWREL-----LPGARLVNLYGPTEATVDAT---- 251
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  351 gaglvshafssaalsagraeaaradeaatvlvgcgavqaghrvaivaraaaeSHESHEADVETETS-------------- 416
Cdd:cd05930    252 ----------------------------------------------------YYRVPPDDEEDGRVpigrpipntrvyvl 279
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  417 -RAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHadgsGPARWLRTGDLG-FVHDGQLYIAGRVKDLVIVR 494
Cdd:cd05930    280 dENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG----PGERMYRTGDLVrWLPDGNLEFLGRIDDQVKIR 355
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  495 GRNLYPQDVEQAVEAHAE------FARKG-----RVIAFgATLGGGETLGLAlEIAPRMKKRFAAAQIvetlrriafdac 563
Cdd:cd05930    356 GYRIELGEIEAALLAHPGvreaavVAREDgdgekRLVAY-VVPDEGGELDEE-ELRAHLAERLPDYMV------------ 421
                          570       580
                   ....*....|....*....|....*..
gi 1888712850  564 getPAAIALLNpgALPKTSSGKLQRAA 590
Cdd:cd05930    422 ---PSAFVVLD--ALPLTPNGKVDRKA 443
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
23-593 1.33e-38

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 153.14  E-value: 1.33e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVA 101
Cdd:PRK07656     7 LPELLARAARRFGDKEAYV----FGDQRLTYAELNARVRRAAAALAALGiGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  102 VPVYPPESKREQHlarlrGIARDAGVRYVLTTAAL-------HER--HADAWSMLAPGADVVAVDT------LDARDTPS 166
Cdd:PRK07656    83 VPLNTRYTADEAA-----YILARGDAKALFVLGLFlgvdysaTTRlpALEHVVICETEEDDPHTEKmktftdFLAAGDPA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  167 DAPLhPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSG--- 243
Cdd:PRK07656   158 ERAP-EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGati 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  244 IPLVLMSPQyflerplRWLDAIARHRGTI-SGAPDFAYRLcaerINDETRAKLDLSSWRLAFSG--SEPVRrdtlddFVA 320
Cdd:PRK07656   237 LPLPVFDPD-------EVFRLIETERITVlPGPPTMYNSL----LQHPDRSAEDLSSLRLAVTGaaSMPVA------LLE 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  321 RFApAGFDAAALYPCYGLAEATLFVTGGVRGAGlvshaFSSAALSAGRAEaaradeaatvlvgcgavqaghrvaivaraa 400
Cdd:PRK07656   300 RFE-SELGVDIVLTGYGLSEASGVTTFNRLDDD-----RKTVAGTIGTAI------------------------------ 343
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  401 aeshesheADVETET-SRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAfVDaprhADGsgparWLRTGDLGFV-HD 478
Cdd:PRK07656   344 --------AGVENKIvNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA-ID----ADG-----WLHTGDLGRLdEE 405
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  479 GQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH---AEFA-------RKGRVI-AFgatlgggetlglaleIAPRMKKRFA 547
Cdd:PRK07656   406 GYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHpavAEAAvigvpdeRLGEVGkAY---------------VVLKPGAELT 470
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1888712850  548 AAQIVETLRRiaFDACGETPAAIALLNpgALPKTSSGKLQRAATRE 593
Cdd:PRK07656   471 EEELIAYCRE--HLAKYKVPRSIEFLD--ELPKNATGKVLKRALRE 512
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
731-1169 2.14e-38

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 149.76  E-value: 2.14e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  731 SHAQQRQLFAWRLDPASRAYHVAagIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYaprteaaaplawaHV 810
Cdd:cd19542      5 TPMQEGMLLSQLRSPGLYFNHFV--FDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFL-------------QV 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  811 DLSDLgDID---EHDRERALRECAQRFADAPFDLLRgPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYR 887
Cdd:cd19542     70 VLKSL-DPPieeVETDEDSLDALTRDLLDDPTLFGQ-PPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  888 AALDGATTHgeaqakaktritYADYAawqrRWLASDAAARQLAYWRAALAdDAPPLALPydhtatdTASENADPRAAARV 967
Cdd:cd19542    148 GQLLPPAPP------------FSDYI----SYLQSQSQEESLQYWRKYLQ-GASPCAFP-------SLSPKRPAERSLSS 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  968 AFALPAPLaqavRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRT--RPETHDVIGFFVNTLVLHSDCEAA 1045
Cdd:cd19542    204 TRRSLAKL----EAFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPD 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1046 TPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARdaqHGPLFETSFNYLSDDY-PALARWPGARAERVEiAETHVKVP 1124
Cdd:cd19542    280 WTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWP---SGTLFNTLVSYQNFEAsPESELSGSSVFELSA-AEDPTEYP 355
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1888712850 1125 LALDLrESRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAFAH 1169
Cdd:cd19542    356 VAVEV-EPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLA 399
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
733-1168 3.17e-38

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 150.32  E-value: 3.17e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  733 AQQRQLFAW---RLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYAPRTEAAAPlawaH 809
Cdd:cd19546      7 ATAGQLRTWllaRLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARP----E 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  810 VDLSDLGdidehdrERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYraa 889
Cdd:cd19546     83 LPVVPAT-------EEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAY--- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  890 ldGATTHGEAQAKAKTRITYADYAAWQRRWLASD-----AAARQLAYWRAALADDAPPLALPYDHTATDTASenadpRAA 964
Cdd:cd19546    153 --GARREGRAPERAPLPLQFADYALWERELLAGEddrdsLIGDQIAYWRDALAGAPDELELPTDRPRPVLPS-----RRA 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  965 ARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRT-RPETHDVIGFFVNTLVLHSDCE 1043
Cdd:cd19546    226 GAVPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLS 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1044 AATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPALARW--PGARAERVEIAETHV 1121
Cdd:cd19546    306 GDPTFRELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDAPelPGLRTSPVPLGTEAM 385
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1888712850 1122 KVPLALDLRESR---------DGSMRayftYASARFDAASVERMAAQYLRAVEAFA 1168
Cdd:cd19546    386 ELDLSLALTERRnddgdpdglDGSLR----YAADLFDRATAAALARRLVRVLEQVA 437
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
27-592 4.62e-38

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 151.37  E-value: 4.62e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   27 LRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFFGCLYAGVVAVPV- 104
Cdd:cd05959     10 DLNLNEGRGDKTAFI----DDAGSLTYAELEAEARRVAGALRALGVKREeRVLLIMLDTVDFPTAFLGAIRAGIVPVPVn 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  105 --YPPEskreqhlaRLRGIARDAGVRYVLTTAALHERHADAWSMLAP---------GADVVAVDTLDARDTPSDAPLHP- 172
Cdd:cd05959     86 tlLTPD--------DYAYYLEDSRARVVVVSGELAPVLAAALTKSEHtlvvlivsgGAGPEAGALLLAELVAAEAEQLKp 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  173 --VRADDLAFLQYTSGSTGSPKGVMVSHGNLLAN-EIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLM 249
Cdd:cd05959    158 aaTHADDPAFWLYSSGSTGRPKGVVHLHADIYWTaELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLM 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  250 SpqyflERPL--RWLDAIARHRGTI-SGAPDfayrLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFapag 326
Cdd:cd05959    238 P-----ERPTpaAVFKRIRRYRPTVfFGVPT----LYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARF---- 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  327 fdaaalypcyGLaeatlfvtggvrgaglvshafssaalsagraeaaradeaaTVLVGCGAVQAGHRVAIvaraaaesheS 406
Cdd:cd05959    305 ----------GL----------------------------------------DILDGIGSTEMLHIFLS----------N 324
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  407 HEADVETETS-------------RAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVdaprhadgsGParWLRTGDl 473
Cdd:cd05959    325 RPGRVRYGTTgkpvpgyevelrdEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ---------GE--WTRTGD- 392
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  474 GFVH--DGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEfarkgrvIAFGATLGGGETLGLaleIAPR----MKKRFA 547
Cdd:cd05959    393 KYVRddDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPA-------VLEAAVVGVEDEDGL---TKPKafvvLRPGYE 462
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 1888712850  548 AAQIVET-LRRIAFDACG--ETPAAIALLNpgALPKTSSGKLQRAATR 592
Cdd:cd05959    463 DSEALEEeLKEFVKDRLApyKYPRWIVFVD--ELPKTATGKIQRFKLR 508
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
76-601 5.11e-38

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 152.50  E-value: 5.11e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   76 RALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESkrEQHLARLRGIARdagVRYVLTTAALHERHADAWSMLAPGADVVA 155
Cdd:cd05905     42 RVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDI--SQQLGFLLGTCK---VRVALTVEACLKGLPKKLLKSKTAAEIAK 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  156 VDT----LDARDTPSDAPLH--------PVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSW 223
Cdd:cd05905    117 KKGwpkiLDFVKIPKSKRSKlkkwgphpPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTV 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  224 LPLYHDMGLIGSLLQPVFSGIPLVLMSPQYFLERPLRWLDAIARH--RGTISGAPDFAYRLCAERINDETRAK--LDLSS 299
Cdd:cd05905    197 LDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTLSQYkvRDAYVKLRTLHWCLKDLSSTLASLKNrdVNLSS 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  300 WR-LAFSGSEPVRRDTLDDFVARFAPAGFDAAALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGRAEAARADEAA 378
Cdd:cd05905    277 LRmCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRVNPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPN 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  379 T-VLVGCGAVQAGHRVaivaraaaeshesheADVETETSragERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAP- 456
Cdd:cd05905    357 SlPLQDSGKVLPGAQV---------------AIVNPETK---GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPs 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  457 -RHADGSGPARWLRTGDLGFVHDGQ-----------LYIAGRVKDLVIVRGRNLYPQDVEQAVEAhAEFARkGRVIAFGA 524
Cdd:cd05905    419 tRLSTGITNNSYARTGLLGFLRPTKctdlnveehdlLFVVGSIDETLEVRGLRHHPSDIEATVMR-VHPYR-GRCAVFSI 496
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1888712850  525 TlgggETLGLALEIAPRMKKRfaAAQIVETLRRIAFDACGETPAAIALLNPGALPKTSSGKLQRAATREGWRARTLD 601
Cdd:cd05905    497 T----GLVVVVAEQPPGSEEE--ALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLH 567
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1236-1705 1.75e-37

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 147.82  E-value: 1.75e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1236 ALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVL 1315
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1316 CeddcsaldlmgvqharidaaqeeaqreqhlraphalpavDPrsaAYVIYTSGSSGAPKGVVIAHGALTNYVdAVLARLD 1395
Cdd:cd05934     81 V---------------------------------------DP---ASILYTSGTTGPPKGVVITHANLTFAG-YYSARRF 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1396 PPPRARFAMVST----IGAdLGHTVLfGALASGGALHLIDRdttLDADRFAQTLAAARIDVLKIVPGHLHALL-QAERAA 1470
Cdd:cd05934    118 GLGEDDVYLTVLplfhINA-QAVSVL-AALSVGATLVLLPR---FSASRFWSDVRRYGATVTNYLGAMLSYLLaQPPSPD 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1471 DAlpAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACraaaTLPLGRPLDNNETWLLDEHLNP 1550
Cdd:cd05934    193 DR--AHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRR----PGSIGRPAPGYEVRIVDDDGQE 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1551 VGTGGTGELYL---GGAGVALGYLHQPALTAARFvPHPFaagarlYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPG 1627
Cdd:cd05934    267 LPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RNGW------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSA 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1628 EIAARLKALDGVRDAAVIVV----AGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQ 1703
Cdd:cd05934    340 EVERAILRHPAVREAAVVAVpdevGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKA 419

                   ..
gi 1888712850 1704 AL 1705
Cdd:cd05934    420 QL 421
PRK07798 PRK07798
acyl-CoA synthetase; Validated
1223-1701 1.93e-37

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 150.04  E-value: 1.93e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1223 ADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRL 1302
Cdd:PRK07798    13 ADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDEL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1303 AQTLRDCGARLVLCEDDCSAL------DLMGVQHA-RIDAAQEEAQR------EQHLRAPHALPAVDPRSA--AYVIYTS 1367
Cdd:PRK07798    93 RYLLDDSDAVALVYEREFAPRvaevlpRLPKLRTLvVVEDGSGNDLLpgavdyEDALAAGSPERDFGERSPddLYLLYTG 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1368 GSSGAPKGVVIAHG----------------ALTNYVDAVLARLDPPPRARFAMVSTI-GAdlGHTVLFGALASGGALhLI 1430
Cdd:PRK07798   173 GTTGMPKGVMWRQEdifrvllggrdfatgePIEDEEELAKRAAAGPGMRRFPAPPLMhGA--GQWAAFAALFSGQTV-VL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1431 DRDTTLDADRFAQTLAAARIDVLKIVpGHLHA--LLQAERAADALPAHTLVL---GGEATSWELLDTIAALRPDCRVHNH 1505
Cdd:PRK07798   250 LPDVRFDADEVWRTIEREKVNVITIV-GDAMArpLLDALEARGPYDLSSLFAiasGGALFSPSVKEALLELLPNVVLTDS 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1506 YGPTETTV-GILTQPAAQACRAAATLPLGRpldnnETWLLDEHLNPV--GTGGTGELYLGGAgVALGYLHQPALTAARFv 1582
Cdd:PRK07798   329 IGSSETGFgGSGTVAKGAVHTGGPRFTIGP-----RTVVLDEDGNPVepGSGEIGWIARRGH-IPLGYYKDPEKTAETF- 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1583 phPFAAGARLYRSGDRARRLADGSLEYLGRidDQVKIR--GYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFA 1656
Cdd:PRK07798   402 --PTIDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVADALVVGVPderwGQEVVAVV 477
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1888712850 1657 TPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLD 1701
Cdd:PRK07798   478 QLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
75-592 6.02e-37

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 146.82  E-value: 6.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAG----VVAVPVYPPESkrEQHLarlRGIARDAGVRYVLTTAALHERHADAWSMlAPG 150
Cdd:cd05922     19 ERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLK--ESVL---RYLVADAGGRIVLADAGAADRLRDALPA-SPD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  151 ADVVaVDTLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDM 230
Cdd:cd05922     93 PGTV-LDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDY 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  231 GLiGSLLQPVFSGIPLVLmSPQYFLERPLrwLDAIARHRGT-ISGAPDFAYRLcaerindeTRAKLD---LSSWRLAFSG 306
Cdd:cd05922    172 GL-SVLNTHLLRGATLVL-TNDGVLDDAF--WEDLREHGATgLAGVPSTYAML--------TRLGFDpakLPSLRYLTQA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  307 SEPVRrdtlDDFVARFAPAGFDaAALYPCYGLAEATlfvtggVRGAGLVSHAFSSAALSAGraeaaradeaaTVLVGCga 386
Cdd:cd05922    240 GGRLP----QETIARLRELLPG-AQVYVMYGQTEAT------RRMTYLPPERILEKPGSIG-----------LAIPGG-- 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  387 vqaghrvaivaraaaesheshEADVETETsraGERLADGRIGEIHVSGPSVAHGYWQradasaqafvDAPRHADGSGPAR 466
Cdd:cd05922    296 ---------------------EFEILDDD---GTPTPPGEPGEIVHRGPNVMKGYWN----------DPPYRRKEGRGGG 341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  467 WLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFarkGRVIAFGATLGGGETLGLALEIAPRMKKR 545
Cdd:cd05922    342 VLHTGDLARRdEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI---IEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1888712850  546 FAAAQIVETLRRIAfdacgeTPAAIALLNpgALPKTSSGKLQRAATR 592
Cdd:cd05922    419 DVLRSLAERLPPYK------VPATVRVVD--ELPLTASGKVDYAALR 457
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
1228-1705 1.21e-36

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 145.51  E-value: 1.21e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1228 DAPAVIDGALRMSYAELDARAAHVAQWLLA-RDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLAlGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLceddcsaldlmgvqharidaaqeeaqreqhlraphalpavDPrsaAYVIYTSGSSGAPKGVVIAHGALTNY 1386
Cdd:cd05941     81 TDSEPSLVL----------------------------------------DP---ALILYTSGTTGRPKGVVLTHANLAAN 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1387 VDAVLARLDPPPRARFAMVstigADLGHT-----VLFGALASGGALHLIDRDttlDADRFAQTLAAARIDVLKIVPGHLH 1461
Cdd:cd05941    118 VRALVDAWRWTEDDVLLHV----LPLHHVhglvnALLCPLFAGASVEFLPKF---DPKEVAISRLMPSITVFMGVPTIYT 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1462 ALLQAERAAD-------ALPAHTLVL---GGEATSWELLDTIAALRPDcRVHNHYGPTETTVgILTQPAAQACRAAAtlp 1531
Cdd:cd05941    191 RLLQYYEAHFtdpqfarAAAAERLRLmvsGSAALPVPTLEEWEAITGH-TLLERYGMTEIGM-ALSNPLDGERRPGT--- 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1532 LGRPLDNNETWLLDEHLNPVGTGGT-GELYLGGAGVALGYLHQPALTAARFVPHPFaagarlYRSGDRARRLADGSLEYL 1610
Cdd:cd05941    266 VGMPLPGVQARIVDEETGEPLPRGEvGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWIL 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1611 GRI-DDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGA-SLDAAALKRALAALLPDYMVPS 1684
Cdd:cd05941    340 GRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPdpdwGERVVAVVVLRAGAaALSLEELKEWAKQRLAPYKRPR 419
                          490       500
                   ....*....|....*....|.
gi 1888712850 1685 VLRVIDALPLNRNGKLDRQAL 1705
Cdd:cd05941    420 RLILVDELPRNAMGKVNKKEL 440
PRK12316 PRK12316
peptide synthase; Provisional
1846-2296 1.67e-36

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 153.19  E-value: 1.67e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIwVVDQLADRALASYNMTAGLDLRGpLDAARLQRSLAALIARHEVLRSAFDADDE-GDPVLKIAPRMEVLMP 1924
Cdd:PRK12316  4104 PLSPMQQGM-LFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGElGRPLQVVHKQVSLPFA 4181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1925 VIEPLAHPDNDAnshtnshtnsdenartqataqALDDAA----RTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADG 2000
Cdd:PRK12316  4182 ELDWRGRADLQA---------------------ALDALAaaerERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDG 4240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2001 GSVHILLDELCELYRaqrdGAPPalAPLAVQYADYAHW-QRarfTPDAVREAqqFWRGYLADAPALLPLSTDRARPTRVS 2079
Cdd:PRK12316  4241 WSNSQLLGEVLERYS----GRPP--AQPGGRYRDYIAWlQR---QDAAASEA--FWREQLAALDEPTRLAQAIARADLRS 4309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2080 HAGAARHFR-LDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGR--ERAELEALIGFFVNVVPL 2156
Cdd:PRK12316  4310 ANGYGEHVReLDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRpaELPGIEGQIGLFINTLPV 4389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2157 RSRIAADganlASFDAWLDAARQSTWDALDHRALPFDRIvdalALKRRRDANPLVQVLFVLRDLPRGNTRVPGLAVELLR 2236
Cdd:PRK12316  4390 IATPRAQ----QSVVEWLQQVQRQNLALREHEHTPLYEI----QRWAGQGGEALFDSLLVFENYPVSEALQQGAPGGLRF 4461
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850 2237 PPTTQSKFDMALFVEAVDGG--YDIEWVYASALFDAATIERAFDAWRATLDAVSADPRAPLA 2296
Cdd:PRK12316  4462 GEVTNHEQTNYPLTLAVGLGetLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLG 4523
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
75-510 1.67e-36

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 145.43  E-value: 1.67e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPpESKREQhlarlrgiardagVRYVLttaalheRHAdawsmlapGADVV 154
Cdd:cd05907     31 DRVAILSRNRPEWTIADLAILAIGAVPVPIYP-TSSAEQ-------------IAYIL-------NDS--------EAKAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  155 AVDTldardtpsdaplhpvrADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIG 234
Cdd:cd05907     82 FVED----------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRA 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  235 SLLQPVFSGiplvlmSPQYFLERPLRWLDAIARHRGTI-SGAPDFAYRLCAE-RINDETRAKLDLSSW------RLAFSG 306
Cdd:cd05907    146 GLYVPLLAG------ARIYFASSAETLLDDLSEVRPTVfLAVPRVWEKVYAAiKVKAVPGLKRKLFDLavggrlRFAASG 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  307 SEPVRRDTLddfvARFAPAGFDaaaLYPCYGLAEatlfvtggvrgaglvshafSSAALSAGRAEAARADEAATVLVGCGA 386
Cdd:cd05907    220 GAPLPAELL----HFFRALGIP---VYEGYGLTE-------------------TSAVVTLNPPGDNRIGTVGKPLPGVEV 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  387 vqaghrvaivaraaaeshesheadvetetsrageRLADGriGEIHVSGPSVAHGYWQRADASAQAFVdaprhADGsgpar 466
Cdd:cd05907    274 ----------------------------------RIADD--GEILVRGPNVMLGYYKNPEATAEALD-----ADG----- 307
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1888712850  467 WLRTGDLGFVH-DGQLYIAGRVKDLVIVR-GRNLYPQDVEQAVEAH 510
Cdd:cd05907    308 WLHTGDLGEIDeDGFLHITGRKKDLIITSgGKNISPEPIENALKAS 353
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
1846-2290 2.10e-36

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 143.87  E-value: 2.10e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIWVVDQLaDRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDEGdPVLKIAPrmevLMPV 1925
Cdd:cd19537      3 ALSPIEREWWHKYQL-STGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGG-LRRSYSS----SPPR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1926 IEPLAHPDndanshtnshtnsdenartqataqaLDDAARTPFDLSRAPLVRATLlrfdaAHHVLIVSLHHIVADGGSVHI 2005
Cdd:cd19537     77 VQRVDTLD-------------------------VWKEINRPFDLEREDPIRVFI-----SPDTLLVVMSHIICDLTTLQL 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2006 LLDELCELYRAQRdgappaLAPLAVQYADYAHWQRarfTPDAvrEAQQFWRGYLADAPAL-LPlstdrARPTRVSHAGAA 2084
Cdd:cd19537    127 LLREVSAAYNGKL------LPPVRREYLDSTAWSR---PASP--EDLDFWSEYLSGLPLLnLP-----RRTSSKSYRGTS 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2085 RHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRERAELEALIGFFVNvvPLRSRIAADG 2164
Cdd:cd19537    191 RVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLE--PLPIRIRFPS 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2165 ANLASFDAWLDAARQSTWDALDHrALPFDRIVDALALKRRRDANPL--VQVLFVLRDLPRGNTRVPGLAVELLRppTTQS 2242
Cdd:cd19537    269 SSDASAADFLRAVRRSSQAALAH-AIPWHQLLEHLGLPPDSPNHPLfdVMVTFHDDRGVSLALPIPGVEPLYTW--AEGA 345
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1888712850 2243 KFD-MALFVEAVDGG--YDIEwvYASALFDAATIERAFDAWRATLDAVSAD 2290
Cdd:cd19537    346 KFPlMFEFTALSDDSllLRLE--YDTDCFSEEEIDRIESLILAALELLVEG 394
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
75-588 2.55e-36

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 144.54  E-value: 2.55e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKREqhlarLRGIARDAGVRYVLTTAALherhadawsmlapgadvv 154
Cdd:cd05935     27 DRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERE-----LEYILNDSGAKVAVVGSEL------------------ 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  155 avdtldardtpsdaplhpvraDDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIG 234
Cdd:cd05935     84 ---------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  235 SLLQPVFSGIPLVLMSpqyflerplRW-----LDAIARHRGTISGApdfAYRLCAERINDETRAKLDLSSWRLAFSGSEP 309
Cdd:cd05935    143 SLNTAVYVGGTYVLMA---------RWdretaLELIEKYKVTFWTN---IPTMLVDLLATPEFKTRDLSSLKVLTGGGAP 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  310 VrrdtlddfvarfAPAgfdaaalypcygLAEATLFVTG--GVRGAGLvshafsSAALSAGRAEAARADEAATVLVGCGAV 387
Cdd:cd05935    211 M------------PPA------------VAEKLLKLTGlrFVEGYGL------TETMSQTHTNPPLRPKLQCLGIP*FGV 260
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  388 qaghrvaivaraaaeshESHEADVETetsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsGPARW 467
Cdd:cd05935    261 -----------------DARVIDIET-----GRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEI-------KGRRF 311
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  468 LRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHaefarkgRVIAFGATLG-----GGETLGLALEIAPR 541
Cdd:cd05935    312 FRTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH-------PAI*EVCVISvpderVGEEVKAFIVLRPE 384
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1888712850  542 MKKRFAAAQIVETLRRIAfdACGETPAAIALLNpgALPKTSSGKLQR 588
Cdd:cd05935    385 YRGKVTEEDIIEWAREQM--AAYKYPREVEFVD--ELPRSASGKILW 427
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
1223-1705 2.65e-36

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 145.97  E-value: 2.65e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1223 ADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRL 1302
Cdd:cd05959     14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1303 AQTLRDCGARLV-----LCEDDCSALDLMGVQHARIDAAQEEAQREQHLRAPHALP---------AVDPRSAAYVIYTSG 1368
Cdd:cd05959     94 AYYLEDSRARVVvvsgeLAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAaeaeqlkpaATHADDPAFWLYSSG 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1369 SSGAPKGVVIAHGALT----NYVDAVLA-----RLDPPPRARFAMvstigaDLGHTVLFGALASGGALHLIDRDTtldAD 1439
Cdd:cd05959    174 STGRPKGVVHLHADIYwtaeLYARNVLGireddVCFSAAKLFFAY------GLGNSLTFPLSVGATTVLMPERPT---PA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1440 RFAQTLAAARIDVLKIVPGHLHALLQAER--------------AADALPAH-----------TLVLGGEATswELLDTIA 1494
Cdd:cd05959    245 AVFKRIRRYRPTVFFGVPTLYAAMLAAPNlpsrdlsslrlcvsAGEALPAEvgerwkarfglDILDGIGST--EMLHIFL 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1495 ALRPDcRVHnhYGPTettvgiltqpaaqacraaatlplGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQP 1574
Cdd:cd05959    323 SNRPG-RVR--YGTT-----------------------GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNR 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1575 ALTAARFVphpfaagARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGA---- 1650
Cdd:cd05959    377 DKTRDTFQ-------GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEdglt 449
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1888712850 1651 RLAAFATPQPGASLDAAALKRALA---ALLPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:cd05959    450 KPKAFVVLRPGYEDSEALEEELKEfvkDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
1230-1705 3.65e-36

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 144.14  E-value: 3.65e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1230 PAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDC 1309
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1310 GARLVLCEDDcsaldlmgvqharidaaqeeaqreqhlraphalpavdprSAAYVIYTSGSSGAPKGVVIAHGALTNYVDA 1389
Cdd:cd05919     82 EARLVVTSAD---------------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADA 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1390 V---LARLDPPPRARFAMVSTIGADLGHTVLFGaLASGGALHLIDrdTTLDADRFAQTLAAARIDVLKIVP-GHLHALLQ 1465
Cdd:cd05919    123 MareALGLTPGDRVFSSAKMFFGYGLGNSLWFP-LAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPtFYANLLDS 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1466 AERAADALPAHTLVL-GGEATSWELLDTIAALRpDCRVHNHYGPTETT-VGILTQPAAQACRAaatlpLGRPLDNNETWL 1543
Cdd:cd05919    200 CAGSPDALRSLRLCVsAGEALPRGLGERWMEHF-GGPILDGIGATEVGhIFLSNRPGAWRLGS-----TGRPVPGYEIRL 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1544 LDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVphpfaagARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYR 1623
Cdd:cd05919    274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1624 VEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQPGASLDAAALKRALAALL---PDYMVPSVLRVIDALPLNR 1696
Cdd:cd05919    347 VSPVEVESLIIQHPAVAEAAVVAVpestGLSRLTAFVVLKSPAAPQESLARDIHRHLLerlSAHKVPRRIAFVDELPRTA 426

                   ....*....
gi 1888712850 1697 NGKLDRQAL 1705
Cdd:cd05919    427 TGKLQRFKL 435
PRK07787 PRK07787
acyl-CoA synthetase; Validated
1217-1707 5.84e-36

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 144.36  E-value: 5.84e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1217 LRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQwllarDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAG 1296
Cdd:PRK07787     4 LNPAAVAAAADIADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1297 NPTQRLAQTLRDCGARLVLCEddcSALDLMGVQHARIDAaqeeaqreqHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGV 1376
Cdd:PRK07787    79 SGVAERRHILADSGAQAWLGP---APDDPAGLPHVPVRL---------HARSWHRYPEPDPDAPALIVYTSGTTGPPKGV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1377 VIAHGALTNYVDAvLARldppprarfAMVSTIGADLGHTV-LF----------GALASGGALHLIDRDTTldaDRFAQTL 1445
Cdd:PRK07787   147 VLSRRAIAADLDA-LAE---------AWQWTADDVLVHGLpLFhvhglvlgvlGPLRIGNRFVHTGRPTP---EAYAQAL 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1446 AAaRIDVLKIVPGHLHALLQAERAADAL-PAHTLVLGGEATSWELLDTIAALRPDcRVHNHYGPTETTVGILTQPAAQAC 1524
Cdd:PRK07787   214 SE-GGTLYFGVPTVWSRIAADPEAARALrGARLLVSGSAALPVPVFDRLAALTGH-RPVERYGMTETLITLSTRADGERR 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1525 RAAatlpLGRPLDNNETWLLDEHLNPVGTGG--TGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlYRSGDRARRL 1602
Cdd:PRK07787   292 PGW----VGLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVD 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1603 ADGSLEYLGRID-DQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALL 1677
Cdd:PRK07787   362 PDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPdddlGQRIVAYVVGADDVAADELIDFVAQQLSV 441
                          490       500       510
                   ....*....|....*....|....*....|
gi 1888712850 1678 pdYMVPSVLRVIDALPLNRNGKLDRQALSA 1707
Cdd:PRK07787   442 --HKRPREVRFVDALPRNAMGKVLKKQLLS 469
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
35-593 7.17e-36

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 144.38  E-value: 7.17e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   35 PEATALIVIDadGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKREq 113
Cdd:cd05926      1 PDAPALVVPG--STPALTYADLAELVDDLARQLAALGiKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAE- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  114 hlarLRGIARDAGVRYVLT-----TAALHERHADAWSMLAPGADV-VAVDTLDARDTPSDAPLHPV-------RADDLAF 180
Cdd:cd05926     78 ----FEFYLADLGSKLVLTpkgelGPASRAASKLGLAILELALDVgVLIRAPSAESLSNLLADKKNaksegvpLPDDLAL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  181 LQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLmsPQYFleRPLR 260
Cdd:cd05926    154 ILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVL--PPRF--SAST 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  261 WLDAIARHRGT-ISGAPDFAYRLCAeRINDETRAKldLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAaalypcYGLA 339
Cdd:cd05926    230 FWPDVRDYNATwYTAVPTIHQILLN-RPEPNPESP--PPKLRFIRSCSASLPPAVLEALEATFGAPVLEA------YGMT 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  340 EAtlfvtggvrgaglvSHAFSSAALSAGRAEAAradeaatvLVGCGAVQaghrvaivaraaaesheshEADVETETsraG 419
Cdd:cd05926    301 EA--------------AHQMTSNPLPPGPRKPG--------SVGKPVGV-------------------EVRILDED---G 336
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  420 ERLADGRIGEIHVSGPSVAHGYWQRADASAQ-AFVDaprhadgsgpaRWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRN 497
Cdd:cd05926    337 EILPPGVVGEICLRGPNVTRGYLNNPEANAEaAFKD-----------GWFRTGDLGyLDADGYLFLTGRIKELINRGGEK 405
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  498 LYPQDVEQAVEAHAEFArkgRVIAFG---ATLggGETLGLAleIAPRMKKRFAAAQIVETLRR--IAFdacgETPAAIAL 572
Cdd:cd05926    406 ISPLEVDGVLLSHPAVL---EAVAFGvpdEKY--GEEVAAA--VVLREGASVTEEELRAFCRKhlAAF----KVPKKVYF 474
                          570       580
                   ....*....|....*....|.
gi 1888712850  573 LNpgALPKTSSGKLQRAATRE 593
Cdd:cd05926    475 VD--ELPKTATGKIQRRKVAE 493
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
10-510 4.26e-35

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 143.18  E-value: 4.26e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   10 PHGIDtdaVPAHGLAARLRALAQQRPEATALIVIDadgdTRYDYAQL-DRRARALAARFARDGA-AAERALILMDSGVDY 87
Cdd:PRK08314     2 PKSLT---LPETSLFHNLEVSARRYPDKTAIVFYG----RAISYRELlEEAERLAGYLQQECGVrKGDRVLLYMQNSPQF 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   88 VSAFFGCLYAGVVAVPVYPPESKREqhlarLRGIARDAGVRYVLTTAALHER-----------------HADA------- 143
Cdd:PRK08314    75 VIAYYAILRANAVVVPVNPMNREEE-----LAHYVTDSGARVAIVGSELAPKvapavgnlrlrhvivaqYSDYlpaepei 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  144 ----W-------SMLAPGADVVAVDTLDARDTPsdaPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGL 212
Cdd:PRK08314   150 avpaWlraepplQALAPGGVVAWKEALAAGLAP---PPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWS 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  213 GVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSpqyflerplRW-----LDAIARHRGTISGAP-----DFayrL 282
Cdd:PRK08314   227 NSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP---------RWdreaaARLIERYRVTHWTNIptmvvDF---L 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  283 CAERIndetrAKLDLSSWRLAFSGS----EPVRRDTLDDFVARFAPAgfdaaalypcYGLAEATLFvtggvrgaglvSHA 358
Cdd:PRK08314   295 ASPGL-----AERDLSSLRYIGGGGaampEAVAERLKELTGLDYVEG----------YGLTETMAQ-----------THS 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  359 FSSAALSagraeaaradeaatvlVGCGAVQaghrvaivaraaaesHESHEA---DVETetsraGERLADGRIGEIHVSGP 435
Cdd:PRK08314   349 NPPDRPK----------------LQCLGIP---------------TFGVDArviDPET-----LEELPPGEVGEIVVHGP 392
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1888712850  436 SVAHGYWQRADASAQAFVDaprhADGSgpaRWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PRK08314   393 QVFKGYWNRPEATAEAFIE----IDGK---RFFRTGDLGRMdEEGYFFITDRLKRMINASGFKVWPAEVENLLYKH 461
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
31-590 5.23e-35

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 142.23  E-value: 5.23e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPeS 109
Cdd:TIGR03098   10 AARLPDATALV----HHDRTLTYAALSERVLALASGLRGLGlARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPL-L 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  110 KREQhlarLRGIARDAGVRYVLTTAALHE--RHADAW----------------SMLAPGADVVAVDTLDArdTPSDAPLH 171
Cdd:TIGR03098   85 KAEQ----VAHILADCNVRLLVTSSERLDllHPALPGchdlrtliivgdpahaSEGHPGEEPASWPKLLA--LGDADPPH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  172 PVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLiGSLLQPVFSGIPLVLMsp 251
Cdd:TIGR03098  159 PVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGF-NQLTTAFYVGATVVLH-- 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  252 QYFLERPLrwLDAIARHRGT-ISGAPDFAYRLCAERINDETRAKLDlsswRLAFSGSEpVRRDTLDDFVARFApagfdAA 330
Cdd:TIGR03098  236 DYLLPRDV--LKALEKHGITgLAAVPPLWAQLAQLDWPESAAPSLR----YLTNSGGA-MPRATLSRLRSFLP-----NA 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  331 ALYPCYGLAEatlfvtggvrgaglvshAFSSAALSAGRAEAARADEAATVlvgcgavqaghrvaivaraaaeshesheAD 410
Cdd:TIGR03098  304 RLFLMYGLTE-----------------AFRSTYLPPEEVDRRPDSIGKAI----------------------------PN 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  411 VETETSRA-GERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHADGS---GPARWlrTGDLGFV-HDGQLYIAG 485
Cdd:TIGR03098  339 AEVLVLREdGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELhlpELAVW--SGDTVRRdEEGFLYFVG 416
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  486 RVKDLVIVRGRNLYPQDVEQAVEAHAEFArkgRVIAFGA---TLGGgetlGLALEIAPRMKKRFAAAQIVETLRRI--AF 560
Cdd:TIGR03098  417 RRDEMIKTSGYRVSPTEVEEVAYATGLVA---EAVAFGVpdpTLGQ----AIVLVVTPPGGEELDRAALLAECRARlpNY 489
                          570       580       590
                   ....*....|....*....|....*....|
gi 1888712850  561 dacgETPAAIALLNpgALPKTSSGKLQRAA 590
Cdd:TIGR03098  490 ----MVPALIHVRQ--ALPRNANGKIDRKA 513
PRK06188 PRK06188
acyl-CoA synthetase; Validated
1227-1707 3.01e-34

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 140.12  E-value: 3.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:PRK06188    26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLCEDDC---SALDL----MGVQH----ARIDAAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKG 1375
Cdd:PRK06188   106 EDAGISTLIVDPAPfveRALALlarvPSLKHvltlGPVPDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKG 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1376 VVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLfGALASGGALHLIDRdttLDADRFAQTLAAARIDVLKI 1455
Cdd:PRK06188   186 VMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFL-PTLLRGGTVIVLAK---FDPAEVLRAIEEQRITATFL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1456 VPGHLHALLQAERAADA-LPAHTLVLGGEA--TSWELLDTIAALRPdcRVHNHYGPTET--TVGILTQPAAQACRAAATL 1530
Cdd:PRK06188   262 VPTMIYALLDHPDLRTRdLSSLETVYYGASpmSPVRLAEAIERFGP--IFAQYYGQTEApmVITYLRKRDHDPDDPKRLT 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1531 PLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFvphpfaAGARLyRSGDRARRLADGSLEYL 1610
Cdd:PRK06188   340 SCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RDGWL-HTGDVAREDEDGFYYIV 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1611 GRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVL 1686
Cdd:PRK06188   413 DRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPdekwGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQV 492
                          490       500
                   ....*....|....*....|.
gi 1888712850 1687 RVIDALPLNRNGKLDRQALSA 1707
Cdd:PRK06188   493 DFVDSLPLTALGKPDKKALRA 513
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
35-590 3.29e-34

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 138.96  E-value: 3.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   35 PEATALividADGDTRYDYAQLDRRARALAARFARDGAAA-ERALILMDSGVDYVSAFFGCLYAGVVAVPVYP--PEskr 111
Cdd:cd12116      1 PDATAV----RDDDRSLSYAELDERANRLAARLRARGVGPgDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPdyPA--- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  112 eqhlARLRGIARDAGVRYVLTTAALHERhadawsmlAPGADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSP 191
Cdd:cd12116     74 ----DRLRYILEDAEPALVLTDDALPDR--------LPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRP 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  192 KGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIgSLLQPVFSGIPLVLMSpqyflerplrwldaiarhRGT 271
Cdd:cd12116    142 KGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLL-ELLLPLLAGARVVIAP------------------RET 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  272 ISGAPDFAYRLCAERIndeTRAKLDLSSWRLAFS-------------GSEPVRRDTLDDFVARfapagfdAAALYPCYGL 338
Cdd:cd12116    203 QRDPEALARLIEAHSI---TVMQATPATWRMLLDagwqgragltalcGGEALPPDLAARLLSR-------VGSLWNLYGP 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  339 AEATLfvtggvrgaglvshaFSSAALsagraeaaradeaatVLVGCGAVQAGHRVAIVARAAAEShesheadvetetsrA 418
Cdd:cd12116    273 TETTI---------------WSTAAR---------------VTAAAGPIPIGRPLANTQVYVLDA--------------A 308
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  419 GERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHADGSgpaRWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRN 497
Cdd:cd12116    309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGS---RLYRTGDLVrRRADGRLEYLGRADGQVKIRGHR 385
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  498 LYPQDVEQAVEAHAEFARkgrviAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDACgeTPAAIALLNpgA 577
Cdd:cd12116    386 IELGEIEAALAAHPGVAQ-----AAVVVREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYM--VPSAFVRLD--A 456
                          570
                   ....*....|...
gi 1888712850  578 LPKTSSGKLQRAA 590
Cdd:cd12116    457 LPLTANGKLDRKA 469
PRK07514 PRK07514
malonyl-CoA synthase; Validated
20-504 3.62e-34

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 139.63  E-value: 3.62e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   20 AHGLAARLRAlAQQRPEATAlivIDADGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAG 98
Cdd:PRK07514     2 NNNLFDALRA-AFADRDAPF---IETPDGLRYTYGDLDAASARLANLLVALGvKPGDRVAVQVEKSPEALALYLATLRAG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   99 VVAVPV---YppeskreqHLARLRGIARDAGVRYVLTTAAlherHADAWSMLAPGADVVAVDTLD----------ARDTP 165
Cdd:PRK07514    78 AVFLPLntaY--------TLAELDYFIGDAEPALVVCDPA----NFAWLSKIAAAAGAPHVETLDadgtgslleaAAAAP 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  166 SDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIP 245
Cdd:PRK07514   146 DDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGAS 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  246 LVLMsPQYFLERPLRWLDaiarhRGT-ISGAPDFAYRLCAE-RINDETRAKLdlsswRLAFSGSEPVRRDTLDDFVARfa 323
Cdd:PRK07514   226 MIFL-PKFDPDAVLALMP-----RATvMMGVPTFYTRLLQEpRLTREAAAHM-----RLFISGSAPLLAETHREFQER-- 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  324 pAGFdaaALYPCYGLAEATLFVT---GGVRGAGLVSHAFSSAALSAgraeaaradeaatvlvgcgavqaghrvaivaraa 400
Cdd:PRK07514   293 -TGH---AILERYGMTETNMNTSnpyDGERRAGTVGFPLPGVSLRV---------------------------------- 334
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  401 aeshesheADVETetsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFvdaprHADGsgparWLRTGDLGFV-HDG 479
Cdd:PRK07514   335 --------TDPET-----GAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF-----RADG-----FFITGDLGKIdERG 391
                          490       500
                   ....*....|....*....|....*
gi 1888712850  480 QLYIAGRVKDLVIVRGRNLYPQDVE 504
Cdd:PRK07514   392 YVHIVGRGKDLIISGGYNVYPKEVE 416
PRK12316 PRK12316
peptide synthase; Provisional
31-691 5.84e-34

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 144.71  E-value: 5.84e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIVidadGDTRYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFFGCLYAGVVAVPVyPPES 109
Cdd:PRK12316  4561 ARMTPDAVAVVF----DEEKLTYAELNRRANRLAHALIARGVGPEvLVGIAMERSAEMMVGLLAVLKAGGAYVPL-DPEY 4635
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  110 KREqhlaRLRGIARDAGVRYVLTtaalhERHADAWSMLAPGADVVAVD-TLDARDTPSDAPLHPVRADDLAFLQYTSGST 188
Cdd:PRK12316  4636 PRE----RLAYMMEDSGAALLLT-----QSHLLQRLPIPDGLASLALDrDEDWEGFPAHDPAVRLHPDNLAYVIYTSGST 4706
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  189 GSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDmGLIGSLLQPVFSGIPLVLMSPQYFLerPLRWLDAIARH 268
Cdd:PRK12316  4707 GRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFD-GSHEGLYHPLINGASVVIRDDSLWD--PERLYAEIHEH 4783
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  269 RGTISGAPDFAYRLCAErindETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGfdaaaLYPCYGLAEATLFVTgg 348
Cdd:PRK12316  4784 RVTVLVFPPVYLQQLAE----HAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVY-----LFNGYGPTETTVTVL-- 4852
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  349 vrgaglvshafsSAALSAGRAEAARADEAATVLVGCGAvqaghrvaivaraaaeshesHEADVEtetsraGERLADGRIG 428
Cdd:PRK12316  4853 ------------LWKARDGDACGAAYMPIGTPLGNRSG--------------------YVLDGQ------LNPLPVGVAG 4894
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  429 EIHVSGPSVAHGYWQRADASAQAFVDAPRHADGSgpaRWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAV 507
Cdd:PRK12316  4895 ELYLGGEGVARGYLERPALTAERFVPDPFGAPGG---RLYRTGDLArYRADGVIDYLGRVDHQVKIRGFRIELGEIEARL 4971
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  508 EAHAEfARKGRVIAF-GATlgGGETLGLALEIAPRMKKRFAA-AQIVETLRRIAFDACGETPAAIALLNPGALPKTSSGK 585
Cdd:PRK12316  4972 REHPA-VREAVVIAQeGAV--GKQLVGYVVPQDPALADADEAqAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGK 5048
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  586 LQRAATREgwrartLDLYALweQGAFViggdddaarapdapAALDARESALAALWCEALD-ARLALapDAHFFASGGSSL 664
Cdd:PRK12316  5049 LDRKALPQ------PDASLL--QQAYV--------------APRSELEQQVAAIWAEVLQlERVGL--DDNFFELGGHSL 5104
                          650       660
                   ....*....|....*....|....*..
gi 1888712850  665 SAARLVALIGARLGRRVALAQIFETPT 691
Cdd:PRK12316  5105 LAIQVTSRIQLELGLELPLRELFQTPT 5131
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
36-510 2.41e-33

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 135.88  E-value: 2.41e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   36 EATALIvidaDGDTRYDYAQL--DRRARALAARFARDGAAAERALILMDSGVDYVSAFFGCLYAGVVAVPVYPpeskreQ 113
Cdd:cd05941      1 DRIAIV----DDGDSITYADLvaRAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNP------S 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  114 H-LARLRGIARDAGVRYVLttaalherhadawsmlapgadvvavdtldardtpsdaplhpvradDLAFLQYTSGSTGSPK 192
Cdd:cd05941     71 YpLAELEYVITDSEPSLVL---------------------------------------------DPALILYTSGTTGRPK 105
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  193 GVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLM---SPQYFLERPL---------- 259
Cdd:cd05941    106 GVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLpkfDPKEVAISRLmpsitvfmgv 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  260 -----RWLDAIARHrgtiSGAPDFAYRLCAERIndetrakldlsswRLAFSGSEPVRRDTLDDFVARFapagfdAAALYP 334
Cdd:cd05941    186 ptiytRLLQYYEAH----FTDPQFARAAAAERL-------------RLMVSGSAALPVPTLEEWEAIT------GHTLLE 242
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  335 CYGLAEATLFVTG---GVRGAGLVSHAFSSaalsagraeaaradeaatvlvgcgaVQAghrvaivaraaaeshesheADV 411
Cdd:cd05941    243 RYGMTEIGMALSNpldGERRPGTVGMPLPG-------------------------VQA-------------------RIV 278
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  412 ETETSRAGERladGRIGEIHVSGPSVAHGYWQRADASAQAFVDaprhaDGsgparWLRTGDLGFV-HDGQLYIAGRVKDL 490
Cdd:cd05941    279 DEETGEPLPR---GEVGEIQVRGPSVFKEYWNKPEATKEEFTD-----DG-----WFKTGDLGVVdEDGYYWILGRSSVD 345
                          490       500
                   ....*....|....*....|.
gi 1888712850  491 VI-VRGRNLYPQDVEQAVEAH 510
Cdd:cd05941    346 IIkSGGYKVSALEIERVLLAH 366
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
25-590 2.83e-33

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 136.64  E-value: 2.83e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   25 ARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVP 103
Cdd:cd17646      2 ALVAEQAARTPDAPAVV----DEGRTLTYRELDERANRLAHLLRARGVGPEDRVaVLLPRSADLVVALLAVLKAGAAYLP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  104 V---YPPEskreqhlaRLRGIARDAGVRYVLTTAALHERhadawsmLAPGADVVAVDTLDARDTPSDAPLHPVRADDLAF 180
Cdd:cd17646     78 LdpgYPAD--------RLAYMLADAGPAVVLTTADLAAR-------LPAGGDVALLGDEALAAPPATPPLVPPRPDNLAY 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  181 LQYTSGSTGSPKGVMVSHGNlLANEIA-IQAGLGVRPDDVFVSWLPLYHDMGlIGSLLQPVFSGIPLVLMSPQyfLER-P 258
Cdd:cd17646    143 VIYTSGSTGRPKGVMVTHAG-IVNRLLwMQDEYPLGPGDRVLQKTPLSFDVS-VWELFWPLVAGARLVVARPG--GHRdP 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  259 LRWLDAIARHRGTisgAPDFAYRLCAERIndETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFapagfdAAALYPCYGL 338
Cdd:cd17646    219 AYLAALIREHGVT---TCHFVPSMLRVFL--AEPAAGSCASLRRVFCSGEALPPELAARFLALP------GAELHNLYGP 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  339 AEATLFVTGG-VRGAglvshafssaalsagraeaaraDEAATVLVGcgavqaghrvaivaraaaesHESHEADVETETSR 417
Cdd:cd17646    288 TEAAIDVTHWpVRGP----------------------AETPSVPIG--------------------RPVPNTRLYVLDDA 325
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  418 aGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPrHADGSgpaRWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGR 496
Cdd:cd17646    326 -LRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDP-FGPGS---RMYRTGDLArWRPDGALEFLGRSDDQVKIRGF 400
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  497 NLYPQDVEQAVEAHAEFARkGRVIAFGATLGGGETLGL------ALEIAPRMKKRFAAAQIVETLrriafdacgeTPAAI 570
Cdd:cd17646    401 RVEPGEIEAALAAHPAVTH-AVVVARAAPAGAARLVGYvvpaagAAGPDTAALRAHLAERLPEYM----------VPAAF 469
                          570       580
                   ....*....|....*....|
gi 1888712850  571 ALLNpgALPKTSSGKLQRAA 590
Cdd:cd17646    470 VVLD--ALPLTANGKLDRAA 487
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1212-1710 4.95e-33

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 136.81  E-value: 4.95e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1212 GEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYV 1291
Cdd:COG1021     24 GETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPV 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1292 -ALdagnPTQR---LAQTLRDCGARLVLCEDDCSALD-----------LMGVQHARIDAAQEEAQREQHLRA---PHALP 1353
Cdd:COG1021    104 fAL----PAHRraeISHFAEQSEAVAYIIPDRHRGFDyralarelqaeVPSLRHVLVVGDAGEFTSLDALLAapaDLSEP 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1354 AVDPRSAAYVIYTSGSSGAPKGVVIAHgalTNYV-----DAVLARLDPppRARFAMVSTIG--ADLGHTVLFGALASGGA 1426
Cdd:COG1021    180 RPDPDDVAFFQLSGGTTGLPKLIPRTH---DDYLysvraSAEICGLDA--DTVYLAALPAAhnFPLSSPGVLGVLYAGGT 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1427 LHLIDrdtTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADA-LPAHTLVLGGEAtswELLDTIAA-LRP--DCRV 1502
Cdd:COG1021    255 VVLAP---DPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYdLSSLRVLQVGGA---KLSPELARrVRPalGCTL 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1503 HNHYG-------------PTETTVGilTQpaaqacraaatlplGRPL-DNNETWLLDEHLNPVGTGGTGELYLGGAGVAL 1568
Cdd:COG1021    329 QQVFGmaeglvnytrlddPEEVILT--TQ--------------GRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIR 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1569 GYLHQPALTAARFVPHPFaagarlYRSGDRARRLADGSLEYLGRIDDQVkIRGyrvepGE-IAAR-----LKALDGVRDA 1642
Cdd:COG1021    393 GYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkIAAEevenlLLAHPAVHDA 460
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850 1643 AVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSALAR 1710
Cdd:COG1021    461 AVVAMPdeylGERSCAFVVPRGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
730-1171 1.20e-32

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 133.34  E-value: 1.20e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  730 ISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYAPRTEAAAPlaWAH 809
Cdd:cd19536      4 LSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVP--VTE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  810 VDLSDLgdideHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLM-LALHHIATDGWSMQLLVEELVDGYRA 888
Cdd:cd19536     82 LDLTPL-----EEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  889 ALDGATthgEAQAKAKtriTYADYAAWQRRWLASDAAARqlaYWRAALAD-DAPPLALPYDhtatdtaSENADPRAAARV 967
Cdd:cd19536    157 LLEYKP---LSLPPAQ---PYRDFVAHERASIQQAASER---YWREYLAGaTLATLPALSE-------AVGGGPEQDSEL 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  968 AFALPAPLAQavRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPET--HDVIGFFVNTLVLHSDCEAA 1045
Cdd:cd19536    221 LVSVPLPVRS--RSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTgaERLLGLFLNTLPLRVTLSEE 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1046 TplaslFSQLRQRTLDaQANQALPFD-VLVEHLRPARDAQhgPLFETSFNYLSDDYPALARWPG---ARAERVEIAETHV 1121
Cdd:cd19536    299 T-----VEDLLKRAQE-QELESLSHEqVPLADIQRCSEGE--PLFDSIVNFRHFDLDFGLPEWGsdeGMRRGLLFSEFKS 370
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1122 KVPLALDLrESRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAFAHAL 1171
Cdd:cd19536    371 NYDVNLSV-LPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
87-510 2.15e-32

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 135.51  E-value: 2.15e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   87 YVSAFFGCLYAGVVAV---PVYPPESKREQ---HLAR-----------LRGIARDAGVRYVLT---TAA--LHERHA--- 141
Cdd:PRK05605    95 HIVAFYAVLRLGAVVVehnPLYTAHELEHPfedHGARvaivwdkvaptVERLRRTTPLETIVSvnmIAAmpLLQRLAlrl 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  142 ---------DAWSMLAPGAdvVAVDTL--DARDTPSDAPLHP-VRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQ 209
Cdd:PRK05605   175 pipalrkarAALTGPAPGT--VPWETLvdAAIGGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGK 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  210 A---GLGVRPdDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMsPQYflERPLrWLDAIARHRGTISGAPDFAYrlcaER 286
Cdd:PRK05605   253 AwvpGLGDGP-ERVLAALPMFHAYGLTLCLTLAVSIGGELVLL-PAP--DIDL-ILDAMKKHPPTWLPGVPPLY----EK 323
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  287 INDETRAK-LDLSSWRLAFSGSEPVRRDTLDDFVArfAPAGFdaaaLYPCYGLAEATLFVTG----GVRGAGLVSHAFSS 361
Cdd:PRK05605   324 IAEAAEERgVDLSGVRNAFSGAMALPVSTVELWEK--LTGGL----LVEGYGLTETSPIIVGnpmsDDRRPGYVGVPFPD 397
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  362 AalsagraeaaradeaatvlvgcgavqaghrvaivaraaaeshESHEADVETETsragERLADGRIGEIHVSGPSVAHGY 441
Cdd:PRK05605   398 T------------------------------------------EVRIVDPEDPD----ETMPDGEEGELLVRGPQVFKGY 431
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  442 WQRADASAQAFVDAprhadgsgparWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PRK05605   432 WNRPEETAKSFLDG-----------WFRTGDVVVMEeDGFIRIVDRIKELIITGGFNVYPAEVEEVLREH 490
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
31-510 2.75e-32

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 132.76  E-value: 2.75e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIVidadGDTRYDYAQLDRRARALAARFARDGAAAERA-LILMDSGVDYVSAFFGCLYAGVVAVPV---YP 106
Cdd:cd05945      1 AAANPDRPAVVE----GGRTLTYRELKERADALAAALASLGLDAGDPvVVYGHKSPDAIAAFLAALKAGHAYVPLdasSP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  107 PEskreqhlaRLRGIARDAGvryvlttaalherhadawsmlapgADVVAVDtldardtpsdaplhpvrADDLAFLQYTSG 186
Cdd:cd05945     77 AE--------RIREILDAAK------------------------PALLIAD-----------------GDDNAYIIFTSG 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  187 STGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHD---MGLIGSLLqpvfSGIPLVLMSPQyFLERPLRWLD 263
Cdd:cd05945    108 STGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDlsvMDLYPALA----SGATLVPVPRD-ATADPKQLFR 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  264 AIARHRGTI-SGAPDFAyRLCAErinDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFaPAgfdaAALYPCYGLAEAT 342
Cdd:cd05945    183 FLAEHGITVwVSTPSFA-AMCLL---SPTFTPESLPSLRHFLFCGEVLPHKTARALQQRF-PD----ARIYNTYGPTEAT 253
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  343 LFVTggvrgaglvSHAFSSAALSAgraeaaradeAATVLVGcgavqaghrvaivaraaaESHESHEADVETEtsrAGERL 422
Cdd:cd05945    254 VAVT---------YIEVTPEVLDG----------YDRLPIG------------------YAKPGAKLVILDE---DGRPV 293
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  423 ADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHadgsgpaRWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQ 501
Cdd:cd05945    294 PPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQ-------RAYRTGDLVRLeADGLLFYRGRLDFQVKLNGYRIELE 366

                   ....*....
gi 1888712850  502 DVEQAVEAH 510
Cdd:cd05945    367 EIEAALRQV 375
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
1227-1706 4.05e-32

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 133.21  E-value: 4.05e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVI--DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQ 1304
Cdd:cd05926      1 PDAPALVvpGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1305 TLRDCGARLVLCEDDCSALDLMGVQH---ARIDAAQEEAQREQHLRA------------PHALPAVDPRSAAYVIYTSGS 1369
Cdd:cd05926     81 YLADLGSKLVLTPKGELGPASRAASKlglAILELALDVGVLIRAPSAeslsnlladkknAKSEGVPLPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1370 SGAPKGVVIAHGALTNYVDAVLA--RLDPPPRARFAMvstigaDLGH-----TVLFGALASGGALHLIDRdttLDADRFA 1442
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNtyKLTPDDRTLVVM------PLFHvhglvASLLSTLAAGGSVVLPPR---FSASTFW 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1443 QTLAAARIDVLKIVPGHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAAL--RPDCRVHNHYGPTETTVGILTQPA 1520
Cdd:cd05926    232 PDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALeaTFGAPVLEAYGMTEAAHQMTSNPL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1521 AQACRAAATLplGRPlDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlYRSGDRAR 1600
Cdd:cd05926    312 PPGPRKPGSV--GKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGY 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1601 RLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAAL 1676
Cdd:cd05926    383 LDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPdekyGEEVAAAVVLREGASVTEEELRAFCRKH 462
                          490       500       510
                   ....*....|....*....|....*....|
gi 1888712850 1677 LPDYMVPSVLRVIDALPLNRNGKLDRQALS 1706
Cdd:cd05926    463 LAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
35-590 4.06e-32

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 132.43  E-value: 4.06e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   35 PEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFFGCLYAGVVAVPV---YPPEsk 110
Cdd:cd17643      1 PEAVAVV----DEDRRLTYGELDARANRLARTLRAEGVGPGdRVALALPRSAELIVALLAILKAGGAYVPIdpaYPVE-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  111 reqhlaRLRGIARDAGVRYVLTtaalherhadawsmlapgadvvavdtldardtpsdaplhpvRADDLAFLQYTSGSTGS 190
Cdd:cd17643     75 ------RIAFILADSGPSLLLT-----------------------------------------DPDDLAYVIYTSGSTGR 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  191 PKGVMVSHGNLLANEIAIQAGLGVRPDDVFVswlpLYHDMG-------LIGSLLqpvfSGIPLVLMsPQYFLERPLRWLD 263
Cdd:cd17643    108 PKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdfsvweIWGALL----HGGRLVVV-PYEVARSPEDFAR 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  264 AIARHRGTISGAPDFAYRLCAERINDETRAKLDLsswRLAFSGSEPVRRDTLDDFVARFapaGFDAAALYPCYGLAEATL 343
Cdd:cd17643    179 LLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLAL---RYVIFGGEALEAAMLRPWAGRF---GLDRPQLVNMYGITETTV 252
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  344 FVTggvrgaglvSHAFSSAALSAGRAeaaradeaatVLVGCGAVQAGHrvaivaraaaeshesHEADvetetsRAGERLA 423
Cdd:cd17643    253 HVT---------FRPLDAADLPAAAA----------SPIGRPLPGLRV---------------YVLD------ADGRPVP 292
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  424 DGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPrhaDGSGPARWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQD 502
Cdd:cd17643    293 PGVVGELYVSGAGVARGYLGRPELTAERFVANP---FGGPGSRMYRTGDLArRLPDGELEYLGRADEQVKIRGFRIELGE 369
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  503 VEQAVEAHAEFarkgRVIAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDACgeTPAAIALLNpgALPKTS 582
Cdd:cd17643    370 IEAALATHPSV----RDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYM--VPARYVPLD--ALPLTV 441

                   ....*...
gi 1888712850  583 SGKLQRAA 590
Cdd:cd17643    442 NGKLDRAA 449
PRK07788 PRK07788
acyl-CoA synthetase; Validated
1156-1705 5.52e-32

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 133.90  E-value: 5.52e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1156 MAAQYLRAVEAFAHALGDrsadMTDAAAptlatLDLLDADERARvSAASVARRTPPGEPIHLRVARHadtqPDAPAVIDG 1235
Cdd:PRK07788     6 SVSGYLTRGSAEAHYLRV----MIRSGA-----VDLERPDNGLR-LAADIRRYGPFAGLVAHAARRA----PDRAALIDE 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1236 ALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVL 1315
Cdd:PRK07788    72 RGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1316 CEDDCSAL-----DLMGVQHARIDAAQEEAQREQHLR---------APHALPAVdPRSAAYVIYTSGSSGAPKGVVIAHG 1381
Cdd:PRK07788   152 YDDEFTDLlsalpPDLGRLRAWGGNPDDDEPSGSTDEtlddliagsSTAPLPKP-PKPGGIVILTSGTTGTPKGAPRPEP 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1382 ALTNYVDAVLARLdpPPRARFAMVstIGADLGHTVLFGALASGGALhlidRDTTLDADRF--AQTLAAA---RIDVLKIV 1456
Cdd:PRK07788   231 SPLAPLAGLLSRV--PFRAGETTL--LPAPMFHATGWAHLTLAMAL----GSTVVLRRRFdpEATLEDIakhKATALVVV 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1457 PGHLHALLqaERAADALPAHTL------VLGGEATSWELLD-TIAALRPdcRVHNHYGPTETTVGILTQPAAQACRAAAt 1529
Cdd:PRK07788   303 PVMLSRIL--DLGPEVLAKYDTsslkiiFVSGSALSPELATrALEAFGP--VLYNLYGSTEVAFATIATPEDLAEAPGT- 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1530 lpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHqpaltaarfVPHPFAAGArLYRSGDRARRLADGSLEY 1609
Cdd:PRK07788   378 --VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD---------GRDKQIIDG-LLSSGDVGYFDEDGLLFV 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1610 LGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPDYMVPSV 1685
Cdd:PRK07788   446 DGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDdeefGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRD 525
                          570       580
                   ....*....|....*....|
gi 1888712850 1686 LRVIDALPLNRNGKLDRQAL 1705
Cdd:PRK07788   526 VVFLDELPRNPTGKVLKREL 545
PRK08316 PRK08316
acyl-CoA synthetase; Validated
1218-1700 1.16e-31

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 132.36  E-value: 1.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1218 RVARHadtQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGN 1297
Cdd:PRK08316    19 RSARR---YPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 PTQRLAQTLRDCGARLVLCEDDC-----SALDLMGVqhARIDAAQEEAQREQ----------HLRAPHALPAVDPRSA-- 1360
Cdd:PRK08316    96 TGEELAYILDHSGARAFLVDPALaptaeAALALLPV--DTLILSLVLGGREApggwldfadwAEAGSVAEPDVELADDdl 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1361 AYVIYTSGSSGAPKGVVIAHGALT-NYVDAVLA-RLDPPPRARFAMVSTIGADLgHTVLFGALASGGALHLIDRDttlDA 1438
Cdd:PRK08316   174 AQILYTSGTESLPKGAMLTHRALIaEYVSCIVAgDMSADDIPLHALPLYHCAQL-DVFLGPYLYVGATNVILDAP---DP 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1439 DRFAQTLAAARIDVLKIVP-------GH-------LHALLQAERAADALPAhtlvlggeatswELLDTIAALRPDCRVHN 1504
Cdd:PRK08316   250 ELILRTIEAERITSFFAPPtvwisllRHpdfdtrdLSSLRKGYYGASIMPV------------EVLKELRERLPGLRFYN 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1505 HYGPTE----TTVgilTQPAAQACRAAATlplGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAAr 1580
Cdd:PRK08316   318 CYGQTEiaplATV---LGPEEHLRRPGSA---GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAE- 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1581 fvphPFAAGarLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGAR----LAAFA 1656
Cdd:PRK08316   391 ----AFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKwieaVTAVV 464
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1888712850 1657 TPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKL 1700
Cdd:PRK08316   465 VPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
27-590 1.90e-31

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 131.31  E-value: 1.90e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   27 LRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVPV- 104
Cdd:cd17651      1 FERQAARTPDAPALV----AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVaLCARRSAELVVALLAILKAGAAYVPLd 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  105 --YPPEskreqhlaRLRGIARDAGVRYVLTtaalHERHADAwsMLAPGADVVAVDTLDARDTPSDAPLHPVRADDLAFLQ 182
Cdd:cd17651     77 paYPAE--------RLAFMLADAGPVLVLT----HPALAGE--LAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVI 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  183 YTSGSTGSPKGVMVSHGNlLANEIAIQAG-LGVRPDDVFVSWLPLYHDMGligslLQPVFS----GIPLVLMSPQYFLER 257
Cdd:cd17651    143 YTSGSTGRPKGVVMPHRS-LANLVAWQARaSSLGPGARTLQFAGLGFDVS-----VQEIFStlcaGATLVLPPEEVRTDP 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  258 P--LRWLDaiaRHRGTISGAPDFAYRLCAERINDETRAKLDLsswRLAFSGSEPVRRDTLddfvARFAPAGFDAAALYPC 335
Cdd:cd17651    217 PalAAWLD---EQRISRVFLPTVALRALAEHGRPLGVRLAAL---RYLLTGGEQLVLTED----LREFCAGLPGLRLHNH 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  336 YGLAEATlFVTGGVRGAGLVSHafsSAALSAGraeaaradeaaTVLVGCgavqaghrvaivaraaaeshESHEADvetet 415
Cdd:cd17651    287 YGPTETH-VVTALSLPGDPAAW---PAPPPIG-----------RPIDNT--------------------RVYVLD----- 326
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  416 sRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRhadgSGPARWLRTGDLG-FVHDGQLYIAGRVKDLVIVR 494
Cdd:cd17651    327 -AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF----VPGARMYRTGDLArWLPDGELEFLGRADDQVKIR 401
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  495 GRNLYPQDVEQAVEAHAEfARKGRVIAFGATLGGGEtlgLALEIAPRMKKRFAAAQIVETLRRIAFDACgeTPAAIALLN 574
Cdd:cd17651    402 GFRIELGEIEAALARHPG-VREAVVLAREDRPGEKR---LVAYVVGDPEAPVDAAELRAALATHLPEYM--VPSAFVLLD 475
                          570
                   ....*....|....*.
gi 1888712850  575 pgALPKTSSGKLQRAA 590
Cdd:cd17651    476 --ALPLTPNGKLDRRA 489
benz_CoA_lig TIGR02262
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ...
28-594 3.28e-31

benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.


Pssm-ID: 274059 [Multi-domain]  Cd Length: 505  Bit Score: 130.73  E-value: 3.28e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   28 RALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFFGCLYAGVVAVPVYP 106
Cdd:TIGR02262   12 RNVVEGRGGKTAFI----DDISSLSYGELEAQVRRLAAALRRLGVKREeRVLLLMLDGVDFPIAFLGAIRAGIVPVALNT 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  107 PESKREqhlarLRGIARDAGVRYVLTTAAL------------HERHADAWSMLAPGADVVAVDTLDARDTPSDAPLHPvr 174
Cdd:TIGR02262   88 LLTADD-----YAYMLEDSRARVVFVSGALlpvikaalgkspHLEHRVVVGRPEAGEVQLAELLATESEQFKPAATQA-- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  175 aDDLAFLQYTSGSTGSPKGVMVSHGNLLAN-EIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSpqy 253
Cdd:TIGR02262  161 -DDPAFWLYSSGSTGMPKGVVHTHSNPYWTaELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMG--- 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  254 flERPL--RWLDAIARHRGTI-SGAPD-FAYRLCAERINDETRAKLdlsswRLAFSGSEPVRRDTLDDFVARFapaGFDa 329
Cdd:TIGR02262  237 --ERPTpdAVFDRLRRHQPTIfYGVPTlYAAMLADPNLPSEDQVRL-----RLCTSAGEALPAEVGQRWQARF---GVD- 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  330 aalypcyglaeatlfVTGGVrGAGLVSHAFSSAAlsagraeaaradeaatvlvgCGAVQAGHRVAIVARAAAESheshea 409
Cdd:TIGR02262  306 ---------------IVDGI-GSTEMLHIFLSNL--------------------PGDVRYGTSGKPVPGYRLRL------ 343
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  410 dveteTSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVdaprhadgsGParWLRTGDLGFVHDGQLYI-AGRVK 488
Cdd:TIGR02262  344 -----VGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQ---------GE--WTRSGDKYVRNDDGSYTyAGRTD 407
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  489 DLVIVRGRNLYPQDVEQAVEAHAEfarkgrvIAFGATLGGGETLGLaleIAPR----MKKRFAAAQivETLRRIAFDACG 564
Cdd:TIGR02262  408 DMLKVSGIYVSPFEIESALIQHPA-------VLEAAVVGVADEDGL---IKPKafvvLRPGQTALE--TELKEHVKDRLA 475
                          570       580       590
                   ....*....|....*....|....*....|..
gi 1888712850  565 --ETPAAIALLNpgALPKTSSGKLQRAATREG 594
Cdd:TIGR02262  476 pyKYPRWIVFVD--DLPKTATGKIQRFKLREG 505
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
75-592 3.76e-31

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 129.12  E-value: 3.76e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVpVYPPESKREQHLArlrgIARDAGVRYVLTTAalherhadawsmlapgadvv 154
Cdd:cd05919     36 DRVLLLMLDSPELVQLFLGCLARGAIAV-VINPLLHPDDYAY----IARDCEARLVVTSA-------------------- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  155 avdtldardtpsdaplhpvraDDLAFLQYTSGSTGSPKGVMVSHGNLL--ANEIAIQAgLGVRPDDVFVSWLPLYHDMGL 232
Cdd:cd05919     91 ---------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAREA-LGLTPGDRVFSSAKMFFGYGL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  233 IGSLLQPVFSGIPLVLMSPQyflERPLRWLDAIARHRGTI-SGAPDFAYRLCAERiNDETRAkldLSSWRLAFSGSEPVR 311
Cdd:cd05919    149 GNSLWFPLAVGASAVLNPGW---PTAERVLATLARFRPTVlYGVPTFYANLLDSC-AGSPDA---LRSLRLCVSAGEALP 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  312 RDTLDDFVARFapaGFDaaalypcyglaeatlfVTGGVrGAGLVSHAFSSAALsagraeaaradeaatvlvgcGAVQAGh 391
Cdd:cd05919    222 RGLGERWMEHF---GGP----------------ILDGI-GATEVGHIFLSNRP--------------------GAWRLG- 260
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  392 rvaiVARAAAESHESHEADvetetsRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTG 471
Cdd:cd05919    261 ----STGRPVPGYEIRLVD------EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-----------WYRTG 319
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  472 DLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFArKGRVIAFGATLGGGETLGLALEIAPRMKKRFAAAQ 550
Cdd:cd05919    320 DKFCRdADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVA-EAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARD 398
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1888712850  551 IVETLR-RIAFDACgetPAAIALLNpgALPKTSSGKLQRAATR 592
Cdd:cd05919    399 IHRHLLeRLSAHKV---PRRIAFVD--ELPRTATGKLQRFKLR 436
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
35-590 3.93e-31

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 130.08  E-value: 3.93e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   35 PEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAA-AERALILMDSGVDYVSAFFGCLYAGVVAVPVYPpeskrEQ 113
Cdd:cd12114      1 PDATAVI----CGDGTLTYGELAERARRVAGALKAAGVRpGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDI-----DQ 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  114 HLARLRGIARDAGVRYVLTTaalherhaDAWSMLAPGADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKG 193
Cdd:cd12114     72 PAARREAILADAGARLVLTD--------GPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKG 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  194 VMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGlIGSLLQPVFSGIPLVLMSPQyflER--PLRWLDAIARHRGT 271
Cdd:cd12114    144 VMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLS-VYDIFGALSAGATLVLPDEA---RRrdPAHWAELIERHGVT 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  272 I-SGAPDFAYRLCAERINDETRakldLSSWRLA-FSGsepvrrdtldDFVARFAPAGFDAAAlypcyglAEATLFVTGGV 349
Cdd:cd12114    220 LwNSVPALLEMLLDVLEAAQAL----LPSLRLVlLSG----------DWIPLDLPARLRALA-------PDARLISLGGA 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  350 RGAGLVSHAfssaalsagraeaaradeaatvlvgcgavqaghrvaivaraaaesHESHEADVETET-------------- 415
Cdd:cd12114    279 TEASIWSIY---------------------------------------------HPIDEVPPDWRSipygrplanqryrv 313
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  416 -SRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDaprHADGsgpARWLRTGDLG-FVHDGQLYIAGRVKDLVIV 493
Cdd:cd12114    314 lDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVT---HPDG---ERLYRTGDLGrYRPDGTLEFLGRRDGQVKV 387
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  494 RGRNLYPQDVEQAVEAHAEFARkgrviAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDACGETPAAIALl 573
Cdd:cd12114    388 RGYRIELGEIEAALQAHPGVAR-----AVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIAL- 461
                          570
                   ....*....|....*..
gi 1888712850  574 npGALPKTSSGKLQRAA 590
Cdd:cd12114    462 --EALPLTANGKVDRAA 476
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
1215-1705 3.30e-30

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 127.63  E-value: 3.30e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1215 IHLRVARHADTQPDAPAVID--GALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVA 1292
Cdd:cd05923      3 VFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1293 LDAGNPTQRLAQTLRDCGARLVLCEDDCSALDLMGVQHARIDA-AQEEAQREQHLRAPH-ALPAVDPRSAAYVIYTSGSS 1370
Cdd:cd05923     83 INPRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLAlSDLVGLGEPESAGPLiEDPPREPEQPAFVFYTSGTT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1371 GAPKGVVIAHGALTnyvdavlarldppPRARFaMVSTIGADLG------------HT-----VLFGALASGGALHLIDRD 1433
Cdd:cd05923    163 GLPKGAVIPQRAAE-------------SRVLF-MSTQAGLRHGrhnvvlglmplyHVigffaVLVAALALDGTYVVVEEF 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1434 TTLDAdrfAQTLAAARIDVLKIVPGHLHALLQAERAA--DALPAHTLVLGGEATSWELLDTIAALRPDCRVhNHYGPTET 1511
Cdd:cd05923    229 DPADA---LKLIEQERVTSLFATPTHLDALAAAAEFAglKLSSLRHVTFAGATMPDAVLERVNQHLPGEKV-NIYGTTEA 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1512 TVGILTQPAAQACRaaatlplGRPLDNNETWLL-----DEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVphpf 1586
Cdd:cd05923    305 MNSLYMRDARTGTE-------MRPGFFSEVRIVriggsPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKKLQ---- 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1587 aagARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGA 1662
Cdd:cd05923    374 ---DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVAderwGQSVTACVVPREGT 450
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1888712850 1663 SLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:cd05923    451 LSADELDQFCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
1212-1705 9.35e-30

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 125.90  E-value: 9.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1212 GEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYV 1291
Cdd:cd05920     14 DEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1292 -ALdagnPTQRLAQTLRDC---GARLVLCEDdcsaldlmgvQHARIDaAQEEAQREQhlrapHALPAVdprsaAYVIYTS 1367
Cdd:cd05920     94 lAL----PSHRRSELSAFCahaEAVAYIVPD----------RHAGFD-HRALARELA-----ESIPEV-----ALFLLSG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1368 GSSGAPKGVVIAHGALTNYVDAV--LARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDAdrFAqTL 1445
Cdd:cd05920    149 GTTGTPKLIPRTHNDYAYNVRASaeVCGLDQDTVYLAVLPAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAA--FP-LI 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1446 AAARIDVLKIVPGHLHALLQA-ERAADALPAHTLVLGGEAtswELLDTIAALRP---DCRVHNHYGPTETTVGiLTQPAA 1521
Cdd:cd05920    226 EREGVTVTALVPALVSLWLDAaASRRADLSSLRLLQVGGA---RLSPALARRVPpvlGCTLQQVFGMAEGLLN-YTRLDD 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1522 QACRAAATlpLGRPLD-NNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlYRSGDRAR 1600
Cdd:cd05920    302 PDEVIIHT--QGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVR 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1601 RLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAAL 1676
Cdd:cd05920    374 RTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPdellGERSCAFVVLRDPPPSAAQLRRFLRERG 453
                          490       500
                   ....*....|....*....|....*....
gi 1888712850 1677 LPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:cd05920    454 LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
1238-1700 1.34e-29

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 124.42  E-value: 1.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1238 RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCE 1317
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1318 DDCSALDlmgvqharidaaqeeaqreqhlraphalPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPP 1397
Cdd:cd05903     81 ERFRQFD----------------------------PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1398 PRARFAMVSTIGADLGHT-VLFGALASGGALHLIDRdttLDADRFAQTLAAARIDVLKIVPGHLHALLQA-ERAADALPA 1475
Cdd:cd05903    133 PGDVFLVASPMAHQTGFVyGFTLPLLLGAPVVLQDI---WDPDKALALMREHGVTFMMGATPFLTDLLNAvEEAGEPLSR 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1476 HTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTvGILTQPAAQACRAAATLPlGRPLDNNETWLLDEHLNPVGTGG 1555
Cdd:cd05903    210 LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECP-GAVTSITPAPEDRRLYTD-GRPLPGVEIKVVDDTGATLAPGV 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1556 TGELYLGGAGVALGYLHQPALTAArfvphpfAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKA 1635
Cdd:cd05903    288 EGELLSRGPSVFLGYLDRPDLTAD-------AAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLG 360
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1636 LDGVRDAAVIVVAGARL----AAFATPQPGASLDAAALKRA-LAALLPDYMVPSVLRVIDALPLNRNGKL 1700
Cdd:cd05903    361 HPGVIEAAVVALPDERLgeraCAVVVTKSGALLTFDELVAYlDRQGVAKQYWPERLVHVDDLPRTPSGKV 430
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
176-588 4.15e-29

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 121.23  E-value: 4.15e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  176 DDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQYfl 255
Cdd:cd05917      2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSF-- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  256 eRPLRWLDAIARHRGT-ISGAPDFayrLCAErINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARfapagFDAAALYP 334
Cdd:cd05917     80 -DPLAVLEAIEKEKCTaLHGVPTM---FIAE-LEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEV-----MNMKDVTI 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  335 CYGLAEATLFVTGGVRGAGLVSHAFSsaalsagraeaaradeaatvlVGCgavqaghrvaivaraAAESHESHEADVETe 414
Cdd:cd05917    150 AYGMTETSPVSTQTRTDDSIEKRVNT---------------------VGR---------------IMPHTEAKIVDPEG- 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  415 tsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFvdaprhadgsGPARWLRTGDLGFVH-DGQLYIAGRVKDLVIV 493
Cdd:cd05917    193 ----GIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAI----------DGDGWLHTGDLAVMDeDGYCRIVGRIKDMIIR 258
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  494 RGRNLYPQDVEQAVEAHAEFA----------RKGRVI-AFgatlgggetlglaleIAPRMKKRFAAAQIVETLR-RIA-F 560
Cdd:cd05917    259 GGENIYPREIEEFLHTHPKVSdvqvvgvpdeRYGEEVcAW---------------IRLKEGAELTEEDIKAYCKgKIAhY 323
                          410       420
                   ....*....|....*....|....*...
gi 1888712850  561 DAcgetPAAIalLNPGALPKTSSGKLQR 588
Cdd:cd05917    324 KV----PRYV--FFVDEFPLTVSGKIQK 345
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
1221-1661 6.58e-29

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 124.27  E-value: 6.58e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1221 RHADTQPDAPAVI------DGALRMSYAELDARAAHVAQWLLARDLQGgEPVAIVAHRSARFVVAMLGVLKAGGAYVALD 1294
Cdd:cd05931      1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVGKPG-DRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1295 AGNPTQ---RLAQTLRDCGARLVLCEDDCSAL---DLMGVQHARIDAAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSG 1368
Cdd:cd05931     80 PPTPGRhaeRLAAILADAGPRVVLTTAAALAAvraFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1369 SSGAPKGVVIAHGALTNYVDAVLARLDPPPRARfaMVSTIGA--DLG-HTVLFGALASGGALHLID-------------- 1431
Cdd:cd05931    160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDV--VVSWLPLyhDMGlIGGLLTPLYSGGPSVLMSpaaflrrplrwlrl 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1432 ----RDTTLDADRFAQTLAAARIDVLKIVPGHLHALlqaeraadalpaHTLVLGGEATSWELLDTIAA------LRPDCr 1501
Cdd:cd05931    238 isryRATISAAPNFAYDLCVRRVRDEDLEGLDLSSW------------RVALNGAEPVRPATLRRFAEafapfgFRPEA- 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1502 VHNHYGPTETTV----GILTQPAAQACRAAATLP------------------LGRPLDnnETWLL---DEHLNPVGTGGT 1556
Cdd:cd05931    305 FRPSYGLAEATLfvsgGPPGTGPVVLRVDRDALAgravavaaddpaarelvsCGRPLP--DQEVRivdPETGRELPDGEV 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1557 GELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRArRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKAL 1636
Cdd:cd05931    383 GEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEA 461
                          490       500
                   ....*....|....*....|....*
gi 1888712850 1637 DGVRDAavivvagARLAAFATPQPG 1661
Cdd:cd05931    462 HPALRP-------GCVAAFSVPDDG 479
PRK08316 PRK08316
acyl-CoA synthetase; Validated
17-510 9.52e-29

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 123.50  E-value: 9.52e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   17 AVPAHGLAARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAA-ERALILMDSGVDYVSAFFGCL 95
Cdd:PRK08316     7 RARRQTIGDILRRSARRYPDKTALV----FGDRSWTYAELDAAVNRVAAALLDLGLKKgDRVAALGHNSDAYALLWLACA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   96 YAGVVAVPV----YPPEskreqhlarLRGIARDAGVRYVLTTAALHERHADA----------WSMLAPGADVVA--VDTL 159
Cdd:PRK08316    83 RAGAVHVPVnfmlTGEE---------LAYILDHSGARAFLVDPALAPTAEAAlallpvdtliLSLVLGGREAPGgwLDFA 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  160 DARDTPSDAPLHP-VRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQ 238
Cdd:PRK08316   154 DWAEAGSVAEPDVeLADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGP 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  239 PVFSGIPLVLM-SPQyflerPLRWLDAIARHRGT-----------ISGAPDFAYRlcaerindetraklDLSSWRLAFSG 306
Cdd:PRK08316   234 YLYVGATNVILdAPD-----PELILRTIEAERITsffapptvwisLLRHPDFDTR--------------DLSSLRKGYYG 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  307 SEPVRRDTLDDFVARFAPAGFdaaalYPCYGLAE-ATLfvtggvrgaglvshafssaalsagraeaaradeaATVLvgcg 385
Cdd:PRK08316   295 ASIMPVEVLKELRERLPGLRF-----YNCYGQTEiAPL----------------------------------ATVL---- 331
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  386 avqaghrvaivaraAAESHESHEA-------DVETE-TSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFvdapr 457
Cdd:PRK08316   332 --------------GPEEHLRRPGsagrpvlNVETRvVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF----- 392
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1888712850  458 hADGsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PRK08316   393 -RGG-----WFHSGDLGVMdEEGYITVVDRKKDMIKTGGENVASREVEEALYTH 440
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
1196-1700 4.25e-28

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 122.30  E-value: 4.25e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1196 ERARVSAASVARRTPPGEPIHL---RVARHADTQPDAPAVI-DGAL-----RMSYAELDARAAHVAQWLLARDLQGGEPV 1266
Cdd:cd17634     33 KNTSFAPGAPSIKWFEDATLNLaanALDRHLRENGDRTAIIyEGDDtsqsrTISYRELHREVCRFAGTLLDLGVKKGDRV 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1267 AIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCED----------------DCSALDLMGVQH 1330
Cdd:cd17634    113 AIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvplkknvdDALNPNVTSVEH 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1331 ARI----------DAAQEEAQREQHLRAP--HALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARL-DPP 1397
Cdd:cd17634    193 VIVlkrtgsdidwQEGRDLWWRDLIAKASpeHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVfDYG 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1398 PRARFAMVSTIGADLGHT-VLFGALASGGALHLID-RDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAEraADALPA 1475
Cdd:cd17634    273 PGDIYWCTADVGWVTGHSyLLYGPLACGATTLLYEgVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAG--DDAIEG 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1476 HTL----VLGGEATSWE------LLDTIAALRpdCRVHNHYGPTETTVGILTqPAAQACRAAATLPLgRPLDNNETWLLD 1545
Cdd:cd17634    351 TDRsslrILGSVGEPINpeayewYWKKIGKEK--CPVVDTWWQTETGGFMIT-PLPGAIELKAGSAT-RPVFGVQPAVVD 426
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1546 EHLNPVGTGGTGELYLGGA--GVALGYLHQPAltaaRFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYR 1623
Cdd:cd17634    427 NEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHR 502
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1624 VEPGEIAARLKALDGVRDAAVI----VVAGARLAAFATPQPGASLDAAALKRALAALLPDY---MVPSVLRVIDALPLNR 1696
Cdd:cd17634    503 LGTAEIESVLVAHPKVAEAAVVgiphAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIgplATPDVVHWVDSLPKTR 582

                   ....
gi 1888712850 1697 NGKL 1700
Cdd:cd17634    583 SGKI 586
PRK09274 PRK09274
peptide synthase; Provisional
23-559 5.49e-28

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 121.54  E-value: 5.49e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIV---IDADGDTRY---DYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCL 95
Cdd:PRK09274     8 IARHLPRAAQERPDQLAVAVpggRGADGKLAYdelSFAELDARSDAIAHGLNAAGiGRGMRAVLMVTPSLEFFALTFALF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   96 YAGVVAVPVYPPESKR------------------EQHLAR-LRGIARDaGVRYVLTTAalherHADAWSMlapgadvVAV 156
Cdd:PRK09274    88 KAGAVPVLVDPGMGIKnlkqclaeaqpdafigipKAHLARrLFGWGKP-SVRRLVTVG-----GRLLWGG-------TTL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  157 DTLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLyhdMGLIGSL 236
Cdd:PRK09274   155 ATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL---FALFGPA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  237 LqpvfsGIPLVLmsPQYFLERPL-----RWLDAIARHR-GTISGAPdfAYrlcAERINDETRAK-LDLSSWRLAFSGSEP 309
Cdd:PRK09274   232 L-----GMTSVI--PDMDPTRPAtvdpaKLFAAIERYGvTNLFGSP--AL---LERLGRYGEANgIKLPSLRRVISAGAP 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  310 VRRDTLDDFVARFAPagfDAAALYPcYGLAEA----------TLFVTGGV--RGAG-LVSHAFSSA-----ALSAGRAea 371
Cdd:PRK09274   300 VPIAVIERFRAMLPP---DAEILTP-YGATEAlpissiesreILFATRAAtdNGAGiCVGRPVDGVevriiAISDAPI-- 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  372 aradeaatvlvgcgavqaghrvaivaraaaesHESHEAdvetetsragERLADGRIGEIHVSGPSVAHGYWQRADASAQA 451
Cdd:PRK09274   374 --------------------------------PEWDDA----------LRLATGEIGEIVVAGPMVTRSYYNRPEATRLA 411
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  452 FVdaprhADGSGPArWLRTGDLGFVHD-GQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRViafGATLGGGE 530
Cdd:PRK09274   412 KI-----PDGQGDV-WHRMGDLGYLDAqGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALV---GVGVPGAQ 482
                          570       580
                   ....*....|....*....|....*....
gi 1888712850  531 TLGLALEIAPRMKKrfAAAQIVETLRRIA 559
Cdd:PRK09274   483 RPVLCVELEPGVAC--SKSALYQELRALA 509
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
85-593 6.97e-28

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 119.41  E-value: 6.97e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   85 VDYVSAFFGCLYAGVVAVPVYPpeskreqhlarlrgIARDAGVRYVLTTAAlherhadawsmlapgADVVAVDTLDARDT 164
Cdd:cd05903     37 WEFAVLYLACLRIGAVTNPILP--------------FFREHELAFILRRAK---------------AKVFVVPERFRQFD 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  165 PSDAPlhpvraDDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGI 244
Cdd:cd05903     88 PAAMP------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  245 PLVLMSpqyfLERPLRWLDAIARHRGTIS-GAPDFAYRLCaeriNDETRAKLDLSSWRLAFSGSEPVRRDtlddfVARFA 323
Cdd:cd05903    162 PVVLQD----IWDPDKALALMREHGVTFMmGATPFLTDLL----NAVEEAGEPLSRLRTFVCGGATVPRS-----LARRA 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  324 PAGFdAAALYPCYGLAEatlfvtggvrgaglVSHAFSSaalsagraeaARADEAATVLVGCGAVQAGhrvaivaraaaes 403
Cdd:cd05903    229 AELL-GAKVCSAYGSTE--------------CPGAVTS----------ITPAPEDRRLYTDGRPLPG------------- 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  404 hesheadVETE-TSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFV-HDGQL 481
Cdd:cd05903    271 -------VEIKvVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEG-----------WFRTGDLARLdEDGYL 332
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  482 YIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEF----------ARKG-RVIAFgATLGGGETLGLALEIAPRMKKRFAAAQ 550
Cdd:cd05903    333 RITGRSKDIIIRGGENIPVLEVEDLLLGHPGVieaavvalpdERLGeRACAV-VVTKSGALLTFDELVAYLDRQGVAKQY 411
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1888712850  551 IVETLRRIAfdacgetpaaiallnpgALPKTSSGKLQRAATRE 593
Cdd:cd05903    412 WPERLVHVD-----------------DLPRTPSGKVQKFRLRE 437
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
1361-1709 7.30e-28

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 116.66  E-value: 7.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1361 AYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARfAMVST----IGadlGHTVLFGALASGGALHLIDRDttl 1436
Cdd:cd17630      3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDS-WLLSLplyhVG---GLAILVRSLLAGAELVLLERN--- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1437 daDRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAHTLVL-GGEATSWELLDTIAALRpdCRVHNHYGPTETTVGI 1515
Cdd:cd17630     76 --QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLlGGAPIPPELLERAADRG--IPLYTTYGMTETASQV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1516 LTQPAAQACRAAatlpLGRPLDNNETWLLDEhlnpvgtggtGELYLGGAGVALGYLhqpaltaaRFVPHPFAAGARLYRS 1595
Cdd:cd17630    152 ATKRPDGFGRGG----VGVLLPGRELRIVED----------GEIWVGGASLAMGYL--------RGQLVPEFNEDGWFTT 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1596 GDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASldAAALKR 1671
Cdd:cd17630    210 KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPdeelGQRPVAVIVGRGPAD--PAELRA 287
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1888712850 1672 ALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSALA 1709
Cdd:cd17630    288 WLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
PRK09088 PRK09088
acyl-CoA synthetase; Validated
1219-1714 9.98e-28

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 119.91  E-value: 9.98e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVIDGAL--RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAG 1296
Cdd:PRK09088     1 IAFHARLQPQRLAAVDLALgrRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1297 NPTQRLAQTLRDCGARLVLCEDDCSALDLMGVQHARIDAAQEEAqreqhlrAPHALPAVDPRSAAYVIYTSGSSGAPKGV 1376
Cdd:PRK09088    81 LSASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADAL-------EPADTPSIPPERVSLILFTSGTSGQPKGV 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1377 VIAHGAL--TNYVDAVLARLDppPRARF----AMVSTIGADlghTVLFGALASGGALhlidrdttLDADRFAQTLAAARI 1450
Cdd:PRK09088   154 MLSERNLqqTAHNFGVLGRVD--AHSSFlcdaPMFHIIGLI---TSVRPVLAVGGSI--------LVSNGFEPKRTLGRL 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1451 DVLKIVPGHLHALLQAERAADALPAH---------TLVLGGEATSWEllDTIAALRPDCRVHNHYGPTETTVgILTQPAA 1521
Cdd:PRK09088   221 GDPALGITHYFCVPQMAQAFRAQPGFdaaalrhltALFTGGAPHAAE--DILGWLDDGIPMVDGFGMSEAGT-VFGMSVD 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1522 QACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFvphpfaAGARLYRSGDRARR 1601
Cdd:PRK09088   298 CDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIARR 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1602 LADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGARLA----AFATPQPGASLDAAALKRALAALL 1677
Cdd:PRK09088   372 DADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGevgyLAIVPADGAPLDLERIRSHLSTRL 451
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1888712850 1678 PDYMVPSVLRVIDALPLNRNGKLDRQALSALARPAAP 1714
Cdd:PRK09088   452 AKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
25-590 1.03e-27

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 119.61  E-value: 1.03e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   25 ARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAA-ERALILMDSGVDYVSAFFGCLYAGVVAVP 103
Cdd:cd12117      1 ELFEEQAARTPDAVAVV----YGDRSLTYAELNERANRLARRLRAAGVGPgDVVGVLAERSPELVVALLAVLKAGAAYVP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  104 VYPpeskrEQHLARLRGIARDAGVRYVLTTAALHERhadawsmlaPGADVVAVDTLDARDT-PSDAPLHPVRADDLAFLQ 182
Cdd:cd12117     77 LDP-----ELPAERLAFMLADAGAKVLLTDRSLAGR---------AGGLEVAVVIDEALDAgPAGNPAVPVSPDDLAYVM 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  183 YTSGSTGSPKGVMVSHGNL--LANEiaiQAGLGVRPDDVFVSWLPLYHDMGLI---GSLLqpvfSGIPLVLMSPQyFLER 257
Cdd:cd12117    143 YTSGSTGRPKGVAVTHRGVvrLVKN---TNYVTLGPDDRVLQTSPLAFDASTFeiwGALL----NGARLVLAPKG-TLLD 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  258 PLRWLDAIARHRGTIS--GAPDFayRLCAERINDEtrakldLSSWRLAFSGSEPVRRDTLDDFVARFAPagfdaAALYPC 335
Cdd:cd12117    215 PDALGALIAEEGVTVLwlTAALF--NQLADEDPEC------FAGLRELLTGGEVVSPPHVRRVLAACPG-----LRLVNG 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  336 YGLAEATLFVTggvrgaglvSHAFSSAALSAGRAEAARADEAATVLVgcgavqaghrvaivaraaaeshesheadveteT 415
Cdd:cd12117    282 YGPTENTTFTT---------SHVVTELDEVAGSIPIGRPIANTRVYV--------------------------------L 320
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  416 SRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRhadgSGPARWLRTGDLGFVH-DGQLYIAGRVKDLVIVR 494
Cdd:cd12117    321 DEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF----GPGERLYRTGDLARWLpDGRLEFLGRIDDQVKIR 396
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  495 GRNLYPQDVEQAVEAHAEfARKGRVIAFGATLGGGEtlgLALEIAPRMKKrfAAAQIVETLRRIAFDacGETPAAIALLn 574
Cdd:cd12117    397 GFRIELGEIEAALRAHPG-VREAVVVVREDAGGDKR---LVAYVVAEGAL--DAAELRAFLRERLPA--YMVPAAFVVL- 467
                          570
                   ....*....|....*.
gi 1888712850  575 pGALPKTSSGKLQRAA 590
Cdd:cd12117    468 -DELPLTANGKVDRRA 482
PRK06164 PRK06164
acyl-CoA synthetase; Validated
1218-1713 1.09e-27

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 120.62  E-value: 1.09e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1218 RVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGN 1297
Cdd:PRK06164    15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 PTQRLAQTLRDCGARLVLCEDDCSALDLMGVQHARIDAAQEEAQR-----------------------EQHLRAPHA--- 1351
Cdd:PRK06164    95 RSHEVAHILGRGRARWLVVWPGFKGIDFAAILAAVPPDALPPLRAiavvddaadatpapapgarvqlfALPDPAPPAaag 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1352 LPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLID 1431
Cdd:PRK06164   175 ERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEP 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1432 rdtTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPaHTLVLGGEATSWELLDTIA-ALRPDCRVHNHYGPTE 1510
Cdd:PRK06164   255 ---VFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFP-SARLFGFASFAPALGELAAlARARGVPLTGLYGSSE 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1511 TTVGILTQPAAQACRAAAtLPLGRPLDNNETWLLDEHLNP--VGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaa 1588
Cdd:PRK06164   331 VQALVALQPATDPVSVRI-EGGGRPASPEARVRARDPQDGalLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY-- 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1589 garlYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV---AGARLAAFATPQPGASLD 1665
Cdd:PRK06164   408 ----FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAtrdGKTVPVAFVIPTDGASPD 483
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1888712850 1666 AAALKRALAALLPDYMVPSVLRVIDALPLNRNG--------KLDRQALSALARPAA 1713
Cdd:PRK06164   484 EAGLMAACREALAGFKVPARVQVVEAFPVTESAngakiqkhRLREMAQARLAAERA 539
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
10-510 1.42e-27

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 120.52  E-value: 1.42e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   10 PHGIDTDAVPAHglaARLRALAQQRPEATALIVIDADgdtrYDYAQLDRRARALAARFARDGAA-AERALILMDSGVDYV 88
Cdd:PRK06710    16 PSTISYDIQPLH---KYVEQMASRYPEKKALHFLGKD----ITFSVFHDKVKRFANYLQKLGVEkGDRVAIMLPNCPQAV 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   89 SAFFGCLYAGVVAVPVYPPESKREqhlarLRGIARDAGVRYVLTTAALHERHADAWS---------------------ML 147
Cdd:PRK06710    89 IGYYGTLLAGGIVVQTNPLYTERE-----LEYQLHDSGAKVILCLDLVFPRVTNVQSatkiehvivtriadflpfpknLL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  148 APGAD------VVAVDTLDA----------RDTPSDAPLHPvrADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAG 211
Cdd:PRK06710   164 YPFVQkkqsnlVVKVSESETihlwnsvekeVNTGVEVPCDP--ENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQW 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  212 L--GVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMsPQYFLERPlrwLDAIARHRGTI-SGAPDFAYRLcaerIN 288
Cdd:PRK06710   242 LynCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI-PKFDMKMV---FEAIKKHKVTLfPGAPTIYIAL----LN 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  289 DETRAKLDLSSWRLAFSGSEPVRRDTLDDFvarfapAGFDAAALYPCYGLAEATlfvtggvrgagLVSHA-FSSAALSAG 367
Cdd:PRK06710   314 SPLLKEYDISSIRACISGSAPLPVEVQEKF------ETVTGGKLVEGYGLTESS-----------PVTHSnFLWEKRVPG 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  368 RAEAARADEAATVLvgcgavqaghrvaivaraaaeshesheaDVETetsraGERLADGRIGEIHVSGPSVAHGYWQRADA 447
Cdd:PRK06710   377 SIGVPWPDTEAMIM----------------------------SLET-----GEALPPGEIGEIVVKGPQIMKGYWNKPEE 423
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1888712850  448 SAQAFVDAprhadgsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PRK06710   424 TAAVLQDG-----------WLHTGDVGYMdEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
1240-1707 1.50e-27

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 118.21  E-value: 1.50e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDD 1319
Cdd:cd05972      2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1320 csaldlmgvqharidaaqeeaqreqhlraphalpavDPrsaAYVIYTSGSSGAPKGVVIAHGA-LTNYVDAVLArLDPPP 1398
Cdd:cd05972     82 ------------------------------------DP---ALIYFTSGTTGLPKGVLHTHSYpLGHIPTAAYW-LGLRP 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1399 RARFAMVSTIGADLG-HTVLFGALASGGALHLIDRDTtLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPA-H 1476
Cdd:cd05972    122 DDIHWNIADPGWAKGaWSSFFGPWLLGATVFVYEGPR-FDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHlR 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1477 TLVLGGEATSWELLDTI-AALRPDcrVHNHYGPTETTVGILTQPaaqacraaaTLPL-----GRPLDNNETWLLDEHLNP 1550
Cdd:cd05972    201 LVVSAGEPLNPEVIEWWrAATGLP--IRDGYGQTETGLTVGNFP---------DMPVkpgsmGRPTPGYDVAIIDDDGRE 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1551 VGTGGTGEL--YLGGAGVALGYLHQPALTAARFVphpfaagARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGE 1628
Cdd:cd05972    270 LPPGEEGDIaiKLPPPGLFLGYVGDPEKTEASIR-------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFE 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1629 IAARLKALDGVRDAAVIV----VAGARLAAFATPQPGASLDAAAL---KRALAALLPDYMVPSVLRVIDALPLNRNGKLD 1701
Cdd:cd05972    343 VESALLEHPAVAEAAVVGspdpVRGEVVKAFVVLTSGYEPSEELAeelQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422

                   ....*.
gi 1888712850 1702 RQALSA 1707
Cdd:cd05972    423 RVELRD 428
PRK06178 PRK06178
acyl-CoA synthetase; Validated
3-522 1.71e-27

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 120.15  E-value: 1.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850    3 AAQHIVFPHGIDTDAVPAHG---LAARLRALAQQRPEATALIVIDadgdTRYDYAQLDRRARALAARFARDGAAA-ERAL 78
Cdd:PRK06178    12 ALQQAAWPAGIPREPEYPHGerpLTEYLRAWARERPQRPAIIFYG----HVITYAELDELSDRFAALLRQRGVGAgDRVA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   79 ILMDSGVDYVSAFFGCLYAGVVAVPVYPpeSKREQHLARLRGiarDAGVRYVLTTAAL--------------HERHADAW 144
Cdd:PRK06178    88 VFLPNCPQFHIVFFGILKLGAVHVPVSP--LFREHELSYELN---DAGAEVLLALDQLapvveqvraetslrHVIVTSLA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  145 SMLAPGADVVAVDTLDA---------------RDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQ 209
Cdd:PRK06178   163 DVLPAEPTLPLPDSLRAprlaaagaidllpalRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAY 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  210 A-GLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSpqyflerplRW-----LDAIARHRGTISGAP-DFAyrl 282
Cdd:PRK06178   243 AvAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLA---------RWdavafMAAVERYRVTRTVMLvDNA--- 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  283 cAERINDETRAKLDLSSWRLAFSGSepvrrdtlddFVARfapagfdaaaLYPCYGLAEATLfvTGGV--RGAGLVSHAFS 360
Cdd:PRK06178   311 -VELMDHPRFAEYDLSSLRQVRVVS----------FVKK----------LNPDYRQRWRAL--TGSVlaEAAWGMTETHT 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  361 SAALSAGRAEAARADEAATVLVGC---GAvqaghrvaivaraaaeshESHEADVETetsraGERLADGRIGEIHVSGPSV 437
Cdd:PRK06178   368 CDTFTAGFQDDDFDLLSQPVFVGLpvpGT------------------EFKICDFET-----GELLPLGAEGEIVVRTPSL 424
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  438 AHGYWQRADASAQAFVDAprhadgsgparWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFA-- 514
Cdd:PRK06178   425 LKGYWNKPEATAEALRDG-----------WLHTGDIGkIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLgs 493
                          570
                   ....*....|....*..
gi 1888712850  515 --------RKGRV-IAF 522
Cdd:PRK06178   494 avvgrpdpDKGQVpVAF 510
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
75-510 1.98e-27

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 119.19  E-value: 1.98e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKREqhlarLRGIARDAGVRYVLTTAalhERHADAWSMLAPG--AD 152
Cdd:PRK06839    54 ERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENE-----LIFQLKDSGTTVLFVEK---TFQNMALSMQKVSyvQR 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  153 VVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHdMGL 232
Cdd:PRK06839   126 VISITSLKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFH-IGG 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  233 IGSLLQP-VFSGIPLVLmsPQYFleRPLRWLDAIARHRGTIS-GAPDFAYRLcaerINDETRAKLDLSSWRLAFSGSEPV 310
Cdd:PRK06839   205 IGLFAFPtLFAGGVIIV--PRKF--EPTKALSMIEKHKVTVVmGVPTIHQAL----INCSKFETTNLQSVRWFYNGGAPC 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  311 RRDTLDDFVARFAPAGfdaaalyPCYGLAEA--TLFVtggvrgagLVSHAFSSAALSAGRAEAAradeaatvlvgcgavq 388
Cdd:PRK06839   277 PEELMREFIDRGFLFG-------QGFGMTETspTVFM--------LSEEDARRKVGSIGKPVLF---------------- 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  389 aghrvaivaraaaeshesheADVETeTSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWL 468
Cdd:PRK06839   326 --------------------CDYEL-IDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDG-----------WL 373
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1888712850  469 RTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PRK06839   374 CTGDLArVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKL 416
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
14-780 2.18e-27

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 122.46  E-value: 2.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   14 DTD-AVPAHGLAARLRALAQQRPEATALividADGDTRYDYAQLDRRARALAARFARDGAAAER--ALILMDSgVDYVSA 90
Cdd:PRK10252   450 ATAvEIPETTLSALVAQQAAKTPDAPAL----ADARYQFSYREMREQVVALANLLRERGVKPGDsvAVALPRS-VFLTLA 524
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   91 FFGCLYAGVVAVPV---YPPEskreqhlaRLRGIARDAGVRYVLTTAALHERHADAwsmlaPGADVVAVDTLDARdtPSD 167
Cdd:PRK10252   525 LHAIVEAGAAWLPLdtgYPDD--------RLKMMLEDARPSLLITTADQLPRFADV-----PDLTSLCYNAPLAP--QGA 589
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  168 APLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGlIGSLLQPVFSGIPLV 247
Cdd:PRK10252   590 APLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVS-VWEFFWPFIAGAKLV 668
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  248 LMSPQYFLErPLRWLDAIARHRGTI-------------SGAPDFAYRLCAerindetrakldlsSWRLAFSGSEPVRRDT 314
Cdd:PRK10252   669 MAEPEAHRD-PLAMQQFFAEYGVTTthfvpsmlaafvaSLTPEGARQSCA--------------SLRQVFCSGEALPADL 733
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  315 LDDFVARFapagfdAAALYPCYGLAEATLFVTGgvrgaglvsHAFSSAALSAgraeaaraDEAATVLVGcgavqaghrva 394
Cdd:PRK10252   734 CREWQQLT------GAPLHNLYGPTEAAVDVSW---------YPAFGEELAA--------VRGSSVPIG----------- 779
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  395 ivaraaaeshesheadveTETSRAGERLADGRI--------GEIHVSGPSVAHGYWQRADASAQAFVDAPrHADGSgpaR 466
Cdd:PRK10252   780 ------------------YPVWNTGLRILDARMrpvppgvaGDLYLTGIQLAQGYLGRPDLTASRFIADP-FAPGE---R 837
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  467 WLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKG---RVIAFGATLGGGETLGLALEIAprm 542
Cdd:PRK10252   838 MYRTGDVArWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVthaCVINQAAATGGDARQLVGYLVS--- 914
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  543 kkRFAAAQIVETLRRIAFDACGETPAAIALLNPGALPKTSSGKLQRAAtregwrartldlYALWEQGAFVIGgdddaara 622
Cdd:PRK10252   915 --QSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKA------------LPLPELKAQVPG-------- 972
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  623 pdaPAALDARESALAALWCEALDaRLALAPDAHFFASGGSSLSAARLVALIGARLGRRVALAQIFETPTLAAMAAALAEP 702
Cdd:PRK10252   973 ---RAPKTGTETIIAAAFSSLLG-CDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAE 1048
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  703 EsveeaqDDAQDEAQDnaPIEPAEEA------VISHAQQrqlFAW-------RLDPASRAYHVAAGiRLDGALdreALRQ 769
Cdd:PRK10252  1049 E------DESRRLGFG--TILPLREGdgptlfCFHPASG---FAWqfsvlsrYLDPQWSIYGIQSP-RPDGPM---QTAT 1113
                          810
                   ....*....|.
gi 1888712850  770 SLDRLCERHAA 780
Cdd:PRK10252  1114 SLDEVCEAHLA 1124
PRK05691 PRK05691
peptide synthase; Validated
1833-2221 2.26e-27

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 122.97  E-value: 2.26e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1833 ATPLHALADRSALPLSLMQQRIwVVDQLADRALASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFdADDEGDPV 1912
Cdd:PRK05691  3246 ALPVPAAEIEDVYPLTPMQEGL-LLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASF-SWNAGETM 3323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1913 LKIaprmeVLMPVIEPLAHPDNDANShtnshtNSDENARTQATAQALDDAArtpFDLSRAPLVRATLLRFDAAHHVLIVS 1992
Cdd:PRK05691  3324 LQV-----IHKPGRTPIDYLDWRGLP------EDGQEQRLQALHKQEREAG---FDLLNQPPFHLRLIRVDEARYWFMMS 3389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1993 LHHIVADGGSVHILLDELCELYRAQRDGAPPALAPlAVQYADYAHW-QRARFTpdavrEAQQFWRGYLADAPALLPLSTD 2071
Cdd:PRK05691  3390 NHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPV-PPRYRDYIGWlQRQDLA-----QARQWWQDNLRGFERPTPIPSD 3463
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2072 raRPTRVSHAGAA-------RHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGR--ERAE 2142
Cdd:PRK05691  3464 --RPFLREHAGDSggmvvgdCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQ 3541
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850 2143 LEALIGFFVNVVPLRSRIAADGANlASFDAWLDAARQSTWDALDHRALPFDRIVDALALKRrrdANPLVQVLFVLRDLP 2221
Cdd:PRK05691  3542 MQRTVGLFINSIALRVQLPAAGQR-CSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPK---GQPLFDSLFVFENAP 3616
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
176-504 3.27e-27

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 117.93  E-value: 3.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  176 DDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSpqyfl 255
Cdd:cd05914     89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLD----- 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  256 ERPLRWLDAIARHRGTISGAPDFAYRLCAERINDE------TRAKLDLSSWRLAFSGSEPVRRDTLDDFVARF-----AP 324
Cdd:cd05914    164 KIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIipkltlKKFKFKLAKKINNRKIRKLAFKKVHEAFGGNIkefviGG 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  325 AGFDA---AALYPC-------YGLAEATLFVTGGVRGaglvshafssaalsagraeaaradeaATVLVGCGAVQAGhrva 394
Cdd:cd05914    244 AKINPdveEFLRTIgfpytigYGMTETAPIISYSPPN--------------------------RIRLGSAGKVIDG---- 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  395 ivaraaaeshesHEADVETETSRAGErladgriGEIHVSGPSVAHGYWQRADASAQAFVdaprhADGsgparWLRTGDLG 474
Cdd:cd05914    294 ------------VEVRIDSPDPATGE-------GEIIVRGPNVMKGYYKNPEATAEAFD-----KDG-----WFHTGDLG 344
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1888712850  475 -FVHDGQLYIAGRVKDLVIV-RGRNLYPQDVE 504
Cdd:cd05914    345 kIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIE 376
PRK12467 PRK12467
peptide synthase; Provisional
16-691 3.29e-27

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 122.19  E-value: 3.29e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   16 DAVPAHGLAARL-RALAQQRPEATALIVidadGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFG 93
Cdd:PRK12467  3089 AAYPSERLVHQLiEAQVARTPEAPALVF----GDQQLSYAELNRRANRLAHRLIAIGVGPDVLVgVAVERSVEMIVALLA 3164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   94 CLYAGVVAVPVyPPESKREqhlaRLRGIARDAGVRYVLTTAALHERHAdawsmLAPGADVVAVDTLDARDTPSDAPLHPV 173
Cdd:PRK12467  3165 VLKAGGAYVPL-DPEYPRE----RLAYMIEDSGVKLLLTQAHLLEQLP-----APAGDTALTLDRLDLNGYSENNPSTRV 3234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  174 RADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDmGLIGSLLQPVFSGIPLVLMSPQy 253
Cdd:PRK12467  3235 MGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFD-GAQERFLWTLICGGCLVVRDND- 3312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  254 fLERPLRWLDAIARHRGTISgapDFAYRLCAERINDETRAklDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGfdaaaLY 333
Cdd:PRK12467  3313 -LWDPEELWQAIHAHRISIA---CFPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKLKPRG-----LT 3381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  334 PCYGLAEATLFVTGGVRGAGLVSHAfssaalsagraeaaradeaatvlvgcGAVQAGHRVAIVARAAAEShesheadvet 413
Cdd:PRK12467  3382 NGYGPTEAVVTVTLWKCGGDAVCEA--------------------------PYAPIGRPVAGRSIYVLDG---------- 3425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  414 etsrAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPrhADGSGpARWLRTGDLGFVH-DGQLYIAGRVKDLVI 492
Cdd:PRK12467  3426 ----QLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP--FSGSG-GRLYRTGDLARYRaDGVIEYLGRIDHQVK 3498
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  493 VRGRNLYPQDVEQAVEAHAeFARKGRVIAFGaTLGGGETLGLALEIAPRmkkrfaaAQIVETLRRIAFDACGE--TPAAI 570
Cdd:PRK12467  3499 IRGFRIELGEIEARLLQHP-SVREAVVLARD-GAGGKQLVAYVVPADPQ-------GDWRETLRDHLAASLPDymVPAQL 3569
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  571 ALLNpgALPKTSSGKLQRAAtregwrartLDLYALWEQGAFViggdddaarapdapAALDARESALAALWCEALDaRLAL 650
Cdd:PRK12467  3570 LVLA--AMPLGPNGKVDRKA---------LPDPDAKGSREYV--------------APRSEVEQQLAAIWADVLG-VEQV 3623
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1888712850  651 APDAHFFASGGSSLSAARLVALIGARLGRRVALAQIFETPT 691
Cdd:PRK12467  3624 GVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPT 3664
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
173-588 3.35e-27

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 116.68  E-value: 3.35e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  173 VRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLiGSLLQPVFSGIPLVLMspQ 252
Cdd:cd05912     74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLV--D 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  253 YFLERPLrwLDAIARHRGT-ISGAPDFAYRLCAERINDETrakldlSSWRLAFSGSEPVRRDTLDDFVARFAPagfdaaa 331
Cdd:cd05912    151 KFDAEQV--LHLINSGKVTiISVVPTMLQRLLEILGEGYP------NNLRCILLGGGPAPKPLLEQCKEKGIP------- 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  332 LYPCYGLAE-ATLFVTggvrgaglVSHAFSSAAL-SAGRAEaaradeaatvlvgcgavqaghrvaivaraaaeshesheA 409
Cdd:cd05912    216 VYQSYGMTEtCSQIVT--------LSPEDALNKIgSAGKPL--------------------------------------F 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  410 DVETETSRAGERLADgrIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFV-HDGQLYIAGRVK 488
Cdd:cd05912    250 PVELKIEDDGQPPYE--VGEILLKGPNVTKGYLNRPDATEESFENG-----------WFKTGDIGYLdEEGFLYVLDRRS 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  489 DLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAFGATLGGGETLGLALEiaprmkKRFAAAQIVETLRRIAfdACGETPA 568
Cdd:cd05912    317 DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE------RPISEEELIAYCSEKL--AKYKVPK 388
                          410       420
                   ....*....|....*....|
gi 1888712850  569 AIALLNpgALPKTSSGKLQR 588
Cdd:cd05912    389 KIYFVD--ELPRTASGKLLR 406
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
75-521 5.64e-27

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 117.43  E-value: 5.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKREqhlarLRGIARDAGVRYVLTTAALHErHADAWSM--LAPGAD 152
Cdd:cd05909     32 ENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRE-----LRACIKLAGIKTVLTSKQFIE-KLKLHHLfdVEYDAR 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  153 VVAVDTLDARDTPSD------------------APLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGV 214
Cdd:cd05909    106 IVYLEDLRAKISKADkckaflagkfppkwllriFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDP 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  215 RPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSpqyfleRPL--RWLDAIARHRG-TISGAPDFAYRLCAERINDEt 291
Cdd:cd05909    186 NPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHP------NPLdyKKIPELIYDKKaTILLGTPTFLRGYARAAHPE- 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  292 raklDLSSWRLAFSGSEPVRRDTLDDFVARFapagfdAAALYPCYGLAEAtlfvtggvrgAGLVSHAFSSAALSAGRaea 371
Cdd:cd05909    259 ----DFSSLRLVVAGAEKLKDTLRQEFQEKF------GIRILEGYGTTEC----------SPVISVNTPQSPNKEGT--- 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  372 aradeaatvlVGcgavqaghrvaivarAAAESHESHEADVETetsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQA 451
Cdd:cd05909    316 ----------VG---------------RPLPGMEVKIVSVET-----HEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFA 365
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1888712850  452 FVDAprhadgsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQavEAHAEFARKGRVIA 521
Cdd:cd05909    366 FGDG-----------WYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIED--ILSEILPEDNEVAV 423
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
1194-1719 5.91e-27

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 118.32  E-value: 5.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1194 ADERARVSAASVARRTPPGEPIHLRV-ARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHR 1272
Cdd:PRK06155     1 GEPLGAGLAARAVDPLPPSERTLPAMlARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1273 SARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCED---------DCSALDLMGVQhaRIDAAQEEAQRE 1343
Cdd:PRK06155    81 RIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAallaaleaaDPGDLPLPAVW--LLDAPASVSVPA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1344 QHLRAP-----HALPAVDPRSA--AYVIYTSGSSGAPKGVVIAHGALtnYVDAVLARLDPPPRARFAMVSTIgaDLGHT- 1415
Cdd:PRK06155   159 GWSTAPlppldAPAPAAAVQPGdtAAILYTSGTTGPSKGVCCPHAQF--YWWGRNSAEDLEIGADDVLYTTL--PLFHTn 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1416 ---VLFGALASGGALHLIDRdttLDADRFAQTLAAARIDVLKIVPGHLHALL-QAERAADAlpAHTLVLG-GEATSWELL 1490
Cdd:PRK06155   235 alnAFFQALLAGATYVLEPR---FSASGFWPAVRRHGATVTYLLGAMVSILLsQPARESDR--AHRVRVAlGPGVPAALH 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1491 DTIAAlRPDCRVHNHYGPTETTVGILTQPAAQACRAaatlpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGA---GVA 1567
Cdd:PRK06155   310 AAFRE-RFGVDLLDGYGSTETNFVIAVTHGSQRPGS-----MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFA 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1568 LGYLHQPALTAArfvphpfAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV 1647
Cdd:PRK06155   384 TGYFGMPEKTVE-------AWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPV 456
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1888712850 1648 ----AGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSALARPAAP-HREAA 1719
Cdd:PRK06155   457 pselGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTADTwDREAA 533
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1218-1662 1.26e-26

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 117.89  E-value: 1.26e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1218 RVARHADTQPDAPAVI---DGALR-MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVAL 1293
Cdd:COG1022     16 LLRRRAARFPDRVALRekeDGIWQsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPI 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1294 DAGNPTQRLAQTLRDCGARLVLCED------------DCSAL-------DLMGVQHARIDAAQEEAQREQHLRAPHALP- 1353
Cdd:COG1022     96 YPTSSAEEVAYILNDSGAKVLFVEDqeqldkllevrdELPSLrhivvldPRGLRDDPRLLSLDELLALGREVADPAELEa 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1354 ---AVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAM---VSTIGAdlgHTVLFGALASGGAL 1427
Cdd:COG1022    176 rraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSflpLAHVFE---RTVSYYALAAGATV 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1428 HLIDrdttlDADRFAQTLAAARIDVLKIVP-----------------GHL------HALLQAERAADALPAHTLVLGGEA 1484
Cdd:COG1022    253 AFAE-----SPDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeaGGLkrklfrWALAVGRRYARARLAGKSPSLLLR 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1485 TSWELLDTI--------------------AALRPD-CR--------VHNHYGPTETTVGILTQPAAQACRAAatlpLGRP 1535
Cdd:COG1022    328 LKHALADKLvfsklrealggrlrfavsggAALGPElARffralgipVLEGYGLTETSPVITVNRPGDNRIGT----VGPP 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1536 LDNNEtwlldehlnpVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlYRSGDRARRLADGSLEYLGRIDD 1615
Cdd:COG1022    404 LPGVE----------VKIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELDEDGFLRITGRKKD 467
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1888712850 1616 QVKIR-GYRVEPGEIAARLKALDGVRDAAVIvvaGAR---LAAFATPQPGA 1662
Cdd:COG1022    468 LIVTSgGKNVAPQPIENALKASPLIEQAVVV---GDGrpfLAALIVPDFEA 515
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1880-2209 1.99e-26

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 114.89  E-value: 1.99e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1880 LDAARLQRSLAALIARHEVLRSAFDADDEgdpvLKIAPrmEVLMPVIEplahpdndanshTNSHTNSDENARTQATAQAL 1959
Cdd:cd19535     37 LDPDRLERAWNKLIARHPMLRAVFLDDGT----QQILP--EVPWYGIT------------VHDLRGLSEEEAEAALEELR 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1960 DDAARTPFDLSRAPL--VRATLLrfDAAHHVLIVSLHHIVADGGSVHILLDELCELYRAQRDgappALAPLAVQYADYAH 2037
Cdd:cd19535     99 ERLSHRVLDVERGPLfdIRLSLL--PEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGE----PLPPLELSFRDYLL 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2038 WQRARfTPDAVREAQQFWRGYLAD---APAlLPLSTD--RARPTRVSHagaaRHFRLDATLGARVRTLAQAHGMTPFAVL 2112
Cdd:cd19535    173 AEQAL-RETAYERARAYWQERLPTlppAPQ-LPLAKDpeEIKEPRFTR----REHRLSAEQWQRLKERARQHGVTPSMVL 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2113 LASFQWFLHRHTGADDLVIGTDVDGRER--AELEALIGFFVNVVPLrsriAADGANLASFdawLDAAR--QST-WDALDH 2187
Cdd:cd19535    247 LTAYAEVLARWSGQPRFLLNLTLFNRLPlhPDVNDVVGDFTSLLLL----EVDGSEGQSF---LERARrlQQQlWEDLDH 319
                          330       340
                   ....*....|....*....|..
gi 1888712850 2188 RAlpFDRIVDALALKRRRDANP 2209
Cdd:cd19535    320 SS--YSGVVVVRRLLRRRGGQP 339
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
35-590 2.76e-26

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 114.77  E-value: 2.76e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   35 PEATALIVidadGDTRYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFFGCLYAGVVAVPV---YPPEsk 110
Cdd:cd17649      1 PDAVALVF----GDQSLSYAELDARANRLAHRLRALGVGPEvRVGIALERSLEMVVALLAILKAGGAYVPLdpeYPAE-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  111 reqhlaRLRGIARDAGVRYVLTTaalherhadawsmlapgadvvavdtldardtpsdaplHPvraDDLAFLQYTSGSTGS 190
Cdd:cd17649     75 ------RLRYMLEDSGAGLLLTH-------------------------------------HP---RQLAYVIYTSGSTGT 108
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  191 PKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDmGLIGSLLQPVFSGIPLVLMSPQYFLErPLRWLDAIARHRG 270
Cdd:cd17649    109 PKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFD-GAHEQLLPPLICGACVVLRPDELWAS-ADELAEMVRELGV 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  271 TISGAPDFAYRLCAERINDETRAklDLSSWRLAFSGSEPVRRDTLddfvARFAPAgfdAAALYPCYGLAEATLFVTGGVR 350
Cdd:cd17649    187 TVLDLPPAYLQQLAEEADRTGDG--RPPSLRLYIFGGEALSPELL----RRWLKA---PVRLFNAYGPTEATVTPLVWKC 257
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  351 GAGLvshAFSSAALSAGraeaaradeaaTVLVGCGAVQAGhrvaivaraaaeshesheadvetetsRAGERLADGRIGEI 430
Cdd:cd17649    258 EAGA---ARAGASMPIG-----------RPLGGRSAYILD--------------------------ADLNPVPVGVTGEL 297
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  431 HVSGPSVAHGYWQRADASAQAFVDAPRHADGSgpaRWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEA 509
Cdd:cd17649    298 YIGGEGLARGYLGRPELTAERFVPDPFGAPGS---RLYRTGDLArWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLE 374
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  510 HAEfARKGRVIAfgATLGGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDACgeTPAAIALLNpgALPKTSSGKLQRA 589
Cdd:cd17649    375 HPG-VREAAVVA--LDGAGGKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYM--VPAHLVFLA--RLPLTPNGKLDRK 447

                   .
gi 1888712850  590 A 590
Cdd:cd17649    448 A 448
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
735-957 5.26e-26

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 113.50  E-value: 5.26e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  735 QRQLFAWRLDPASRaYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYApRTEAAAPLAWAHVDLSD 814
Cdd:cd19534      8 QRWFFEQNLAGRHH-FNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRI-RGDVEELFRLEVVDLSS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  815 LgdidehDRERALRECAQRfADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAALDGat 894
Cdd:cd19534     86 L------AQAAAIEALAAE-AQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAG-- 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1888712850  895 thGEAQAKAKTriTYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHTATDTASE 957
Cdd:cd19534    157 --EPIPLPSKT--SFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQTYGDARTV 215
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1844-2164 7.58e-26

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 117.07  E-value: 7.58e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1844 ALPLSLMQQRIWVVDQLADRALAsYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFdADDEGDPVLKIAPRMEVLM 1923
Cdd:PRK10252     7 HLPLVAAQPGIWMAEKLSPLPSA-WSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRF-TEDNGEVWQWVDPALTFPL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1924 PVIEPLAHpdndanshtnshtnsdeNARTQATAQALDDA-ARTPFDLSRA-PLVRATLLRFDAAHHVLIVSLHHIVADGG 2001
Cdd:PRK10252    85 PEIIDLRT-----------------QPDPHAAAQALMQAdLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGF 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2002 SVHILLDELCELYRAQRDGAPPA---LAPLAVQYADYAHWQrarfTPDAVREAQQFWRGYLADAPALLPLSTDRArPTRV 2078
Cdd:PRK10252   148 SFPAITRRIAAIYCAWLRGEPTPaspFTPFADVVEEYQRYR----ASEAWQRDAAFWAEQRRQLPPPASLSPAPL-PGRS 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2079 SHAGAARhFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGR-ERAELEAlIGFFVNVVPLR 2157
Cdd:PRK10252   223 ASADILR-LKLEFTDGAFRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlGSAALTA-TGPVLNVLPLR 300

                   ....*..
gi 1888712850 2158 SRIAADG 2164
Cdd:PRK10252   301 VHIAAQE 307
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
31-588 8.58e-26

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 113.90  E-value: 8.58e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGA-AAERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPES 109
Cdd:PRK03640    12 AFLTPDRTAIE----FEEKKVTFMELHEAVVSVAGKLAALGVkKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLS 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  110 KRE--QHLArlrgiarDAGVRYVLTTAALHERHAdawsmlapGADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSGS 187
Cdd:PRK03640    88 REEllWQLD-------DAEVKCLITDDDFEAKLI--------PGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  188 TGSPKGVMVSHGNLLANEIAIQAGLGVRPDDvfvSWL---PLYHDMGLiGSLLQPVFSGIPLVLMspQYFLERplRWLDA 264
Cdd:PRK03640   153 TGKPKGVIQTYGNHWWSAVGSALNLGLTEDD---CWLaavPIFHISGL-SILMRSVIYGMRVVLV--EKFDAE--KINKL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  265 IARHRGT-ISGAPDFAYRLcAERINDETRAkldlSSWRLAFSGSEPVRRDTLDDFVARFAPagfdaaaLYPCYGLAE-AT 342
Cdd:PRK03640   225 LQTGGVTiISVVSTMLQRL-LERLGEGTYP----SSFRCMLLGGGPAPKPLLEQCKEKGIP-------VYQSYGMTEtAS 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  343 LFVTggvrgaglVSHAFSSAAL-SAGRAeaaradeaatvLVGCgavqaghrvaivaraaaeshesheadvETETSRAGER 421
Cdd:PRK03640   293 QIVT--------LSPEDALTKLgSAGKP-----------LFPC---------------------------ELKIEKDGVV 326
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  422 LADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYP 500
Cdd:PRK03640   327 VPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG-----------WFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYP 395
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  501 QDVEQAVEAHAEFARKGRV-----------IAFgatLGGGETLGLAlEIAPRMKKRFAAAQIvetlrriafdacgetPAA 569
Cdd:PRK03640   396 AEIEEVLLSHPGVAEAGVVgvpddkwgqvpVAF---VVKSGEVTEE-ELRHFCEEKLAKYKV---------------PKR 456
                          570
                   ....*....|....*....
gi 1888712850  570 IALLNpgALPKTSSGKLQR 588
Cdd:PRK03640   457 FYFVE--ELPRNASGKLLR 473
PRK06178 PRK06178
acyl-CoA synthetase; Validated
1221-1709 1.04e-25

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 114.75  E-value: 1.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1221 RH-ADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPT 1299
Cdd:PRK06178    40 RAwARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFRE 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1300 QRLAQTLRDCGARLVLCEDD--------CSALDLMGVQHAR----------------IDAAQEEA-------QREQHLRA 1348
Cdd:PRK06178   120 HELSYELNDAGAEVLLALDQlapvveqvRAETSLRHVIVTSladvlpaeptlplpdsLRAPRLAAagaidllPALRACTA 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1349 PHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHG-----ALTNYVDAVLARLDPPPRARFAMVSTIGADLGhtVLFgALAS 1423
Cdd:PRK06178   200 PVPLPPPALDALAALNYTGGTTGMPKGCEHTQRdmvytAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFG--LLF-PLFS 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1424 GGALHLIDRdttLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADA-LPAHTLVlggEATSWelldtIAALRPDCRV 1502
Cdd:PRK06178   277 GATLVLLAR---WDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYdLSSLRQV---RVVSF-----VKKLNPDYRQ 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1503 HNH-----------YGPTET------TVG-------ILTQPAAqacraaatlpLGRPLDNNETWLLD-EHLNPVGTGGTG 1557
Cdd:PRK06178   346 RWRaltgsvlaeaaWGMTEThtcdtfTAGfqdddfdLLSQPVF----------VGLPVPGTEFKICDfETGELLPLGAEG 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1558 ELYLGGAGVALGYLHQPALTAARFVPHpfaagarLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALD 1637
Cdd:PRK06178   416 EIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHP 488
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1888712850 1638 GVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVlRVIDALPLNRNGKLDRQALSALA 1709
Cdd:PRK06178   489 AVLGSAVVGRPdpdkGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEI-RIVDALPMTATGKVRKQDLQALA 563
PRK07529 PRK07529
AMP-binding domain protein; Validated
114-597 1.83e-25

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 114.28  E-value: 1.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  114 HLARLRGIARDAGVRYVlttaALHERHADAWSMLAPGADVVAVDTLDARDtPSDAPL--HPVRADDLAFLQYTSGSTGSP 191
Cdd:PRK07529   154 ALPELRTVVEVDLARYL----PGPKRLAVPLIRRKAHARILDFDAELARQ-PGDRLFsgRPIGPDDVAAYFHTGGTTGMP 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  192 KGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQYFLERPL--RWLDAIARHR 269
Cdd:PRK07529   229 KLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGPGViaNFWKIVERYR 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  270 -GTISGAPDfAYRLCAERINDETraklDLSSWRLAFSGSEPVRRDTLDDFVARfapagfDAAALYPCYGLAEATLFVT-- 346
Cdd:PRK07529   309 iNFLSGVPT-VYAALLQVPVDGH----DISSLRYALCGAAPLPVEVFRRFEAA------TGVRIVEGYGLTEATCVSSvn 377
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  347 --GGVRGAGLVSHAFSSAALSAgraeaaradeaatvlvgcgavqaghrvaivARAAAESHESHEADVetetsragerlad 424
Cdd:PRK07529   378 ppDGERRIGSVGLRLPYQRVRV------------------------------VILDDAGRYLRDCAV------------- 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  425 GRIGEIHVSGPSVAHGYwQRADASAQAFVDaprhadgsgpARWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDV 503
Cdd:PRK07529   415 DEVGVLCIAGPNVFSGY-LEAAHNKGLWLE----------DGWLNTGDLGRIdADGYFWLTGRAKDLIIRGGHNIDPAAI 483
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  504 EQAVEAHAEfarkgrvIAFGATLG-----GGE------TLGLALEIAPRMKKRFAAAQIVEtlrRIAFdacgetPAAIAL 572
Cdd:PRK07529   484 EEALLRHPA-------VALAAAVGrpdahAGElpvayvQLKPGASATEAELLAFARDHIAE---RAAV------PKHVRI 547
                          490       500       510
                   ....*....|....*....|....*....|
gi 1888712850  573 LNpgALPKTSSGK-----LQRAATREGWRA 597
Cdd:PRK07529   548 LD--ALPKTAVGKifkpaLRRDAIRRVLRA 575
PRK12467 PRK12467
peptide synthase; Provisional
1846-2311 3.66e-25

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 115.64  E-value: 3.66e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIwVVDQLADRALASYNMTAGLDLRGpLDAARLQRSLAALIARHEVLRSAFDADDEGDPVLKIApRMEVLMPV 1925
Cdd:PRK12467  2648 PLSPMQQGM-LFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQVV-YKQARLPF 2724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1926 IEplahpdndanshtnsHTNSDEnARTQATAQALDDAARTP-FDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVH 2004
Cdd:PRK12467  2725 SR---------------LDWRDR-ADLEQALDALAAADRQQgFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGS 2788
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2005 ILLDELCELYRAQrdgappALAPLAVQYADYAHWQRARftPDAVREAqqFWRGYLAD--APALLpLSTDRARPTRVSHAG 2082
Cdd:PRK12467  2789 QLLGEVLQRYFGQ------PPPAREGRYRDYIAWLQAQ--DAEASEA--FWKEQLAAleEPTRL-ARALYPAPAEAVAGH 2857
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2083 AARHFRLDATLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRErAEL---EALIGFFVNVVPLrsr 2159
Cdd:PRK12467  2858 GAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRP-AQLrgaEQQLGLFINTLPV--- 2933
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2160 IAADGANlASFDAWLDAARQSTWDALDHRALPFDRIvdalalkrRRDANPLVQVLF-------------VLRDLPRGNTR 2226
Cdd:PRK12467  2934 IASPRAE-QTVSDWLQQVQAQNLALREFEHTPLADI--------QRWAGQGGEALFdsilvfenypiseALKQGAPSGLR 3004
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2227 VPGLAVEllrpptTQSKFDMALFVEAVDgGYDIEWVYASALFDAATIERAFDAWRATLDAVSADPRAPLAS-SLSTSPLS 2305
Cdd:PRK12467  3005 FGAVSSR------EQTNYPLTLAVGLGD-TLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGElPTLAAHER 3077

                   ....*.
gi 1888712850 2306 ADVAHD 2311
Cdd:PRK12467  3078 RQVLHA 3083
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
176-510 6.81e-25

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 112.07  E-value: 6.81e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  176 DDLAFLQYTSGSTGSPKGVMVSHGNLLANeiAIQAGLGVRP-----DDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMS 250
Cdd:PRK08974   206 EDLAFLQYTGGTTGVAKGAMLTHRNMLAN--LEQAKAAYGPllhpgKELVVTALPLYHIFALTVNCLLFIELGGQNLLIT 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  251 -----PQYFLErplrwldaIARHRGT-ISGAPDFAYRLcaerINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFvarfap 324
Cdd:PRK08974   284 nprdiPGFVKE--------LKKYPFTaITGVNTLFNAL----LNNEEFQELDFSSLKLSVGGGMAVQQAVAERW------ 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  325 AGFDAAALYPCYGLAEATLFVTGGvrGAGLVSHAFSsaalsagraeaaradeaatvlVGCGAvqaghrvaivaraaaesh 404
Cdd:PRK08974   346 VKLTGQYLLEGYGLTECSPLVSVN--PYDLDYYSGS---------------------IGLPV------------------ 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  405 ESHEADVETEtsrAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFVHD-GQLYI 483
Cdd:PRK08974   385 PSTEIKLVDD---DGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDG-----------WLATGDIAVMDEeGFLRI 450
                          330       340
                   ....*....|....*....|....*..
gi 1888712850  484 AGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PRK08974   451 VDRKKDMILVSGFNVYPNEIEDVVMLH 477
PRK06188 PRK06188
acyl-CoA synthetase; Validated
19-514 1.03e-24

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 111.23  E-value: 1.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   19 PAHGLAARLRALAQqRPEATALividADGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYA 97
Cdd:PRK06188    11 GATYGHLLVSALKR-YPDRPAL----VLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVaLLSLNRPEVLMAIGAAQLA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   98 GVVAVPVYPPESkREQHLArlrgIARDAGV--------RYVLTTAALHERHADAWSMLAPGADVVAVDTLDARDTPSDAP 169
Cdd:PRK06188    86 GLRRTALHPLGS-LDDHAY----VLEDAGIstlivdpaPFVERALALLARVPSLKHVLTLGPVPDGVDLLAAAAKFGPAP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  170 LHPV-RADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIgsLLQPVFSGIPLVL 248
Cdd:PRK06188   161 LVAAaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF--FLPTLLRGGTVIV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  249 MspQYFleRPLRWLDAIARHRGTISG-APDFAYRLcaerINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGF 327
Cdd:PRK06188   239 L--AKF--DPAEVLRAIEEQRITATFlVPTMIYAL----LDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFA 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  328 DAaalypcYGLAEATLFVTGGVRGaglvSHAFSSAALsagraeaaradeaatvLVGCGAVQAGhrvaivaraaaeshesh 407
Cdd:PRK06188   311 QY------YGQTEAPMVITYLRKR----DHDPDDPKR----------------LTSCGRPTPG----------------- 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  408 eADVETETSrAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFvdaprhADGsgparWLRTGDLGFV-HDGQLYIAGR 486
Cdd:PRK06188   348 -LRVALLDE-DGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RDG-----WLHTGDVAREdEDGFYYIVDR 414
                          490       500
                   ....*....|....*....|....*...
gi 1888712850  487 VKDLVIVRGRNLYPQDVEQAVEAHAEFA 514
Cdd:PRK06188   415 KKDMIVTGGFNVFPREVEDVLAEHPAVA 442
PRK06145 PRK06145
acyl-CoA synthetase; Validated
1219-1707 1.43e-24

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 110.36  E-value: 1.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNP 1298
Cdd:PRK06145     8 IAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1299 TQRLAQTLRDCGARLVLCEDDCSALDLMGVQHARIDA-AQEEAQR--EQHLRAPHALPaVDPRSAAYVIYTSGSSGAPKG 1375
Cdd:PRK06145    88 ADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAaAQADSRRlaQGGLEIPPQAA-VAPTDLVRLMYTSGTTDRPKG 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1376 VVIAHGALT-NYVDAVLArLDPPPRARFAMVST---IGA-DL-GHTVLfgalASGGALHlIDRDttLDADRFAQTLAAAR 1449
Cdd:PRK06145   167 VMHSYGNLHwKSIDHVIA-LGLTASERLLVVGPlyhVGAfDLpGIAVL----WVGGTLR-IHRE--FDPEAVLAAIERHR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1450 IDVLKIVPGHLHALLQA-ERAADALPAHTLVL-GGEATSWELLDTIAALRPDCRVHNHYGPTETTVG-ILTQPAAQACRA 1526
Cdd:PRK06145   239 LTCAWMAPVMLSRVLTVpDRDRFDLDSLAWCIgGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGdTLMEAGREIEKI 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1527 AATlplGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlyRSGDRARRLADGS 1606
Cdd:PRK06145   319 GST---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGF 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1607 LEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPDYMV 1682
Cdd:PRK06145   389 LYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHddrwGERITAVVVLNPGATLTLEALDRHCRQRLASFKV 468
                          490       500
                   ....*....|....*....|....*
gi 1888712850 1683 PSVLRVIDALPLNRNGKLDRQALSA 1707
Cdd:PRK06145   469 PRQLKVRDELPRNPSGKVLKRVLRD 493
PRK06145 PRK06145
acyl-CoA synthetase; Validated
31-593 1.53e-24

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 110.36  E-value: 1.53e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIVidadGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVY---- 105
Cdd:PRK06145    12 ARRTPDRAALVY----RDQEISYAEFHQRILQAAGMLHARGiGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINyrla 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  106 PPESKReqhlarlrgIARDAGVRYVLTTAALHERHADAWSMLAPGADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTS 185
Cdd:PRK06145    88 ADEVAY---------ILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  186 GSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHdmglIGSLLQPvfsGIPLVLMSPQYFLER---PLRWL 262
Cdd:PRK06145   159 GTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYH----VGAFDLP---GIAVLWVGGTLRIHRefdPEAVL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  263 DAIARHRGTisgAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAalypcYGLAEAT 342
Cdd:PRK06145   232 AAIERHRLT---CAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDA-----YGLTETC 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  343 LFVTGGVRGAGLVSHAFSSAALsagraeaaradeaatvlvgcgavqaghrvaivaraaaeshesheADVETE-TSRAGER 421
Cdd:PRK06145   304 SGDTLMEAGREIEKIGSTGRAL--------------------------------------------AHVEIRiADGAGRW 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  422 LADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFVHD-GQLYIAGRVKDLVIVRGRNLYP 500
Cdd:PRK06145   340 LPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-----------WFRSGDVGYLDEeGFLYLTDRKKDMIISGGENIAS 408
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  501 QDVEQAVEAHAEFA----------RKGRVIAFGATLGGGETLGLAlEIAPRMKKRFAAAQIVETLRRIAfdacgetpaai 570
Cdd:PRK06145   409 SEVERVIYELPEVAeaavigvhddRWGERITAVVVLNPGATLTLE-ALDRHCRQRLASFKVPRQLKVRD----------- 476
                          570       580
                   ....*....|....*....|...
gi 1888712850  571 allnpgALPKTSSGKLQRAATRE 593
Cdd:PRK06145   477 ------ELPRNPSGKVLKRVLRD 493
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1219-1710 1.81e-24

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 109.95  E-value: 1.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLAR-DLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGN 1297
Cdd:PRK06839     8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 PTQRLAQTLRDCGARLVLCEDDCSALDLM-----GVQHA-RIDAAQEEAQREQhlraphaLPAVDP-RSAAYVI-YTSGS 1369
Cdd:PRK06839    88 TENELIFQLKDSGTTVLFVEKTFQNMALSmqkvsYVQRViSITSLKEIEDRKI-------DNFVEKnESASFIIcYTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1370 SGAPKGVVIAH-GALTNYVDAVLArLDppprARFAMVSTIGADLGHT-----VLFGALASGGALHLIDRdttLDADRFAQ 1443
Cdd:PRK06839   161 TGKPKGAVLTQeNMFWNALNNTFA-ID----LTMHDRSIVLLPLFHIggiglFAFPTLFAGGVIIVPRK---FEPTKALS 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1444 TLAAARIDVLKIVPGHLHALLQAERAADALPAHTLVL--GGEATSWELLDtiAALRPDCRVHNHYGPTET--TVGILTQP 1519
Cdd:PRK06839   233 MIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFynGGAPCPEELMR--EFIDRGFLFGQGFGMTETspTVFMLSEE 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1520 AAQACRAAatlpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAArfvphpfAAGARLYRSGDRA 1599
Cdd:PRK06839   311 DARRKVGS----IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE-------TIQDGWLCTGDLA 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1600 RRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAA 1675
Cdd:PRK06839   380 RVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQhvkwGEIPIAFIVKKSSSVLIEKDVIEHCRL 459
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1888712850 1676 LLPDYMVPSVLRVIDALPLNRNGKLDRQALSALAR 1710
Cdd:PRK06839   460 FLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
741-1169 1.92e-24

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 108.43  E-value: 1.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  741 WRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHlyapRTEAAAPlawAHVDLSDLGDIde 820
Cdd:cd19537     15 YQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLR----RSYSSSP---PRVQRVDTLDV-- 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  821 hdreralrecaQRFADAPFDLLRGPLLRaglVRMSDERhvLMLALHHIATDGWSMQLLVEELVDGYRAALDGATTHgeaq 900
Cdd:cd19537     86 -----------WKEINRPFDLEREDPIR---VFISPDT--LLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRR---- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  901 akaktriTYADYAAWQRRwlasdAAARQLAYWRAALAdDAPPLALPydhtatdTASENADPRAAARVaFALPAPLAQAVR 980
Cdd:cd19537    146 -------EYLDSTAWSRP-----ASPEDLDFWSEYLS-GLPLLNLP-------RRTSSKSYRGTSRV-FQLPGSLYRSLL 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  981 ASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLV--LHSDCEAATPLASLFSQLRQR 1058
Cdd:cd19537    205 QFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPirIRFPSSSDASAADFLRAVRRS 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1059 TLDAQANqALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPALARW-PGaraerVEIAETH---VKVPLALDLRESRD 1134
Cdd:cd19537    285 SQAALAH-AIPWHQLLEHLGLPPDSPNHPLFDVMVTFHDDRGVSLALPiPG-----VEPLYTWaegAKFPLMFEFTALSD 358
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1888712850 1135 GSMRAYFTYASARFDAASVERMAAQYLRAVEAFAH 1169
Cdd:cd19537    359 DSLLLRLEYDTDCFSEEEIDRIESLILAALELLVE 393
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
31-598 1.98e-24

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 110.61  E-value: 1.98e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATAliVIDADGdTRYDYAQLDRraralaarfardgAAAERALILMDSGV---DYVS-----------AFFGCLY 96
Cdd:PRK06087    33 ARAMPDKIA--VVDNHG-ASYTYSALDH-------------AASRLANWLLAKGIepgDRVAfqlpgwceftiIYLACLK 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   97 AGVVAVPVYPPESKRE----QHLARLR---GIARDAGVRYVLTTAAL-----HERHADAWSMLAPGADVVAVDTLDARDT 164
Cdd:PRK06087    97 VGAVSVPLLPSWREAElvwvLNKCQAKmffAPTLFKQTRPVDLILPLqnqlpQLQQIVGVDKLAPATSSLSLSQIIADYE 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  165 PSDAPLhPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGI 244
Cdd:PRK06087   177 PLTTAI-TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGA 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  245 PLVLMspQYFleRPLRWLDAIARHRGTIS-GAPDFAYRLcaerINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARfa 323
Cdd:PRK06087   256 RSVLL--DIF--TPDACLALLEQQRCTCMlGATPFIYDL----LNLLEKQPADLSALRFFLCGGTTIPKKVARECQQR-- 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  324 pagfdAAALYPCYGLAEAtlfvtggvrgaglVSHAFssaalsagraeaaradeaatvlvgcgaVQAGHRVAIVARAAAES 403
Cdd:PRK06087   326 -----GIKLLSVYGSTES-------------SPHAV---------------------------VNLDDPLSRFMHTDGYA 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  404 HESHEADVETETSRAgerLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDaprhaDGsgparWLRTGDLGFV-HDGQLY 482
Cdd:PRK06087   361 AAGVEIKVVDEARKT---LPPGCEGEEASRGPNVFMGYLDEPELTARALDE-----EG-----WYYSGDLCRMdEAGYIK 427
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  483 IAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFA----------RKG-RVIAFGATLGGGETLGLALEIAPRMKKRFAAAQI 551
Cdd:PRK06087   428 ITGRKKDIIVRGGENISSREVEDILLQHPKIHdacvvampdeRLGeRSCAYVVLKAPHHSLTLEEVVAFFSRKRVAKYKY 507
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1888712850  552 VETLRRIafdacgetpaaiallnpGALPKTSSGKLQRAATREGWRAR 598
Cdd:PRK06087   508 PEHIVVI-----------------DKLPRTASGKIQKFLLRKDIMRR 537
PLN02246 PLN02246
4-coumarate--CoA ligase
78-514 5.09e-24

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 108.91  E-value: 5.09e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   78 LILMDSGVDYVSAFFGCLYAGVV---AVPVYPPESKREQhlarlrgiARDAGVRYVLTTAALHERHADawsmLAPGADVV 154
Cdd:PLN02246    79 MLLLPNCPEFVLAFLGASRRGAVtttANPFYTPAEIAKQ--------AKASGAKLIITQSCYVDKLKG----LAEDDGVT 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  155 AVDTLDARD-----------TPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANeIAIQA-----GLGVRPDD 218
Cdd:PLN02246   147 VVTIDDPPEgclhfseltqaDENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTS-VAQQVdgenpNLYFHSDD 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  219 VFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMsPQYFLerpLRWLDAIARHRGTIsgAPDFAYRLCAERINDETrAKLDLS 298
Cdd:PLN02246   226 VILCVLPMFHIYSLNSVLLCGLRVGAAILIM-PKFEI---GALLELIQRHKVTI--APFVPPIVLAIAKSPVV-EKYDLS 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  299 SWRLAFSGSEPVRRDTLDDFVARFApagfdAAALYPCYGLAEAtlfvtGGVRGAGLvshAFSSAALSAGRAEaaradeaa 378
Cdd:PLN02246   299 SIRMVLSGAAPLGKELEDAFRAKLP-----NAVLGQGYGMTEA-----GPVLAMCL---AFAKEPFPVKSGS-------- 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  379 tvlvgCGAVqaghrvaivaraaaesheSHEAD---VETETsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAfVDa 455
Cdd:PLN02246   358 -----CGTV------------------VRNAElkiVDPET---GASLPRNQPGEICIRGPQIMKGYLNDPEATANT-ID- 409
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  456 prhADGsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFA 514
Cdd:PLN02246   410 ---KDG-----WLHTGDIGYIdDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIA 461
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
176-592 6.04e-24

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 106.03  E-value: 6.04e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  176 DDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQYFL 255
Cdd:cd05944      2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  256 ERPL--RWLDAIARHRGT-ISGAPDfAYRLCAERINDEtraklDLSSWRLAFSGSEPVRrdtlddfVARFapAGFDAAAL 332
Cdd:cd05944     82 NPGLfdNFWKLVERYRITsLSTVPT-VYAALLQVPVNA-----DISSLRFAMSGAAPLP-------VELR--ARFEDATG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  333 YPC---YGLAEATLfvtggvrgagLVSHAFSSAALSAGRAEAARADEAATVLVgcgavqaghrvaivaraaaeshesheA 409
Cdd:cd05944    147 LPVvegYGLTEATC----------LVAVNPPDGPKRPGSVGLRLPYARVRIKV--------------------------L 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  410 DVETETSRageRLADGRIGEIHVSGPSVAHGYWQRADAsaqafvdapRHADGSGpaRWLRTGDLGFV-HDGQLYIAGRVK 488
Cdd:cd05944    191 DGVGRLLR---DCAPDEVGEICVAGPGVFGGYLYTEGN---------KNAFVAD--GWLNTGDLGRLdADGYLFITGRAK 256
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  489 DLVIVRGRNLYPQDVEQAVEAHAEfarkgrvIAFGATLG-----GGE------TLGLALEIAPRMKKRFAAAQIVEtlrR 557
Cdd:cd05944    257 DLIIRGGHNIDPALIEEALLRHPA-------VAFAGAVGqpdahAGElpvayvQLKPGAVVEEEELLAWARDHVPE---R 326
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1888712850  558 IAfdacgeTPAAIALLNPgaLPKTSSGKLQRAATR 592
Cdd:cd05944    327 AA------VPKHIEVLEE--LPVTAVGKVFKPALR 353
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
1219-1700 6.48e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 108.71  E-value: 6.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNP 1298
Cdd:PRK07786    23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1299 TQRLAQTLRDCGARLVLCE-----------DDCSALDLMGVQHARIDAAQ---EEAQREQHlrAPHALPAVDPRSAAYVI 1364
Cdd:PRK07786   103 PPEIAFLVSDCGAHVVVTEaalapvatavrDIVPLLSTVVVAGGSSDDSVlgyEDLLAEAG--PAHAPVDIPNDSPALIM 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1365 YTSGSSGAPKGVVIAHGALTNYVDAVL--ARLDPPPRARFamvstIGADLGHTVLFGALASG---GALHLIDRDTTLDAD 1439
Cdd:PRK07786   181 YTSGTTGRPKGAVLTHANLTGQAMTCLrtNGADINSDVGF-----VGVPLFHIAGIGSMLPGlllGAPTVIYPLGAFDPG 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1440 RFAQTLAAARIDVLKIVPGHLHALLQAERAAD-ALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVgiLTQ 1518
Cdd:PRK07786   256 QLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPrDLALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSP--VTC 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1519 PAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAarfvpHPFAAGarLYRSGDR 1598
Cdd:PRK07786   334 MLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATA-----EAFAGG--WFHSGDL 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1599 ARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGAR-----LAAFATPQPGASLDAAALKRAL 1673
Cdd:PRK07786   407 VRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwgevpVAVAAVRNDDAALTLEDLAEFL 486
                          490       500
                   ....*....|....*....|....*..
gi 1888712850 1674 AALLPDYMVPSVLRVIDALPLNRNGKL 1700
Cdd:PRK07786   487 TDRLARYKHPKALEIVDALPRNPAGKV 513
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
75-589 7.23e-24

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 106.99  E-value: 7.23e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPpeskreqhlaRLRGiardAGVRYVLttaalheRHADAWSMLApgadvv 154
Cdd:cd05934     29 DRVALMLDNCPEFLFAWFALAKLGAVLVPINT----------ALRG----DELAYII-------DHSGAQLVVV------ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  155 avdtldardtpsdaplhpvradDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIG 234
Cdd:cd05934     82 ----------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAV 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  235 SLLQPVFSGIPLVLmspqyfLER--PLRWLDAIARHRGTIS---GAPdFAYRLCAERINDETRAKLdlsswRLAFSGseP 309
Cdd:cd05934    140 SVLAALSVGATLVL------LPRfsASRFWSDVRRYGATVTnylGAM-LSYLLAQPPSPDDRAHRL-----RAAYGA--P 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  310 VRRDTLDDFVARFapaGFdaaALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAalsagraeaaradeaatvlvgcgavqa 389
Cdd:cd05934    206 NPPELHEEFEERF---GV---RLLEGYGMTETIVGVIGPRDEPRRPGSIGRPA--------------------------- 252
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  390 ghrvaivaraaaeshesHEADVETeTSRAGERLADGRIGEIHV---SGPSVAHGYWQRADASAQAFvdaprhADGsgpar 466
Cdd:cd05934    253 -----------------PGYEVRI-VDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM------RNG----- 303
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  467 WLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEfARKGRVIAFGATLGGGEtlgLALEIAPRMKKR 545
Cdd:cd05934    304 WFHTGDLGyRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPA-VREAAVVAVPDEVGEDE---VKAVVVLRPGET 379
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1888712850  546 FAAAQIVETLR-RIAFDAcgeTPAAIALLNpgALPKTSSGKLQRA 589
Cdd:cd05934    380 LDPEELFAFCEgQLAYFK---VPRYIRFVD--DLPKTPTEKVAKA 419
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
1210-1663 1.03e-23

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 107.71  E-value: 1.03e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1210 PPGEPIHLRVARHADTQPDAPAVIDGAL--RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAG 1287
Cdd:cd05904      2 PTDLPLDSVSFLFASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1288 GAYVALDAGNPTQRLAQTLRDCGARLVLC----EDDCSALDLMGVQHARIDAAQEEAQREQHLRAPHALPAVD--PRSAA 1361
Cdd:cd05904     82 AVVTTANPLSTPAEIAKQVKDSGAKLAFTtaelAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVikQDDVA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1362 YVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIgaDLGH-----TVLFGALASGGALHLIDRdttL 1436
Cdd:cd05904    162 ALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVL--PMFHiyglsSFALGLLRLGATVVVMPR---F 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1437 DADRFAQTLAAARIDVLKIVPGHLHALLQAERAA--DALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTvG 1514
Cdd:cd05904    237 DLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDkyDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST-G 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1515 ILTQPAAQACRAAATLPLGRPLDNNETWLLD-EHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlY 1593
Cdd:cd05904    316 VVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW------L 389
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1888712850 1594 RSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQPGAS 1663
Cdd:cd05904    390 HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYpdeeAGEVPMAFVVRKPGSS 463
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
1866-2291 1.22e-23

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 105.84  E-value: 1.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1866 ASYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDEGDP---VLKiaprmevlmpvieplahpdnDANSHTNS 1942
Cdd:cd19545     20 GAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLlqvVVK--------------------ESPISWTE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1943 HTNSDEnartqataqALDDAARTPFDLSrAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVHILLDELCELYRAQRDGAP 2022
Cdd:cd19545     80 STSLDE---------YLEEDRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2023 PALAPLaVQYADYaHWQRArftpdavreAQQFWRGYLADAPAL----LPLSTDRARPtrvshagaarhfrlDATLGARVR 2098
Cdd:cd19545    150 PPFSRF-VKYLRQ-LDDEA---------AAEFWRSYLAGLDPAvfppLPSSRYQPRP--------------DATLEHSIS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2099 TLAQA-HGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGRER--AELEALIGFFVNVVPLRSRIAADGaNLASFdawLD 2175
Cdd:cd19545    205 LPSSAsSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNApvPGIEQIVGPTIATVPLRVRIDPEQ-SVEDF---LQ 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2176 AARQSTWDALDHRALPFDRIvdaLALKRRRDANPLVQVLFVLRDlPRGNTRVPGLAVELLRPPTTQSKFD---MALFVEA 2252
Cdd:cd19545    281 TVQKDLLDMIPFEHTGLQNI---RRLGPDARAACNFQTLLVVQP-ALPSSTSESLELGIEEESEDLEDFSsygLTLECQL 356
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1888712850 2253 VDGGYDIEWVYASALFDAATIERAFDAWRATLDAVSADP 2291
Cdd:cd19545    357 SGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
14-593 1.49e-23

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 107.66  E-value: 1.49e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   14 DTDAVPahGLAARLRALAQQRPEATALIVidADGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFF 92
Cdd:PRK05852    11 ASDFGP--RIADLVEVAATRLPEAPALVV--TADRIAISYRDLARLVDDLAGQLTRSGlLPGDRVALRMGSNAEFVVALL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   93 GCLYAGVVAVPVYPPESKREQhlarlRGIARDAGVRYVLTTAALHERHADAWSMLAPGADVVAVDTLDARDTPS---DAP 169
Cdd:PRK05852    87 AASRADLVVVPLDPALPIAEQ-----RVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSvhlDAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  170 LHP---------VRADDlAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPV 240
Cdd:PRK05852   162 TEPtpatstpegLRPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  241 FSGIPLVLMSPQYFLERPLrWLDAIARHRGTISGAPDFaYRLCAERiNDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVA 320
Cdd:PRK05852   241 ASGGAVLLPARGRFSAHTF-WDDIKAVGATWYTAVPTI-HQILLER-AATEPSGRKPAALRFIRSCSAPLTAETAQALQT 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  321 RFapagfdAAALYPCYGLAEATLFV-TGGVRGAGLVSHAFSSaalsagraeaaradeaaTVLVGcgavqaghrvaivara 399
Cdd:PRK05852   318 EF------AAPVVCAFGMTEATHQVtTTQIEGIGQTENPVVS-----------------TGLVG---------------- 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  400 aaeshESHEADVETETSRAGErLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFVH-D 478
Cdd:PRK05852   359 -----RSTGAQIRIVGSDGLP-LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG-----------WLRTGDLGSLSaA 421
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  479 GQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH------AEFARKGRVIafgatlggGETLGLAleIAPRMKKRFAAAQIV 552
Cdd:PRK05852   422 GDLSIRGRIKELINRGGEKISPERVEGVLASHpnvmeaAVFGVPDQLY--------GEAVAAV--IVPRESAPPTAEELV 491
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1888712850  553 ETLRRIAfdACGETPAAIALLNpgALPKTSSGKLQRAATRE 593
Cdd:PRK05852   492 QFCRERL--AAFEIPASFQEAS--GLPHTAKGSLDRRAVAE 528
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
170-486 2.17e-23

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 109.24  E-value: 2.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  170 LHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLM 249
Cdd:PRK08633   776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYH 855
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  250 -SPqyflerplrwLDA------IARHRGTI-SGAPDF--AYrLCAERINdetraKLDLSSWRLAFSGSEPVRRDTLDDFV 319
Cdd:PRK08633   856 pDP----------TDAlgiaklVAKHRATIlLGTPTFlrLY-LRNKKLH-----PLMFASLRLVVAGAEKLKPEVADAFE 919
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  320 ARFapaGFDaaaLYPCYGLAEATLFVT---GGVRGAGLVSHAFSSAAlSAGRAeaaradeaatvLVGCgAVQAghrvaiv 396
Cdd:PRK08633   920 EKF---GIR---ILEGYGATETSPVASvnlPDVLAADFKRQTGSKEG-SVGMP-----------LPGV-AVRI------- 973
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  397 araaaeshesheadVETETsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFvdapRHADGSgpaRWLRTGDLGFV 476
Cdd:PRK08633   974 --------------VDPET---FEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVI----KDIDGI---GWYVTGDKGHL 1029
                          330
                   ....*....|.
gi 1888712850  477 -HDGQLYIAGR 486
Cdd:PRK08633  1030 dEDGFLTITDR 1040
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
75-594 2.51e-23

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 107.16  E-value: 2.51e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKRE-QH------------LARLRGIARD----AGVRYVLTT--AA 135
Cdd:PRK05677    76 DRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREmEHqfndsgakalvcLANMAHLAEKvlpkTGVKHVIVTevAD 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  136 LH---------------ERHADAWSMlaPGA----DVVAvdtLDARDTPSDAPLHPvraDDLAFLQYTSGSTGSPKGVMV 196
Cdd:PRK05677   156 MLpplkrllinavvkhvKKMVPAYHL--PQAvkfnDALA---KGAGQPVTEANPQA---DDVAVLQYTGGTTGVAKGAML 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  197 SHGNLLANEIAIQAGLGVRPDD---VFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQYFLERPLRWLdAIARHRGTIs 273
Cdd:PRK05677   228 THRNLVANMLQCRALMGSNLNEgceILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKEL-GKWKFSGFV- 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  274 GAPDFAYRLCaeriNDETRAKLDLSSWRLAFSGSEPVRRDTLDDFvarfapAGFDAAALYPCYGLAEATLFVTGGVRGAg 353
Cdd:PRK05677   306 GLNTLFVALC----NNEAFRKLDFSALKLTLSGGMALQLATAERW------KEVTGCAICEGYGMTETSPVVSVNPSQA- 374
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  354 lvshafssaalsagraeaaradeaatvlvgcgaVQAGHRVAIVARAAAEShesheadveteTSRAGERLADGRIGEIHVS 433
Cdd:PRK05677   375 ---------------------------------IQVGTIGIPVPSTLCKV-----------IDDDGNELPLGEVGELCVK 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  434 GPSVAHGYWQRADASAQAFvdaprHADGsgparWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAE 512
Cdd:PRK05677   411 GPQVMKGYWQRPEATDEIL-----DSDG-----WLKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPG 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  513 FArkgRVIAFGAT-LGGGETLGLAleIAPRMKKRFAAAQIVETLRR--IAFdacgETPAAIALLNpgALPKTSSGKLQRA 589
Cdd:PRK05677   481 VL---QCAAIGVPdEKSGEAIKVF--VVVKPGETLTKEQVMEHMRAnlTGY----KVPKAVEFRD--ELPTTNVGKILRR 549

                   ....*
gi 1888712850  590 ATREG 594
Cdd:PRK05677   550 ELRDE 554
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
1215-1707 2.72e-23

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 107.58  E-value: 2.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1215 IHLRVARHADTQPDAPAVI----DGALR-MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGA 1289
Cdd:cd05968     63 VEQLLDKWLADTRTRPALRwegeDGTSRtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1290 YVALDAGNPTQRLAQTLRDCGARLVLCEDDCS----ALDLMGV--QHARIDAAQEEAQREQHLRAPHALPAVDPRSAA-- 1361
Cdd:cd05968    143 VVPIFSGFGKEAAATRLQDAEAKALITADGFTrrgrEVNLKEEadKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDee 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1362 -----------------YVIYTSGSSGAPKGVVIAHGA--LTNYVDAVLArLDPPPRARFAMVSTIGADLGHTVLFGALA 1422
Cdd:cd05968    223 ketagdgaertesedplMIIYTSGTTGKPKGTVHVHAGfpLKAAQDMYFQ-FDLKPGDLLTWFTDLGWMMGPWLIFGGLI 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1423 SGGALHLIDRDTTLD-ADRFAQTLAAARIDVLKIVPGHLHALlqAERAADALPAHTL----VLGGEATSWE------LLD 1491
Cdd:cd05968    302 LGATMVLYDGAPDHPkADRLWRMVEDHEITHLGLSPTLIRAL--KPRGDAPVNAHDLsslrVLGSTGEPWNpepwnwLFE 379
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1492 TIaaLRPDCRVHNHYGPTETTVGIL----TQPAAQACraaatlpLGRPLDNNETWLLDEHLNPVgTGGTGELYLGGA--G 1565
Cdd:cd05968    380 TV--GKGRNPIINYSGGTEISGGILgnvlIKPIKPSS-------FNGPVPGMKADVLDESGKPA-RPEVGELVLLAPwpG 449
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1566 VALGYLHQPaltaARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVI 1645
Cdd:cd05968    450 MTRGFWRDE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAI 525
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850 1646 ----VVAGARLAAFATPQPGASLDAAALKRALAALLPDY---MVPSVLRVIDALPLNRNGKLDRQALSA 1707
Cdd:cd05968    526 gvphPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELgkpLSPERILFVKDLPKTRNAKVMRRVIRA 594
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
127-593 3.17e-23

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 106.78  E-value: 3.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  127 VRYVLTTAALHERHADAWSMLAPGADVVAVDTLDARDtpsdAPLHPvraDDLAFLQYTSGSTGSPKGVMVSHGNLLANEI 206
Cdd:PRK12583   159 LRGVVSLAPAPPPGFLAWHELQARGETVSREALAERQ----ASLDR---DDPINIQYTSGTTGFPKGATLSHHNILNNGY 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  207 AIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLmsPQ-YFleRPLRWLDAIARHRGT-ISGAPDFayrLCA 284
Cdd:PRK12583   232 FVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVY--PNeAF--DPLATLQAVEEERCTaLYGVPTM---FIA 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  285 ErINDETRAKLDLSSWRLAFSGSEPVRRDtlddfVARFAPAGFDAAALYPCYGLAEATlfvtggvrgagLVSHAFSSAal 364
Cdd:PRK12583   305 E-LDHPQRGNFDLSSLRTGIMAGAPCPIE-----VMRRVMDEMHMAEVQIAYGMTETS-----------PVSLQTTAA-- 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  365 sagraeAARADEAATVlvgcGAVQAghrvaivaraaaeSHESHEADVEtetsraGERLADGRIGEIHVSGPSVAHGYWQR 444
Cdd:PRK12583   366 ------DDLERRVETV----GRTQP-------------HLEVKVVDPD------GATVPRGEIGELCTRGYSVMKGYWNN 416
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  445 ADASAQAfVDaprhADGsgparWLRTGDLGfVHDGQLY--IAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFArkgRVIAF 522
Cdd:PRK12583   417 PEATAES-ID----EDG-----WMHTGDLA-TMDEQGYvrIVGRSKDMIIRGGENIYPREIEEFLFTHPAVA---DVQVF 482
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1888712850  523 GATLGG-GEtlglalEIAPRMKKRFAAAQIVETLRRIAFD--ACGETPAAIALLNpgALPKTSSGKLQRAATRE 593
Cdd:PRK12583   483 GVPDEKyGE------EIVAWVRLHPGHAASEEELREFCKAriAHFKVPRYFRFVD--EFPMTVTGKVQKFRMRE 548
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
1846-2163 4.44e-23

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 104.70  E-value: 4.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQRIWVVDQLADRALASYNMTAgLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDEGDPvlkiaprmevLMPV 1925
Cdd:cd19547      3 PLAPMQEGMLFRGLFWPDSDAYFNQNV-LELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEP----------LQYV 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1926 IEPLAHPdndanSHTNSHTNSDENARTQATAQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVHI 2005
Cdd:cd19547     72 RDDLAPP-----WALLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSL 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2006 LLDELCELYRAQRDGAPPALAPLAvQYADYAHWQRARFTPDavREAQQFWRGYLADapallplstdrARPTRVSHAGAAR 2085
Cdd:cd19547    147 IWGDVFRVYEELAHGREPQLSPCR-PYRDYVRWIRARTAQS--EESERFWREYLRD-----------LTPSPFSTAPADR 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2086 HFRLDA-------TLGARVRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGTDVDGR--ERAELEALIGFFVNVVPL 2156
Cdd:cd19547    213 EGEFDTvvhefpeQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPL 292

                   ....*..
gi 1888712850 2157 RSRIAAD 2163
Cdd:cd19547    293 RIRLDPD 299
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
116-592 1.66e-22

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 102.80  E-value: 1.66e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  116 ARLRGIARDAGVRYVLTTAALHERHADAW-SMLA---------PGADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTS 185
Cdd:cd05972     11 AKAANVLAKLGLRKGDRVAVLLPRVPELWaVILAviklgavyvPLTTLLGPKDIEYRLEAAGAKAIVTDAEDPALIYFTS 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  186 GSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVS-----WLplyhdMGLIGSLLQPVFSGIPLVLmspqYFLER--P 258
Cdd:cd05972     91 GTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNiadpgWA-----KGAWSSFFGPWLLGATVFV----YEGPRfdA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  259 LRWLDAIARHRGTISGAPDFAYRLCAErindETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPagfdaaALYPCYGL 338
Cdd:cd05972    162 ERILELLERYGVTSFCGPPTAYRMLIK----QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGL------PIRDGYGQ 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  339 AEATLFVTggvrgaglVSHAFSSAALSAGRaeaaradeaatvlvgcgavqaghrvaivaraaaeSHESHEADVeteTSRA 418
Cdd:cd05972    232 TETGLTVG--------NFPDMPVKPGSMGR----------------------------------PTPGYDVAI---IDDD 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  419 GERLADGRIGEI--HVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLG-FVHDGQLYIAGRVKDLVIVRG 495
Cdd:cd05972    267 GRELPPGEEGDIaiKLPPPGLFLGYVGDPEKTEASIRGD-----------YYLTGDRAyRDEDGYFWFVGRADDIIKSSG 335
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  496 RNLYPQDVEQAVEAH---AEFARKGR--------VIAFGA-TLGGGETLGLALEIAPRMKKRFAAAQIVetlRRIAFdac 563
Cdd:cd05972    336 YRIGPFEVESALLEHpavAEAAVVGSpdpvrgevVKAFVVlTSGYEPSEELAEELQGHVKKVLAPYKYP---REIEF--- 409
                          490       500
                   ....*....|....*....|....*....
gi 1888712850  564 getpaaiallnPGALPKTSSGKLQRAATR 592
Cdd:cd05972    410 -----------VEELPKTISGKIRRVELR 427
PRK06164 PRK06164
acyl-CoA synthetase; Validated
23-599 2.38e-22

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 104.05  E-value: 2.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGC--LYAGV 99
Cdd:PRK06164    12 LASLLDAHARARPDAVALI----DEDRPLSRAELRALVDRLAAWLAAQGvRRGDRVAVWLPNCIEWVVLFLACarLGATV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  100 VAVP--------------------VYPPESKREQHLARLRGIARDAgvRYVLTTAALHERHADAWSMLAPGADVVAVDTL 159
Cdd:PRK06164    88 IAVNtryrshevahilgrgrarwlVVWPGFKGIDFAAILAAVPPDA--LPPLRAIAVVDDAADATPAPAPGARVQLFALP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  160 DaRDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLiGSLLQP 239
Cdd:PRK06164   166 D-PAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGA 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  240 VFSGIPLVLMsPQYFLERPLRwldAIARHRGTISGAPDFAYRlcaeRINDETRAKLDLSSWRLAFsgsepvrrdtlddfV 319
Cdd:PRK06164   244 LAGGAPLVCE-PVFDAARTAR---ALRRHRVTHTFGNDEMLR----RILDTAGERADFPSARLFG--------------F 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  320 ARFAPAGFDAAALypcyglAEATLFVTGGVRGAGLVSHAFSSAALSAGRAEAAradeaatvlVGCGAVQaghrvaivara 399
Cdd:PRK06164   302 ASFAPALGELAAL------ARARGVPLTGLYGSSEVQALVALQPATDPVSVRI---------EGGGRPA----------- 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  400 aaesheSHEADVETETSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDaprhaDGsgparWLRTGDLGF-VHD 478
Cdd:PRK06164   356 ------SPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTD-----DG-----YFRTGDLGYtRGD 419
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  479 GQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRViafGATLgGGETLGLALEIaPRMKKRFAAAQIVETLRRI 558
Cdd:PRK06164   420 GQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVV---GATR-DGKTVPVAFVI-PTDGASPDEAGLMAACREA 494
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1888712850  559 AfdACGETPAAIALLNpgALPKTSSG---KLQRAATREGWRART 599
Cdd:PRK06164   495 L--AGFKVPARVQVVE--AFPVTESAngaKIQKHRLREMAQARL 534
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
1240-1709 2.97e-22

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 102.58  E-value: 2.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLcedd 1319
Cdd:cd05969      2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI---- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1320 csaldlmgvqharidAAQEEAQReqhlraphalpaVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPR 1399
Cdd:cd05969     78 ---------------TTEELYER------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPD 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1400 ARFAMVSTIGADLGHTV-LFGALASGGALHLIDRDttLDADRFAQTLAAARIDVLKIVPGHLHALLqaeRAADALpahtl 1478
Cdd:cd05969    131 DIYWCTADPGWVTGTVYgIWAPWLNGVTNVVYEGR--FDAESWYGIIERVKVTVWYTAPTAIRMLM---KEGDEL----- 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1479 vlggeATSWEL--LDTIAA----LRPDC----------RVHNHYGPTET-TVGILTQPAAQACRAAatlpLGRPLDNNET 1541
Cdd:cd05969    201 -----ARKYDLssLRFIHSvgepLNPEAirwgmevfgvPIHDTWWQTETgSIMIANYPCMPIKPGS----MGKPLPGVKA 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1542 WLLDEHLNPVGTGGTGELYL--GGAGVALGYLHQPALTAARFVphpfaagARLYRSGDRARRLADGSLEYLGRIDDQVKI 1619
Cdd:cd05969    272 AVVDENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFI-------DGWYLTGDLAYRDEDGYFWFVGRADDIIKT 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1620 RGYRVEPGEIAARLKALDGVRDAAVI----VVAGARLAAFATPQPG---ASLDAAALKRALAALLPDYMVPSVLRVIDAL 1692
Cdd:cd05969    345 SGHRVGPFEVESALMEHPAVAEAGVIgkpdPLRGEIIKAFISLKEGfepSDELKEEIINFVRQKLGAHVAPREIEFVDNL 424
                          490
                   ....*....|....*..
gi 1888712850 1693 PLNRNGKLDRQALSALA 1709
Cdd:cd05969    425 PKTRSGKIMRRVLKAKE 441
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
158-509 3.07e-22

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 103.98  E-value: 3.07e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  158 TLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDV----FVSWLPLYH----- 228
Cdd:cd05933    132 GRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesVVSYLPLSHiaaqi 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  229 -DM----------------GLIGSLL------QP-VFSGIPLVLmspQYFLER---------PLR-----W-----LDAI 265
Cdd:cd05933    212 lDIwlpikvggqvyfaqpdALKGTLVktlrevRPtAFMGVPRVW---EKIQEKmkavgaksgTLKrkiasWakgvgLETN 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  266 ARHRGTISGAPDFaYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPagfdaaaLYPCYGLAEATlfv 345
Cdd:cd05933    289 LKLMGGESPSPLF-YRLAKKLVFKKVRKALGLDRCQKFFTGAAPISRETLEFFLSLNIP-------IMELYGMSETS--- 357
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  346 tggvrGAGLVSHAFSSAALSAGRaeaaradeaatVLVGCgavqaghrvaivaraaaeSHESHEADvetetsragerlADG 425
Cdd:cd05933    358 -----GPHTISNPQAYRLLSCGK-----------ALPGC------------------KTKIHNPD------------ADG 391
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  426 rIGEIHVSGPSVAHGYWQRADASAQAfVDaprhADGsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVR-GRNLYPQDV 503
Cdd:cd05933    392 -IGEICFWGRHVFMGYLNMEDKTEEA-ID----EDG-----WLHSGDLGKLdEDGFLYITGRIKELIITAgGENVPPVPI 460

                   ....*.
gi 1888712850  504 EQAVEA 509
Cdd:cd05933    461 EDAVKK 466
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1238-1707 2.14e-21

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 99.81  E-value: 2.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1238 RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLce 1317
Cdd:cd05971      6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV-- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1318 ddcsaldlmgvqharIDAAQEEAqreqhlraphalpavdprsaaYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPP 1397
Cdd:cd05971     84 ---------------TDGSDDPA---------------------LIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLF 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1398 PRARFAMVST-----IGADLGhtVLFGALASGGALhLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAAD- 1471
Cdd:cd05971    128 PRDGDLYWTPadwawIGGLLD--VLLPSLYFGVPV-LAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKh 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1472 -ALPAHTLVLGGEATSWELL----DTIAAlrpdcRVHNHYGPTETTVGILTQPAAQACRAAAtlpLGRPLDNNETWLLDE 1546
Cdd:cd05971    205 aQVKLRAIATGGESLGEELLgwarEQFGV-----EVNEFYGQTECNLVIGNCSALFPIKPGS---MGKPIPGHRVAIVDD 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1547 HLNPVGTGGTGE--LYLGGAGVALGYLHQPALTAARFvphpfaAGARLyRSGDRARRLADGSLEYLGRIDDQVKIRGYRV 1624
Cdd:cd05971    277 NGTPLPPGEVGEiaVELPDPVAFLGYWNNPSATEKKM------AGDWL-LTGDLGRKDSDGYFWYVGRDDDVITSSGYRI 349
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1625 EPGEIAARLKALDGVRDAAVI----VVAGARLAAFATPQPGASLDAAALKRAL---AALLPDYMVPSVLRVIDALPLNRN 1697
Cdd:cd05971    350 GPAEIEECLLKHPAVLMAAVVgipdPIRGEIVKAFVVLNPGETPSDALAREIQelvKTRLAAHEYPREIEFVNELPRTAT 429
                          490
                   ....*....|
gi 1888712850 1698 GKLDRQALSA 1707
Cdd:cd05971    430 GKIRRRELRA 439
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
1239-1662 2.21e-21

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 99.98  E-value: 2.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1239 MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCED 1318
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1319 dcsaldlmgvqharidaaqeeaqreqhlraphalpavdPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPP 1398
Cdd:cd05907     86 --------------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATE 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1399 RAR---FAMVSTIGADLghTVLFGALASGGALHLIDRDTTLDAD--RFAQT--LAAARI-------DVLKIVPGHLHALL 1464
Cdd:cd05907    128 GDRhlsFLPLAHVFERR--AGLYVPLLAGARIYFASSAETLLDDlsEVRPTvfLAVPRVwekvyaaIKVKAVPGLKRKLF 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1465 qAERAADALPAhtLVLGGEATSWELLDTIAALrpDCRVHNHYGPTETTVGILTQPAAQACRAAatlpLGRPLDNNETWLL 1544
Cdd:cd05907    206 -DLAVGGRLRF--AASGGAPLPAELLHFFRAL--GIPVYEGYGLTETSAVVTLNPPGDNRIGT----VGKPLPGVEVRIA 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1545 DEhlnpvgtggtGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlYRSGDRARRLADGSLEYLGRIDD-QVKIRGYR 1623
Cdd:cd05907    277 DD----------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDlIITSGGKN 340
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1888712850 1624 VEPGEIAARLKALDGVRDAAVIVVAGARLAAFATPQPGA 1662
Cdd:cd05907    341 ISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPEA 379
PRK09088 PRK09088
acyl-CoA synthetase; Validated
32-593 2.89e-21

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 99.88  E-value: 2.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   32 QQRPEATALIVIDADGDTRYDYAQLDRRARALAARFARDGAA-AERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESK 110
Cdd:PRK09088     4 HARLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVdGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  111 REQHlarlrGIARDAGVRYVLTTAAlherhadawsMLAPGADVVAVDTLDAR-DTPSDAPLHPVRADDLAFLQYTSGSTG 189
Cdd:PRK09088    84 SELD-----ALLQDAEPRLLLGDDA----------VAAGRTDVEDLAAFIASaDALEPADTPSIPPERVSLILFTSGTSG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  190 SPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLlQPVFSGIPLVLMSPQYFLERPLRWLdaiarhr 269
Cdd:PRK09088   149 QPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSV-RPVLAVGGSILVSNGFEPKRTLGRL------- 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  270 gtisGAPDFA--YRLCAERINDETRAK--LDLSSWR---LAFSGSEPVRRDTLDDFVARFAPagfdaaaLYPCYGLAEAT 342
Cdd:PRK09088   221 ----GDPALGitHYFCVPQMAQAFRAQpgFDAAALRhltALFTGGAPHAAEDILGWLDDGIP-------MVDGFGMSEAG 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  343 LfVTGGVRGAGLVSHAFSSAALSAgraeaaraDEAATVLVgcgavqaghrvaivaraaaeshESHEADVETetsragerl 422
Cdd:PRK09088   290 T-VFGMSVDCDVIRAKAGAAGIPT--------PTVQTRVV----------------------DDQGNDCPA--------- 329
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  423 adGRIGEIHVSGPSVAHGYWQRADASAQAFvdaprhaDGSGparWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQ 501
Cdd:PRK09088   330 --GVPGELLLRGPNLSPGYWRRPQATARAF-------TGDG---WFRTGDIARRDaDGFFWVVDRKKDMFISGGENVYPA 397
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  502 DVEQAVEAHAEF----------ARKGRVIAFGATLGGGETLGLAlEIAPRMKKRFAAAQIVETLRRIAfdacgetpaaia 571
Cdd:PRK09088   398 EIEAVLADHPGIrecavvgmadAQWGEVGYLAIVPADGAPLDLE-RIRSHLSTRLAKYKVPKHLRLVD------------ 464
                          570       580
                   ....*....|....*....|..
gi 1888712850  572 llnpgALPKTSSGKLQRAATRE 593
Cdd:PRK09088   465 -----ALPRTASGKLQKARLRD 481
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
1881-2165 3.96e-21

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 98.66  E-value: 3.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1881 DAARLQRSLAAL---IARHEVLRSAFDADDEGDP---VLKIAPrmevlMPVIEPLAHPDNDAnshtnshtnsdenartQA 1954
Cdd:cd19544     34 SRARLDAFLAALqqvIDRHDILRTAILWEGLSEPvqvVWRQAE-----LPVEELTLDPGDDA----------------LA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1955 TAQALDDAARTPFDLSRAPLVRATLLRfDAAH--HVLIVSLHHIVADGGSVHILLDELCELYRAQRDGAPPAlaplaVQY 2032
Cdd:cd19544     93 QLRARFDPRRYRLDLRQAPLLRAHVAE-DPANgrWLLLLLFHHLISDHTSLELLLEEIQAILAGRAAALPPP-----VPY 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2033 ADY-AHwqrARFTPDAvREAQQFWRGYLAD-----AP-ALLPLSTDRARPTRVshagaarHFRLDATLGARVRTLAQAHG 2105
Cdd:cd19544    167 RNFvAQ---ARLGASQ-AEHEAFFREMLGDvdeptAPfGLLDVQGDGSDITEA-------RLALDAELAQRLRAQARRLG 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1888712850 2106 MTPfAVL--LAsfqW--FLHRHTGADDLVIGT-------DVDGRERAelealIGFFVNVVPLRSRIAADGA 2165
Cdd:cd19544    236 VSP-ASLfhLA---WalVLARCSGRDDVVFGTvlsgrmqGGAGADRA-----LGMFINTLPLRVRLGGRSV 297
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
183-511 4.47e-21

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 96.96  E-value: 4.47e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  183 YTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLiGSLLQPVFSGIPLVLMspqyflER--PLR 260
Cdd:cd17637      7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVM------EKfdPAE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  261 WLDAIARHRGTISGapDFAYRLcaERINDE-TRAKLDLSSWRLAFSGSEPvrrdtldDFVARF---APAGFdaaalYPCY 336
Cdd:cd17637     80 ALELIEEEKVTLMG--SFPPIL--SNLLDAaEKSGVDLSSLRHVLGLDAP-------ETIQRFeetTGATF-----WSLY 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  337 GLAEATLFVTGgvrgaglvsHAFSSAALSAGRAEAAradeaatVLVGCgavqaghrvaivaraaaeshesheADVETETS 416
Cdd:cd17637    144 GQTETSGLVTL---------SPYRERPGSAGRPGPL-------VRVRI------------------------VDDNDRPV 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  417 RAGErladgrIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLG-FVHDGQLYIAGRV--KDLVIV 493
Cdd:cd17637    184 PAGE------TGEIVVRGPLVFQGYWNLPELTAYTFRNG-----------WHHTGDLGrFDEDGYLWYAGRKpeKELIKP 246
                          330
                   ....*....|....*...
gi 1888712850  494 RGRNLYPQDVEQAVEAHA 511
Cdd:cd17637    247 GGENVYPAEVEKVILEHP 264
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
75-514 7.52e-21

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 99.51  E-value: 7.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKREqhlarLRGIARDAGVRYVL--------------TTAALHERH 140
Cdd:PRK12492    76 DRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTARE-----MRHQFKDSGARALVylnmfgklvqevlpDTGIEYLIE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  141 ADAWSML--APGADV-VAVDTLD----ARDTPSDAPL--------------HPVRADDLAFLQYTSGSTGSPKGVMVSHG 199
Cdd:PRK12492   151 AKMGDLLpaAKGWLVnTVVDKVKkmvpAYHLPQAVPFkqalrqgrglslkpVPVGLDDIAVLQYTGGTTGLAKGAMLTHG 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  200 NLLANEIAIQAGLG-VRPD---------DVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMS-PQY---FLERPLRWLDAI 265
Cdd:PRK12492   231 NLVANMLQVRACLSqLGPDgqplmkegqEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITnPRDipgFIKELGKWRFSA 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  266 ARHRGTISGA----PDFAyrlcaerindetraKLDLSSWRLAFSGSEPVRRDTLDDFvarfapAGFDAAALYPCYGLAEA 341
Cdd:PRK12492   311 LLGLNTLFVAlmdhPGFK--------------DLDFSALKLTNSGGTALVKATAERW------EQLTGCTIVEGYGLTET 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  342 TLFVTGGVRGA----GLVSHAFSSAALSAgraeaaradeaatvlvgcgavqaghrvaivaraaaeshesheadveteTSR 417
Cdd:PRK12492   371 SPVASTNPYGElarlGTVGIPVPGTALKV------------------------------------------------IDD 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  418 AGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFvdaprhaDGSGparWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGR 496
Cdd:PRK12492   403 DGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL-------DAEG---WFKTGDIAVIDpDGFVRIVDRKKDLIIVSGF 472
                          490
                   ....*....|....*...
gi 1888712850  497 NLYPQDVEQAVEAHAEFA 514
Cdd:PRK12492   473 NVYPNEIEDVVMAHPKVA 490
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
1219-1710 1.32e-20

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 98.86  E-value: 1.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVI------DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVA 1292
Cdd:TIGR02188   63 VDRHLEARPDKVAIIwegdepGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSV 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1293 LDAGNPTQRLAQTLRDCGARLVLCEDDC----SALDLMGVqharIDAAQEEA----------QR---------------- 1342
Cdd:TIGR02188  143 VFGGFSAEALADRINDAGAKLVITADEGlrggKVIPLKAI----VDEALEKCpvsvehvlvvRRtgnpvvpwvegrdvww 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1343 ---EQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVV------IAHGALT-NYVdavlarLDPPPRARFAMVSTIGADL 1412
Cdd:TIGR02188  219 hdlMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLhttggyLLYAAMTmKYV------FDIKDGDIFWCTADVGWIT 292
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1413 GHT-VLFGALASGGalhlidrdTTL---------DADRFAQTLAAARIDVLKIVPGHLHALLqaeRAADALP-AHTL--- 1478
Cdd:TIGR02188  293 GHSyIVYGPLANGA--------TTVmfegvptypDPGRFWEIIEKHKVTIFYTAPTAIRALM---RLGDEWVkKHDLssl 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1479 -VLG--GE---ATSWELLDTIAAlRPDCRVHNHYGPTETTvGILTQPaaqACRAAATLP--LGRPLDNNETWLLDEHLNP 1550
Cdd:TIGR02188  362 rLLGsvGEpinPEAWMWYYKVVG-KERCPIVDTWWQTETG-GIMITP---LPGATPTKPgsATLPFFGIEPAVVDEEGNP 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1551 V-GTGGTGELYLGGA--GVALGYLHQPaltaARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPG 1627
Cdd:TIGR02188  437 VeGPGEGGYLVIKQPwpGMLRTIYGDH----ERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTA 512
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1628 EIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPD---YMVPSVLRVIDALPLNRNGKL 1700
Cdd:TIGR02188  513 EIESALVSHPAVAEAAVVGIPddikGQAIYAFVTLKDGYEPDDELRKELRKHVRKEigpIAKPDKIRFVPGLPKTRSGKI 592
                          570
                   ....*....|
gi 1888712850 1701 DRQALSALAR 1710
Cdd:TIGR02188  593 MRRLLRKIAA 602
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1219-1706 2.18e-20

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 97.65  E-value: 2.18e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVIDGALR--MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAG 1296
Cdd:PRK05852    22 VEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPA 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1297 NPTQRLAQTLRDCGARLVL------CEDDCSALDL--MGVQHARiDAAQEEAQREQHLRA---PHALPAVDP---RSAAY 1362
Cdd:PRK05852   102 LPIAEQRVRSQAAGARVVLidadgpHDRAEPTTRWwpLTVNVGG-DSGPSGGTLSVHLDAatePTPATSTPEglrPDDAM 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1363 VIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRArfAMVSTIGADLGH---TVLFGALASGGALHLIDRdTTLDAD 1439
Cdd:PRK05852   181 IMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRD--ATVAVMPLYHGHgliAALLATLASGGAVLLPAR-GRFSAH 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1440 RFAQTLAAARIDVLKIVPGHLHALLQ---AERAADALPAHTLVLGGEA-----TSWELLDTIAAlrpdcRVHNHYGPTET 1511
Cdd:PRK05852   258 TFWDDIKAVGATWYTAVPTIHQILLEraaTEPSGRKPAALRFIRSCSApltaeTAQALQTEFAA-----PVVCAFGMTEA 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1512 TVGILTQPAAQACR----AAATLPLGRPlDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFa 1587
Cdd:PRK05852   333 THQVTTTQIEGIGQtenpVVSTGLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1588 agarlyRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGAS 1663
Cdd:PRK05852   411 ------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPdqlyGEAVAAVIVPRESAP 484
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1888712850 1664 LDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALS 1706
Cdd:PRK05852   485 PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVA 527
PRK13382 PRK13382
bile acid CoA ligase;
1227-1707 2.24e-20

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 97.52  E-value: 2.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLArdLQGGEP--VAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQ 1304
Cdd:PRK13382    57 PDRPGLIDELGTLTWRELDERSDALAAALQA--LPIGEPrvVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAE 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1305 TLRDCGARLVLCEDDCSAL---DLMGVQHA-RIDAAQEEAQREQH--LRAPHA--LPAVDPRSAAYVIYTSGSSGAPKGV 1376
Cdd:PRK13382   135 VVTREGVDTVIYDEEFSATvdrALADCPQAtRIVAWTDEDHDLTVevLIAAHAgqRPEPTGRKGRVILLTSGTTGTPKGA 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1377 viAHGALTNYVD--AVLARLdpPPRARFAMVstIGADLGHTVLFGALASGGALhlidRDTTLDADRFAQTLAAARID--- 1451
Cdd:PRK13382   215 --RRSGPGGIGTlkAILDRT--PWRAEEPTV--IVAPMFHAWGFSQLVLAASL----ACTIVTRRRFDPEATLDLIDrhr 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1452 --VLKIVPGHLHALLQaeraadaLPAHTLvlggEATSWELLDTIAA----LRPDCRV----------HNHYGPTETTVGI 1515
Cdd:PRK13382   285 atGLAVVPVMFDRIMD-------LPAEVR----NRYSGRSLRFAAAsgsrMRPDVVIafmdqfgdviYNNYNATEAGMIA 353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1516 LTQPAAQACRAAATlplGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYlhQPALTAArfvphpFAAGarLYRS 1595
Cdd:PRK13382   354 TATPADLRAAPDTA---GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD------FHDG--FMAS 420
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1596 GDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKR 1671
Cdd:PRK13382   421 GDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDdeqyGQRLAAFVVLKPGASATPETLKQ 500
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1888712850 1672 ALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSA 1707
Cdd:PRK13382   501 HVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
23-604 2.88e-20

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 97.52  E-value: 2.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVA 101
Cdd:PRK06155    23 LPAMLARQAERYPDRPLLV----FGGTRWTYAEAARAAAAAAHALAAAGvKRGDRVALMCGNRIEFLDVFLGCAWLGAIA 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  102 VPVyppeskreQHLAR---LRGIARDAGVRYVLTTAALHERHADAWSMLAPGADVVAVDTLDARDT----------PSDA 168
Cdd:PRK06155    99 VPI--------NTALRgpqLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpagwstaplpPLDA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  169 PLHP--VRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLiGSLLQPVFSGIPL 246
Cdd:PRK06155   171 PAPAaaVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNAL-NAFFQALLAGATY 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  247 VLmspqyfLER--PLRWLDAIARHRGTIS---GApdFAYRLCAERINDETRAkldlSSWRLAFSGSEPVRrdTLDDFVAR 321
Cdd:PRK06155   250 VL------EPRfsASGFWPAVRRHGATVTyllGA--MVSILLSQPARESDRA----HRVRVALGPGVPAA--LHAAFRER 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  322 FAPAGFDAaalypcYGLAEaTLFVTGGVRGaglvshafSSAALSAGRaeaaradeaatvlvgcgaVQAGhrvaivaraaA 401
Cdd:PRK06155   316 FGVDLLDG------YGSTE-TNFVIAVTHG--------SQRPGSMGR------------------LAPG----------F 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  402 ESHESHEADVETETSRAGERLAdgRIGEIHvsgpSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFV-HDGQ 480
Cdd:PRK06155   353 EARVVDEHDQELPDGEPGELLL--RADEPF----AFATGYFGMPEKTVEAWRNL-----------WFHTGDRVVRdADGW 415
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  481 LYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGrVIAFGATLGGGEtlgLALEIAPRMKKRFAAAQIVE-TLRRIA 559
Cdd:PRK06155   416 FRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAA-VFPVPSELGEDE---VMAAVVLRDGTALEPVALVRhCEPRLA 491
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1888712850  560 FDAcgeTPAAIALLNpgALPKTSSGKLQRAATRE-GWRARTLDLYA 604
Cdd:PRK06155   492 YFA---VPRYVEFVA--ALPKTENGKVQKFVLREqGVTADTWDREA 532
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
758-1058 3.13e-20

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 96.02  E-value: 3.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  758 LDGA-LDREALRQSLDRLCERHAALRTHFVETGdaahlyapRTEAAAPLAWAHVDLSDLGDIDEHDRERALRECAQRFAD 836
Cdd:cd19535     32 FDGEdLDPDRLERAWNKLIARHPMLRAVFLDDG--------TQQILPEVPWYGITVHDLRGLSEEEAEAALEELRERLSH 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  837 APFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRaaldgatthGEAQAKAKTRITYADYAAWQ 916
Cdd:cd19535    104 RVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYE---------DPGEPLPPLELSFRDYLLAE 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  917 RRwLASDAAARQLAYWRAALADDAPPLALPydhTATDTASEnADPRaAARVAFALPAPLAQAVRASAARHRATPFVVLLA 996
Cdd:cd19535    175 QA-LRETAYERARAYWQERLPTLPPAPQLP---LAKDPEEI-KEPR-FTRREHRLSAEQWQRLKERARQHGVTPSMVLLT 248
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1888712850  997 AYHAWLYRVTGQRAIRTGVPVANRTR--PETHDVIGFFVNTLVLHSDCEAATPLASLFSQLRQR 1058
Cdd:cd19535    249 AYAEVLARWSGQPRFLLNLTLFNRLPlhPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQ 312
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
172-510 4.08e-20

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 97.01  E-value: 4.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  172 PVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGV------RPDD-VFVSWLPLYHDMGL-IGSLLQPVFSG 243
Cdd:PRK07059   200 KLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPafekkpRPDQlNFVCALPLYHIFALtVCGLLGMRTGG 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  244 IPLVLMSPqyfleRPLR-WLDAIARHRGTISGAPDFAYRLCaerINDETRAKLDLSSWRLAFSGSEPVRRdtlddfvarf 322
Cdd:PRK07059   280 RNILIPNP-----RDIPgFIKELKKYQVHIFPAVNTLYNAL---LNNPDFDKLDFSKLIVANGGGMAVQR---------- 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  323 apagfdaaalypcyGLAEATLFVTGG--VRGAGLVShafSSAALSAGRAEAaradeaaTVLVGCGAVQAghrvaivaraa 400
Cdd:PRK07059   342 --------------PVAERWLEMTGCpiTEGYGLSE---TSPVATCNPVDA-------TEFSGTIGLPL----------- 386
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  401 aeshESHEADVETEtsrAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVdaprhADGsgparWLRTGDLGFVH-DG 479
Cdd:PRK07059   387 ----PSTEVSIRDD---DGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMT-----ADG-----FFRTGDVGVMDeRG 449
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1888712850  480 QLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PRK07059   450 YTKIVDRKKDMILVSGFNVYPNEIEEVVASH 480
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
721-1038 4.20e-20

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 95.46  E-value: 4.20e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  721 PIEPAEEAVIShaqqRQLFaWrldPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYAPRTE 800
Cdd:cd19547      3 PLAPMQEGMLF----RGLF-W---PDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  801 AAAPlaWAHVDLSDlgdiDEHDRERALREcaQRFAD---APFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQL 877
Cdd:cd19547     75 LAPP--WALLDWSG----EDPDRRAELLE--RLLADdraAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSL 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  878 LVEELVDGYRaaldgATTHGEAQAKAKTRiTYADYAAWQR-RWLASDAAARqlaYWRAALADDAPPlalPYDHTATDTAS 956
Cdd:cd19547    147 IWGDVFRVYE-----ELAHGREPQLSPCR-PYRDYVRWIRaRTAQSEESER---FWREYLRDLTPS---PFSTAPADREG 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  957 EnadpraAARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTrPE---THDVIGFFV 1033
Cdd:cd19547    215 E------FDTVVHEFPEQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRP-PElegSEHMVGIFI 287

                   ....*
gi 1888712850 1034 NTLVL 1038
Cdd:cd19547    288 NTIPL 292
PRK08315 PRK08315
AMP-binding domain protein; Validated
76-504 4.60e-20

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 96.80  E-value: 4.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   76 RALILMDS--GVDYVsaffGCLYAGVvavpvypPESKrEQHLARLRGiARDAGVRYVLTTAALHERHADAWSMLAPGADV 153
Cdd:PRK08315   117 KALIAADGfkDSDYV----AMLYELA-------PELA-TCEPGQLQS-ARLPELRRVIFLGDEKHPGMLNFDELLALGRA 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  154 VAVDTLDARDtpsdAPLHPvraDDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLI 233
Cdd:PRK08315   184 VDDAELAARQ----ATLDP---DDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMV 256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  234 GSLLQPVFSGIPLVLMSPQYfleRPLRWLDAIARHRGT-ISGAPD-FayrlCAErINDETRAKLDLSSWR---LAfsGS- 307
Cdd:PRK08315   257 LGNLACVTHGATMVYPGEGF---DPLATLAAVEEERCTaLYGVPTmF----IAE-LDHPDFARFDLSSLRtgiMA--GSp 326
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  308 --EPVRRDTLDDFvarfapagfDAAALYPCYGLAEATLfvtggvrgaglVSHAfSSAALSagraeaaRADEAATVlvgcG 385
Cdd:PRK08315   327 cpIEVMKRVIDKM---------HMSEVTIAYGMTETSP-----------VSTQ-TRTDDP-------LEKRVTTV----G 374
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  386 AVQAghrvaivaraaaesH-ESHEADVETetsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAfVDAprhadgsgp 464
Cdd:PRK08315   375 RALP--------------HlEVKIVDPET-----GETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDA--------- 425
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1888712850  465 ARWLRTGDLGfVHDGQLY--IAGRVKDLVIVRGRNLYPQDVE 504
Cdd:PRK08315   426 DGWMHTGDLA-VMDEEGYvnIVGRIKDMIIRGGENIYPREIE 466
PRK07470 PRK07470
acyl-CoA synthetase; Validated
23-510 4.75e-20

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 96.65  E-value: 4.75e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVA 101
Cdd:PRK07470     9 LAHFLRQAARRFPDRIALV----WGDRSWTWREIDARVDALAAALAARGvRKGDRILVHSRNCNQMFESMFAAFRLGAVW 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  102 VPV----YPPEskreqhlarLRGIARDAGVRYVLTTAALHErHADAWSMLAPGADVV----------AVDTLDARDTPSD 167
Cdd:PRK07470    85 VPTnfrqTPDE---------VAYLAEASGARAMICHADFPE-HAAAVRAASPDLTHVvaiggaraglDYEALVARHLGAR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  168 APLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNL---LANEIAiqaGL--GVRPDDVFVSWLPLYHDMGlIGSLLQpVFS 242
Cdd:PRK07470   155 VANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMafvITNHLA---DLmpGTTEQDASLVVAPLSHGAG-IHQLCQ-VAR 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  243 GIPLVLMSPQYFlERPLRWlDAIARHRGTISGAPDFAYRLCAErinDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARF 322
Cdd:PRK07470   230 GAATVLLPSERF-DPAEVW-ALVERHRVTNLFTVPTILKMLVE---HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKL 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  323 APAgfdaaaLYPCYGLAEATLFVTggvrgagLVSHAFSSAAlsagraeaaradEAATVLVG-CGAVQAGHrvaivaraaa 401
Cdd:PRK07470   305 GKV------LVQYFGLGEVTGNIT-------VLPPALHDAE------------DGPDARIGtCGFERTGM---------- 349
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  402 esheshEADVETEtsrAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFV-HDGQ 480
Cdd:PRK07470   350 ------EVQIQDD---EGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDG-----------WFRTGDLGHLdARGF 409
                          490       500       510
                   ....*....|....*....|....*....|
gi 1888712850  481 LYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PRK07470   410 LYITGRASDMYISGGSNVYPREIEEKLLTH 439
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1336-1708 7.56e-20

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 93.57  E-value: 7.56e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1336 AQEEAQREQHLRAPHALPAVDPrSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGAdlGHT 1415
Cdd:PRK07824    14 AQDERRAALLRDALRVGEPIDD-DVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPGQWLLALPAHHIA--GLQ 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1416 VLFGALASGGALHLIDRDTTLDADRFAQTLAAARID--VLKIVPGHLHALLQAERAADALPAHTLVL-GGEATSWELLDT 1492
Cdd:PRK07824    91 VLVRSVIAGSEPVELDVSAGFDPTALPRAVAELGGGrrYTSLVPMQLAKALDDPAATAALAELDAVLvGGGPAPAPVLDA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1493 IAALRpdCRVHNHYGPTETTVGILTQpaaqacraaatlplGRPLDNNETWLLDEHLnpvgtggtgelYLGGAGVALGYLH 1572
Cdd:PRK07824   171 AAAAG--INVVRTYGMSETSGGCVYD--------------GVPLDGVRVRVEDGRI-----------ALGGPTLAKGYRN 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1573 QPaltaarfVPHPFAAGArLYRSGDrARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA---- 1648
Cdd:PRK07824   224 PV-------DPDPFAEPG-WFRTDD-LGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPddrl 294
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1649 GARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSAL 1708
Cdd:PRK07824   295 GQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
120-559 1.19e-19

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 94.45  E-value: 1.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  120 GIARdaGVRYVLTTAALHERHADAWSMLAPGADVVAVDTLDAR--------DTPSDAPLHPVRADDLAFLQYTSGSTGSP 191
Cdd:cd05910     23 GIRR--GMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRknlkqclqEAEPDAFIGIPKADEPAAILFTSGSTGTP 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  192 KGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYhdmGLIGSLLQpVFSGIPlvLMSPQyfleRPLR-----WLDAIA 266
Cdd:cd05910    101 KGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF---ALFGPALG-LTSVIP--DMDPT----RPARadpqkLVGAIR 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  267 RHRGTIS-GAP---DFAYRLCAerindetRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPagfDAAALYPcYGLAEAt 342
Cdd:cd05910    171 QYGVSIVfGSPallERVARYCA-------QHGITLPSLRRVLSAGAPVPIALAARLRKMLSD---EAEILTP-YGATEA- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  343 lfvtggvrgagLVSHAFSSAALSAGRAEAARADEAATVlvgcGAVQAGHRVAIVARAAAESHESHEAdvetetsragERL 422
Cdd:cd05910    239 -----------LPVSSIGSRELLATTTAATSGGAGTCV----GRPIPGVRVRIIEIDDEPIAEWDDT----------LEL 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  423 ADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHadgsgpARWLRTGDLGFVHD-GQLYIAGRVKDLVIVRGRNLYPQ 501
Cdd:cd05910    294 PRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSE------GFWHRMGDLGYLDDeGRLWFCGRKAHRVITTGGTLYTE 367
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1888712850  502 DVEQAVEAHAEFARKGRViafGATLGGGETlgLALEIAPRMKKRFAAAQIVETLRRIA 559
Cdd:cd05910    368 PVERVFNTHPGVRRSALV---GVGKPGCQL--PVLCVEPLPGTITPRARLEQELRALA 420
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
75-507 1.20e-19

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 95.71  E-value: 1.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAV---PVYPPESKREQHL--------------ARLRGIARDAGVRYVLTT---- 133
Cdd:PRK08751    77 DRVALMMPNCLQYPIATFGVLRAGLTVVnvnPLYTPRELKHQLIdsgasvlvvidnfgTTVQQVIADTPVKQVITTglgd 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  134 ------AALHERHADAWSMLAPGADVV-AVDTLDARDTPSDAPLHPVR--ADDLAFLQYTSGSTGSPKGVMVSHGNLLAN 204
Cdd:PRK08751   157 mlgfpkAALVNFVVKYVKKLVPEYRINgAIRFREALALGRKHSMPTLQiePDDIAFLQYTGGTTGVAKGAMLTHRNLVAN 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  205 EIAIQAGLGV-----RPDDVFVSWLPLYHDMGLIG-SLLQPVFSGIPLVLMSPqyfleRPLR-WLDAIARHRGT-ISGAP 276
Cdd:PRK08751   237 MQQAHQWLAGtgkleEGCEVVITALPLYHIFALTAnGLVFMKIGGCNHLISNP-----RDMPgFVKELKKTRFTaFTGVN 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  277 DFAYRLcaerINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFvarfapAGFDAAALYPCYGLAEATlfvtggvRGAGLVS 356
Cdd:PRK08751   312 TLFNGL----LNTPGFDQIDFSSLKMTLGGGMAVQRSVAERW------KQVTGLTLVEAYGLTETS-------PAACINP 374
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  357 HAFSSAALSAGRAEaaradeaatvlvgcgavqaghrvaivaraaaeshESHEADVETEtsrAGERLADGRIGEIHVSGPS 436
Cdd:PRK08751   375 LTLKEYNGSIGLPI----------------------------------PSTDACIKDD---AGTVLAIGEIGELCIKGPQ 417
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850  437 VAHGYWQRADASAQAFvdaprHADGsgparWLRTGDLGFVHD-GQLYIAGRVKDLVIVRGRNLYPQDVEQAV 507
Cdd:PRK08751   418 VMKGYWKRPEETAKVM-----DADG-----WLHTGDIARMDEqGFVYIVDRKKDMILVSGFNVYPNEIEDVI 479
PRK07514 PRK07514
malonyl-CoA synthase; Validated
1220-1699 1.27e-19

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 94.94  E-value: 1.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1220 ARHADtqPDAPAV-IDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNP 1298
Cdd:PRK07514    11 AAFAD--RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1299 TQRLAQTLRDCGARLVLC----EDDCSAL-DLMGVQHAR-IDAAQEEAQREQHLRAPHALPAVdPRSA---AYVIYTSGS 1369
Cdd:PRK07514    89 LAELDYFIGDAEPALVVCdpanFAWLSKIaAAAGAPHVEtLDADGTGSLLEAAAAAPDDFETV-PRGAddlAAILYTSGT 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1370 SGAPKGVVIAHGAL-TNyvDAVLARLdppprARFamvsTIGADLGHTV-------LF----GALASGGALHLIDRdttLD 1437
Cdd:PRK07514   168 TGRSKGAMLSHGNLlSN--ALTLVDY-----WRF----TPDDVLIHALpifhthgLFvatnVALLAGASMIFLPK---FD 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1438 ADRFAQTLAAAriDVLKIVPGHLHALLQAERAADALPAHT-LVLGGEATSweLLDTIAAL--RPDCRVHNHYGPTETtvG 1514
Cdd:PRK07514   234 PDAVLALMPRA--TVMMGVPTFYTRLLQEPRLTREAAAHMrLFISGSAPL--LAETHREFqeRTGHAILERYGMTET--N 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1515 ILTQPAAQACRAAATLplGRPLDNNETWLLD-EHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlY 1593
Cdd:PRK07514   308 MNTSNPYDGERRAGTV--GFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------F 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1594 RSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAAL 1669
Cdd:PRK07514   380 ITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPhpdfGEGVTAVVVPKPGAALDEAAI 459
                          490       500       510
                   ....*....|....*....|....*....|
gi 1888712850 1670 KRALAALLPDYMVPSVLRVIDALPLNRNGK 1699
Cdd:PRK07514   460 LAALKGRLARFKQPKRVFFVDELPRNTMGK 489
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
23-510 1.40e-19

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 95.21  E-value: 1.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVA 101
Cdd:COG1021     27 LGDLLRRRAERHPDRIAVV----DGERRLSYAELDRRADRLAAGLLALGlRPGDRVVVQLPNVAEFVIVFFALFRAGAIP 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  102 VPVYPPESKRE-QHLARL---RGI---ARDAGVRYVLTTAALHERHAD--AWSMLAPGADVVAVDTLdaRDTPSDAPLHP 172
Cdd:COG1021    103 VFALPAHRRAEiSHFAEQseaVAYiipDRHRGFDYRALARELQAEVPSlrHVLVVGDAGEFTSLDAL--LAAPADLSEPR 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  173 VRADDLAFLQYTSGSTGSPKGVMVSHGNLL-----ANEIAiqaglGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLV 247
Cdd:COG1021    181 PDPDDVAFFQLSGGTTGLPKLIPRTHDDYLysvraSAEIC-----GLDADTVYLAALPAAHNFPLSSPGVLGVLYAGGTV 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  248 LMSPQyflERPLRWLDAIARHRGTISGAPDFAYRLCaerINDETRAKLDLSSWRLAFSGSepvrrdtlddfvARFAPAgf 327
Cdd:COG1021    256 VLAPD---PSPDTAFPLIERERVTVTALVPPLALLW---LDAAERSRYDLSSLRVLQVGG------------AKLSPE-- 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  328 DAAALYP---C-----YGLAEatlfvtggvrgaGLVSHafssaalsagraeaaradeaaTVLvgcgavqaghrvaivara 399
Cdd:COG1021    316 LARRVRPalgCtlqqvFGMAE------------GLVNY---------------------TRL------------------ 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  400 aaesHESHEADVETE------------TSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVdaprhADGsgparW 467
Cdd:COG1021    345 ----DDPEEVILTTQgrpispddevriVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFT-----PDG-----F 410
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1888712850  468 LRTGDL-GFVHDGQLYIAGRVKDlVIVR-GRNLYPQDVEQAVEAH 510
Cdd:COG1021    411 YRTGDLvRRTPDGYLVVEGRAKD-QINRgGEKIAAEEVENLLLAH 454
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1362-1701 1.84e-19

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 92.83  E-value: 1.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1362 YVIYTSGSSGAPKGVVIAHGAL-------TNYVDAVLARLDPPPRARFA---MVSTIGADLGH----TVLFGALASGGAL 1427
Cdd:cd05924      7 YILYTGGTTGMPKGVMWRQEDIfrmlmggADFGTGEFTPSEDAHKAAAAaagTVMFPAPPLMHgtgsWTAFGGLLGGQTV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1428 HLIDrdTTLDADRFAQTLAAARIDVLKIVpGHLHA--LLQAERAADALPAHTLVL---GGEATSWELLDTIAALRPDCRV 1502
Cdd:cd05924     87 VLPD--DRFDPEEVWRTIEKHKVTSMTIV-GDAMArpLIDALRDAGPYDLSSLFAissGGALLSPEVKQGLLELVPNITL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1503 HNHYGPTETTVGILTQPAAQACRAAAtlplgRPLDNNETWLLDEHLNPVGTGGTGELYLGGAG-VALGYLHQPALTAARF 1581
Cdd:cd05924    164 VDAFGSSETGFTGSGHSAGSGPETGP-----FTRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAETF 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1582 vphPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFAT 1657
Cdd:cd05924    239 ---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPderwGQEVVAVVQ 315
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1888712850 1658 PQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLD 1701
Cdd:cd05924    316 LREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1846-2287 2.18e-19

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 93.47  E-value: 2.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1846 PLSLMQQriWVVDQ-LADRAlaSYNMTAGLDLRGPLDAARLQRSLAALIARHEVLRSAFDADDEGdpvlkiaprmevlmp 1924
Cdd:cd19534      3 PLTPIQR--WFFEQnLAGRH--HFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGG--------------- 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1925 vIEpLAHPDNDANSHTNSHTNSDENARTQATAQALDDAARTpFDLSRAPLVRATLLRFDAAHHVLIVSLHHIVADGGSVH 2004
Cdd:cd19534     64 -WQ-QRIRGDVEELFRLEVVDLSSLAQAAAIEALAAEAQSS-LDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWR 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2005 ILLDELCELYRAQRDGAPPALaPLAVQYADYAHWQRARFTPDAVREAQQFWRGYLADAPALLPLSTDRARPTRVShagaa 2084
Cdd:cd19534    141 ILLEDLEAAYEQALAGEPIPL-PSKTSFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQTYGDART----- 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2085 RHFRLDATLGARVrtLAQAHGM---TPFAVLLASFQWFLHRHTGADDLVIGTDVDGRErAELEAL-----IGFFVNVVPL 2156
Cdd:cd19534    215 VSFTLDEEETEAL--LQEANAAyrtEINDLLLAALALAFQDWTGRAPPAIFLEGHGRE-EIDPGLdlsrtVGWFTSMYPV 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2157 RsriaadgANLASFDAWLDAARQsTWDALdhRALPfDRIVDALALK-------RRRDANPLVQVLF----VLRDLPRGNT 2225
Cdd:cd19534    292 V-------LDLEASEDLGDTLKR-VKEQL--RRIP-NKGIGYGILRyltpegtKRLAFHPQPEISFnylgQFDQGERDDA 360
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1888712850 2226 RVPGLAVELLRP--PTTQSKFDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDAV 2287
Cdd:cd19534    361 LFVSAVGGGGSDigPDTPRFALLDINAVVEGGQLVITVSYSRNMYHEETIQQLADSYKEALEAL 424
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1220-1705 2.89e-19

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 94.04  E-value: 2.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1220 ARHADTQPDAPAVID--GAlRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGN 1297
Cdd:PRK06087    30 QQTARAMPDKIAVVDnhGA-SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSW 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 PTQRLAQTLRDCGARLVLC---------EDDCSAL--DLMGVQHARI----------DAAQEEAQREQHLRAPhalPAVD 1356
Cdd:PRK06087   109 REAELVWVLNKCQAKMFFAptlfkqtrpVDLILPLqnQLPQLQQIVGvdklapatssLSLSQIIADYEPLTTA---ITTH 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1357 PRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMvstiGADLGHTVlfgalasgGALHLIdrdttl 1436
Cdd:PRK06087   186 GDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMM----PAPLGHAT--------GFLHGV------ 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1437 dadrFAQTLAAARIDVLKIV-PGHLHALLQAERAadalpahTLVLGGEATSWELLDTI-------AALR---------P- 1498
Cdd:PRK06087   248 ----TAPFLIGARSVLLDIFtPDACLALLEQQRC-------TCMLGATPFIYDLLNLLekqpadlSALRfflcggttiPk 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1499 ----DCRVHN-----HYGPTETTVGILTQPAAQACRAAATLplGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALG 1569
Cdd:PRK06087   317 kvarECQQRGikllsVYGSTESSPHAVVNLDDPLSRFMHTD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMG 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1570 YLHQPALTAARFVPHPFaagarlYRSGDRARRLADGSLEYLGRIDDqVKIRGyrvepGE-IAAR-----LKALDGVRDAA 1643
Cdd:PRK06087   395 YLDEPELTARALDEEGW------YYSGDLCRMDEAGYIKITGRKKD-IIVRG-----GEnISSRevediLLQHPKIHDAC 462
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1888712850 1644 VIVVA----GARLAAFATPQPGASLDAAALKRA--LAALLPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:PRK06087   463 VVAMPderlGERSCAYVVLKAPHHSLTLEEVVAffSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
31-597 3.26e-19

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 94.07  E-value: 3.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIVIdadGDTRyDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPV----Y 105
Cdd:PRK07786    27 ALMQPDAPALRFL---GNTT-TWRELDDRVAALAGALSRRGvGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVnfrlT 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  106 PPEskreqhlarLRGIARDAGVRYVLTTAALhERHADAWSMLAPGADVVAV------------DTLDARDTPSDAPLHpV 173
Cdd:PRK07786   103 PPE---------IAFLVSDCGAHVVVTEAAL-APVATAVRDIVPLLSTVVVaggssddsvlgyEDLLAEAGPAHAPVD-I 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  174 RADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGV-RPDDVFVSWLPLYHDMGLiGSLLQPVFSGIPLVLMSPQ 252
Cdd:PRK07786   172 PNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGAdINSDVGFVGVPLFHIAGI-GSMLPGLLLGAPTVIYPLG 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  253 YFleRPLRWLDAIARHRGT-ISGAPDFAYRLCAERINDETRAKLDLSSWrlafsGSEPVRRDTLDDFVARFAPAGFDAAa 331
Cdd:PRK07786   251 AF--DPGQLLDVLEAEKVTgIFLVPAQWQAVCAEQQARPRDLALRVLSW-----GAAPASDTLLRQMAATFPEAQILAA- 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  332 lypcYGLAE---ATLFVTG--GVRGAGLVSHAFSSAAlsagraeaaradeaatvlvgcgavqaghrvaivaraaaeshes 406
Cdd:PRK07786   323 ----FGQTEmspVTCMLLGedAIRKLGSVGKVIPTVA------------------------------------------- 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  407 heADVETETSragERLADGRIGEIHVSGPSVAHGYWQRADASAQAFvdaprhADGsgparWLRTGDLGFV-HDGQLYIAG 485
Cdd:PRK07786   356 --ARVVDENM---NDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AGG-----WFHSGDLVRQdEEGYVWVVD 419
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  486 RVKDLVIVRGRNLYPQDVEQAVEAH---AEFARKGRV--------IAFGATLGGGETLGLAlEIAPRMKKRFAAAQivet 554
Cdd:PRK07786   420 RKKDMIISGGENIYCAEVENVLASHpdiVEVAVIGRAdekwgevpVAVAAVRNDDAALTLE-DLAEFLTDRLARYK---- 494
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1888712850  555 lrriafdacgeTPAAIALLNpgALPKTSSGKLQRAATREGWRA 597
Cdd:PRK07786   495 -----------HPKALEIVD--ALPRNPAGKVLKTELRERYGA 524
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
31-593 4.85e-19

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 92.99  E-value: 4.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATAlivIDADgDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVPVYPpes 109
Cdd:cd05918      9 ARSQPDAPA---VCAW-DGSLTYAELDRLSSRLAHHLRSLGVGPGVFVpLCFEKSKWAVVAMLAVLKAGGAFVPLDP--- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  110 krEQHLARLRGIARDAGVRYVLTTaalherhadawsmlapgadvvavdtldardtpsdaplhpvRADDLAFLQYTSGSTG 189
Cdd:cd05918     82 --SHPLQRLQEILQDTGAKVVLTS----------------------------------------SPSDAAYVIFTSGSTG 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  190 SPKGVMVSHGNLLANEIAIQAGLGVRPDD-VF--------VSWLPLYhdMGLIgsllqpvfSGIPLVLMSPQyflERPLR 260
Cdd:cd05918    120 KPKGVVIEHRALSTSALAHGRALGLTSESrVLqfasytfdVSILEIF--TTLA--------AGGCLCIPSEE---DRLND 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  261 WLDAIARHRGTISGA-PDFAyRLcaerINDEtraklDLSSWRLAFSGSEPVRRDTLDDFVARfapagfdaAALYPCYGLA 339
Cdd:cd05918    187 LAGFINRLRVTWAFLtPSVA-RL----LDPE-----DVPSLRTLVLGGEALTQSDVDTWADR--------VRLINAYGPA 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  340 EATLFVTGGVRG----AGLVSHAFSSAALsagraeaaradeaatVLvgcgavqaghrvaivaraAAESHESHeadvetet 415
Cdd:cd05918    249 ECTIAATVSPVVpstdPRNIGRPLGATCW---------------VV------------------DPDNHDRL-------- 287
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  416 sragerLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAP--RHADGSGPARWL-RTGDLG-FVHDGQLYIAGRVKDLV 491
Cdd:cd05918    288 ------VPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawLKQEGSGRGRRLyRTGDLVrYNPDGSLEYVGRKDTQV 361
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  492 IVRG------------RNLYPQDVEQAVEA--HAEFARKGRVIAF----GATLGGGETLGLALEIAPRMKKRFAAAQive 553
Cdd:cd05918    362 KIRGqrvelgeiehhlRQSLPGAKEVVVEVvkPKDGSSSPQLVAFvvldGSSSGSGDGDSLFLEPSDEFRALVAELR--- 438
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1888712850  554 tlrriafDACGET------PAAIALLNpgALPKTSSGKLQRAATRE 593
Cdd:cd05918    439 -------SKLRQRlpsymvPSVFLPLS--HLPLTASGKIDRRALRE 475
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
1209-1707 5.52e-19

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 93.14  E-value: 5.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1209 TPPGEPIHLRVARhadtQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGG 1288
Cdd:PRK13383    35 TNPYTLLAVTAAR----WPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGA 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1289 AYVALDAGNPTQRLAQTLRDCGARLVLCEDD-CSALDLMGVQHARIDAAQEEAqreqhlRAPHALPAVDPrSAAYVIYTS 1367
Cdd:PRK13383   111 DVVPISTEFRSDALAAALRAHHISTVVADNEfAERIAGADDAVAVIDPATAGA------EESGGRPAVAA-PGRIVLLTS 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1368 GSSGAPKGVVIA---HGALTNYVdAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALhLIDRDttLDADRFAQT 1444
Cdd:PRK13383   184 GTTGKPKGVPRApqlRSAVGVWV-TILDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTV-LTHRH--FDAEAALAQ 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1445 LAAARIDVLKIVPGHLHALLQAE---RAADALPAHTLVLggeaTSWELLDTIAALR-----PDCrVHNHYGPTETTVGIL 1516
Cdd:PRK13383   260 ASLHRADAFTAVPVVLARILELPprvRARNPLPQLRVVM----SSGDRLDPTLGQRfmdtyGDI-LYNGYGSTEVGIGAL 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1517 TQPAAQACRAAAtlpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYlhqpALTAARFVPHPFAAgarlyrSG 1596
Cdd:PRK13383   335 ATPADLRDAPET---VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY----TDGGGKAVVDGMTS------TG 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1597 DRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRA 1672
Cdd:PRK13383   402 DMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPderfGHRLAAFVVLHPGSGVDAAQLRDY 481
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1888712850 1673 LAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSA 1707
Cdd:PRK13383   482 LKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
PRK07787 PRK07787
acyl-CoA synthetase; Validated
72-486 7.29e-19

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 92.36  E-value: 7.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   72 AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKREqhlarLRGIARDAGvryvlttaalherhADAWSMLAPGA 151
Cdd:PRK07787    43 AGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAE-----RRHILADSG--------------AQAWLGPAPDD 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  152 D----VVAVDtLDARdtpSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLY 227
Cdd:PRK07787   104 PaglpHVPVR-LHAR---SWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLF 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  228 HDMGLIGSLLQPVFSGIPLV-LMSPqyfleRPLRWLDAIARHRGTISGAPDFAYRLCAERinDETRAkldLSSWRLAFSG 306
Cdd:PRK07787   180 HVHGLVLGVLGPLRIGNRFVhTGRP-----TPEAYAQALSEGGTLYFGVPTVWSRIAADP--EAARA---LRGARLLVSG 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  307 SEPVRRDTLDDFVArfapagfdAAALYPC--YGLAEaTLFVTG----GVRGAGLVSHAFSSAAlsagraeaaradeaaTV 380
Cdd:PRK07787   250 SAALPVPVFDRLAA--------LTGHRPVerYGMTE-TLITLStradGERRPGWVGLPLAGVE---------------TR 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  381 LVGcgavqaghrvaivaraaaESHESHEADVETetsragerladgrIGEIHVSGPSVAHGYWQRADASAQAFvdaprHAD 460
Cdd:PRK07787   306 LVD------------------EDGGPVPHDGET-------------VGELQVRGPTLFDGYLNRPDATAAAF-----TAD 349
                          410       420
                   ....*....|....*....|....*..
gi 1888712850  461 GsgparWLRTGDLGFVH-DGQLYIAGR 486
Cdd:PRK07787   350 G-----WFRTGDVAVVDpDGMHRIVGR 371
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
1198-1692 7.52e-19

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 93.02  E-value: 7.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1198 ARVSAASVARRTPPGEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFV 1277
Cdd:PRK08279    22 LRGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1278 VAMLGVLKAGGAyVALDagNPTQR---LAQTLRDCGARLVLCEDDCSA-----------------LDLMGVQHARIDAAQ 1337
Cdd:PRK08279   102 AAWLGLAKLGAV-VALL--NTQQRgavLAHSLNLVDAKHLIVGEELVEafeearadlarpprlwvAGGDTLDDPEGYEDL 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1338 EEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVL 1417
Cdd:PRK08279   179 AAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVA 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1418 FG-ALASGGALHLIDRdttLDADRFAQTLAAARIDVLKIVpGHL--HALLQAERAADAlpAHTLVLGgeatswelldTIA 1494
Cdd:PRK08279   259 WSsVLAAGATLALRRK---FSASRFWDDVRRYRATAFQYI-GELcrYLLNQPPKPTDR--DHRLRLM----------IGN 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1495 ALRPDC-----------RVHNHYGPTETTVGILTQPAAQACRAAATLPLGRPLD------NNETWLLDE--HLNPVGTGG 1555
Cdd:PRK08279   323 GLRPDIwdefqqrfgipRILEFYAASEGNVGFINVFNFDGTVGRVPLWLAHPYAivkydvDTGEPVRDAdgRCIKVKPGE 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1556 TGELY--LGGAGVALGYLhQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARL 1633
Cdd:PRK08279   403 VGLLIgrITDRGPFDGYT-DPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENAL 481
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1888712850 1634 KALDGVRDAAVIVV--------AGarLAAFaTPQPGASLDAAALKRALAALLPDYMVPSVLRVIDAL 1692
Cdd:PRK08279   482 SGFPGVEEAVVYGVevpgtdgrAG--MAAI-VLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPEL 545
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
29-590 8.27e-19

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 92.00  E-value: 8.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   29 ALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVPV--- 104
Cdd:cd12115      7 AQAARTPDAIALV----CGDESLTYAELNRRANRLAARLRAAGVGPESRVgVCLERTPDLVVALLAVLKAGAAYVPLdpa 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  105 YPPEskreqhlaRLRGIARDAGVRYVLTTaalherhadawsmlapgadvvavdtldardtpsdaplhpvrADDLAFLQYT 184
Cdd:cd12115     83 YPPE--------RLRFILEDAQARLVLTD-----------------------------------------PDDLAYVIYT 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  185 SGSTGSPKGVMVSHGNLLAneiAIQAGLGVRPDDVFVSWL---PLYHDMGlIGSLLQPVFSGIPLVLMSPQYFLerplrw 261
Cdd:cd12115    114 SGSTGRPKGVAIEHRNAAA---FLQWAAAAFSAEELAGVLastSICFDLS-VFELFGPLATGGKVVLADNVLAL------ 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  262 ldaiarhrgtisgaPDFAYRLCAERIN---DETRAKLDL----SSWRLAFSGSEPVRRDTLDDFVARfapagFDAAALYP 334
Cdd:cd12115    184 --------------PDLPAAAEVTLINtvpSAAAELLRHdalpASVRVVNLAGEPLPRDLVQRLYAR-----LQVERVVN 244
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  335 CYGLAEATLFVTGgvrgaglvshafssAALSAGRAEAaradeaatvlVGCGAVQAGHRvaivaraaaeshesheADVete 414
Cdd:cd12115    245 LYGPSEDTTYSTV--------------APVPPGASGE----------VSIGRPLANTQ----------------AYV--- 281
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  415 TSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHadgsGPARWLRTGDLG-FVHDGQLYIAGRVKDLVIV 493
Cdd:cd12115    282 LDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG----PGARLYRTGDLVrWRPDGLLEFLGRADNQVKV 357
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  494 RGRNLYPQDVEQAVEAHAEfARKGRVIAFGATLGGGETLGL-----ALEIAPRMKKRFAAAQIVETLrriafdacgeTPA 568
Cdd:cd12115    358 RGFRIELGEIEAALRSIPG-VREAVVVAIGDAAGERRLVAYivaepGAAGLVEDLRRHLGTRLPAYM----------VPS 426
                          570       580
                   ....*....|....*....|..
gi 1888712850  569 AIALLNpgALPKTSSGKLQRAA 590
Cdd:cd12115    427 RFVRLD--ALPLTPNGKIDRSA 446
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
1229-1705 1.04e-18

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 91.39  E-value: 1.04e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1229 APAVIDGALRMSYAELDARAAHVAQWLLAR-DLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLR 1307
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1308 DCGARLVLCEddcsaldlmgvqharidaaqeeaqreqhlrapHALPAVDprSAAYVIYTSGSSGAPKGVVIAHGALTNYV 1387
Cdd:cd05958     81 KARITVALCA--------------------------------HALTASD--DICILAFTSGTTGAPKATMHFHRDPLASA 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1388 DAvLAR--LDPPPRARFAMVS----TIGADLghtVLFGALASGGALHLIDRDTtldADRFAQTLAAARIDVLKIVPGHLH 1461
Cdd:cd05958    127 DR-YAVnvLRLREDDRFVGSPplafTFGLGG---VLLFPFGVGASGVLLEEAT---PDLLLSAIARYKPTVLFTAPTAYR 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1462 ALLQAER--------------AADALPAHTLVLGGEATSWELLDTIaalrpdcrvhnhyGPTETT-VGILTQPAAQACRA 1526
Cdd:cd05958    200 AMLAHPDaagpdlsslrkcvsAGEALPAALHRAWKEATGIPIIDGI-------------GSTEMFhIFISARPGDARPGA 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1527 aatlpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAgvaLGYLHQPALTAARFVphpfaAGARLYrSGDRARRLADGS 1606
Cdd:cd05958    267 -----TGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYV-----QGGWNI-TGDTYSRDPDGY 332
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1607 LEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKR---ALAALLPD 1679
Cdd:cd05958    333 FRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPdesrGVVVKAFVVLRPGVIPGPVLARElqdHAKAHIAP 412
                          490       500
                   ....*....|....*....|....*.
gi 1888712850 1680 YMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:cd05958    413 YKYPRAIEFVTELPRTATGKLQRFAL 438
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
174-491 1.26e-18

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 91.89  E-value: 1.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  174 RADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLG--VRPDDVFVSWLPLYHDM------------GLIG----- 234
Cdd:cd17639     86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLAYLPLAHIFelaaenvclyrgGTIGygspr 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  235 --------------SLLQP-VFSGIPLVL----------MSPQYFLERPLRWLdAIARHRGTISGAPDFAY--RLCAERI 287
Cdd:cd17639    166 tltdkskrgckgdlTEFKPtLMVGVPAIWdtirkgvlakLNPMGGLKRTLFWT-AYQSKLKALKEGPGTPLldELVFKKV 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  288 NDETRAKLdlsswRLAFSGSEPVRRDT---LDDFVARFAPAgfdaaalypcYGLAEATlfvtggvrGAGLVSHAFSSAAL 364
Cdd:cd17639    245 RAALGGRL-----RYMLSGGAPLSADTqefLNIVLCPVIQG----------YGLTETC--------AGGTVQDPGDLETG 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  365 SAGRaeaaradeaatvLVGCGAVQ------AGHRvaivaraaaeshesheadveteTSRAGERladgriGEIHVSGPSVA 438
Cdd:cd17639    302 RVGP------------PLPCCEIKlvdweeGGYS----------------------TDKPPPR------GEILIRGPNVF 341
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1888712850  439 HGYWQRADASAQAFvdaprhaDGSGparWLRTGDLGFVH-DGQLYIAGRVKDLV 491
Cdd:cd17639    342 KGYYKNPEKTKEAF-------DGDG---WFHTGDIGEFHpDGTLKIIDRKKDLV 385
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
1238-1705 1.52e-18

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 91.00  E-value: 1.52e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1238 RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVlce 1317
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVA--- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1318 ddcsaldlmgVQHARIDaaqeeaqreqhlraphalpavdprSAAYVIYTSGSSGAPKGVVIAHGAL--TNYVDAVLARLD 1395
Cdd:cd05935     78 ----------VVGSELD------------------------DLALIPYTSGTTGLPKGCMHTHFSAaaNALQSAVWTGLT 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1396 PPPRARFAMVSTIGADLGHTVLfGALASGGALHLI---DRDTTLDA-DRFAQTLAAAridvlkiVPGHLHALLQAERAAD 1471
Cdd:cd05935    124 PSDVILACLPLFHVTGFVGSLN-TAVYVGGTYVLMarwDRETALELiEKYKVTFWTN-------IPTMLVDLLATPEFKT 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1472 ALPAHTLVLGG------EATSWELLDTiAALRpdcrvHNH-YGPTETTVGILTQPAAQACRAAatlpLGRPLDNNETWLL 1544
Cdd:cd05935    196 RDLSSLKVLTGggapmpPAVAEKLLKL-TGLR-----FVEgYGLTETMSQTHTNPPLRPKLQC----LGIP*FGVDARVI 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1545 D-EHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVphpFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYR 1623
Cdd:cd05935    266 DiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1624 VEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQPG--ASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRN 1697
Cdd:cd05935    343 VWPAEVEAKLYKHPAI*EVCVISVpderVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSAS 422

                   ....*...
gi 1888712850 1698 GKLDRQAL 1705
Cdd:cd05935    423 GKILWRLL 430
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1238-1705 1.62e-18

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 91.54  E-value: 1.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1238 RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCE 1317
Cdd:cd12119     25 RYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVD 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1318 DDCSAL------DLMGVQH--------ARIDAAQEEAQREQHLRAPHA----LPAVDPRSAAYVIYTSGSSGAPKGVVIA 1379
Cdd:cd12119    105 RDFLPLleaiapRLPTVEHvvvmtddaAMPEPAGVGVLAYEELLAAESpeydWPDFDENTAAAICYTSGTTGNPKGVVYS 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1380 HGALtnyvdaVLARLdppprarfAMVSTIGADLGH--TVL--------------FGALASGGALHLIDRDttLDADRFAQ 1443
Cdd:cd12119    185 HRSL------VLHAM--------AALLTDGLGLSEsdVVLpvvpmfhvnawglpYAAAMVGAKLVLPGPY--LDPASLAE 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1444 TLAAARIDVLKIVPGHLHALLQAERAADA--LPAHTLVLGGEATSWELLDTIAALrpDCRVHNHYGPTET----TVGILT 1517
Cdd:cd12119    249 LIEREGVTFAAGVPTVWQGLLDHLEANGRdlSSLRRVVIGGSAVPRSLIEAFEER--GVRVIHAWGMTETsplgTVARPP 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1518 ---QPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGG--TGELYLGGAGVALGYLHQPALTAARFVPHPFaagarl 1592
Cdd:cd12119    327 sehSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWDGkaVGELQVRGPWVTKSYYKNDEESEALTEDGWL------ 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1593 yRSGDRARRLADGSLEYLGRIDDQVKIRG---YRVEPGEIAArlkALDGVRDAAVIVVA----GARLAAFATPQPGASLD 1665
Cdd:cd12119    401 -RTGDVATIDEDGYLTITDRSKDVIKSGGewiSSVELENAIM---AHPAVAEAAVIGVPhpkwGERPLAVVVLKEGATVT 476
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1888712850 1666 AAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:cd12119    477 AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
75-592 1.80e-18

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 90.95  E-value: 1.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPpeskreqhlarlrgiardagvryVLTTAALHERHADAwsmlapGADVV 154
Cdd:cd05971     32 DRVGVFLSQGPECAIAHIAILRSGAIAVPLFA-----------------------LFGPEALEYRLSNS------GASAL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  155 AVDTldardtpsdaplhpvrADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLyhDMGLIG 234
Cdd:cd05971     83 VTDG----------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPA--DWAWIG 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  235 SLLQPVFS----GIPLVLMSPQYFleRPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLDLSSwrlAFSGSEPV 310
Cdd:cd05971    145 GLLDVLLPslyfGVPVLAHRMTKF--DPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRA---IATGGESL 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  311 -------RRDTLDDFVARFapagfdaaalypcYGLAEATLFVTggvrgaglvshafSSAALSAGRAEAAradeaatvlvg 383
Cdd:cd05971    220 geellgwAREQFGVEVNEF-------------YGQTECNLVIG-------------NCSALFPIKPGSM----------- 262
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  384 cGAVQAGHrvaivaraaaeshesheaDVETETSrAGERLADGRIGEIHVSGP-SVAH-GYWQRADASAQAFVdaprhadg 461
Cdd:cd05971    263 -GKPIPGH------------------RVAIVDD-NGTPLPPGEVGEIAVELPdPVAFlGYWNNPSATEKKMA-------- 314
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  462 sgpARWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH---AEFARKGR--------VIAFgATLGGG 529
Cdd:cd05971    315 ---GDWLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHpavLMAAVVGIpdpirgeiVKAF-VVLNPG 390
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850  530 ETLG--LALEIAPRMKKRFAAAqivetlrriafdacgETPAAIAllNPGALPKTSSGKLQRAATR 592
Cdd:cd05971    391 ETPSdaLAREIQELVKTRLAAH---------------EYPREIE--FVNELPRTATGKIRRRELR 438
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
1221-1709 1.96e-18

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 91.85  E-value: 1.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1221 RHADTQPDAPAVI------DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALD 1294
Cdd:cd05966     61 RHLKERGDKVAIIwegdepDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVF 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1295 AGNPTQRLAQTLRDCGARLVLCEDDCS--------------ALDLMG-------VQHARIDAAQEE-----AQREQHLRA 1348
Cdd:cd05966    141 AGFSAESLADRINDAQCKLVITADGGYrggkviplkeivdeALEKCPsvekvlvVKRTGGEVPMTEgrdlwWHDLMAKQS 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1349 PHALP-AVDPRSAAYVIYTSGSSGAPKGVVIAHG------ALT-NYVdavlarLDPPPRARFAMVSTIGADLGHT-VLFG 1419
Cdd:cd05966    221 PECEPeWMDSEDPLFILYTSGSTGKPKGVVHTTGgyllyaATTfKYV------FDYHPDDIYWCTADIGWITGHSyIVYG 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1420 ALASGGalhlidrdTTL---------DADRFAQTLAAARIDVLKIVPGHLHALLQAerAADALPAHTL----VLG--GE- 1483
Cdd:cd05966    295 PLANGA--------TTVmfegtptypDPGRYWDIVEKHKVTIFYTAPTAIRALMKF--GDEWVKKHDLsslrVLGsvGEp 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1484 --ATSWELLDTIAAlRPDCRVHNHYGPTETTvGILTQPaaqacraaatLP---------LGRPLDNNETWLLDEHLNPVG 1552
Cdd:cd05966    365 inPEAWMWYYEVIG-KERCPIVDTWWQTETG-GIMITP----------LPgatplkpgsATRPFFGIEPAILDEEGNEVE 432
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1553 TGGTGELYLGGA--GVALGYL--HQpaltaaRFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGE 1628
Cdd:cd05966    433 GEVEGYLVIKRPwpGMARTIYgdHE------RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAE 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1629 IAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPD---YMVPSVLRVIDALPLNRNGKLD 1701
Cdd:cd05966    507 VESALVAHPAVAEAAVVGRPhdikGEAIYAFVTLKDGEEPSDELRKELRKHVRKEigpIATPDKIQFVPGLPKTRSGKIM 586

                   ....*...
gi 1888712850 1702 RQALSALA 1709
Cdd:cd05966    587 RRILRKIA 594
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
177-514 2.01e-18

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 89.10  E-value: 2.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  177 DLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSG---IPLVLMSPQY 253
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGatvVPVAVFDVDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  254 FLErplrwldAIARHRGTI-SGAPDFAYRLCAErindETRAKLDLSSWRLAFSGSEPVRRDtlddFVARF-APAGFDAAA 331
Cdd:cd17638     81 ILE-------AIERERITVlPGPPTLFQSLLDH----PGRKKFDLSSLRAAVTGAATVPVE----LVRRMrSELGFETVL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  332 lyPCYGLAEAtlfvtggvrGAGLVSHAFSSAalsagraeaaradeaATVLVGCGAVQAGhrvaivaraaaeshesheadv 411
Cdd:cd17638    146 --TAYGLTEA---------GVATMCRPGDDA---------------ETVATTCGRACPG--------------------- 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  412 eTETsrageRLADGriGEIHVSGPSVAHGYWQRADASAQAfVDAprhaDGsgparWLRTGDLGFVHD-GQLYIAGRVKDL 490
Cdd:cd17638    179 -FEV-----RIADD--GEVLVRGYNVMQGYLDDPEATAEA-IDA----DG-----WLHTGDVGELDErGYLRITDRLKDM 240
                          330       340
                   ....*....|....*....|....
gi 1888712850  491 VIVRGRNLYPQDVEQAVEAHAEFA 514
Cdd:cd17638    241 YIVGGFNVYPAEVEGALAEHPGVA 264
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
31-510 2.12e-18

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 91.24  E-value: 2.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIVidadGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVPV---YP 106
Cdd:cd17655      7 AEKTPDHTAVVF----EDQTLTYRELNERANQLARTLREKGVGPDTIVgIMAERSLEMIVGILGILKAGGAYLPIdpdYP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  107 PEskreqhlaRLRGIARDAGVRYVLTTAALHERHADAwsmlapgADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSG 186
Cdd:cd17655     83 EE--------RIQYILEDSGADILLTQSHLQPPIAFI-------GLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  187 STGSPKGVMVSHGNL----LANEIAIQAGLGVRpddvFVSWLPLYHDMGlIGSLLQPVFSGIPLVLmSPQYFLERPLRWL 262
Cdd:cd17655    148 STGKPKGVMIEHRGVvnlvEWANKVIYQGEHLR----VALFASISFDAS-VTEIFASLLSGNTLYI-VRKETVLDGQALT 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  263 DAIARHRGTI-SGAPDFAYRLCAERINDEtrakldlSSWRLAFSGSEPVRRDTLDDFVARFApagfDAAALYPCYGLAEA 341
Cdd:cd17655    222 QYIRQNRITIiDLTPAHLKLLDAADDSEG-------LSLKHLIVGGEALSTELAKKIIELFG----TNPTITNAYGPTET 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  342 TlfvtggvrgaglvshafssaalsagraeaaradeaatvlVGCgavqaghrvaivaraaaESHESHEADVETETSRAGER 421
Cdd:cd17655    291 T---------------------------------------VDA-----------------SIYQYEPETDQQVSVPIGKP 314
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  422 LADGRI---------------GEIHVSGPSVAHGYWQRADASAQAFVDAPRHADGsgpaRWLRTGDLG-FVHDGQLYIAG 485
Cdd:cd17655    315 LGNTRIyildqygrpqpvgvaGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGE----RMYRTGDLArWLPDGNIEFLG 390
                          490       500
                   ....*....|....*....|....*
gi 1888712850  486 RVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:cd17655    391 RIDHQVKIRGYRIELGEIEARLLQH 415
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
1231-1705 2.89e-18

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 90.91  E-value: 2.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1231 AVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCG 1310
Cdd:PRK12406     4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1311 ARLVLCEDDC---------SALDLMGV-------QHARIDAAQE---------EAQREQHlrAPHALPAVdpRSAAYVIY 1365
Cdd:PRK12406    84 ARVLIAHADLlhglasalpAGVTVLSVptppeiaAAYRISPALLtppagaidwEGWLAQQ--EPYDGPPV--PQPQSMIY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1366 TSGSSGAPKGVVIA-----HGALTNYVDAVLARLDPPPRArfamvsTIGADLGHTV--LFG--ALASGGALHLIDRdttL 1436
Cdd:PRK12406   160 TSGTTGHPKGVRRAaptpeQAAAAEQMRALIYGLKPGIRA------LLTGPLYHSApnAYGlrAGRLGGVLVLQPR---F 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1437 DADRFAQTLAAARIDVLKIVPGHLHALLQ---AERAADALPAHTLVLGGEA-----TSWELLDTIAALrpdcrVHNHYGP 1508
Cdd:PRK12406   231 DPEELLQLIERHRITHMHMVPTMFIRLLKlpeEVRAKYDVSSLRHVIHAAApcpadVKRAMIEWWGPV-----IYEYYGS 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1509 TETTVGILTQPAAQACRAAAtlpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVAL-GYLHQPALTAArfvphpfA 1587
Cdd:PRK12406   306 TESGAVTFATSEDALSHPGT---VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-------I 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1588 AGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGAS 1663
Cdd:PRK12406   376 DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPdaefGEALMAVVEPQPGAT 455
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1888712850 1664 LDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:PRK12406   456 LDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1239-1705 3.06e-18

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 89.88  E-value: 3.06e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1239 MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCED 1318
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1319 DcsaldlmgvQHARIDAaqeeaqreqhlraphalpavDPrsaAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPP 1398
Cdd:cd05973     81 A---------NRHKLDS--------------------DP---FVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRP 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1399 RARFAMVSTIGADLG-HTVLFGALASGGALHLIDR----DTTLDA-DRFAQT-LAAAridvlkivPGHLHALLQAERAAD 1471
Cdd:cd05973    129 EDSFWNAADPGWAYGlYYAITGPLALGHPTILLEGgfsvESTWRViERLGVTnLAGS--------PTAYRLLMAAGAEVP 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1472 ALPAHTLVL---GGEATSWELLDTIAAlRPDCRVHNHYGPTEttVGILTQPAAQACRAAATLPLGRPLDNNETWLLDEHL 1548
Cdd:cd05973    201 ARPKGRLRRvssAGEPLTPEVIRWFDA-ALGVPIHDHYGQTE--LGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDG 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1549 NPVGTGGTGELYLGGAGVAL----GYLHQPALTAArfvphpfaagARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRV 1624
Cdd:cd05973    278 DELGPGEPGRLAIDIANSPLmwfrGYQLPDTPAID----------GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1625 EPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPDYMV---PSVLRVIDALPLNRN 1697
Cdd:cd05973    348 GPFDVESALIEHPAVAEAAVIGVPdperTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAhayPRTIHFVDELPKTPS 427

                   ....*...
gi 1888712850 1698 GKLDRQAL 1705
Cdd:cd05973    428 GKIQRFLL 435
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
35-590 3.85e-18

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 89.62  E-value: 3.85e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   35 PEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVPV---YPPEsk 110
Cdd:cd17652      1 PDAPAVV----FGDETLTYAELNARANRLARLLAARGVGPERLVaLALPRSAELVVAILAVLKAGAAYLPLdpaYPAE-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  111 reqhlaRLRGIARDAGVRYVLTTAalherhadawsmlapgadvvavdtldardtpsdaplhpvraDDLAFLQYTSGSTGS 190
Cdd:cd17652     75 ------RIAYMLADARPALLLTTP-----------------------------------------DNLAYVIYTSGSTGR 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  191 PKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDmGLIGSLLQPVFSGIPLVLmSPQYFLERPLRWLDAIARHRG 270
Cdd:cd17652    108 PKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFD-ASVWELLMALLAGATLVL-APAEELLPGEPLADLLREHRI 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  271 TISGAPDFAYRLCAERindetraklDLSSWRLAFSGSEPVRRDtlddFVARFAPAgfdaAALYPCYGLAEATLFVTggvr 350
Cdd:cd17652    186 THVTLPPAALAALPPD---------DLPDLRTLVVAGEACPAE----LVDRWAPG----RRMINAYGPTETTVCAT---- 244
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  351 gaglvshafSSAALSAGRaeaaradeaaTVLVGCGAVQAghrvaivaraaaeshESHEADvetetsRAGERLADGRIGEI 430
Cdd:cd17652    245 ---------MAGPLPGGG----------VPPIGRPVPGT---------------RVYVLD------ARLRPVPPGVPGEL 284
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  431 HVSGPSVAHGYWQRADASAQAFVDAPRHADGSgpaRWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEA 509
Cdd:cd17652    285 YIAGAGLARGYLNRPGLTAERFVADPFGAPGS---RMYRTGDLArWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTE 361
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  510 HAEFARkGRVIAFGATLGGGEtlgLALEIAPRMKKRFAAAQIVETLRRIAFDACgeTPAAIALLNpgALPKTSSGKLQRA 589
Cdd:cd17652    362 HPGVAE-AVVVVRDDRPGDKR---LVAYVVPAPGAAPTAAELRAHLAERLPGYM--VPAAFVVLD--ALPLTPNGKLDRR 433

                   .
gi 1888712850  590 A 590
Cdd:cd17652    434 A 434
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
28-593 3.98e-18

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 89.68  E-value: 3.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   28 RALAQQRPEATALividADGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVyp 106
Cdd:cd17653      4 ERIAAAHPDAVAV----ESLGGSLTYGELDAASNALANRLLQLGvVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL-- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  107 pesKREQHLARLRGIARDAGVRYVLTTAAlherhadawsmlapgadvvavdtldardtpsdaplhpvrADDLAFLQYTSG 186
Cdd:cd17653     78 ---DAKLPSARIQAILRTSGATLLLTTDS---------------------------------------PDDLAYIIFTSG 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  187 STGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGlIGSLLQPVFSGIPLVLMSPQYFLERPLRWLDAIA 266
Cdd:cd17653    116 STGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDAC-IGEIFSTLCNGGTLVLADPSDPFAHVARTVDALM 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  267 rhrgtisGAPDFAYRLCAErindetraklDLSSWRLAFSGSEPVRRDTLDDFVARfapagfdaAALYPCYGLAEATLFVT 346
Cdd:cd17653    195 -------STPSILSTLSPQ----------DFPNLKTIFLGGEAVPPSLLDRWSPG--------RRLYNAYGPTECTISST 249
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  347 ggvrgaglvshafsSAALSAGRAeaaradeaaTVL------VGCGAVQAGhrvaivaraaaeshesheadvetetsraGE 420
Cdd:cd17653    250 --------------MTELLPGQP---------VTIgkpipnSTCYILDAD----------------------------LQ 278
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  421 RLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHaDGSgpaRWLRTGDLGF-VHDGQLYIAGRVKDLVIVRGRNLY 499
Cdd:cd17653    279 PVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW-PGS---RMYRTGDYGRwTEDGGLEFLGREDNQVKVRGFRIN 354
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  500 PQDVEQAVEAHAEFARK-------GRVIAFGATlgggETLGLALeIAPRMKKRFAAAQIVETLRRIAfdacgetpaaial 572
Cdd:cd17653    355 LEEIEEVVLQSQPEVTQaaaivvnGRLVAFVTP----ETVDVDG-LRSELAKHLPSYAVPDRIIALD------------- 416
                          570       580
                   ....*....|....*....|.
gi 1888712850  573 lnpgALPKTSSGKLQRAATRE 593
Cdd:cd17653    417 ----SFPLTANGKVDRKALRE 433
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
1363-1700 4.26e-18

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 87.94  E-value: 4.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1363 VIYTSGSSGAPKGVVIAH----GALTNYVDAVLARLDppprARFAMVSTIGADLGHTVLFGALASGGALhlIDRDTTLDA 1438
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHrqtlRAAAAWADCADLTED----DRYLIINPFFHTFGYKAGIVACLLTGAT--VVPVAVFDV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1439 DRFAQTLAAARIDVLKIVPGHLHALLQ--AERAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGIL 1516
Cdd:cd17638     79 DAILEAIERERITVLPGPPTLFQSLLDhpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVATM 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1517 TQPAAQACRAAATLplGRPLDNNEtwlldehlnpVGTGGTGELYLGGAGVALGYLHQPALTAArfvphpfAAGARLY-RS 1595
Cdd:cd17638    159 CRPGDDAETVATTC--GRACPGFE----------VRIADDGEVLVRGYNVMQGYLDDPEATAE-------AIDADGWlHT 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1596 GDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGARLA----AFATPQPGASLDAAALKR 1671
Cdd:cd17638    220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGevgkAFVVARPGVTLTEEDVIA 299
                          330       340
                   ....*....|....*....|....*....
gi 1888712850 1672 ALAALLPDYMVPSVLRVIDALPLNRNGKL 1700
Cdd:cd17638    300 WCRERLANYKVPRFVRFLDELPRNASGKV 328
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
747-1170 6.62e-18

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 88.51  E-value: 6.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  747 SRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYAPRTEAaaPLAWAHVDLsdlgdidehdrera 826
Cdd:cd19545     19 PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKES--PISWTESTS-------------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  827 LRECAQRFADAPFDLLrGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELvdgyRAALDGatTHGEAQAKAKTR 906
Cdd:cd19545     83 LDEYLEEDRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQV----LAAYQG--EPVPQPPPFSRF 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  907 ITYADYaawqrrwlASDAAARQlaYWRAALADDAPPlalpyDHTATDTASENADPRAAARVAFALPAPlaqavrasaARH 986
Cdd:cd19545    156 VKYLRQ--------LDDEAAAE--FWRSYLAGLDPA-----VFPPLPSSRYQPRPDATLEHSISLPSS---------ASS 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  987 RATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETH--DVIGFFVNTLVLHSDCEAATPLASLFSQLRQRTLDaqa 1064
Cdd:cd19545    212 GVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGieQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLD--- 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1065 nqALPFdvlvEHL------RPARDAQHGPLFETSFN--YLSDDYPALARWPGARAERVEIAETHvKVPLALDLRESrDGS 1136
Cdd:cd19545    289 --MIPF----EHTglqnirRLGPDARAACNFQTLLVvqPALPSSTSESLELGIEEESEDLEDFS-SYGLTLECQLS-GSG 360
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1888712850 1137 MRAYFTYASARFDAASVERMAAQYLRAVEAFAHA 1170
Cdd:cd19545    361 LRVRARYDSSVISEEQVERLLDQFEHVLQQLASA 394
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
51-592 6.72e-18

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 89.10  E-value: 6.72e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   51 YDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVYP---PESKREqhlaRLRgiarDAG 126
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGvGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSafgPEAIRD----RLE----NSE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  127 VRYVLTTAALHERhadawsmlapgadvvavdtldardtpsdaplhpVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEI 206
Cdd:cd05969     73 AKVLITTEELYER---------------------------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYF 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  207 AIQAGLGVRPDDVF-----VSWLplyhdMGLIGSLLQPVFSGIPLVLMSPQYfleRPLRWLDAIARHRGTI-SGAPDfAY 280
Cdd:cd05969    120 TGKYVLDLHPDDIYwctadPGWV-----TGTVYGIWAPWLNGVTNVVYEGRF---DAESWYGIIERVKVTVwYTAPT-AI 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  281 RLCAeRINDETRAKLDLSSWRLAFSGSEPVRRDtlddfVARFAPAGFDaAALYPCYGLAEatlfvTGGVRGAGLVshafs 360
Cdd:cd05969    191 RMLM-KEGDELARKYDLSSLRFIHSVGEPLNPE-----AIRWGMEVFG-VPIHDTWWQTE-----TGSIMIANYP----- 253
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  361 saalsagraeaaradeaatvlvgCGAVQAGHRVAIVARAaaesheshEADVeteTSRAGERLADGRIGEIHVSG--PSVA 438
Cdd:cd05969    254 -----------------------CMPIKPGSMGKPLPGV--------KAAV---VDENGNELPPGTKGILALKPgwPSMF 299
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  439 HGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKG 517
Cdd:cd05969    300 RGIWNDEERYKNSFIDG-----------WYLTGDLAYRdEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAG 368
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  518 -----------RVIAFGATLGGGE-TLGLALEIAPRMKKRFAAAQIVetlRRIAFdaCGEtpaaiallnpgaLPKTSSGK 585
Cdd:cd05969    369 vigkpdplrgeIIKAFISLKEGFEpSDELKEEIINFVRQKLGAHVAP---REIEF--VDN------------LPKTRSGK 431

                   ....*..
gi 1888712850  586 LQRAATR 592
Cdd:cd05969    432 IMRRVLK 438
PLN02574 PLN02574
4-coumarate--CoA ligase-like
1220-1662 7.38e-18

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 89.90  E-value: 7.38e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1220 ARHAdtQPDAPAVIDGA--LRMSYAELDARAAHVAQWLLAR-DLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAG 1296
Cdd:PLN02574    48 SHHN--HNGDTALIDSStgFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPS 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1297 NPTQRLAQTLRDCGARLVLCE-DDCSALDLMGVQHARIDAAQEEAQREQHLRAPHAL----------PAVDPRSAAYVIY 1365
Cdd:PLN02574   126 SSLGEIKKRVVDCSVGLAFTSpENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFYELikedfdfvpkPVIKQDDVAAIMY 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1366 TSGSSGAPKGVVIAHGALTNYVDaVLARLDPpprARFAMVSTIGADLGHTVLF----------GALASGGALHLIDRdtt 1435
Cdd:PLN02574   206 SSGTTGASKGVVLTHRNLIAMVE-LFVRFEA---SQYEYPGSDNVYLAALPMFhiyglslfvvGLLSLGSTIVVMRR--- 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1436 LDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAHTLVL---GGEATSWELLDTIAALRPDCRVHNHYGPTETT 1512
Cdd:PLN02574   279 FDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQvscGAAPLSGKFIQDFVQTLPHVDFIQGYGMTEST 358
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1513 V----GILTQPAAQACRAAATLP--LGRPLDnnetWLLDEHLNPvgtGGTGELYLGGAGVALGYLHQPALTAARFVPHPF 1586
Cdd:PLN02574   359 AvgtrGFNTEKLSKYSSVGLLAPnmQAKVVD----WSTGCLLPP---GNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW 431
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1587 aagarlYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQPGA 1662
Cdd:PLN02574   432 ------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVpdkeCGEIPVAFVVRRQGS 505
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
1234-1633 1.29e-17

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 88.57  E-value: 1.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1234 DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARL 1313
Cdd:cd17640      1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1314 VLCEDDcsaldlmgvqharidaaqeeaqreqhlraphalpavdPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLAR 1393
Cdd:cd17640     81 LVVEND-------------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDI 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1394 LDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLidrdTTLDAdrFAQTLAAARIDVLKIVPGHLHAL-------LQA 1466
Cdd:cd17640    124 VPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY----TSIRT--LKDDLKRVKPHYIVSVPRLWESLysgiqkqVSK 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1467 ERAADALPAHTLVLGGEATSweLLDTIAALRP---------DCRVHNHYGPTET----TVGILTQPAAQAcraaatlpLG 1533
Cdd:cd17640    198 SSPIKQFLFLFFLSGGIFKF--GISGGGALPPhvdtffeaiGIEVLNGYGLTETspvvSARRLKCNVRGS--------VG 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1534 RPLDNNETWLLDEHLN-PVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlYRSGDRARRLADGSLEYLGR 1612
Cdd:cd17640    268 RPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGR 341
                          410       420
                   ....*....|....*....|..
gi 1888712850 1613 IDDQVKIR-GYRVEPGEIAARL 1633
Cdd:cd17640    342 AKDTIVLSnGENVEPQPIEEAL 363
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
174-508 1.43e-17

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 88.18  E-value: 1.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  174 RADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYH------DMGLIGSLLQPVFSGIP-- 245
Cdd:cd17640     86 DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHsyersaEYFIFACGCSQAYTSIRtl 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  246 ---LVLMSPQYFLERPLRWLDAIARHRGTISGAPDFAYRLcaerindeTRAKLDLSSWRLAFSGSepvrrDTLDDFVARF 322
Cdd:cd17640    166 kddLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFL--------FLFFLSGGIFKFGISGG-----GALPPHVDTF 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  323 apagFDAAA--LYPCYGLAEatlfvTGGVRGAGLVSHafssaalsagraeaaradeaatVLVGcgavQAGHRVaivaraa 400
Cdd:cd17640    233 ----FEAIGieVLNGYGLTE-----TSPVVSARRLKC----------------------NVRG----SVGRPL------- 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  401 aeshesHEADVETETSRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFvdaprHADGsgparWLRTGDLG-FVHDG 479
Cdd:cd17640    271 ------PGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVL-----DSDG-----WFNTGDLGwLTCGG 334
                          330       340       350
                   ....*....|....*....|....*....|
gi 1888712850  480 QLYIAGRVKD-LVIVRGRNLYPQDVEQAVE 508
Cdd:cd17640    335 ELVLTGRAKDtIVLSNGENVEPQPIEEALM 364
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
27-510 1.81e-17

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 88.33  E-value: 1.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   27 LRALAQQRPEATALIviDADGDTRYDYAQLDRRARALAARFARDGAA-AERALILMDSGVDYVSAFFGCLYAGVVAVPVY 105
Cdd:cd05923      7 LRRAASRAPDACAIA--DPARGLRLTYSELRARIEAVAARLHARGLRpGQRVAVVLPNSVEAVIALLALHRLGAVPALIN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  106 PpeSKREQHLARLrgIARDAGVRYVLTTAALHERhADAWSmlapGADVVAVDTL-DARDTPSDAPL---HPVRADDLAFL 181
Cdd:cd05923     85 P--RLKAAELAEL--IERGEMTAAVIAVDAQVMD-AIFQS----GVRVLALSDLvGLGEPESAGPLiedPPREPEQPAFV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  182 QYTSGSTGSPKGVMVSHGNL--LANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLmsPQYFleRPL 259
Cdd:cd05923    156 FYTSGTTGLPKGAVIPQRAAesRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVV--VEEF--DPA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  260 RWLDAIARHRGT-ISGAPDFAYRLCAErindETRAKLDLSSWR-LAFSGSepVRRDTLDDFVARFAPAGFdaaalYPCYG 337
Cdd:cd05923    232 DALKLIEQERVTsLFATPTHLDALAAA----AEFAGLKLSSLRhVTFAGA--TMPDAVLERVNQHLPGEK-----VNIYG 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  338 LAEA--TLFVTGGVRGAGLVSHAFSSAALsagraeaaradeaatVLVGCGAVQAghrvaivaraaaeshesheadvetet 415
Cdd:cd05923    301 TTEAmnSLYMRDARTGTEMRPGFFSEVRI---------------VRIGGSPDEA-------------------------- 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  416 sragerLADGRIGEIHV--SGPSVAHGYWQRADASAQAFVDaprhadgsgpaRWLRTGDLGFVH-DGQLYIAGRVKDLVI 492
Cdd:cd05923    340 ------LANGEEGELIVaaAADAAFTGYLNQPEATAKKLQD-----------GWYRTGDVGYVDpSGDVRILGRVDDMII 402
                          490
                   ....*....|....*...
gi 1888712850  493 VRGRNLYPQDVEQAVEAH 510
Cdd:cd05923    403 SGGENIHPSEIERVLSRH 420
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
177-593 2.03e-17

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 85.85  E-value: 2.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  177 DLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLiGSLLQPVFSGIPLVLMSPqyfle 256
Cdd:cd17630      1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLER----- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  257 rplRWLDAIARHRGT---ISGAPDFAYRLCAERINDETRAKLdlsswRLAFSGSEPVRRDTLDDFVARFAPagfdaaaLY 333
Cdd:cd17630     75 ---NQALAEDLAPPGvthVSLVPTQLQRLLDSGQGPAALKSL-----RAVLLGGAPIPPELLERAADRGIP-------LY 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  334 PCYGLAEATLFVTGGVRGaglvshafssaalsagraeaaradeaatvlvgcgavqaghrvaivaraaaeshesheadvET 413
Cdd:cd17630    140 TTYGMTETASQVATKRPD------------------------------------------------------------GF 159
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  414 ETSRAGERLADGRI-----GEIHVSGPSVAHGYWQRadasaqafvDAPRHADGSGparWLRTGDLGFVH-DGQLYIAGRV 487
Cdd:cd17630    160 GRGGVGVLLPGRELrivedGEIWVGGASLAMGYLRG---------QLVPEFNEDG---WFTTKDLGELHaDGRLTVLGRA 227
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  488 KDLVIVRGRNLYPQDVEQAVEAHAEFArkgRVIAFGAtlgGGETLGLALEIAPRMKKRFAAAQIVETLRriafDACG--E 565
Cdd:cd17630    228 DNMIISGGENIQPEEIEAALAAHPAVR---DAFVVGV---PDEELGQRPVAVIVGRGPADPAELRAWLK----DKLArfK 297
                          410       420
                   ....*....|....*....|....*...
gi 1888712850  566 TPAAIALLNpgALPKTSSGKLQRAATRE 593
Cdd:cd17630    298 LPKRIYPVP--ELPRTGGGKVDRRALRA 323
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
139-504 2.74e-17

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 88.25  E-value: 2.74e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  139 RHADAWsmLAPGADVVAV-DTLDARDtPS--DAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVR 215
Cdd:cd17641    121 KYDDPR--LISFEDVVALgRALDRRD-PGlyEREVAAGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLG 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  216 PDDVFVSWLPLYHDMGLIGSLLQPVFSGI-------PLVLMS------PQYFLERPLRWLDAIARHRGtisgapdfayrl 282
Cdd:cd17641    198 PGDEYVSVLPLPWIGEQMYSVGQALVCGFivnfpeePETMMEdlreigPTFVLLPPRVWEGIAADVRA------------ 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  283 caeRINDETRAKLDLSSW--RLAFSGSEPVRRDTLDDFVARFAPAGFDA---AALYPCYGLAEATLFVTGgvrGAGLVSH 357
Cdd:cd17641    266 ---RMMDATPFKRFMFELgmKLGLRALDRGKRGRPVSLWLRLASWLADAllfRPLRDRLGFSRLRSAATG---GAALGPD 339
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  358 AFsSAALSAGRAEAARADEAATvlvgCGAVQAghrvaivaraaaesHESHEADVET-ETSRAGERLADGRIGEIHVSGPS 436
Cdd:cd17641    340 TF-RFFHAIGVPLKQLYGQTEL----AGAYTV--------------HRDGDVDPDTvGVPFPGTEVRIDEVGEILVRSPG 400
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  437 VAHGYWQRADASAQAFVDaprhaDGsgparWLRTGDLGFV-HDGQLYIAGRVKDL-VIVRGRNLYPQDVE 504
Cdd:cd17641    401 VFVGYYKNPEATAEDFDE-----DG-----WLHTGDAGYFkENGHLVVIDRAKDVgTTSDGTRFSPQFIE 460
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
1219-1702 3.39e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 87.75  E-value: 3.39e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHadtqPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGgAYVALDagNP 1298
Cdd:PRK05605    42 VARF----GDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLG-AVVVEH--NP 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1299 ---TQRLAQTLRDCGARLVLCEDDCSALdlmgVQHARIDAAQE--------------------------EAQREQ-HLRA 1348
Cdd:PRK05605   115 lytAHELEHPFEDHGARVAIVWDKVAPT----VERLRRTTPLEtivsvnmiaampllqrlalrlpipalRKARAAlTGPA 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1349 PHAL-------------------PAVDPRSAAYVIYTSGSSGAPKGVVIAHGALtnYVDAVLARldppprarfAMVSTIG 1409
Cdd:PRK05605   191 PGTVpwetlvdaaiggdgsdvshPRPTPDDVALILYTSGTTGKPKGAQLTHRNL--FANAAQGK---------AWVPGLG 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1410 aDLGHTVL--------FG-------ALASGGALHLI---DRDTTLDA----------------DRFAQTLAAARIDvlki 1455
Cdd:PRK05605   260 -DGPERVLaalpmfhaYGltlcltlAVSIGGELVLLpapDIDLILDAmkkhpptwlpgvpplyEKIAEAAEERGVD---- 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1456 vpghLHALLQAERAADALPAHTLVLGGEATSWELLDTiaalrpdcrvhnhYGPTETTVGILTQPAAQACRAAAtlpLGRP 1535
Cdd:PRK05605   335 ----LSGVRNAFSGAMALPVSTVELWEKLTGGLLVEG-------------YGLTETSPIIVGNPMSDDRRPGY---VGVP 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1536 LDNNETWLLDEHlNPVGT---GGTGELYLGGAGVALGYLHQPALTAARFVPHpfaagarLYRSGDRARRLADGSLEYLGR 1612
Cdd:PRK05605   395 FPDTEVRIVDPE-DPDETmpdGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDR 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1613 IDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGA----RLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRV 1688
Cdd:PRK05605   467 IKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREdgseEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYH 546
                          570
                   ....*....|....
gi 1888712850 1689 IDALPLNRNGKLDR 1702
Cdd:PRK05605   547 VDELPRDQLGKVRR 560
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
27-593 3.79e-17

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 87.42  E-value: 3.79e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   27 LRALAQQRPEATALIVIDADGD--TRYDYAQLDrraralaarfardgAAAER-ALILMDSGV---DYVSA---------- 90
Cdd:PRK13295    30 LDACVASCPDKTAVTAVRLGTGapRRFTYRELA--------------ALVDRvAVGLARLGVgrgDVVSCqlpnwweftv 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   91 -FFGCLYAGVVAVPVYPpeSKREQHLARLRGIArDAGVRYVLTT------AALHERHADAWSML-----APGADVVAVDT 158
Cdd:PRK13295    96 lYLACSRIGAVLNPLMP--IFRERELSFMLKHA-ESKVLVVPKTfrgfdhAAMARRLRPELPALrhvvvVGGDGADSFEA 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  159 L---DARDTPSDAP-----LHPvRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDM 230
Cdd:PRK13295   173 LlitPAWEQEPDAPailarLRP-GPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQT 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  231 GLIGSLLQPVFSGIPLVLMSpqyfLERPLRWLDAIARHRGTIS-GAPDFAYRLCaeRINDETRakLDLSSWRLAFSGSEP 309
Cdd:PRK13295   252 GFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVTFTmASTPFLTDLT--RAVKESG--RPVSSLRTFLCAGAP 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  310 VRRDtlddfVARFAPAGFdAAALYPCYGLAEATLfVTGGVRGAGLvshafSSAALSAGRaeaaradeaatVLVGcgavqa 389
Cdd:PRK13295   324 IPGA-----LVERARAAL-GAKIVSAWGMTENGA-VTLTKLDDPD-----ERASTTDGC-----------PLPG------ 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  390 ghrvaivaraaaeshesheadVETETSRA-GERLADGRIGEIHVSGPSVAHGYWQRADASAQAfvdaprhADGsgparWL 468
Cdd:PRK13295   375 ---------------------VEVRVVDAdGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTD-------ADG-----WF 421
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  469 RTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFA----------RKG-RVIAFgATLGGGETLGLAL 536
Cdd:PRK13295   422 DTGDLARIDaDGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAqvaivaypdeRLGeRACAF-VVPRPGQSLDFEE 500
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1888712850  537 EIAPRMKKRFAAAQIVETLrrIAFDacgetpaaiallnpgALPKTSSGKLQRAATRE 593
Cdd:PRK13295   501 MVEFLKAQKVAKQYIPERL--VVRD---------------ALPRTPSGKIQKFRLRE 540
PRK07638 PRK07638
acyl-CoA synthetase; Validated
1221-1705 3.87e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 87.14  E-value: 3.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1221 RHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLArdlQGGEP--VAIVAHRSARFVVAMLGVLKAGGAYVALDAGNP 1298
Cdd:PRK07638     9 KHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNE---KESKNktIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1299 TQRLAQTLRDCGARLVLCEDDCSAlDLMGVQHARIDAAQEEAQREQHLRAPHalPAVDPRSAA-YVIYTSGSSGAPKGVV 1377
Cdd:PRK07638    86 QDELKERLAISNADMIVTERYKLN-DLPDEEGRVIEIDEWKRMIEKYLPTYA--PIENVQNAPfYMGFTSGSTGKPKAFL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1378 IAHGALTNYVDavlarldpPPRARFAMVST----IGADLGHTV-LFGALAS---GGALHLIDRDTTLDAdrfAQTLAAAR 1449
Cdd:PRK07638   163 RAQQSWLHSFD--------CNVHDFHMKREdsvlIAGTLVHSLfLYGAISTlyvGQTVHLMRKFIPNQV---LDKLETEN 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1450 IDVLKIVPGHLHALLQAERaadaLPAHTLVLGGEATSWELL--DTIAALRPDCRVHNHYGPTETT-VGILTQPAAQACRA 1526
Cdd:PRK07638   232 ISVMYTVPTMLESLYKENR----VIENKMKIISSGAKWEAEakEKIKNIFPYAKLYEFYGASELSfVTALVDEESERRPN 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1527 AatlpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHqpaltAARFVPHPFAAGARLYRsgDRARRLADGS 1606
Cdd:PRK07638   308 S----VGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII-----GGVLARELNADGWMTVR--DVGYEDEEGF 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1607 LEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVL 1686
Cdd:PRK07638   377 IYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEW 456
                          490
                   ....*....|....*....
gi 1888712850 1687 RVIDALPLNRNGKLDRQAL 1705
Cdd:PRK07638   457 HFVDEIPYTNSGKIARMEA 475
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
75-592 3.95e-17

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 86.76  E-value: 3.95e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGVVAVPVYPpeskreqhlaRLRGIARDAGVRYVLTTAALherhadawsmlapgadvv 154
Cdd:cd05958     37 NRVLLRGSNSPELVACWFGIQKAGAIAVATMP----------LLRPKELAYILDKARITVAL------------------ 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  155 avdtLDARDTPSDaplhpvradDLAFLQYTSGSTGSPKGVMVSHGNLLA--NEIAIQAgLGVRPDDVFVSWLPLYHDMGL 232
Cdd:cd05958     89 ----CAHALTASD---------DICILAFTSGTTGAPKATMHFHRDPLAsaDRYAVNV-LRLREDDRFVGSPPLAFTFGL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  233 IGSLLQPVFSGIPLVLmspqyfLER--PLRWLDAIARHRGTISGAPDFAYRLCAERINDETRaklDLSSWRLAFSGSEPV 310
Cdd:cd05958    155 GGVLLFPFGVGASGVL------LEEatPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGP---DLSSLRKCVSAGEAL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  311 RRDTlddFVARFAPAGFDaaalypcyglaeatlfVTGGVrGAGLVSHAFSSAAlsagraeaaradeaatvlvgcgavqAG 390
Cdd:cd05958    226 PAAL---HRAWKEATGIP----------------IIDGI-GSTEMFHIFISAR-------------------------PG 260
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  391 HRVAIVARAAAESHESHEADVEtetsraGERLADGRIGEIHVSGPSvahGYWQRADASAQAFVDaprhaDGsgparWLRT 470
Cdd:cd05958    261 DARPGATGKPVPGYEAKVVDDE------GNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQ-----GG-----WNIT 321
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  471 GDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQDVEQ-----------AVEAHAEFARKGRVIAFgATLGGGETLGLALei 538
Cdd:cd05958    322 GDTYSRDpDGYFRHQGRSDDMIVSGGYNIAPPEVEDvllqhpavaecAVVGHPDESRGVVVKAF-VVLRPGVIPGPVL-- 398
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1888712850  539 aprmkkrfaAAQIVETLRRIAfdACGETPAAIALLNpgALPKTSSGKLQRAATR 592
Cdd:cd05958    399 ---------ARELQDHAKAHI--APYKYPRAIEFVT--ELPRTATGKLQRFALR 439
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
1230-1705 5.31e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 86.88  E-value: 5.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1230 PAVI---DGAlRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:PRK08276     1 PAVImapSGE-VVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLCEDDCS-----ALDLM--GVQHARIDAAQEEAQR--EQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVV 1377
Cdd:PRK08276    80 DDSGAKVLIVSAALAdtaaeLAAELpaGVPLLLVVAGPVPGFRsyEEALAAQPDTPIADETAGADMLYSSGTTGRPKGIK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1378 IA------HGALTNYVDAVLARLDPPPRARFAMvstiGADLGHT--VLFG--ALASGGALHLIDRdttLDADRFAQTLAA 1447
Cdd:PRK08276   160 RPlpgldpDEAPGMMLALLGFGMYGGPDSVYLS----PAPLYHTapLRFGmsALALGGTVVVMEK---FDAEEALALIER 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1448 ARIDVLKIVPGHLHALL---QAERAADALPAHTLVLGGEA-----TSWELLDTIAALrpdcrVHNHYGPTE-------TT 1512
Cdd:PRK08276   233 YRVTHSQLVPTMFVRMLklpEEVRARYDVSSLRVAIHAAApcpveVKRAMIDWWGPI-----IHEYYASSEgggvtviTS 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1513 VGILTQPAAqacraaatlpLGRPLDnNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAgarl 1592
Cdd:PRK08276   308 EDWLAHPGS----------VGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVT---- 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1593 yrSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAA 1668
Cdd:PRK08276   373 --VGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPdeemGERVKAVVQPADGADAGDAL 450
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1888712850 1669 LKRALAALLPD---YMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:PRK08276   451 AAELIAWLRGRlahYKCPRSIDFEDELPRTPTGKLYKRRL 490
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
19-231 5.51e-17

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 87.24  E-value: 5.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   19 PAHGLAARLRALAQQRPEATALIVIDADGD-TRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLY 96
Cdd:PRK08180    37 YPRRLTDRLVHWAQEAPDRVFLAERGADGGwRRLTYAEALERVRAIAQALLDRGLSAERPLmILSGNSIEHALLALAAMY 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   97 AGVVAVPVYPPESKREQHLARLRGIAR-----------------------DAGVRYVLTTAALHERHADAWSMLAPGADV 153
Cdd:PRK08180   117 AGVPYAPVSPAYSLVSQDFGKLRHVLElltpglvfaddgaafaralaavvPADVEVVAVRGAVPGRAATPFAALLATPPT 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  154 VAVDTLDARdtpsdaplhpVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDD--VFVSWLPLYHDMG 231
Cdd:PRK08180   197 AAVDAAHAA----------VGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFG 266
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
35-590 1.30e-16

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 85.22  E-value: 1.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   35 PEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAER-ALILMDSGVDYVSAFFGCLYAGVVAVPV---YPPEsk 110
Cdd:cd17656      2 PDAVAVV----FENQKLTYRELNERSNQLARFLREKGVKKDSiVAIMMERSAEMIVGILGILKAGGAFVPIdpeYPEE-- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  111 reqhlaRLRGIARDAGVRYVLTTAALHERHADAWSMLAPGADVVAVDtlDARDTPSDaplhpVRADDLAFLQYTSGSTGS 190
Cdd:cd17656     76 ------RRIYIMLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQE--DTSNIDYI-----NNSDDLLYIIYTSGTTGK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  191 PKGVMVSH---GNLLANEiaIQAGLGVRPDDVF----VSWLPLYHDmgLIGSLLqpvfSGIPLVLMSPQyfLERPLRWL- 262
Cdd:cd17656    143 PKGVQLEHknmVNLLHFE--REKTNINFSDKVLqfatCSFDVCYQE--IFSTLL----SGGTLYIIREE--TKRDVEQLf 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  263 DAIARHRGTISGAPDFAYRLCAErindETRAKLDLSSW--RLAFSGSEPVRRDTLDDFVARfapagfDAAALYPCYGLAE 340
Cdd:cd17656    213 DLVKRHNIEVVFLPVAFLKFIFS----EREFINRFPTCvkHIITAGEQLVITNEFKEMLHE------HNVHLHNHYGPSE 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  341 ATLFVTGGVrgaglvshafssaalsagraeaaradeaatvlvgcgavqaghrvaivaraaaeSHESHEAD--------VE 412
Cdd:cd17656    283 THVVTTYTI-----------------------------------------------------NPEAEIPElppigkpiSN 309
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  413 TET---SRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHADgsgpARWLRTGDLG-FVHDGQLYIAGRVK 488
Cdd:cd17656    310 TWIyilDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPN----ERMYRTGDLArYLPDGNIEFLGRAD 385
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  489 DLVIVRGRNLYPQDVEQAVEAHaEFARKGRVIAFGATLGGGETLGLAL---EIAPRMKKRFAAAQIVETLrriafdacge 565
Cdd:cd17656    386 HQVKIRGYRIELGEIEAQLLNH-PGVSEAVVLDKADDKGEKYLCAYFVmeqELNISQLREYLAKQLPEYM---------- 454
                          570       580
                   ....*....|....*....|....*
gi 1888712850  566 TPAAIALLNpgALPKTSSGKLQRAA 590
Cdd:cd17656    455 IPSFFVPLD--QLPLTPNGKVDRKA 477
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1223-1708 2.45e-16

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 84.63  E-value: 2.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1223 ADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRL 1302
Cdd:PRK03640    12 AFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREEL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1303 AQTLRDCGARLVLCEDDCSAlDLMGVQHARIDAAQEEAQREQHLraphaLPAVDPRSAAYVIYTSGSSGAPKGVVIAHGa 1382
Cdd:PRK03640    92 LWQLDDAEVKCLITDDDFEA-KLIPGISVKFAELMNGPKEEAEI-----QEEFDLDEVATIMYTSGTTGKPKGVIQTYG- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1383 lTNYVDAVLARLDPPPRAR----FAM----VStigadlGHTVLFGALASGGALHLIDRdttLDADRFAQTLAAARIDVLK 1454
Cdd:PRK03640   165 -NHWWSAVGSALNLGLTEDdcwlAAVpifhIS------GLSILMRSVIYGMRVVLVEK---FDAEKINKLLQTGGVTIIS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1455 IVPGHLHALLqAERAADALPAH--TLVLGGEATSWELLDTiaalrpdCRVHN-----HYGPTETTVGILTQPAAQACRAA 1527
Cdd:PRK03640   235 VVSTMLQRLL-ERLGEGTYPSSfrCMLLGGGPAPKPLLEQ-------CKEKGipvyqSYGMTETASQIVTLSPEDALTKL 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1528 ATlpLGRPLDNNETWLLDeHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlyRSGDRARRLADGSL 1607
Cdd:PRK03640   307 GS--AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFL 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1608 EYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATpqPGASLDAAALKRALAALLPDYMVP 1683
Cdd:PRK03640   377 YVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddkwGQVPVAFVV--KSGEVTEEELRHFCEEKLAKYKVP 454
                          490       500
                   ....*....|....*....|....*
gi 1888712850 1684 SVLRVIDALPLNRNGKLDRQALSAL 1708
Cdd:PRK03640   455 KRFYFVEELPRNASGKLLRHELKQL 479
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
148-592 3.08e-16

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 83.72  E-value: 3.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  148 APGADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLY 227
Cdd:cd05973     60 GPKAIEHRLRTSGARLVVTDAANRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPG 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  228 HDMGLIGSLLQPVFSGIPLVLMSPQYFLErpLRWlDAIARHRGT-ISGAPDfAYR-LCAERINDETRAKLDLsswRLAFS 305
Cdd:cd05973    140 WAYGLYYAITGPLALGHPTILLEGGFSVE--STW-RVIERLGVTnLAGSPT-AYRlLMAAGAEVPARPKGRL---RRVSS 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  306 GSEPVRRDTLDDFVARFapagfdAAALYPCYGLAEATLFVTggvrgaglvSHAFSSAALSAGRAeaaradeaatvlvgcG 385
Cdd:cd05973    213 AGEPLTPEVIRWFDAAL------GVPIHDHYGQTELGMVLA---------NHHALEHPVHAGSA---------------G 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  386 AVQAGHRVaivaraaaeshesheadveTETSRAGERLADGRIG----EIHVSGPSVAHGYWQRADASaqafvdaprhADG 461
Cdd:cd05973    263 RAMPGWRV-------------------AVLDDDGDELGPGEPGrlaiDIANSPLMWFRGYQLPDTPA----------IDG 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  462 sgpaRWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH---AEFARKGR--------VIAFGATLGGG 529
Cdd:cd05973    314 ----GYYLTGDTVeFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHpavAEAAVIGVpdpertevVKAFVVLRGGH 389
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1888712850  530 E-TLGLALEIAPRMKKRFAAAQIVETLRRIAfdacgetpaaiallnpgALPKTSSGKLQRAATR 592
Cdd:cd05973    390 EgTPALADELQLHVKKRLSAHAYPRTIHFVD-----------------ELPKTPSGKIQRFLLR 436
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
1209-1723 3.09e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 84.63  E-value: 3.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1209 TPPGEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLAR-DLQGGEPVAIVAHRSARFVVAMLGVLKAG 1287
Cdd:PRK08314     6 TLPETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRAN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1288 GAYVALDAGNPTQRLAQTLRDCGARLVLC-------------------------------EDDCSALDLMGVQHARIDAA 1336
Cdd:PRK08314    86 AVVVPVNPMNREEELAHYVTDSGARVAIVgselapkvapavgnlrlrhvivaqysdylpaEPEIAVPAWLRAEPPLQALA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1337 QEEAQR-EQHLRAPHALPA--VDPRSAAYVIYTSGSSGAPKGVVIAHG-ALTNYVDAVLARLDPPprarfAMVSTIGADL 1412
Cdd:PRK08314   166 PGGVVAwKEALAAGLAPPPhtAGPDDLAVLPYTSGTTGVPKGCMHTHRtVMANAVGSVLWSNSTP-----ESVVLAVLPL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1413 GHT-----VLFGALASGGALHLI---DRDTTLDAdrfaqtLAAARIDVLKIVPGHLHALLQAERAADA-LPAHTLVLGG- 1482
Cdd:PRK08314   241 FHVtgmvhSMNAPIYAGATVVLMprwDREAAARL------IERYRVTHWTNIPTMVVDFLASPGLAERdLSSLRYIGGGg 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1483 ----EATSWELLDtiaalRPDCRVHNHYGPTETTVGILTQPAAQACRAAatlpLGRPLDNNETWLLD-EHLNPVGTGGTG 1557
Cdd:PRK08314   315 aampEAVAERLKE-----LTGLDYVEGYGLTETMAQTHSNPPDRPKLQC----LGIPTFGVDARVIDpETLEELPPGEVG 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1558 ELYLGGAGVALGYLHQPALTAARFVPhpfAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALD 1637
Cdd:PRK08314   386 EIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHP 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1638 GVRDAAVIVV----AGARLAAFATPQPGASLDAAALKRAL--AALLPDYMVPSVLRVIDALPLNRNGKLDRQALSalarp 1711
Cdd:PRK08314   463 AIQEACVIATpdprRGETVKAVVVLRPEARGKTTEEEIIAwaREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQ----- 537
                          570
                   ....*....|..
gi 1888712850 1712 aapHREAARAAP 1723
Cdd:PRK08314   538 ---EQEKARAAK 546
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
1227-1702 3.22e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 84.44  E-value: 3.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVI--DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQ 1304
Cdd:PRK12583    32 PDREALVvrHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEY 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1305 TLRDCGARLVLCEDDCSALD----LMGVQHARIDAAQEEAQREQ--HLR---------APHAL--------------PAV 1355
Cdd:PRK12583   112 ALGQSGVRWVICADAFKTSDyhamLQELLPGLAEGQPGALACERlpELRgvvslapapPPGFLawhelqargetvsrEAL 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1356 DPRSAAY-------VIYTSGSSGAPKGVVIAHGALTNYVDAVLARLD---------PPPRAR-FAMVStigADLGhtvlf 1418
Cdd:PRK12583   192 AERQASLdrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGltehdrlcvPVPLYHcFGMVL---ANLG----- 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1419 gALASGGALhlIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQ-AERAA-DALPAHTLVLGGEATSWELLDTIAAL 1496
Cdd:PRK12583   264 -CMTVGACL--VYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDhPQRGNfDLSSLRTGIMAGAPCPIEVMRRVMDE 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1497 RPDCRVHNHYGPTETT-VGILTQPAAQACRAAATLplGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPA 1575
Cdd:PRK12583   341 MHMAEVQIAYGMTETSpVSLQTTAADDLERRVETV--GRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPE 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1576 LTAarfvpHPFAAGARLYrSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GAR 1651
Cdd:PRK12583   419 ATA-----ESIDEDGWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPdekyGEE 492
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1888712850 1652 LAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDR 1702
Cdd:PRK12583   493 IVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
1216-1661 3.88e-16

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 84.56  E-value: 3.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1216 HLRVARHADT-QPDAPAVI----DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAY 1290
Cdd:PRK04319    46 YEAIDRHADGgRKDKVALRyldaSRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIV 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1291 VALDAGNPTQRLAQTLRDCGARLVLCEDDC----SALDLMGVQHA-RIDAAQEEAQREQHLR-----APHAL--PAVDPR 1358
Cdd:PRK04319   126 GPLFEAFMEEAVRDRLEDSEAKVLITTPALlerkPADDLPSLKHVlLVGEDVEEGPGTLDFNalmeqASDEFdiEWTDRE 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1359 SAAYVIYTSGSSGAPKGVVIAHGA-LTNYVDAVLArLDPPPRARFAmvSTigADLGHTV-----LFGALASGgALHLIDR 1432
Cdd:PRK04319   206 DGAILHYTSGSTGKPKGVLHVHNAmLQHYQTGKYV-LDLHEDDVYW--CT--ADPGWVTgtsygIFAPWLNG-ATNVIDG 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1433 DTtLDADRFAQTLAAARIDVLKIVPGHLHALLqaeRAADALPA--------HTLVLG----GEATSW--ELLDTiaalrp 1498
Cdd:PRK04319   280 GR-FSPERWYRILEDYKVTVWYTAPTAIRMLM---GAGDDLVKkydlsslrHILSVGeplnPEVVRWgmKVFGL------ 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1499 dcRVHNHYGPTETTvGILTqpaaqacraaATLP--------LGRPLDNNETWLLDEHLNPVGTGGTGELYL--GGAGVAL 1568
Cdd:PRK04319   350 --PIHDNWWMTETG-GIMI----------ANYPamdikpgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMR 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1569 GYLHQPAltaaRFvPHPFAAGarLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVI--- 1645
Cdd:PRK04319   417 GIWNNPE----KY-ESYFAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIgkp 489
                          490
                   ....*....|....*..
gi 1888712850 1646 -VVAGARLAAFATPQPG 1661
Cdd:PRK04319   490 dPVRGEIIKAFVALRPG 506
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
1216-1896 7.65e-16

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 83.98  E-value: 7.65e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1216 HLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDA 1295
Cdd:COG3319      4 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1296 GNPTQRLAQTLRDCGARLVLCEDDCSALDLMGVQHARIDAAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKG 1375
Cdd:COG3319     84 LALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGV 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1376 VVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLDADRFAQTLAAARIDVLKI 1455
Cdd:COG3319    164 LVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLL 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1456 VPGHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRAAATLPLGRP 1535
Cdd:COG3319    244 LAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPG 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1536 LDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDD 1615
Cdd:COG3319    324 LLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRL 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1616 QVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLN 1695
Cdd:COG3319    404 QRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLL 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1696 RNGKLDRQALSALARPAAPHREAARAAPQGETETALAQCWAALLDPSngtdnatdnatatpsltIARDDSFFALGGHSLA 1775
Cdd:COG3319    484 LLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGL-----------------VGDDDDFFGGGGGSLL 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1776 AMRLASRVRSRWSVELPLREIFASPTLAALAARIEAQRADSDRASNQVSNKAAnaeSATPLHALADRSALPLSLMQqriw 1855
Cdd:COG3319    547 ALLLLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGG---SGPPLFCVHPAGGNVLCYRP---- 619
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1888712850 1856 vvdqLADRALASYNMTaGLDLRGPLDAARLQRSLAALIARH 1896
Cdd:COG3319    620 ----LARALGPDRPVY-GLQAPGLDGGEPPPASVEEMAARY 655
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
1219-1705 1.38e-15

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 82.54  E-value: 1.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVI----DGALR-MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGG----- 1288
Cdd:cd05970     23 VDAMAKEYPDKLALVwcddAGEERiFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAiaipa 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1289 -------------------AYVALDAGNPTQRLAQTLRDCGA--RLVLCEDDcsaldlmgVQHARIDAAQEEAQREQHLR 1347
Cdd:cd05970    103 thqltakdivyriesadikMIVAIAEDNIPEEIEKAAPECPSkpKLVWVGDP--------VPEGWIDFRKLIKNASPDFE 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1348 APHALPAVDPRSAAYVIYTSGSSGAPKgvVIAHGALTNYVDAVLARL--DPPPRARFAMVSTIGadLGHTV---LFGALA 1422
Cdd:cd05970    175 RPTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYwqNVREGGLHLTVADTG--WGKAVwgkIYGQWI 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1423 SGGALHLIDRDTtLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAA-DALPAHTLVLGGEATSWELLDTIAALrPDCR 1501
Cdd:cd05970    251 AGAAVFVYDYDK-FDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRyDLSSLRYCTTAGEALNPEVFNTFKEK-TGIK 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1502 VHNHYGPTETTVGILTQPAAQACRAAatlpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGA-----GVALGYLHQPAL 1576
Cdd:cd05970    329 LMEGFGQTETTLTIATFPWMEPKPGS----MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEK 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1577 TAARFVPHpfaagarLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARL 1652
Cdd:cd05970    405 TAEVWHDG-------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPdpirGQVV 477
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1888712850 1653 AAF----ATPQPGASLDAAALKRALAALLPdYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:cd05970    478 KATivlaKGYEPSEELKKELQDHVKKVTAP-YKYPRIVEFVDELPKTISGKIRRVEI 533
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
1238-1706 1.46e-15

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 82.42  E-value: 1.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1238 RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCE 1317
Cdd:PRK08008    37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1318 DD-------------------CSALDLMGVQHARIDAAQEEAQREQHLRAPHALPAVDPrsaAYVIYTSGSSGAPKGVVI 1378
Cdd:PRK08008   117 AQfypmyrqiqqedatplrhiCLTRVALPADDGVSSFTQLKAQQPATLCYAPPLSTDDT---AEILFTSGTTSRPKGVVI 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1379 AHGAL--TNYVDAVLARLdpppRARFAMVSTIGA---DLGHTVLFGALASGGALHLIDRdttLDADRFAQTLAAARIDVL 1453
Cdd:PRK08008   194 THYNLrfAGYYSAWQCAL----RDDDVYLTVMPAfhiDCQCTAAMAAFSAGATFVLLEK---YSARAFWGQVCKYRATIT 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1454 KIVPGHLHAL-LQAERAADAlpAHTL--VLGGEATSWELLDTIAAlRPDCRVHNHYGPTETTVGILTQPAAQACRaaatL 1530
Cdd:PRK08008   267 ECIPMMIRTLmVQPPSANDR--QHCLreVMFYLNLSDQEKDAFEE-RFGVRLLTSYGMTETIVGIIGDRPGDKRR----W 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1531 P-LGRPLDNNETWLLDEHLNPVGTGGTGELYLGG-AGVAL--GYLHQPALTAARFVPhpfaaGARLYrSGDRARRLADGS 1606
Cdd:PRK08008   340 PsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGKTIfkEYYLDPKATAKVLEA-----DGWLH-TGDTGYVDEEGF 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1607 LEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGA----RLAAFATPQPGASLDAAALKRALAALLPDYMV 1682
Cdd:PRK08008   414 FYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSirdeAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKV 493
                          490       500
                   ....*....|....*....|....
gi 1888712850 1683 PSVLRVIDALPLNRNGKLDRQALS 1706
Cdd:PRK08008   494 PSYLEIRKDLPRNCSGKIIKKNLK 517
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
28-593 1.49e-15

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 81.96  E-value: 1.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   28 RAlAQQRPEATALIvidaDGDTRYDYAQldrraralaarfardgaAAER----ALILMDSGV---DYVS----------- 89
Cdd:cd12118     12 RA-AAVYPDRTSIV----YGDRRYTWRQ-----------------TYDRcrrlASALAALGIsrgDTVAvlapntpamye 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   90 AFFGCLYAGVVAVPVyppeskreqhlarlrgiardaGVRYVLTTAALHERHADAwsmlapgaDVVAVDT------LDARD 163
Cdd:cd12118     70 LHFGVPMAGAVLNAL---------------------NTRLDAEEIAFILRHSEA--------KVLFVDRefeyedLLAEG 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  164 TPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSG 243
Cdd:cd12118    121 DPDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGG 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  244 IPLVLMSpqyfLERPLRWlDAIARHRGT-ISGAPDFAYRLCAERinDETRAKLdlsSWRLAF--SGSEPVRRdtlddFVA 320
Cdd:cd12118    201 TNVCLRK----VDAKAIY-DLIEKHKVThFCGAPTVLNMLANAP--PSDARPL---PHRVHVmtAGAPPPAA-----VLA 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  321 RFAPAGFDAAALypcYGLAEATlfvtggvrGAGLVS---------HAFSSAALSAgraeaaradeaatvlvgcgavQAGH 391
Cdd:cd12118    266 KMEELGFDVTHV---YGLTETY--------GPATVCawkpewdelPTEERARLKA---------------------RQGV 313
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  392 rvaivaraaaESHESHEADVE-TETSRAGERlaDGR-IGEIHVSGPSVAHGYWQRADASAQAFvdaprhADGsgparWLR 469
Cdd:cd12118    314 ----------RYVGLEEVDVLdPETMKPVPR--DGKtIGEIVFRGNIVMKGYLKNPEATAEAF------RGG-----WFH 370
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  470 TGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAFGATLggGETLGLALEIAPRMKKRfaA 548
Cdd:cd12118    371 SGDLAVIHpDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKW--GEVPCAFVELKEGAKVT--E 446
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 1888712850  549 AQIVETLRRiaFDACGETPAAIALlnpGALPKTSSGKLQRAATRE 593
Cdd:cd12118    447 EEIIAFCRE--HLAGFMVPKTVVF---GELPKTSTGKIQKFVLRD 486
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
123-314 2.32e-15

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 82.71  E-value: 2.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  123 RDAGVRYVLTTAALHE--RHADAWSMLAPGADVVAVDTLDARDTPSD------------APLHPVRADDLAFLQYTSGST 188
Cdd:PRK06814   726 KAAQVKTVLTSRAFIEkaRLGPLIEALEFGIRIIYLEDVRAQIGLADkikgllagrfplVYFCNRDPDDPAVILFTSGSE 805
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  189 GSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLvlmspqYFLERPLrwldaiarH 268
Cdd:PRK06814   806 GTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKV------FLYPSPL--------H 871
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1888712850  269 rgtisgapdfaYRLCAERINDeTRAKL------------------DLSSWRLAFSGSEPVRRDT 314
Cdd:PRK06814   872 -----------YRIIPELIYD-TNATIlfgtdtflngyaryahpyDFRSLRYVFAGAEKVKEET 923
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
1219-1699 2.73e-15

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 81.19  E-value: 2.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNP 1298
Cdd:cd12118     10 LERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1299 TQRLAQTLRDCGARLVLCEDDCSALDLMgvqhARIDaaqeeaqreqhlRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVI 1378
Cdd:cd12118     90 AEEIAFILRHSEAKVLFVDREFEYEDLL----AEGD------------PDFEWIPPADEWDPIALNYTSGTTGRPKGVVY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1379 AH-GALTNYVDAVLA-RLDPPPR-------------------ARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLD 1437
Cdd:cd12118    154 HHrGAYLNALANILEwEMKQHPVylwtlpmfhcngwcfpwtvAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLN 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1438 adrfaqTLAAARIDVLKIVPGHLHALLqaerAADALPAHTLV----LGGeatswelldtiaalrpdcRVHNHYGPTET-- 1511
Cdd:cd12118    234 ------MLANAPPSDARPLPHRVHVMT----AGAPPPAAVLAkmeeLGF------------------DVTHVYGLTETyg 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1512 --TVGIL-----TQPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGT--GELYLGGAGVALGYLHQPALTAArfv 1582
Cdd:cd12118    286 paTVCAWkpewdELPTEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAE--- 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1583 phPFAAGarLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATP 1658
Cdd:cd12118    363 --AFRGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPdekwGEVPCAFVEL 438
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1888712850 1659 QPGASLDAAALKRALAALLPDYMVPSVLrVIDALPLNRNGK 1699
Cdd:cd12118    439 KEGAKVTEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGK 478
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
79-510 3.65e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 81.10  E-value: 3.65e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   79 ILMDSGVDYVSAFFGCLYAGVVAVPVyppeskrEQHL--ARLRGIARDAGVRYVLTTAALHERHADAWSMLAPGADVVAV 156
Cdd:PRK08276    41 ILLENNPEFFEVYWAARRSGLYYTPI-------NWHLtaAEIAYIVDDSGAKVLIVSAALADTAAELAAELPAGVPLLLV 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  157 DTLD---------ARDTPSDAPLHPVRADDLafLQYTSGSTGSPKGVMVS------HGNLLANEIAIQAGLGVRPDDVFV 221
Cdd:PRK08276   114 VAGPvpgfrsyeeALAAQPDTPIADETAGAD--MLYSSGTTGRPKGIKRPlpgldpDEAPGMMLALLGFGMYGGPDSVYL 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  222 SWLPLYHD--MGLIGSLLQpvfSGIPLVLMspqyflER--PLRWLDAIARHRGTISG-APDFAYRLCAerINDETRAKLD 296
Cdd:PRK08276   192 SPAPLYHTapLRFGMSALA---LGGTVVVM------EKfdAEEALALIERYRVTHSQlVPTMFVRMLK--LPEEVRARYD 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  297 LSSWRLAFSGSEP----VRRDTLDDFvarfapagfdAAALYPCYGLAEAtlfvtGGVrgaglvshAFSSAAL------SA 366
Cdd:PRK08276   261 VSSLRVAIHAAAPcpveVKRAMIDWW----------GPIIHEYYASSEG-----GGV--------TVITSEDwlahpgSV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  367 GRaeaaradeaatvlvgcgAVQAghrvaivaraaaeshESHEADvetetsRAGERLADGRIGEIHVSGPSVAHGYWQRAD 446
Cdd:PRK08276   318 GK-----------------AVLG---------------EVRILD------EDGNELPPGEIGTVYFEMDGYPFEYHNDPE 359
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850  447 ASAQAfvdapRHADGsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PRK08276   360 KTAAA-----RNPHG-----WVTVGDVGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTH 414
PLN02574 PLN02574
4-coumarate--CoA ligase-like
78-512 3.81e-15

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 81.04  E-value: 3.81e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   78 LILMDSGVDYVSAFFGCLYAGVVAVPVYPPESkreqhLARLRGIARDAGVRYVLTTAALHERhadawsmLAP-GADVVAV 156
Cdd:PLN02574    96 LLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSS-----LGEIKKRVVDCSVGLAFTSPENVEK-------LSPlGVPVIGV 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  157 -DTLDARD-TPSDAPLH-------------PVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANE---IAIQAGLGVRP-- 216
Cdd:PLN02574   164 pENYDFDSkRIEFPKFYelikedfdfvpkpVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVelfVRFEASQYEYPgs 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  217 DDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMspqyflerplRWLDA----IARHRGTISGAPDFAYRLCAERINDETR 292
Cdd:PLN02574   244 DNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVM----------RRFDAsdmvKVIDRFKVTHFPVVPPILMALTKKAKGV 313
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  293 AKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAalypcYGLAEATLFVTGGVRGAGLvsHAFSSAALSAgraeaa 372
Cdd:PLN02574   314 CGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQG-----YGMTESTAVGTRGFNTEKL--SKYSSVGLLA------ 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  373 radeaatvlvgcgavqaghrvaivaraaaESHESHEADVETetsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAF 452
Cdd:PLN02574   381 -----------------------------PNMQAKVVDWST-----GCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTI 426
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1888712850  453 VDaprhaDGsgparWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAE 512
Cdd:PLN02574   427 DK-----DG-----WLRTGDIAyFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPE 477
PLN02736 PLN02736
long-chain acyl-CoA synthetase
150-504 6.14e-15

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 80.91  E-value: 6.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  150 GADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPL--- 226
Cdd:PLN02736   195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLahi 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  227 YHDMGLIGSLLQPV----FSGIPLVLMS------PQYFLERPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLD 296
Cdd:PLN02736   275 YERVNQIVMLHYGVavgfYQGDNLKLMDdlaalrPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALEN 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  297 LSS----W-RLAF---------------SGSEPVRRDTLDdfvarFAPAGFDAAALyPCYGLAEATLFVTGGVRGAGLVS 356
Cdd:PLN02736   355 GKNpspmWdRLVFnkikaklggrvrfmsSGASPLSPDVME-----FLRICFGGRVL-EGYGMTETSCVISGMDEGDNLSG 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  357 HAFSSAAlsagraeaaradeaatvlvgcgavqaghrvaivaraaaeSHESHEADVeTETSRAGERLADGRiGEIHVSGPS 436
Cdd:PLN02736   429 HVGSPNP---------------------------------------ACEVKLVDV-PEMNYTSEDQPYPR-GEICVRGPI 467
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  437 VAHGYWqRADASAQAFVDaprhADGsgparWLRTGDLG-FVHDGQLYIAGRVKDLV-IVRGRNLYPQDVE 504
Cdd:PLN02736   468 IFKGYY-KDEVQTREVID----EDG-----WLHTGDIGlWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIE 527
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1229-1847 1.18e-14

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 80.08  E-value: 1.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1229 APAVIdgalrmSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGgaYVALDAGNPTQRLAQTL-- 1306
Cdd:PRK06060    27 AADVV------THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARG--VMAFLANPELHRDDHALaa 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLCEDD-CSALDLMGVqharIDAAQ--EEAQREQhlraPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGAL 1383
Cdd:PRK06060    99 RNTEPALVVTSDAlRDRFQPSRV----AEAAElmSEAARVA----PGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADP 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1384 TNYVDAVLA---RLDPPPRARFAMVSTIGADLGHTVLFgALASGGALhlIDRDTTLDADRFAQTLAAARIDVLKIVPGHL 1460
Cdd:PRK06060   171 LTFVDAMCRkalRLTPEDTGLCSARMYFAYGLGNSVWF-PLATGGSA--VINSAPVTPEAAAILSARFGPSVLYGVPNFF 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1461 HALLQAERAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQACRAAatlpLGRPLDNNE 1540
Cdd:PRK06060   248 ARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGT----LGRVLPPYE 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1541 TWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPaltaarfvpHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIR 1620
Cdd:PRK06060   324 IRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIG 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1621 GYRVEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQPGA---SLDAAALKRALAALLPDYMVPSVLRVIDALP 1693
Cdd:PRK06060   395 GVNVDPREVERLIIEDEAVAEAAVVAVrestGASTLQAFLVATSGAtidGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLP 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1694 LNRNGKLDRQALSALArPAAPHREAARAAPQGETETAL-AQCWAALLDPSNGTDNATDN-------------------AT 1753
Cdd:PRK06060   475 RTPNGKLVRGALRKQS-PTKPIWELSLTEPGSGVRAQRdDLSASNMTIAGGNDGGATLRerlvalrqerqrlvvdavcAE 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1754 ATPSL------TIARDDSFFALGGHSLAAMRLASRVRSRWSVELPLREIFASPTLAALAARIEAQRADSDRasnqvsnka 1827
Cdd:PRK06060   554 AAKMLgepdpwSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAGGHG--------- 624
                          650       660
                   ....*....|....*....|
gi 1888712850 1828 anaESATPLHALADRSALPL 1847
Cdd:PRK06060   625 ---RLKSAGPVNSGATGLWA 641
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1239-1645 1.37e-14

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 78.76  E-value: 1.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1239 MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGayVALDAgnPTQRLAQTLRDcgarlvlced 1318
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGA--VVIPA--TTLLTPDDLRD---------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1319 dcsaldlmgvqhaRIDaaqeeaqreqhlRAPHALPAVDPRSAA----YVIYTSGSSGAPKGVVIAHGALTNYVDAVLARL 1394
Cdd:cd05974     67 -------------RVD------------RGGAVYAAVDENTHAddpmLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWI 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1395 DPPPRARFAMVSTIG-ADLGHTVLFGALASGGALHLIDRdTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADAL 1473
Cdd:cd05974    122 GLKPGDVHWNISSPGwAKHAWSCFFAPWNAGATVFLFNY-ARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDV 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1474 PAHTLVLGGEATSWELLDTIAALRpDCRVHNHYGPTETTVGILTQPAAQACRAAatlpLGRPLDNNETWLLDEHLNPVgT 1553
Cdd:cd05974    201 KLREVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTETTALVGNSPGQPVKAGS----MGRPLPGYRVALLDPDGAPA-T 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1554 GGTGELYLGG---AGVALGYLHQPALTAArfvphpfAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIA 1630
Cdd:cd05974    275 EGEVALDLGDtrpVGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
                          410
                   ....*....|....*
gi 1888712850 1631 ARLKALDGVRDAAVI 1645
Cdd:cd05974    348 SVLIEHPAVAEAAVV 362
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
168-490 2.05e-14

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 78.80  E-value: 2.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  168 APLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLG----VRPDDVFVSWLPLYH------------DMG 231
Cdd:cd05927    106 VPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEilnkINPTDVYISYLPLAHifervvealflyHGA 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  232 LIGsllqpVFSGIPLVLM------SPQYFLERPlRWLDAI-ARHRGTISGAP-------DFAYRLCAERINdetRAKLDL 297
Cdd:cd05927    186 KIG-----FYSGDIRLLLddikalKPTVFPGVP-RVLNRIyDKIFNKVQAKGplkrklfNFALNYKLAELR---SGVVRA 256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  298 SSW-----------------RLAFSGSEPVRRDTLDdfvarFAPAGFDaAALYPCYGLAEATlfvtggvrGAGLVSHAFS 360
Cdd:cd05927    257 SPFwdklvfnkikqalggnvRLMLTGSAPLSPEVLE-----FLRVALG-CPVLEGYGQTECT--------AGATLTLPGD 322
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  361 SaalSAGRaeaaradeaatvlvgCGAVQAghrvaivaraaaeSHESHEADV-ETETSRAGErlaDGRiGEIHVSGPSVAH 439
Cdd:cd05927    323 T---SVGH---------------VGGPLP-------------CAEVKLVDVpEMNYDAKDP---NPR-GEVCIRGPNVFS 367
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1888712850  440 GYWQRADASAQAFvdaprHADGsgparWLRTGDLG-FVHDGQLYIAGRVKDL 490
Cdd:cd05927    368 GYYKDPEKTAEAL-----DEDG-----WLHTGDIGeWLPNGTLKIIDRKKNI 409
PRK07470 PRK07470
acyl-CoA synthetase; Validated
1227-1700 2.24e-14

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 78.54  E-value: 2.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1227 PDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:PRK07470    21 PDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLA 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLCEDD---------CSALDLMGV---QHARIDAAQEEAQREqHLRAPHALPAVDPRSAAYVIYTSGSSGAPK 1374
Cdd:PRK07470   101 EASGARAMICHADfpehaaavrAASPDLTHVvaiGGARAGLDYEALVAR-HLGARVANAAVDHDDPCWFFFTSGTTGRPK 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1375 GVVIAHGALTNYVDAVLARLDPPPRARFAmvSTIGADLGHtvlfGA-------LASGGALHLIDRDtTLDADRFAQTLAA 1447
Cdd:PRK07470   180 AAVLTHGQMAFVITNHLADLMPGTTEQDA--SLVVAPLSH----GAgihqlcqVARGAATVLLPSE-RFDPAEVWALVER 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1448 ARIDVLKIVPGHLHALLQAErAADALPAHTL---VLGGEATSWEllDTIAALRPDCRVH-NHYGPTETTVGILTQPAAQA 1523
Cdd:PRK07470   253 HRVTNLFTVPTILKMLVEHP-AVDRYDHSSLryvIYAGAPMYRA--DQKRALAKLGKVLvQYFGLGEVTGNITVLPPALH 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1524 CRAAATL----PLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlyRSGDRA 1599
Cdd:PRK07470   330 DAEDGPDarigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------RTGDLG 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1600 RRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAA 1675
Cdd:PRK07470   403 HLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPdpvwGEVGVAVCVARDGAPVDEAELLAWLDG 482
                          490       500
                   ....*....|....*....|....*
gi 1888712850 1676 LLPDYMVPSVLRVIDALPLNRNGKL 1700
Cdd:PRK07470   483 KVARYKLPKRFFFWDALPKSGYGKI 507
PRK07867 PRK07867
acyl-CoA synthetase; Validated
1228-1707 2.35e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 78.57  E-value: 2.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1228 DAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEP-VAIVAHRSARFVVAMLGVLKAGGAYVALdagNPTQRLAQTL 1306
Cdd:PRK07867    18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGL---NPTRRGAALA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RD---CGARLVLCEDDCSAL---DLMGVQHARIDAAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAH 1380
Cdd:PRK07867    95 RDiahADCQLVLTESAHAELldgLDPGVRVINVDSPAWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTH 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1381 GALTnYVDAVLArldppprARFAM----VSTIGADLGHT--VLFG---ALASGGALHLIDRdttLDADRFAQTLAAARID 1451
Cdd:PRK07867   175 RKVA-SAGVMLA-------QRFGLgpddVCYVSMPLFHSnaVMAGwavALAAGASIALRRK---FSASGFLPDVRRYGAT 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1452 VLKIVPGHLHALLQA-ERAADALPAHTLVLGGEATSWElLDTIAAlRPDCRVHNHYGPTETTVGILTQPaaqacraaATL 1530
Cdd:PRK07867   244 YANYVGKPLSYVLATpERPDDADNPLRIVYGNEGAPGD-IARFAR-RFGCVVVDGFGSTEGGVAITRTP--------DTP 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1531 P--LGRPLD-----NNETW------LLDEHLNPVGTGGTGELY-LGGAGVALGYLHQPALTAARfvphpfAAGARlYRSG 1596
Cdd:PRK07867   314 PgaLGPLPPgvaivDPDTGtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAER------MRGGV-YWSG 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1597 DRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVI----VVAGARLAAFATPQPGASlDAAALKRA 1672
Cdd:PRK07867   387 DLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYavpdPVVGDQVMAALVLAPGAK-FDPDAFAE 465
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1888712850 1673 LAALLPDY---MVPSVLRVIDALPLNRNGKLDRQALSA 1707
Cdd:PRK07867   466 FLAAQPDLgpkQWPSYVRVCAELPRTATFKVLKRQLSA 503
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
177-588 2.39e-14

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 76.92  E-value: 2.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  177 DLAFLQYTSGSTGSPKGVMVSHGNL-LANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQYFL 255
Cdd:cd17635      2 DPLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  256 ErplrWLDAIARHRGTISG-APDFAYRLCAERIN-DETRAKLDLsswrLAFSGSEPVRRDTlddfvaRFAPAgFDAAALY 333
Cdd:cd17635     82 S----LFKILTTNAVTTTClVPTLLSKLVSELKSaNATVPSLRL----IGYGGSRAIAADV------RFIEA-TGLTNTA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  334 PCYGLAEATlfvtggvRGAGLVSHAFSSAALSAGraeaaradeaatvlvgcgavqaghrvaivaraaaesHESHEADVET 413
Cdd:cd17635    147 QVYGLSETG-------TALCLPTDDDSIEINAVG------------------------------------RPYPGVDVYL 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  414 ETSRAGERLADGRiGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFV-HDGQLYIAGRVKDLVI 492
Cdd:cd17635    184 AATDGIAGPSASF-GTIWIKSPANMLGYWNNPERTAEVLIDG-----------WVNTGDLGERrEDGFLFITGRSSESIN 251
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  493 VRGRNLYPQDVEQAVEaHAEFARKGRVIAFGATLgGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDAcgeTPAAIAL 572
Cdd:cd17635    252 CGGVKIAPDEVERIAE-GVSGVQECACYEISDEE-FGELVGLAVVASAELDENAIRALKHTIRRELEPYA---RPSTIVI 326
                          410
                   ....*....|....*.
gi 1888712850  573 LNpgALPKTSSGKLQR 588
Cdd:cd17635    327 VT--DIPRTQSGKVKR 340
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
1240-1705 2.59e-14

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 77.77  E-value: 2.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDcgarlvlcedd 1319
Cdd:cd05912      3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKD----------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1320 csaldlmgvqharIDAAQEEAqreqhlraphalpavdprsaAYVIYTSGSSGAPKGVVIAHGalTNYVDAVLARLdpppr 1399
Cdd:cd05912     72 -------------SDVKLDDI--------------------ATIMYTSGTTGKPKGVQQTFG--NHWWSAIGSAL----- 111
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1400 arfamvsTIGAD--------------LGHTVLFGALASGGALHLIDRdttLDADRFAQTLAAARIDVLKIVPGHLHALLq 1465
Cdd:cd05912    112 -------NLGLTeddnwlcalplfhiSGLSILMRSVIYGMTVYLVDK---FDAEQVLHLINSGKVTIISVVPTMLQRLL- 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1466 aERAADALPAH--TLVLGGEATSWELLDTIAALrpDCRVHNHYGPTETTVGILTQPAAQACRAAATLplGRPLDNNETWL 1543
Cdd:cd05912    181 -EILGEGYPNNlrCILLGGGPAPKPLLEQCKEK--GIPVYQSYGMTETCSQIVTLSPEDALNKIGSA--GKPLFPVELKI 255
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1544 LDEHLNPvgtGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlyRSGDRARRLADGSLEYLGRIDDQVKIRGYR 1623
Cdd:cd05912    256 EDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGEN 325
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1624 VEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLpdYMVPSVLRVIDALPLNRNGK 1699
Cdd:cd05912    326 IYPAEIEEVLLSHPAIKEAGVVGIPddkwGQVPVAFVVSERPISEEELIAYCSEKLAK--YKVPKKIYFVDELPRTASGK 403

                   ....*.
gi 1888712850 1700 LDRQAL 1705
Cdd:cd05912    404 LLRHEL 409
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
1355-1709 2.96e-14

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 78.14  E-value: 2.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1355 VDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTV-LFGALASGgaLHLIDRD 1433
Cdd:cd05909    144 VQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGcLWLPLLSG--IKVVFHP 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1434 TTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAAlRPDCRVHNHYGPTETT- 1512
Cdd:cd05909    222 NPLDYKKIPELIYDKKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQE-KFGIRILEGYGTTECSp 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1513 VGILTQPAAQACRAAatlpLGRPLDNNETWLLD-EHLNPVGTGGTGELYLGGAGVALGYLHQPALTAarfvphpFAAGAR 1591
Cdd:cd05909    301 VISVNTPQSPNKEGT----VGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDG 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1592 LYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDG--VRDAAVIVV---AGARLAAFATPQpgASLDA 1666
Cdd:cd05909    370 WYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPedNEVAVVSVPdgrKGEKIVLLTTTT--DTDPS 447
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1888712850 1667 AALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSALA 1709
Cdd:cd05909    448 SLNDILKNAGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
1216-1710 4.49e-14

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 77.74  E-value: 4.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1216 HLRVARHA-DTQPDAPAVI-DGAL-----RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGG 1288
Cdd:cd05967     53 YNALDRHVeAGRGDQIALIyDSPVtgterTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGA 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1289 AYVALDAGNPTQRLAQTLRDCGARLVLCEDdC---------------SALDLMGVQHARI---DAAQEEAQREQHLR--- 1347
Cdd:cd05967    133 IHSVVFGGFAAKELASRIDDAKPKLIVTAS-CgiepgkvvpykplldKALELSGHKPHHVlvlNRPQVPADLTKPGRdld 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1348 --------APHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHG----ALTNYVDAVLarlDPPPRARFAMVSTIGADLGHT 1415
Cdd:cd05967    212 wsellakaEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGghavALNWSMRNIY---GIKPGDVWWAASDVGWVVGHS 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1416 -VLFGALASGGALHLID--RDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAH------TLVLGGEATS 1486
Cdd:cd05967    289 yIVYGPLLHGATTVLYEgkPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIKKYdlsslrTLFLAGERLD 368
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1487 WELLDTIAAL--RPdcrVHNHYGPTETTVGILTQPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGA 1564
Cdd:cd05967    369 PPTLEWAENTlgVP---VIDHWWQTETGWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP 445
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1565 ---GVALGYLHQPAltaaRFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRD 1641
Cdd:cd05967    446 lppGCLLTLWKNDE----RFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAE 521
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1888712850 1642 AAVIVV----AGARLAAFATPQPGASLDAAALKRALAALLPDYMVP----SVLRVIDALPLNRNGKLDRQALSALAR 1710
Cdd:cd05967    522 CAVVGVrdelKGQVPLGLVVLKEGVKITAEELEKELVALVREQIGPvaafRLVIFVKRLPKTRSGKILRRTLRKIAD 598
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
97-556 5.18e-14

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 77.51  E-value: 5.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   97 AGVVAVPVYP---PESkreqhlarlrgiardagVRYVLT---TAALHERHADAWSMLAPG--ADVVAV------------ 156
Cdd:cd05932     54 AGHISVPLYPtlnPDT-----------------IRYVLEhseSKALFVGKLDDWKAMAPGvpEGLISIslpppsaancqy 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  157 --DTLDARDTPS-DAPLHpvRADDLAFLQYTSGSTGSPKGVMVSHGNLlanEIAIQAG---LGVRPDDVFVSWLPLYHDM 230
Cdd:cd05932    117 qwDDLIAQHPPLeERPTR--FPEQLATLIYTSGTTGQPKGVMLTFGSF---AWAAQAGiehIGTEENDRMLSYLPLAHVT 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  231 GLIGSLLQPVFSGIPLvlmspqYFLERPLRWLDAIARHRGTISGAPDFAYRLCAERINDET-RAKLDLsSWRLAFSGSeP 309
Cdd:cd05932    192 ERVFVEGGSLYGGVLV------AFAESLDTFVEDVQRARPTLFFSVPRLWTKFQQGVQDKIpQQKLNL-LLKIPVVNS-L 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  310 VRRDTLDDFvarfapaGFDAAALYPCyglaeatlfvtggvrGAGLVSHAFSSAALSAGraeaaradeaATVLVGCGAVQA 389
Cdd:cd05932    264 VKRKVLKGL-------GLDQCRLAGC---------------GSAPVPPALLEWYRSLG----------LNILEAYGMTEN 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  390 ghrvaivaraAAESHESHEADVETETsrAGERLADGRI-----GEIHVSGPSVAHGYWQRADASAQAFVDaprhaDGsgp 464
Cdd:cd05932    312 ----------FAYSHLNYPGRDKIGT--VGNAGPGVEVrisedGEILVRSPALMMGYYKDPEATAEAFTA-----DG--- 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  465 arWLRTGDLGFV-HDGQLYIAGRVKDLV-IVRGRNLYPQDVEQAVeahAEFARKGRVIAFGATLGGGETLGLALEIAPRM 542
Cdd:cd05932    372 --FLRTGDKGELdADGNLTITGRVKDIFkTSKGKYVAPAPIENKL---AEHDRVEMVCVIGSGLPAPLALVVLSEEARLR 446
                          490
                   ....*....|....
gi 1888712850  543 KKRFAAAQIVETLR 556
Cdd:cd05932    447 ADAFARAELEASLR 460
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
176-510 7.79e-14

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 77.15  E-value: 7.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  176 DDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHdMGLIGSLLQPVFSGIPLVLMsPQYfl 255
Cdd:PLN02860   172 DDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCH-IGGLSSALAMLMVGACHVLL-PKF-- 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  256 ERPLRwLDAIARHRGT--ISGAPDFA--YRLCAERINDETRakldlSSWRLAFSGSEPVRRDTLDDfvarfAPAGFDAAA 331
Cdd:PLN02860   248 DAKAA-LQAIKQHNVTsmITVPAMMAdlISLTRKSMTWKVF-----PSVRKILNGGGSLSSRLLPD-----AKKLFPNAK 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  332 LYPCYGLAEAT---LFVTggVRGAGLVShaFSSAALSAGRAEAARADEAATVLVGCGAvqaghrvaivaraaaesheSHe 408
Cdd:PLN02860   317 LFSAYGMTEACsslTFMT--LHDPTLES--PKQTLQTVNQTKSSSVHQPQGVCVGKPA-------------------PH- 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  409 adVETETSRAGErladGRIGEIHVSGPSVAHGYWQRADASAQAfvdapRHADGsgparWLRTGDLGFVHD-GQLYIAGRV 487
Cdd:PLN02860   373 --VELKIGLDES----SRVGRILTRGPHVMLGYWGQNSETASV-----LSNDG-----WLDTGDIGWIDKaGNLWLIGRS 436
                          330       340
                   ....*....|....*....|...
gi 1888712850  488 KDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PLN02860   437 NDRIKTGGENVYPEEVEAVLSQH 459
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
1238-1692 9.30e-14

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 76.24  E-value: 9.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1238 RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAyVALDagNPTQR---LAQTLRDCGARLV 1314
Cdd:cd05940      3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV-AALI--NYNLRgesLAHCLNVSSAKHL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1315 LceddcsaldlmgvqharidaaqeeaqreqhlraphalpaVDPrsaAYVIYTSGSSGAPKGVVIAHGALTNYvdavlarl 1394
Cdd:cd05940     80 V---------------------------------------VDA---ALYIYTSGTTGLPKAAIISHRRAWRG-------- 109
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1395 dppprARFAMVSTIGAD---------LGH----TVLFGA-LASGGALHLIDRdttLDADRFAQTLAAARIDVLKIVpGHL 1460
Cdd:cd05940    110 -----GAFFAGSGGALPsdvlytclpLYHstalIVGWSAcLASGATLVIRKK---FSASNFWDDIRKYQATIFQYI-GEL 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1461 HALLQAERAADALPAH--TLVLGGeatswelldtiaALRPDC-----------RVHNHYGPTETTVGILTQPAAQAC--R 1525
Cdd:cd05940    181 CRYLLNQPPKPTERKHkvRMIFGN------------GLRPDIweefkerfgvpRIAEFYAATEGNSGFINFFGKPGAigR 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1526 AAATLPLGRP-------LDNNETWLLDEHL-NPVGTGGTGEL--YLGGAGVALGYLhQPALTAARFVPHPFAAGARLYRS 1595
Cdd:cd05940    249 NPSLLRKVAPlalvkydLESGEPIRDAEGRcIKVPRGEPGLLisRINPLEPFDGYT-DPAATEKKILRDVFKKGDAWFNT 327
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1596 GDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAV--IVVAG----ARLAAFATPqPGASLDAAAL 1669
Cdd:cd05940    328 GDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGtdgrAGMAAIVLQ-PNEEFDLSAL 406
                          490       500
                   ....*....|....*....|...
gi 1888712850 1670 KRALAALLPDYMVPSVLRVIDAL 1692
Cdd:cd05940    407 AAHLEKNLPGYARPLFLRLQPEM 429
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
1363-1663 1.95e-13

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 73.88  E-value: 1.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1363 VIYTSGSSGAPKGVVIAHGAL--TNYVDAVLARLDPPPRarFAMVSTigadLGHT-VLFGALAS---GGALHLIDRdttL 1436
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALlaQALVLAVLQAIDEGTV--FLNSGP----LFHIgTLMFTLATfhaGGTNVFVRR---V 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1437 DADRFAQTLAAARIDVLKIVPGHLHALLQAErAADALPAHTLVLGGEATSWELLDTIAAlRPDCRVHNHYGPTETTvGIL 1516
Cdd:cd17636     76 DAEEVLELIEAERCTHAFLLPPTIDQIVELN-ADGLYDLSSLRSSPAAPEWNDMATVDT-SPWGRKPGGYGQTEVM-GLA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1517 TQPAAQACRAAATlplGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVphpfaagARLYRSG 1596
Cdd:cd17636    153 TFAALGGGAIGGA---GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-------GGWHHTN 222
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1888712850 1597 DRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGARLA----AFATPQPGAS 1663
Cdd:cd17636    223 DLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAqsvkAIVVLKPGAS 293
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
183-588 2.83e-13

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 73.21  E-value: 2.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  183 YTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGsLLQPVFSGIPLVLMSpqyfLERPLRWL 262
Cdd:cd17633      7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYG-AISALYLGGTFIGQR----KFNPKSWI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  263 DAIARHRGT-ISGAPDFAYRLCAERINDetrakldlSSWRLAFSGSepvrrDTLDDFVARFAPAGFDAAALYPCYGLAEA 341
Cdd:cd17633     82 RKINQYNATvIYLVPTMLQALARTLEPE--------SKIKSIFSSG-----QKLFESTKKKLKNIFPKANLIEFYGTSEL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  342 TlFVTGGVRGAglvshafSSAALSAGRAEaaradeaatvlvgcgavqaghrvaivaraaaeshesheADVETETSRAGer 421
Cdd:cd17633    149 S-FITYNFNQE-------SRPPNSVGRPF--------------------------------------PNVEIEIRNAD-- 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  422 laDGRIGEIHVSGPSVAHGYWQradasaqafvdaprhADGSGPARWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYP 500
Cdd:cd17633    181 --GGEIGKIFVKSEMVFSGYVR---------------GGFSNPDGWMSVGDIGYVdEEGYLYLVGRESDMIIIGGINIFP 243
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  501 QDVEQAVEAHAEFARKGrVIAFGATlGGGEtLGLALEIAPRMKKRFAAAQIVETLRRIafdacgETPAAIALLNpgALPK 580
Cdd:cd17633    244 TEIESVLKAIPGIEEAI-VVGIPDA-RFGE-IAVALYSGDKLTYKQLKRFLKQKLSRY------EIPKKIIFVD--SLPY 312

                   ....*...
gi 1888712850  581 TSSGKLQR 588
Cdd:cd17633    313 TSSGKIAR 320
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
1210-1647 3.45e-13

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 75.06  E-value: 3.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1210 PPGEPIHLRVARHAD----------TQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVA 1279
Cdd:PRK07059    10 PPGVPAEIDASQYPSladlleesfrQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1280 MLGVLKAGgaYVALDAgNP--TQR-LAQTLRDCGAR-LVLCEDDCSAL------------------DLMGV--------- 1328
Cdd:PRK07059    90 IAAVLRAG--YVVVNV-NPlyTPReLEHQLKDSGAEaIVVLENFATTVqqvlaktavkhvvvasmgDLLGFkghivnfvv 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1329 -------------QHARIDAAQEEAQReQHLRAPHalpaVDPRSAAYVIYTSGSSGAPKGVVIAHGaltNYVDAVL---- 1391
Cdd:PRK07059   167 rrvkkmvpawslpGHVRFNDALAEGAR-QTFKPVK----LGPDDVAFLQYTGGTTGVSKGATLLHR---NIVANVLqmea 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1392 ----ARLDPPPRARFAMVSTIgaDLGH----TVLF-GALASGGALHLIdrDTTLDADRFAQTLAAARIDVLKIVPGHLHA 1462
Cdd:PRK07059   239 wlqpAFEKKPRPDQLNFVCAL--PLYHifalTVCGlLGMRTGGRNILI--PNPRDIPGFIKELKKYQVHIFPAVNTLYNA 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1463 LLQAERAADALPAHTLV-LGGeatswelldTIAALRP---------DCRVHNHYGPTETTVGILTQPaaqACRAAATLPL 1532
Cdd:PRK07059   315 LLNNPDFDKLDFSKLIVaNGG---------GMAVQRPvaerwlemtGCPITEGYGLSETSPVATCNP---VDATEFSGTI 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1533 GRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlYRSGDRARRLADGSLEYLGR 1612
Cdd:PRK07059   383 GLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDR 456
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1888712850 1613 IDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV 1647
Cdd:PRK07059   457 KKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGV 491
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
174-510 3.94e-13

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 74.49  E-value: 3.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  174 RADDLAFLQYTSGSTGSPKGVMVSHGNLLAN-EIAIQAGLG--VRPDDVFVSWLPLYHDMGLIgSLLQPVFSGIPLVLMs 250
Cdd:cd17642    182 RDEQVALIMNSSGSTGLPKGVQLTHKNIVARfSHARDPIFGnqIIPDTAILTVIPFHHGFGMF-TTLGYLICGFRVVLM- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  251 pqYFLERPLrWLDAIARHR--GTISGAPDFAYRLCAERINdetraKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFD 328
Cdd:cd17642    260 --YKFEEEL-FLRSLQDYKvqSALLVPTLFAFFAKSTLVD-----KYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIR 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  329 AAalypcYGLAEATLFV----TGGVR-GAglvshafssaalsagraeaaradeaatvlvgCGAVQAGhrvaivaraaaes 403
Cdd:cd17642    332 QG-----YGLTETTSAIlitpEGDDKpGA-------------------------------VGKVVPF------------- 362
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  404 HESHEADVETetsraGERLADGRIGEIHVSGPSVAHGYWQRADASaQAFVDaprhADGsgparWLRTGDLGFV-HDGQLY 482
Cdd:cd17642    363 FYAKVVDLDT-----GKTLGPNERGELCVKGPMIMKGYVNNPEAT-KALID----KDG-----WLHSGDIAYYdEDGHFF 427
                          330       340
                   ....*....|....*....|....*...
gi 1888712850  483 IAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:cd17642    428 IVDRLKSLIKYKGYQVPPAELESILLQH 455
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1219-1714 3.96e-13

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 74.64  E-value: 3.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADtqPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYV-ALDAGN 1297
Cdd:PRK10946    31 LTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVnALFSHQ 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 PTQRLAQTLRDCGARLV------LCEDDCSALDLM----GVQHARIDAAQEEAQREQHLRAPHALPAVDPRSAAYVIY-- 1365
Cdd:PRK10946   109 RSELNAYASQIEPALLIadrqhaLFSDDDFLNTLVaehsSLRVVLLLNDDGEHSLDDAINHPAEDFTATPSPADEVAFfq 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1366 -TSGSSGAPKGVVIAHgalTNYVDAVLA-----RLDPP-------PRARFAMVSTIGAdlghtvlFGALASGGALHLIdr 1432
Cdd:PRK10946   189 lSGGSTGTPKLIPRTH---NDYYYSVRRsveicGFTPQtrylcalPAAHNYPMSSPGA-------LGVFLAGGTVVLA-- 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1433 dTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAAD---ALPAHTLVLGGEAtswELLDTIAALRPD---CRVHNHY 1506
Cdd:PRK10946   257 -PDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGsraQLASLKLLQVGGA---RLSETLARRIPAelgCQLQQVF 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1507 GPTETTVG-----------ILTQpaaqacraaatlplGRPL-DNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQP 1574
Cdd:PRK10946   333 GMAEGLVNytrlddsderiFTTQ--------------GRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSP 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1575 ALTAARFVPHPFaagarlYRSGDRARRLADGSLEYLGRIDDQV-----KIRGYRVE------PGEIAARLKALD----GV 1639
Cdd:PRK10946   399 QHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQInrggeKIAAEEIEnlllrhPAVIHAALVSMEdelmGE 472
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850 1640 RDAAVIVVAGA----RLAAFATPQPGAsldaaalkralaallpDYMVPSVLRVIDALPLNRNGKLDRQALSALARPAAP 1714
Cdd:PRK10946   473 KSCAFLVVKEPlkavQLRRFLREQGIA----------------EFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
1542-1817 5.74e-13

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 72.09  E-value: 5.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1542 WLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRG 1621
Cdd:COG3433     31 LLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRA 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1622 YRVEPGEIAARLKALDGVRDAAVIVVAGARLAAFAT---PQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNG 1698
Cdd:COG3433    111 ERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIvgaVAALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLALK 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1699 KLDRQALSALARPAAPHREAARAAPQ-GETETALAQCWAALLDpsngtdnatdnataTPSLTIARDDSFFALGGHSLAAM 1777
Cdd:COG3433    191 VVARAAPALAAAEALLAAASPAPALEtALTEEELRADVAELLG--------------VDPEEIDPDDNLFDLGLDSIRLM 256
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1888712850 1778 RLASRVRSRwSVELPLREIFASPTLAALAARIEAQRADSD 1817
Cdd:COG3433    257 QLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
1191-1714 6.28e-13

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 73.93  E-value: 6.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1191 LLDADERArvsaASVARRTPPGEPIHLRVARHADTQPDAPAVIDGAL------RMSYAELDARAAHVAQWLLARDLQGGE 1264
Cdd:PRK13295     6 VLLPPRRA----ASIAAGHWHDRTINDDLDACVASCPDKTAVTAVRLgtgaprRFTYRELAALVDRVAVGLARLGVGRGD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1265 PVAIVAHRSARFVVAMLGVLKAGGAYvaldagNPtqrLAQTLRDCGARLVLCEDDCSAL--------------------D 1324
Cdd:PRK13295    82 VVSCQLPNWWEFTVLYLACSRIGAVL------NP---LMPIFRERELSFMLKHAESKVLvvpktfrgfdhaamarrlrpE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1325 LMGVQHARI---------DAAQEEAQREQHLRAPHAL--PAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLAR 1393
Cdd:PRK13295   153 LPALRHVVVvggdgadsfEALLITPAWEQEPDAPAILarLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAER 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1394 LDPPPRARFAMVSTIGADLGhtVLFGALAS---GGALHLIDrdtTLDADRFAQTLAAARIDVLKIVPGHLHALLQA-ERA 1469
Cdd:PRK13295   233 LGLGADDVILMASPMAHQTG--FMYGLMMPvmlGATAVLQD---IWDPARAAELIRTEGVTFTMASTPFLTDLTRAvKES 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1470 ADALPAHTLVLGGEA--------TSWELLDTiaalrpdcRVHNHYGPTETTVGILTQPAAQACRAAATLplGRPLDNNET 1541
Cdd:PRK13295   308 GRPVSSLRTFLCAGApipgalveRARAALGA--------KIVSAWGMTENGAVTLTKLDDPDERASTTD--GCPLPGVEV 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1542 WLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARfvphpfAAGarLYRSGDRARRLADGSLEYLGRIDDqVKIRG 1621
Cdd:PRK13295   378 RVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTD------ADG--WFDTGDLARIDADGYIRISGRSKD-VIIRG 448
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1622 YRVEP-GEIAARLKALDGVRDAAVIVVAGARLA----AFATPQPGASLDAAALKR--ALAALLPDYMvPSVLRVIDALPL 1694
Cdd:PRK13295   449 GENIPvVEIEALLYRHPAIAQVAIVAYPDERLGeracAFVVPRPGQSLDFEEMVEflKAQKVAKQYI-PERLVVRDALPR 527
                          570       580
                   ....*....|....*....|
gi 1888712850 1695 NRNGKLDRQALSALARPAAP 1714
Cdd:PRK13295   528 TPSGKIQKFRLREMLRGEDA 547
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
1358-1702 6.54e-13

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 72.29  E-value: 6.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1358 RSAAYVIYTSGSSGAPKGVVIAH----GALTNYVDAVL------ARLDPPPRARfamvsTIGADLGHTVLFgalASGGAL 1427
Cdd:cd17635      1 EDPLAVIFTSGTTGEPKAVLLANktffAVPDILQKEGLnwvvgdVTYLPLPATH-----IGGLWWILTCLI---HGGLCV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1428 HLIDRDTTLDADRFAQTLAAAridVLKIVPGHLHALLQAERAADA-LPAHTLVLGGEATSWELLDTIAALRPDCRVHNHY 1506
Cdd:cd17635     73 TGGENTTYKSLFKILTTNAVT---TTCLVPTLLSKLVSELKSANAtVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVY 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1507 GPTETTVGILTQPAAQACRAAAtlpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVphpf 1586
Cdd:cd17635    150 GLSETGTALCLPTDDDSIEINA---VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI---- 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1587 aaGARLYrSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGARLAAFATPQPGASL-- 1664
Cdd:cd17635    223 --DGWVN-TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAel 299
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1888712850 1665 ---DAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDR 1702
Cdd:cd17635    300 denAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
1219-1662 7.40e-13

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 74.01  E-value: 7.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVID-----GALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVAL 1293
Cdd:cd05921      1 LAHWARQAPDRTWLAEregngGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1294 dagNPTQRLAQT----LRDCGARL----VLCEDD------CSALDLMGVQ--HARIDAAQEE-------AQREQHLRAPH 1350
Cdd:cd05921     81 ---SPAYSLMSQdlakLKHLFELLkpglVFAQDAapfaraLAAIFPLGTPlvVSRNAVAGRGaisfaelAATPPTAAVDA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1351 ALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTN---YVDAVLARLDPPPrarfaMVSTIGADLGHTvlFGA------- 1420
Cdd:cd05921    158 AFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCAnqaMLEQTYPFFGEEP-----PVLVDWLPWNHT--FGGnhnfnlv 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1421 LASGGALHLIDRDTTldADRFAQTLAAARiDVLKI----VPGHLHALLQAERAADALPA------HTLVLGGEATS---W 1487
Cdd:cd05921    231 LYNGGTLYIDDGKPM--PGGFEETLRNLR-EISPTvyfnVPAGWEMLVAALEKDEALRRrffkrlKLMFYAGAGLSqdvW 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1488 ELLDTIAALRPDCRV--HNHYGPTET------TVGILTQPAAqacraaatlpLGRPLDNNETWLldehlnpVGTGGTGEL 1559
Cdd:cd05921    308 DRLQALAVATVGERIpmMAGLGATETaptatfTHWPTERSGL----------IGLPAPGTELKL-------VPSGGKYEV 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1560 YLGGAGVALGYLHQPALTAARFVPHPFaagarlYRSGDrARRLADGS-----LEYLGRIDDQVKIR-GYRVEPGEIAARL 1633
Cdd:cd05921    371 RVKGPNVTPGYWRQPELTAQAFDEEGF------YCLGD-AAKLADPDdpakgLVFDGRVAEDFKLAsGTWVSVGPLRARA 443
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1888712850 1634 KALDG--VRDAAVIVVAGARLAAFATPQPGA 1662
Cdd:cd05921    444 VAACAplVHDAVVAGEDRAEVGALVFPDLLA 474
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
29-510 7.75e-13

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 73.56  E-value: 7.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   29 ALAQQRPEATALIVIDADGDTR-YDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVyp 106
Cdd:PRK08008    15 DLADVYGHKTALIFESSGGVVRrYSYLELNEEINRTANLFYSLGiRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI-- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  107 peskREQHL-ARLRGIARDAGVRYVLTTAA--------LHERHADAWSMLAPGA------DVVAVDTLDARDTPSDAPLH 171
Cdd:PRK08008    93 ----NARLLrEESAWILQNSQASLLVTSAQfypmyrqiQQEDATPLRHICLTRValpaddGVSSFTQLKAQQPATLCYAP 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  172 PVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEI--AIQAGLgvRPDDVFVSWLPLYH-DMGLigSLLQPVFS-GIPLV 247
Cdd:PRK08008   169 PLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYysAWQCAL--RDDDVYLTVMPAFHiDCQC--TAAMAAFSaGATFV 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  248 LM---SPQYFlerplrWlDAIARHRGTISGA-PDFAYRLCAERIN-DETRAKLDLSSWRLAFSGSEPvrrdtlDDFVARF 322
Cdd:PRK08008   245 LLekySARAF------W-GQVCKYRATITECiPMMIRTLMVQPPSaNDRQHCLREVMFYLNLSDQEK------DAFEERF 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  323 apagfdAAALYPCYGLAEATLFVTGGVRG----------AGLvshafssaalsagraeaaradeaatvlvgcgavqaghr 392
Cdd:PRK08008   312 ------GVRLLTSYGMTETIVGIIGDRPGdkrrwpsigrPGF-------------------------------------- 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  393 vaivaraaaesheSHEADVETETSRAgerLADGRIGEIH---VSGPSVAHGYWQRADASAQAFvdaprHADGsgparWLR 469
Cdd:PRK08008   348 -------------CYEAEIRDDHNRP---LPAGEIGEICikgVPGKTIFKEYYLDPKATAKVL-----EADG-----WLH 401
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1888712850  470 TGDLGFVHD-GQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PRK08008   402 TGDTGYVDEeGFFYFVDRRCNMIKRGGENVSCVELENIIATH 443
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
1177-1662 9.45e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 73.54  E-value: 9.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1177 DMTDAAAPTLA-----TLDLL--DADERARVSAASVAR-RTPPGE-PIHL--RVARHADTQPDAPAVI-----DGALR-M 1239
Cdd:PRK12582     2 PMGSSAAAVLTkppfrPLNWKppDISVERRADGSIVIKsRHPLGPyPRSIphLLAKWAAEAPDRPWLAqrepgHGQWRkV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAG-------GAYVALDAGNptQRLAQTLRDCGAR 1312
Cdd:PRK12582    82 TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGvpaapvsPAYSLMSHDH--AKLKHLFDLVKPR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1313 LVLCEDDC------SALDLMGVQ--HARIDAAQEEAQREQHLRA-------PHALPAVDPRSAAYVIYTSGSSGAPKGVV 1377
Cdd:PRK12582   160 VVFAQSGApfaralAALDLLDVTvvHVTGPGEGIASIAFADLAAtpptaavAAAIAAITPDTVAKYLFTSGSTGMPKAVI 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1378 IAHGALTNYVDAVLARLDPPPRARFAMV-------STIGadlGHTVLFGALASGGALHLIDRDTTldADRFAQTLAAAR- 1449
Cdd:PRK12582   240 NTQRMMCANIAMQEQLRPREPDPPPPVSldwmpwnHTMG---GNANFNGLLWGGGTLYIDDGKPL--PGMFEETIRNLRe 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1450 --IDVLKIVPGHLHALLQAERAADALPA------HTLVLGGEATSWELLDTIAALRpdCRVHNH-------YGPTETTVG 1514
Cdd:PRK12582   315 isPTVYGNVPAGYAMLAEAMEKDDALRRsffknlRLMAYGGATLSDDLYERMQALA--VRTTGHripfytgYGATETAPT 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1515 ILTQPAAQACRAAATLPL-GRPLdnnetwlldeHLNPVGTggTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlY 1593
Cdd:PRK12582   393 TTGTHWDTERVGLIGLPLpGVEL----------KLAPVGD--KYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------Y 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1594 RSGDRAR-----RLADGsLEYLGRIDDQVKI-RGYRVEPGEIaaRLKALDG----VRDAaviVVAG---ARLAAFATPQP 1660
Cdd:PRK12582   455 RLGDAARfvdpdDPEKG-LIFDGRVAEDFKLsTGTWVSVGTL--RPDAVAAcspvIHDA---VVAGqdrAFIGLLAWPNP 528

                   ..
gi 1888712850 1661 GA 1662
Cdd:PRK12582   529 AA 530
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1365-1702 1.06e-12

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 71.93  E-value: 1.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1365 YTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRAR----------FAMVSTIGADLGH--TVLFGAlasggalhlidr 1432
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRlcipvplfhcFGSVLGVLACLTHgaTMVFPS------------ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1433 dTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAH--TLVLGGEATSWELLDTIAALRPDCRVHNHYGPTE 1510
Cdd:cd05917     77 -PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSlrTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1511 TTVGIlTQPAAQACRAAATLPLGRPLDNNETWLLDEHLNPV-GTGGTGELYLGGAGVALGYLHQPALTAARfvphpfAAG 1589
Cdd:cd05917    156 TSPVS-TQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVpPVGVPGELCIRGYSVMKGYWNDPEKTAEA------IDG 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1590 ARLYRSGDRARRLADGSLEYLGRIDDQVkIRG-YRVEPGEIAARLKALDGVRDAAVIVVAGARL----AAFATPQPGASL 1664
Cdd:cd05917    229 DGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERYgeevCAWIRLKEGAEL 307
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1888712850 1665 DAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDR 1702
Cdd:cd05917    308 TEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
28-309 1.42e-12

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 73.01  E-value: 1.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   28 RALAQQRPEATALIVIDADGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVYP 106
Cdd:PRK04319    51 RHADGGRKDKVALRYLDASRKEKYTYKELKELSNKFANVLKELGvEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFE 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  107 ---PESKREqhlaRLRgiarDAGVRYVLTTAALHER----------HadawsMLAPGADVVAVD-TLD----ARDTPSDA 168
Cdd:PRK04319   131 afmEEAVRD----RLE----DSEAKVLITTPALLERkpaddlpslkH-----VLLVGEDVEEGPgTLDfnalMEQASDEF 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  169 PLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVF-----------VSWlplyhdmGLIGSLL 237
Cdd:PRK04319   198 DIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDVYwctadpgwvtgTSY-------GIFAPWL 270
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1888712850  238 QPVFSGIPLVLMSPQyflerplRWLDAIARHRGTI-SGAPDfAYRLCAeRINDETRAKLDLSSWRLAFSGSEP 309
Cdd:PRK04319   271 NGATNVIDGGRFSPE-------RWYRILEDYKVTVwYTAPT-AIRMLM-GAGDDLVKKYDLSSLRHILSVGEP 334
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
1238-1663 1.83e-12

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 72.31  E-value: 1.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1238 RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGnPTQRLA-----------QTL 1306
Cdd:cd05906     39 FQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVP-PTYDEPnarlrklrhiwQLL 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCgarLVLCEDD--CSALDLMGVQHARIDAAQEEAQREQHLRaPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALT 1384
Cdd:cd05906    118 GSP---VVLTDAElvAEFAGLETLSGLPGIRVLSIEELLDTAA-DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNIL 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1385 NYVDAVLARLDPPPRARFamVSTIGAD----LGHTVLFgALASGGA----------------LHLIDR---DTTLdADRF 1441
Cdd:cd05906    194 ARSAGKIQHNGLTPQDVF--LNWVPLDhvggLVELHLR-AVYLGCQqvhvpteeiladplrwLDLIDRyrvTITW-APNF 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1442 AQTLAAARIDVLKIVPGHLHALLQaeraadalpahtLVLGGEA----TSWELLDTIA--ALRPDCrVHNHYGPTETTVGI 1515
Cdd:cd05906    270 AFALLNDLLEEIEDGTWDLSSLRY------------LVNAGEAvvakTIRRLLRLLEpyGLPPDA-IRPAFGMTETCSGV 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1516 ---LTQPAAQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarl 1592
Cdd:cd05906    337 iysRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------ 410
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1888712850 1593 YRSGDRArRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVivvagarlAAFATPQPGAS 1663
Cdd:cd05906    411 FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFT--------AAFAVRDPGAE 472
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
146-593 2.14e-12

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 72.02  E-value: 2.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  146 MLAPGADVVAVDTLDARDTPSDAPLHPVRADDLAFlqYTSGSTGSPKGVMVSH-GNLLANE--IAIQAGLGVRPDDVFVS 222
Cdd:cd05929     97 FTGGGALDGLEDYEAAEGGSPETPIEDEAAGWKML--YSGGTTGRPKGIKRGLpGGPPDNDtlMAAALGFGPGADSVYLS 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  223 WLPLYHDMGLIGSLLQpVFSGIPLVLMspqyflER--PLRWLDAIARHRGT-ISGAPDFAYRLCAerINDETRAKLDLSS 299
Cdd:cd05929    175 PAPLYHAAPFRWSMTA-LFMGGTLVLM------EKfdPEEFLRLIERYRVTfAQFVPTMFVRLLK--LPEAVRNAYDLSS 245
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  300 WRLAFSGSEPVRRDTLDDFVARFAPAgfdaaaLYPCYGLAEATLFVTggVRGAGLVSHAFSsaalsagraeaaradeaat 379
Cdd:cd05929    246 LKRVIHAAAPCPPWVKEQWIDWGGPI------IWEYYGGTEGQGLTI--INGEEWLTHPGS------------------- 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  380 vlVGcGAVQAghrvaivaraaaeshESHEADvetetsRAGERLADGRIGEIHVSGPSvAHGYWQRADASAQAfvdapRHA 459
Cdd:cd05929    299 --VG-RAVLG---------------KVHILD------EDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAA-----RNE 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  460 DGsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFArkgRVIAFGATlggGETLGLALE- 537
Cdd:cd05929    349 GG-----WSTLGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVL---DAAVVGVP---DEELGQRVHa 417
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850  538 -IAPrMKKRFAAAQIVETLRRIAFDACG--ETPAAIALLNpgALPKTSSGKLQRAATRE 593
Cdd:cd05929    418 vVQP-APGADAGTALAEELIAFLRDRLSryKCPRSIEFVA--ELPRDDTGKLYRRLLRD 473
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
31-590 2.51e-12

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 71.43  E-value: 2.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAE-RALILMDSGVDYVSAFFGCLYAGVVAVPV---YP 106
Cdd:cd17645      8 VERTPDHVAVV----DRGQSLTYKQLNEKANQLARHLRGKGVKPDdQVGIMLDKSLDMIAAILGVLKAGGAYVPIdpdYP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  107 PEskreqhlaRLRGIARDAGVRYVLTtaalherhadawsmlapgadvvavdtldardtpsdaplhpvRADDLAFLQYTSG 186
Cdd:cd17645     84 GE--------RIAYMLADSSAKILLT-----------------------------------------NPDDLAYVIYTSG 114
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  187 STGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDmGLIGSLLQPVFSGIPLVLMSPQ--YFLERPLRWLDa 264
Cdd:cd17645    115 STGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFD-ASAWEIFPHLTAGAALHVVPSErrLDLDALNDYFN- 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  265 iaRHRGTISGAPDfayRLCaerindETRAKLDLSSWRLAFSGSepvrrdtldDFVARFAPAGFdaaALYPCYGLAEATLF 344
Cdd:cd17645    193 --QEGITISFLPT---GAA------EQFMQLDNQSLRVLLTGG---------DKLKKIERKGY---KLVNNYGPTENTVV 249
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  345 VTggvrgaglvshafssaalsagraeaaradeaatvlvgcgavqaghrvaivaraAAESHESH------EADVETETSRA 418
Cdd:cd17645    250 AT-----------------------------------------------------SFEIDKPYanipigKPIDNTRVYIL 276
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  419 GERLA---DGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHADgsgpARWLRTGDLG-FVHDGQLYIAGRVKDLVIVR 494
Cdd:cd17645    277 DEALQlqpIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPG----ERMYRTGDLAkFLPDGNIEFLGRLDQQVKIR 352
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  495 GRNLYPQDVEQAVEAHAEFaRKGRVIAfgATLGGGETLGLALEIAPrmkKRFAAAQIVETLRRIAFDACgeTPAAIALLN 574
Cdd:cd17645    353 GYRIEPGEIEPFLMNHPLI-ELAAVLA--KEDADGRKYLVAYVTAP---EEIPHEELREWLKNDLPDYM--IPTYFVHLK 424
                          570
                   ....*....|....*.
gi 1888712850  575 pgALPKTSSGKLQRAA 590
Cdd:cd17645    425 --ALPLTANGKVDRKA 438
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
35-590 3.34e-12

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 71.34  E-value: 3.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   35 PEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVPV---YPPEsk 110
Cdd:cd17650      1 PDAIAVS----DATRQLTYRELNERANQLARTLRGLGVAPGSVVgVCADRSLDAIVGLLAVLKAGGAYVPIdpdYPAE-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  111 reqhlaRLRGIARDAGVRYVLTtaalherhadawsmlapgadvvavdtldardtpsdaplhpvRADDLAFLQYTSGSTGS 190
Cdd:cd17650     75 ------RLQYMLEDSGAKLLLT-----------------------------------------QPEDLAYVIYTSGTTGK 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  191 PKGVMVSHGNLLaneiaiqaglgvrpdDVFVSWLPLYHDMGLIGSLLQ------PVFSGIPL--------VLMSPQYFLE 256
Cdd:cd17650    108 PKGVMVEHRNVA---------------HAAHAWRREYELDSFPVRLLQmasfsfDVFAGDFArsllnggtLVICPDEVKL 172
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  257 RPLRWLDAIARHRGTISGA-PDFAYRLCAERindeTRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFApagfDAAALYPC 335
Cdd:cd17650    173 DPAALYDLILKSRITLMEStPALIRPVMAYV----YRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFG----QGMRIINS 244
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  336 YGLAEATLfvtggvrgaglVSHAFSSAALSAGraeaaradeaatvlvGCGAVQAGHRVAIVARAAAESHESHEADvetet 415
Cdd:cd17650    245 YGVTEATI-----------DSTYYEEGRDPLG---------------DSANVPIGRPLPNTAMYVLDERLQPQPV----- 293
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  416 sragerladGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRhadGSGpARWLRTGDLG-FVHDGQLYIAGRVKDLVIVR 494
Cdd:cd17650    294 ---------GVAGELYIGGAGVARGYLNRPELTAERFVENPF---APG-ERMYRTGDLArWRADGNVELLGRVDHQVKIR 360
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  495 GRNLYPQDVEQAVEAHAEFARKGRVIAFGAtlgGGETlGLALEIAPRMKKRFAA--AQIVETLRRIAFdacgetPAAIAL 572
Cdd:cd17650    361 GFRIELGEIESQLARHPAIDEAVVAVREDK---GGEA-RLCAYVVAAATLNTAElrAFLAKELPSYMI------PSYYVQ 430
                          570
                   ....*....|....*...
gi 1888712850  573 LNpgALPKTSSGKLQRAA 590
Cdd:cd17650    431 LD--ALPLTPNGKVDRRA 446
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
12-237 3.63e-12

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 71.83  E-value: 3.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   12 GIDTDAVPAHGLAARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAArfardgAAAERAL-------ILMDSG 84
Cdd:PRK08279    28 TALITPDSKRSLGDVFEEAAARHPDRPALL----FEDQSISYAELNARANRYAH------WAAARGVgkgdvvaLLMENR 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   85 VDYVSAFFGCLYAGVVAVPV-YPPESKREQH---LARLRGIARDAGVRYVLTTAALH-ERHADAWSM-LAPGADVVAVDT 158
Cdd:PRK08279    98 PEYLAAWLGLAKLGAVVALLnTQQRGAVLAHslnLVDAKHLIVGEELVEAFEEARADlARPPRLWVAgGDTLDDPEGYED 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  159 LD--ARDTPSDAPLH--PVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLI- 233
Cdd:PRK08279   178 LAaaAAGAPTTNPASrsGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTv 257

                   ....*.
gi 1888712850  234 --GSLL 237
Cdd:PRK08279   258 awSSVL 263
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
179-593 4.52e-12

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 71.12  E-value: 4.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  179 AFLQYTSGSTGSPKGVMVSHGNLLANEIAIQA--GLGVRPDDVFVSWLPLYHDMGLiGSLLQPVFSGIPLVLmsPQYFLE 256
Cdd:cd12119    166 AAICYTSGTTGNPKGVVYSHRSLVLHAMAALLtdGLGLSESDVVLPVVPMFHVNAW-GLPYAAAMVGAKLVL--PGPYLD 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  257 rPLRWLDAIARHRGTIS-GAPDFAYRLCAERindeTRAKLDLSS-WRLAFSGSEPVRrdtldDFVARFAPAGFDaaaLYP 334
Cdd:cd12119    243 -PASLAELIEREGVTFAaGVPTVWQGLLDHL----EANGRDLSSlRRVVIGGSAVPR-----SLIEAFEERGVR---VIH 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  335 CYGLAEATLFVTGGVRGAGLVshafssaalsagraeAARADEAATVLVGCGAVQAGhrvaivaraaaeshesheadVETE 414
Cdd:cd12119    310 AWGMTETSPLGTVARPPSEHS---------------NLSEDEQLALRAKQGRPVPG--------------------VELR 354
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  415 TSR-AGERL-ADGR-IGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFVH-DGQLYIAGRVKDL 490
Cdd:cd12119    355 IVDdDGRELpWDGKaVGELQVRGPWVTKSYYKNDEESEALTEDG-----------WLRTGDVATIDeDGYLTITDRSKDV 423
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  491 VIVRGRNLYPQDVEQAVEAH---AEFARKG--------RVIAFgATLGGGETLGlALEIAPRMKKRFAAAQIvetlrria 559
Cdd:cd12119    424 IKSGGEWISSVELENAIMAHpavAEAAVIGvphpkwgeRPLAV-VVLKEGATVT-AEELLEFLADKVAKWWL-------- 493
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1888712850  560 fdacgetPAAIALLNpgALPKTSSGKLQRAATRE 593
Cdd:cd12119    494 -------PDDVVFVD--EIPKTSTGKIDKKALRE 518
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
157-510 4.83e-12

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 71.16  E-value: 4.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  157 DTLDARDTPSDAPLHP-VRADDLAFLQYTSGSTGSPKGVMVSHGNLLANeiAIQAGLGVRPDDV----FVSWLPLYHDMG 231
Cdd:PLN02330   164 ELLEAADRAGDTSDNEeILQTDLCALPFSSGTTGISKGVMLTHRNLVAN--LCSSLFSVGPEMIgqvvTLGLIPFFHIYG 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  232 LIGSLLQPVFSGIPLVLMSpQYFLErplRWLDAIARHRGTISG-APDFAYRLCAERINDEtrakLDLSSWRL--AFSGSE 308
Cdd:PLN02330   242 ITGICCATLRNKGKVVVMS-RFELR---TFLNALITQEVSFAPiVPPIILNLVKNPIVEE----FDLSKLKLqaIMTAAA 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  309 PVRRDTLDDFVARFAPAGFDAAalypcYGLAEATLFVtggvrgaglVSHafssaalsagraeaaradeaatvlvgcGAVQ 388
Cdd:PLN02330   314 PLAPELLTAFEAKFPGVQVQEA-----YGLTEHSCIT---------LTH---------------------------GDPE 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  389 AGHRVAIVARA--AAESHESHEADVETetsraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAfVDaprhADGsgpar 466
Cdd:PLN02330   353 KGHGIAKKNSVgfILPNLEVKFIDPDT-----GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRT-ID----EDG----- 417
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1888712850  467 WLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PLN02330   418 WLHTGDIGYIdDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTH 462
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
1363-1702 5.32e-12

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 69.61  E-value: 5.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1363 VIYTSGSSGAPKGVVIAHGAL--TNYVDAVLARLDPpprarfAMVSTIGADLGH-TVLFGALAS---GGALHLIDRdttL 1436
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNLiaANLQLIHAMGLTE------ADVYLNMLPLFHiAGLNLALATfhaGGANVVMEK---F 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1437 DADRFAQTLAAARIDVLKIVPGHLHALLQAERAADA-LPAHTLVLGGEATswellDTIAALRPDC--RVHNHYGPTETTV 1513
Cdd:cd17637     76 DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVdLSSLRHVLGLDAP-----ETIQRFEETTgaTFWSLYGQTETSG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1514 GILTQPAAQACRAAatlplGRPLDNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAarfvpHPFAAGarLY 1593
Cdd:cd17637    151 LVTLSPYRERPGSA-----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTA-----YTFRNG--WH 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1594 RSGDRARRLADGSLEYLGRI--DDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAA 1667
Cdd:cd17637    219 HTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPdpkwGEGIKAVCVLKPGATLTAD 298
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1888712850 1668 ALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDR 1702
Cdd:cd17637    299 ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
1221-1377 8.69e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 70.11  E-value: 8.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1221 RHADTQPDAPAVIDGALR--MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNP 1298
Cdd:PRK13391     5 IHAQTTPDKPAVIMASTGevVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1299 TQRLAQTLRDCGARLVLCE----DDCSAL--DLMGVQH---ARIDAAQEEAQR-EQHLRAPHALPAVDPRSAAYVIYTSG 1368
Cdd:PRK13391    85 PAEAAYIVDDSGARALITSaaklDVARALlkQCPGVRHrlvLDGDGELEGFVGyAEAVAGLPATPIADESLGTDMLYSSG 164

                   ....*....
gi 1888712850 1369 SSGAPKGVV 1377
Cdd:PRK13391   165 TTGRPKGIK 173
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
26-487 8.84e-12

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 70.31  E-value: 8.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   26 RLRALAQQRPEATALIVIDadgdTRYDYAQLDRRAralaarfarDGAAA--------ERALILMDSGVDY--VSAFFGCL 95
Cdd:PRK04813     7 TIEEFAQTQPDFPAYDYLG----EKLTYGQLKEDS---------DALAAfidslklpDKSPIIVFGHMSPemLATFLGAV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   96 YAGVVAVPVyppeskrEQHLA--RLRGIARDAGVRYVLTTAALHERHADAwsmlaPGADVVAVDTLDARDTPSDaPLHPV 173
Cdd:PRK04813    74 KAGHAYIPV-------DVSSPaeRIEMIIEVAKPSLIIATEELPLEILGI-----PVITLDELKDIFATGNPYD-FDHAV 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  174 RADDLAFLQYTSGSTGSPKGVMVSHGNLLAneiaiqaglgvrpddvFVSWlpLYHDMGLIGS---LLQPVFSgIPLVLMS 250
Cdd:PRK04813   141 KGDDNYYIIFTSGTTGKPKGVQISHDNLVS----------------FTNW--MLEDFALPEGpqfLNQAPYS-FDLSVMD 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  251 pqyflerplrWLDAIArhrgtiSGAPDFAyrLCAERIND-----ETRAKLDLSSW------------------------- 300
Cdd:PRK04813   202 ----------LYPTLA------SGGTLVA--LPKDMTANfkqlfETLPQLPINVWvstpsfadmclldpsfneehlpnlt 263
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  301 RLAFSGSE-PVRrdTLDDFVARFaPagfdAAALYPCYGLAEATLFVTGgvrgaglvshafssaalsagraeaarADEAAT 379
Cdd:PRK04813   264 HFLFCGEElPHK--TAKKLLERF-P----SATIYNTYGPTEATVAVTS--------------------------IEITDE 310
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  380 VLVGCGAVQAGHRvaivaraaaesheshEADVETET-SRAGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDaprh 458
Cdd:PRK04813   311 MLDQYKRLPIGYA---------------KPDSPLLIiDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---- 371
                          490       500
                   ....*....|....*....|....*....
gi 1888712850  459 ADGSgpaRWLRTGDLGFVHDGQLYIAGRV 487
Cdd:PRK04813   372 FDGQ---PAYHTGDAGYLEDGLLFYQGRI 397
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
1362-1702 9.55e-12

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 68.59  E-value: 9.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1362 YVIYTSGSSGAPKG------------VVIAHGALTNYVDAVLArldPPPrarfamvstigadLGHTV-LFG---ALASGG 1425
Cdd:cd17633      4 YIGFTSGTTGLPKAyyrserswiesfVCNEDLFNISGEDAILA---PGP-------------LSHSLfLYGaisALYLGG 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1426 ALHLidrDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAAdaLPAHTLVLGGEATSWELLDTIAALRPDCRVHNH 1505
Cdd:cd17633     68 TFIG---QRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE--SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEF 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1506 YGPTETTvgILTqpAAQACRAAATLPLGRPLDNNETWLLDEhlnpvGTGGTGELYLGGAGVALGYLHQPALTAARFvphp 1585
Cdd:cd17633    143 YGTSELS--FIT--YNFNQESRPPNSVGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNPDGW---- 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1586 faagarlYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGARLAAFATP-QPGASL 1664
Cdd:cd17633    210 -------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVAlYSGDKL 282
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1888712850 1665 DAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDR 1702
Cdd:cd17633    283 TYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
23-512 9.78e-12

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 70.05  E-value: 9.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVA 101
Cdd:cd05920     17 LGDLLARSAARHPDRIAVV----DGDRRLTYRELDRRADRLAAGLRGLGiRPGDRVVVQLPNVAEFVVLFFALLRLGAVP 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  102 VPVYPPESKREqhlarLRGIARDAGVryvlTTAALHERHAdawsmlapGADVVAvdtlDARDTPSDAPlhpvradDLAFL 181
Cdd:cd05920     93 VLALPSHRRSE-----LSAFCAHAEA----VAYIVPDRHA--------GFDHRA----LARELAESIP-------EVALF 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  182 QYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDM-----GLIGSLLqpvFSGIPLVLMSPqyfle 256
Cdd:cd05920    145 LLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFplacpGVLGTLL---AGGRVVLAPDP----- 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  257 RPLRWLDAIARHRGTISGA-PDFAYRLCAERIndetRAKLDLSSWRLAFSGSEPvrrdtLDDFVARFAPAGFDaAALYPC 335
Cdd:cd05920    217 SPDAAFPLIEREGVTVTALvPALVSLWLDAAA----SRRADLSSLRLLQVGGAR-----LSPALARRVPPVLG-CTLQQV 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  336 YGLAEatlfvtggvrgaGLVSHafssaalsagraeaaradeaaTVLVGCGAVQAGHRVAIVARAAaeshESHEADVEtet 415
Cdd:cd05920    287 FGMAE------------GLLNY---------------------TRLDDPDEVIIHTQGRPMSPDD----EIRVVDEE--- 326
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  416 sraGERLADGRIGEIHVSGPSVAHGYWQRADASAQAFVdaprhADGsgparWLRTGDLGFVH-DGQLYIAGRVKDLVIVR 494
Cdd:cd05920    327 ---GNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFT-----PDG-----FYRTGDLVRRTpDGYLVVEGRIKDQINRG 393
                          490
                   ....*....|....*...
gi 1888712850  495 GRNLYPQDVEQAVEAHAE 512
Cdd:cd05920    394 GEKIAAEEVENLLLRHPA 411
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
31-592 1.05e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 70.04  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIVidADGDTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPV----Y 105
Cdd:PRK13390     7 AQIAPDRPAVIV--AETGEQVSYRQLDDDSAALARVLYDAGlRTGDVVALLSDNSPEALVVLWAALRSGLYITAInhhlT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  106 PPESKReqhlarlrgIARDAGVRYVLTTAALH----ERHADAWSMLAPGADVVAVDTLDARDTPSDAPL--HPVRAddla 179
Cdd:PRK13390    85 APEADY---------IVGDSGARVLVASAALDglaaKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLteQPCGA---- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  180 FLQYTSGSTGSPKGVMVSHGNLLANE-----IAIQAGL-GVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIplVLMSPQY 253
Cdd:PRK13390   152 VMLYSSGTTGFPKGIQPDLPGRDVDApgdpiVAIARAFyDISESDIYYSSAPIYHAAPLRWCSMVHALGGT--VVLAKRF 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  254 FLERPLRWldaIARHRGTISG-APDFAYRLCaeRINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAAAL 332
Cdd:PRK13390   230 DAQATLGH---VERYRITVTQmVPTMFVRLL--KLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSS 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  333 YPCYGLaeaTLFVTGGvrgagLVSHAFSSAALSAGRAeaaradeaatvlvgcgavqaghrvaivaraaaeshesHEADVE 412
Cdd:PRK13390   305 TEAHGM---TFIDSPD-----WLAHPGSVGRSVLGDL-------------------------------------HICDDD 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  413 tetsraGERLADGRIGEIhvsgpsvahgYWQRaDASAQAFVDAP-RHADGSGPAR--WLRTGDLGFV-HDGQLYIAGRVK 488
Cdd:PRK13390   340 ------GNELPAGRIGTV----------YFER-DRLPFRYLNDPeKTAAAQHPAHpfWTTVGDLGSVdEDGYLYLADRKS 402
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  489 DLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFdacGETPA 568
Cdd:PRK13390   403 FMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAH---YKAPR 479
                          570       580
                   ....*....|....*....|....
gi 1888712850  569 AIALLNpgALPKTSSGKLQRAATR 592
Cdd:PRK13390   480 SVEFVD--ELPRTPTGKLVKGLLR 501
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
1722-1814 1.15e-11

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 62.56  E-value: 1.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1722 APQGETETALAQCWAALLDpsngtdnatdnataTPSLTIARDDSFFA-LGGHSLAAMRLASRVRSRWSVELPLREIFASP 1800
Cdd:COG0236      1 MPREELEERLAEIIAEVLG--------------VDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYP 66
                           90
                   ....*....|....
gi 1888712850 1801 TLAALAARIEAQRA 1814
Cdd:COG0236     67 TVADLADYLEEKLA 80
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
1223-1648 1.51e-11

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 69.13  E-value: 1.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1223 ADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRL 1302
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1303 AQTLRDCGARLVLCEDDCSALDLMGVQHARIDAAQEEAqreqhlraphalpAVDPRSAAYVIYTSGSSGAPKGVVIAHGA 1382
Cdd:PRK09029    93 EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAV-------------AWQPQRLATMTLTSGSTGLPKAAVHTAQA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1383 -LTNyVDAVLARLDPPPRARFAM------VStigadlGHTVLFGALASGGALHLidrdttldadRFAQTLAAARIDV--L 1453
Cdd:PRK09029   160 hLAS-AEGVLSLMPFTAQDSWLLslplfhVS------GQGIVWRWLYAGATLVV----------RDKQPLEQALAGCthA 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1454 KIVPGHLHALLQAERAADALPAhtLVLGGEATSWELldTIAALRPDCRVHNHYGPTE--TTV---------GIltqpaaq 1522
Cdd:PRK09029   223 SLVPTQLWRLLDNRSEPLSLKA--VLLGGAAIPVEL--TEQAEQQGIRCWCGYGLTEmaSTVcakradglaGV------- 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1523 acraaatlplGRPLDNNETWLLDehlnpvgtggtGELYLGGAGVALGYLHQPALTaarfvphPFAAGARLYRSGDRArRL 1602
Cdd:PRK09029   292 ----------GSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRG-EW 342
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1888712850 1603 ADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA 1648
Cdd:PRK09029   343 QNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVA 388
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
1228-1709 2.20e-11

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 69.08  E-value: 2.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1228 DAPAVIDGALRMSYAELDARAAHVAQWLLAR-DLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTL 1306
Cdd:PRK12492    39 DRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQF 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1307 RDCGARLVLceddcsALDLMG--VQHARIDAAQE---EAQREQHLRA------------------PHALP-AVDPRSA-- 1360
Cdd:PRK12492   119 KDSGARALV------YLNMFGklVQEVLPDTGIEyliEAKMGDLLPAakgwlvntvvdkvkkmvpAYHLPqAVPFKQAlr 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1361 -----------------AYVIYTSGSSGAPKGVVIAHGALT---NYVDAVLARLDPPPRARF-----AMVSTIgaDLGHT 1415
Cdd:PRK12492   193 qgrglslkpvpvglddiAVLQYTGGTTGLAKGAMLTHGNLVanmLQVRACLSQLGPDGQPLMkegqeVMIAPL--PLYHI 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1416 VLFGA-----LASGGALHLID--RD-----TTLDADRFA-----QTLAAARIDVLKIVPGHLHALLQAERAADALPAHTl 1478
Cdd:PRK12492   271 YAFTAncmcmMVSGNHNVLITnpRDipgfiKELGKWRFSallglNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKAT- 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1479 vlggeATSWELLDtiaalrpDCRVHNHYGPTETTVGILTQPAAQACRAAAtlpLGRPLDNNETWLLDEHLNPVGTGGTGE 1558
Cdd:PRK12492   350 -----AERWEQLT-------GCTIVEGYGLTETSPVASTNPYGELARLGT---VGIPVPGTALKVIDDDGNELPLGERGE 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1559 LYLGGAGVALGYLHQPALTAARFVphpfAAGarLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDG 1638
Cdd:PRK12492   415 LCIKGPQVMKGYWQQPEATAEALD----AEG--WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPK 488
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1888712850 1639 VRDAAVIVV----AGARLAAFATPQ-PGASLDAAALKRALAALLpdYMVPSVLRVIDALPLNRNGKLDRQALSALA 1709
Cdd:PRK12492   489 VANCAAIGVpderSGEAVKLFVVARdPGLSVEELKAYCKENFTG--YKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
27-231 2.21e-11

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 69.00  E-value: 2.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   27 LRALAQQRPEATALIVIDADGD-TRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVPV 104
Cdd:cd05921      1 LAHWARQAPDRTWLAEREGNGGwRRVTYAEALRQVRAIAQGLLDLGLSAERPLlILSGNSIEHALMALAAMYAGVPAAPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  105 YPPESKREQHLARLRGI----------ARDA-------------GVRYVLTTAALHERHADAWSMLAPGADVVAVDTLDA 161
Cdd:cd05921     81 SPAYSLMSQDLAKLKHLfellkpglvfAQDAapfaralaaifplGTPLVVSRNAVAGRGAISFAELAATPPTAAVDAAFA 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850  162 RDTPsdaplhpvraDDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDD--VFVSWLPLYHDMG 231
Cdd:cd05921    161 AVGP----------DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFG 222
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
1239-1618 2.80e-11

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 68.40  E-value: 2.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1239 MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAG----GAYVAL--DAgnptqrLAQTLRDCGAR 1312
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNipivTVYATLgeDA------LIHSLNETECS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1313 LVLCEDDCSALdlmgvqharidaaqeeaqreqhlraphalpavdprsaAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLA 1392
Cdd:cd17639     80 AIFTDGKPDDL-------------------------------------ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGD 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1393 RLDPPPRARFAMVSTIgaDLGH----TVLFGALASGGAL------HLID---RDTTLDADRFAQTLAAA--------RID 1451
Cdd:cd17639    123 RVPELLGPDDRYLAYL--PLAHifelAAENVCLYRGGTIgygsprTLTDkskRGCKGDLTEFKPTLMVGvpaiwdtiRKG 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1452 VLKIVP--GHL------HALLQAERAADALPAHTL-----------VLGGEATSweLLDTIAALRPD---------CRVH 1503
Cdd:cd17639    201 VLAKLNpmGGLkrtlfwTAYQSKLKALKEGPGTPLldelvfkkvraALGGRLRY--MLSGGAPLSADtqeflnivlCPVI 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1504 NHYGPTETT-VGILTQPAAQACRAaatlpLGRPLDNNETWLLD-EHLNPVGTGGT--GELYLGGAGVALGYLHQPALTAA 1579
Cdd:cd17639    279 QGYGLTETCaGGTVQDPGDLETGR-----VGPPLPCCEIKLVDwEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKE 353
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1888712850 1580 RFvphpfaAGARLYRSGDRARRLADGSLEYLGRIDDQVK 1618
Cdd:cd17639    354 AF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVK 386
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
162-228 3.16e-11

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 68.99  E-value: 3.16e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  162 RDTPSDAPLhPvRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQA---GLGvrPDDVFVSWLPLYH 228
Cdd:PLN02387   238 KENPVDPDL-P-SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTvvpKLG--KNDVYLAYLPLAH 303
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
1228-1707 3.23e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 68.51  E-value: 3.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1228 DAPAVIDGALRMSYAE-LDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALdagNPTQR---LA 1303
Cdd:PRK13388    16 DTIAVRYGDRTWTWREvLAEAAARAAALIALADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGL---NTTRRgaaLA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1304 QTLRDCGARLVLCEDD----CSALDLMGVQHARIDAAqEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIA 1379
Cdd:PRK13388    93 ADIRRADCQLLVTDAEhrplLDGLDLPGVRVLDVDTP-AYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCS 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1380 HGALTNYVDAVLARLDPPPRArfamVSTIGADLGHT--VLFG---ALASGGALHLIDRdttLDADRFAQTLAAARIDVLK 1454
Cdd:PRK13388   172 HGRLAFAGRALTERFGLTRDD----VCYVSMPLFHSnaVMAGwapAVASGAAVALPAK---FSASGFLDDVRRYGATYFN 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1455 IVPGHLHALL-QAERAADALPAHTLVLGGEATSwellDTIAAL--RPDCRVHNHYGPTETTVGILTQPAAQACRaaatlp 1531
Cdd:PRK13388   245 YVGKPLAYILaTPERPDDADNPLRVAFGNEASP----RDIAEFsrRFGCQVEDGYGSSEGAVIVVREPGTPPGS------ 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1532 LGRPLD-----NNETW------LLDEH---LNPvgTGGTGELY-LGGAGVALGYLHQPALTAARFvphpfAAGarLYRSG 1596
Cdd:PRK13388   315 IGRGAPgvaiyNPETLtecavaRFDAHgalLNA--DEAIGELVnTAGAGFFEGYYNNPEATAERM-----RHG--MYWSG 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1597 DRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQPGASlDAAALKRA 1672
Cdd:PRK13388   386 DLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVpderVGDQVMAALVLRDGAT-FDPDAFAA 464
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1888712850 1673 LAALLPDY---MVPSVLRVIDALPLNRNGKLDRQALSA 1707
Cdd:PRK13388   465 FLAAQPDLgtkAWPRYVRIAADLPSTATNKVLKRELIA 502
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
23-231 3.94e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 68.53  E-value: 3.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   23 LAARLRALAQQRPEATALIVIDADGD--TRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGV 99
Cdd:PRK12582    51 IPHLLAKWAAEAPDRPWLAQREPGHGqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVmILSGNSIEHALMTLAAMQAGV 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  100 VAVPVYPPESKREQHLARLRGIARDAGVRYVLT------TAALHERHADAWSMLAPGADVVAVDTLDARDTPSDAPLHPV 173
Cdd:PRK12582   131 PAAPVSPAYSLMSHDHAKLKHLFDLVKPRVVFAqsgapfARALAALDLLDVTVVHVTGPGEGIASIAFADLAATPPTAAV 210
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1888712850  174 RA-------DDLAFLQYTSGSTGSPKGVMVSHGNLLANeiaIQAGLGVRPDD------VFVSWLPLYHDMG 231
Cdd:PRK12582   211 AAaiaaitpDTVAKYLFTSGSTGMPKAVINTQRMMCAN---IAMQEQLRPREpdppppVSLDWMPWNHTMG 278
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
738-1009 4.89e-11

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 67.46  E-value: 4.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  738 LFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGdaahLYAP-----RTeaaAPLAWAHVDL 812
Cdd:cd19544     12 LFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEG----LSEPvqvvwRQ---AELPVEELTL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  813 SDLGDIDEhdrerALRECAQRfADAPFDLLRGPLLRAGLVR-MSDERHVLMLALHHIATDGWSMQLLVEELvdgyRAALD 891
Cdd:cd19544     85 DPGDDALA-----QLRARFDP-RRYRLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEI----QAILA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  892 GattHGEAQAKAktrITYADYAAwqrRWLASDAAARQLAYWRAALAD-DAPplALPYDHTATdtaseNADPRAAARVAFA 970
Cdd:cd19544    155 G---RAAALPPP---VPYRNFVA---QARLGASQAEHEAFFREMLGDvDEP--TAPFGLLDV-----QGDGSDITEARLA 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1888712850  971 LPAPLAQAVRASAARHRATPFVVLlaayH-AW---LYRVTGQR 1009
Cdd:cd19544    219 LDAELAQRLRAQARRLGVSPASLF----HlAWalvLARCSGRD 257
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
72-592 6.23e-11

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 67.75  E-value: 6.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   72 AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPESKREQHLARlrgiaRDAGVRYVLTTAALHERhadawsmLAPGA 151
Cdd:PRK06060    53 SSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAA-----RNTEPALVVTSDALRDR-------FQPSR 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  152 DVVAVDTLD--ARDTPSDapLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLA-NEIAIQAGLGVRPDDVFVSWLPLYH 228
Cdd:PRK06060   121 VAEAAELMSeaARVAPGG--YEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTfVDAMCRKALRLTPEDTGLCSARMYF 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  229 DMGLIGSLLQPVFSGIPLVLMSPQYFLErplrwLDAIARHR---GTISGAPDFAYRLCAERINDETRakldlsSWRLAFS 305
Cdd:PRK06060   199 AYGLGNSVWFPLATGGSAVINSAPVTPE-----AAAILSARfgpSVLYGVPNFFARVIDSCSPDSFR------SLRCVVS 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  306 GSEpvrrdtlddfvarfapagfdaaALYPcyGLAEATLFVTGGVrgaglvshafssaalsagraeaaradeaaTVLVGCG 385
Cdd:PRK06060   268 AGE----------------------ALEL--GLAERLMEFFGGI-----------------------------PILDGIG 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  386 AVQAGHRVAIVAR------AAAESHESHEADVeteTSRAGERLADGRIGEIHVSGPSVAHGYWQRADasaqafvdaPRHA 459
Cdd:PRK06060   295 STEVGQTFVSNRVdewrlgTLGRVLPPYEIRV---VAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVA 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  460 DGSgparWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQDVEQAV---EAHAEFARKGRVIAFGATLgggetlgLA 535
Cdd:PRK06060   363 NEG----WLDTRDRVCIDsDGWVTYRCRADDTEVIGGVNVDPREVERLIiedEAVAEAAVVAVRESTGAST-------LQ 431
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850  536 LEIAPRMKKRFAAAQIVETLRRI-----AFdacgETPAAIALLNpgALPKTSSGKLQRAATR 592
Cdd:PRK06060   432 AFLVATSGATIDGSVMRDLHRGLlnrlsAF----KVPHRFAVVD--RLPRTPNGKLVRGALR 487
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
172-243 7.81e-11

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 67.43  E-value: 7.81e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850  172 PVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSG 243
Cdd:PRK08043   361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTG 432
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
1212-1705 8.50e-11

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 67.17  E-value: 8.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1212 GEPIHLRVARHADTqPDAPAVIDG--ALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGA 1289
Cdd:cd17642     17 GEQLHKAMKRYASV-PGTIAFTDAhtGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVG 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1290 YVALDAGNPTQRLAQTLRDCGARLVLCEDDC---------------------SALDLMGVQharidaaQEEAQREQHLRA 1348
Cdd:cd17642     96 VAPTNDIYNERELDHSLNISKPTIVFCSKKGlqkvlnvqkklkiiktiiildSKEDYKGYQ-------CLYTFITQNLPP 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1349 PHALPAVDPRSA------AYVIYTSGSSGAPKGVVIAHgaltnyvDAVLARLD----------PPPRARFAMVSTIGADL 1412
Cdd:cd17642    169 GFNEYDFKPPSFdrdeqvALIMNSSGSTGLPKGVQLTH-------KNIVARFShardpifgnqIIPDTAILTVIPFHHGF 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1413 GHTVLFGALASGGALHLIdrdTTLDADRFAQTLAAARIDVLKIVPGHL-----HALLQAeraADALPAHTLVLGGEATSW 1487
Cdd:cd17642    242 GMFTTLGYLICGFRVVLM---YKFEEELFLRSLQDYKVQSALLVPTLFaffakSTLVDK---YDLSNLHEIASGGAPLSK 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1488 ELLDTIAALRPDCRVHNHYGPTETTVGILTQPAAQAC--RAAATLPL--GRPLDNNETWLLdehlnpvGTGGTGELYLGG 1563
Cdd:cd17642    316 EVGEAVAKRFKLPGIRQGYGLTETTSAILITPEGDDKpgAVGKVVPFfyAKVVDLDTGKTL-------GPNERGELCVKG 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1564 AGVALGYLHQPALTAARFVPHPFaagarlYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAA 1643
Cdd:cd17642    389 PMIMKGYVNNPEATKALIDKDGW------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAG 462
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850 1644 VIVV----AGARLAAFATPQPGASLDAAALKralaallpDYMVPSV---------LRVIDALPLNRNGKLDRQAL 1705
Cdd:cd17642    463 VAGIpdedAGELPAAVVVLEAGKTMTEKEVM--------DYVASQVstakrlrggVKFVDEVPKGLTGKIDRRKI 529
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
1234-1656 9.59e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 66.94  E-value: 9.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1234 DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLA----QTLRDC 1309
Cdd:PRK07768    25 DAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAvwaeDTLRVI 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1310 ---GARLVLC----EDDCSALDLMGVQHARIDAAQEEAqreqhlraPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGA 1382
Cdd:PRK07768   105 gmiGAKAVVVgepfLAAAPVLEEKGIRVLTVADLLAAD--------PIDPVETGEDDLALMQLTSGSTGSPKAVQITHGN 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1383 LTNYVDA--VLARLDPpprARFAMVS------------------TIGAD---------LGHTVLFGALASGgalhliDRD 1433
Cdd:PRK07768   177 LYANAEAmfVAAEFDV---ETDVMVSwlplfhdmgmvgfltvpmYFGAElvkvtpmdfLRDPLLWAELISK------YRG 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1434 TTLDADRFAQTLAAARIDVlkivpghlhallQAERAADALPAHTLVL-GGEATSWELLDTIAA------LRPDCrVHNHY 1506
Cdd:PRK07768   248 TMTAAPNFAYALLARRLRR------------QAKPGAFDLSSLRFALnGAEPIDPADVEDLLDagarfgLRPEA-ILPAY 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1507 GPTETTVGILTQPA----------------------AQACRAAATLPLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGA 1564
Cdd:PRK07768   315 GMAEATLAVSFSPCgaglvvdevdadllaalrravpATKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGE 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1565 GVALGYlhqpaLTAARFVPHPFAAGarLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRD--- 1641
Cdd:PRK07768   395 SVTPGY-----LTMDGFIPAQDADG--WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPgna 467
                          490
                   ....*....|....*
gi 1888712850 1642 AAVIVVAGARLAAFA 1656
Cdd:PRK07768   468 VAVRLDAGHSREGFA 482
PRK07867 PRK07867
acyl-CoA synthetase; Validated
79-515 1.20e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 66.63  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   79 ILMDSGVDYVSAFFGCLYAGVVAVPVYPpeSKREQHLARlrGIARdAGVRYVLTTAAlherHADAWSMLAPGADVVAVDT 158
Cdd:PRK07867    59 VLLDNTPEFSLLLGAAALSGIVPVGLNP--TRRGAALAR--DIAH-ADCQLVLTESA----HAELLDGLDPGVRVINVDS 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  159 L---DARDTPSDAPLHP--VRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLI 233
Cdd:PRK07867   130 PawaDELAAHRDAEPPFrvADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVM 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  234 GSLLQPVFSGIPLVLmsPQYFleRPLRWLDAIARHRGTIS---GAPdFAYRLCAERINDETRAKLdlsswRLAFsGSEPV 310
Cdd:PRK07867   210 AGWAVALAAGASIAL--RRKF--SASGFLPDVRRYGATYAnyvGKP-LSYVLATPERPDDADNPL-----RIVY-GNEGA 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  311 RRDtLDDFVARFAPAGFDAaalypcYGLAEatlfvtGGVrgagLVSHAFSSAALSAGraeaaradeaatVLVGCGAVqag 390
Cdd:PRK07867   279 PGD-IARFARRFGCVVVDG------FGSTE------GGV----AITRTPDTPPGALG------------PLPPGVAI--- 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  391 hrvaivaraaaeshesheADVET-------ETSRAGERLADGRIGE-IHVSGPSVAHGYWQRADAsaqafvDAPRHADGs 462
Cdd:PRK07867   327 ------------------VDPDTgtecppaEDADGRLLNADEAIGElVNTAGPGGFEGYYNDPEA------DAERMRGG- 381
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1888712850  463 gparWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFAR 515
Cdd:PRK07867   382 ----VYWSGDLAYRDaDGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATE 431
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
79-495 1.32e-10

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 66.30  E-value: 1.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   79 ILMDSGVDYVSAFFGCLYAGVVAVPV---YPPEskreqhlaRLRGIARDAGVRYVLTtaalherhadawsmlapgadvva 155
Cdd:cd17644     55 ICVERSLEMIIGLLAILKAGGAYVPLdpnYPQE--------RLTYILEDAQISVLLT----------------------- 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  156 vdtldardtpsdaplhpvRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGlIGS 235
Cdd:cd17644    104 ------------------QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVA-AEE 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  236 LLQPVFSGIPLVLMsPQYFLERPLRWLDAIARHRGTISGAPDFAYRLCaerINDETRAKLDL-SSWRLAFSGSEPVrrdt 314
Cdd:cd17644    165 IYVTLLSGATLVLR-PEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLL---VLELLLSTIDLpSSLRLVIVGGEAV---- 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  315 LDDFVARFAPAGFDAAALYPCYGLAEATLFVTggvrgaglVSHafssaalsagrAEAARADEAATVLVG--CGAVQAghr 392
Cdd:cd17644    237 QPELVRQWQKNVGNFIQLINVYGPTEATIAAT--------VCR-----------LTQLTERNITSVPIGrpIANTQV--- 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  393 vaivaraaaeshesHEADVETETsragerLADGRIGEIHVSGPSVAHGYWQRADASAQAFVDAPRHadGSGPARWLRTGD 472
Cdd:cd17644    295 --------------YILDENLQP------VPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFN--SSESERLYKTGD 352
                          410       420
                   ....*....|....*....|....
gi 1888712850  473 LG-FVHDGQLYIAGRVKDLVIVRG 495
Cdd:cd17644    353 LArYLPDGNIEYLGRIDNQVKIRG 376
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
143-491 1.45e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 66.54  E-value: 1.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  143 AWSmlapgaDVVAvdtlDARDTPSDAPLH-PVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGL-----GVRP 216
Cdd:PTZ00216   240 AWT------DVVA----KGHSAGSHHPLNiPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLndligPPEE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  217 DDVFVSWLPLYHDMGL-IGSLLqpVFSGIPLVLMSPqyfleRPLrwLDAIARHRGtisgapdfayrlcaerindetrakl 295
Cdd:PTZ00216   310 DETYCSYLPLAHIMEFgVTNIF--LARGALIGFGSP-----RTL--TDTFARPHG------------------------- 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  296 DLSSWRLAFSGSEPVRRDTLDDFV-ARFAPAG------FDAA------ALY-----PCY-----GLAEATLfvTGGVRga 352
Cdd:PTZ00216   356 DLTEFRPVFLIGVPRIFDTIKKAVeAKLPPVGslkrrvFDHAyqsrlrALKegkdtPYWnekvfSAPRAVL--GGRVR-- 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  353 glvshafssAALSAGRAEAARADEAATVL-------------VGCGAVQ-AGHRVAIVARAAAESHESHEADVE----TE 414
Cdd:PTZ00216   432 ---------AMLSGGGPLSAATQEFVNVVfgmviqgwgltetVCCGGIQrTGDLEPNAVGQLLKGVEMKLLDTEeykhTD 502
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1888712850  415 TsragerlADGRiGEIHVSGPSVAHGYWQRADASAQAFvdaprHADGsgparWLRTGDLG-FVHDGQLYIAGRVKDLV 491
Cdd:PTZ00216   503 T-------PEPR-GEILLRGPFLFKGYYKQEELTREVL-----DEDG-----WFHTGDVGsIAANGTLRIIGRVKALA 562
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1219-1647 1.72e-10

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 66.05  E-value: 1.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTqpdaPAVIDGALRMSYAELDARAAHVAQWLLAR-DLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGN 1297
Cdd:PRK08751    35 VAKFADR----PAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLY 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 PTQRLAQTLRDCGAR-LVLCEDDCSAL------------------DLMGVQHARI-------------DAAQEEAQREQH 1345
Cdd:PRK08751   111 TPRELKHQLIDSGASvLVVIDNFGTTVqqviadtpvkqvittglgDMLGFPKAALvnfvvkyvkklvpEYRINGAIRFRE 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1346 ---LRAPHALPA--VDPRSAAYVIYTSGSSGAPKGVVIAH-----------------GALTNYVDAVLARLdpPPRARFA 1403
Cdd:PRK08751   191 alaLGRKHSMPTlqIEPDDIAFLQYTGGTTGVAKGAMLTHrnlvanmqqahqwlagtGKLEEGCEVVITAL--PLYHIFA 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1404 MVStigadlgHTVLFgaLASGGALHLIDRDTtlDADRFAQTLAAARIDVLKIVPGHLHALLQAErAADALPAHTL--VLG 1481
Cdd:PRK08751   269 LTA-------NGLVF--MKIGGCNHLISNPR--DMPGFVKELKKTRFTAFTGVNTLFNGLLNTP-GFDQIDFSSLkmTLG 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1482 GE-------ATSWELLDTIAALRPdcrvhnhYGPTETTVGILTQPAaqacraaaTLP-----LGRPLDNNETWLLDEHLN 1549
Cdd:PRK08751   337 GGmavqrsvAERWKQVTGLTLVEA-------YGLTETSPAACINPL--------TLKeyngsIGLPIPSTDACIKDDAGT 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1550 PVGTGGTGELYLGGAGVALGYLHQPALTAarfvpHPFAAGARLyRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEI 1629
Cdd:PRK08751   402 VLAIGEIGELCIKGPQVMKGYWKRPEETA-----KVMDADGWL-HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEI 475
                          490
                   ....*....|....*...
gi 1888712850 1630 AARLKALDGVRDAAVIVV 1647
Cdd:PRK08751   476 EDVIAMMPGVLEVAAVGV 493
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
75-346 1.77e-10

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 65.99  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   75 ERALILMDSGVDYVSAFFGCLYAGvvAVPVYPPESkreQHLARLRGIARDAGVRYVLTTAA----LHERHADAwsmLAPG 150
Cdd:PRK06334    68 QHIGIMMPASAGAYIAYFATLLSG--KIPVMINWS---QGLREVTACANLVGVTHVLTSKQlmqhLAQTHGED---AEYP 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  151 ADVVAVDTLDARDTPSDA------------------PLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGL 212
Cdd:PRK06334   140 FSLIYMEEVRKELSFWEKcrigiymsipfewlmrwfGVSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFF 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  213 GVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMS-PQYflerPLRWLDAIARHRGTISGAPD--FAYRLCAERIND 289
Cdd:PRK06334   220 SPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYnPLY----PKKIVEMIDEAKVTFLGSTPvfFDYILKTAKKQE 295
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1888712850  290 ETrakldLSSWRLAFSGSEpVRRDTLDDFVARFAPagfdAAALYPCYGLAEATLFVT 346
Cdd:PRK06334   296 SC-----LPSLRFVVIGGD-AFKDSLYQEALKTFP----HIQLRQGYGTTECSPVIT 342
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
177-510 2.14e-10

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 65.45  E-value: 2.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  177 DLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVL---MSPQY 253
Cdd:cd05940     82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFSASN 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  254 FlerplrWLDAIaRHRGTIsgapdFAY--RLCAERIN-----DETRAKLdlsswRLAFSGSepVRRDTLDDFVARFApag 326
Cdd:cd05940    162 F------WDDIR-KYQATI-----FQYigELCRYLLNqppkpTERKHKV-----RMIFGNG--LRPDIWEEFKERFG--- 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  327 fdAAALYPCYGLAEAT--LFVTGGVRGAglvshafssaalsAGRAEAARADEAATVLVGCgavqaghrvaivaraaaesh 404
Cdd:cd05940    220 --VPRIAEFYAATEGNsgFINFFGKPGA-------------IGRNPSLLRKVAPLALVKY-------------------- 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  405 esheaDVETETSRAGE-----RLADGRIGEI--HVSGPSVAHGYWQRADASAQAFVDAPRHADgsgpaRWLRTGDLGFVH 477
Cdd:cd05940    265 -----DLESGEPIRDAegrciKVPRGEPGLLisRINPLEPFDGYTDPAATEKKILRDVFKKGD-----AWFNTGDLMRLD 334
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1888712850  478 D-GQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:cd05940    335 GeGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAF 368
PRK08162 PRK08162
acyl-CoA synthetase; Validated
1220-1392 2.38e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 65.74  E-value: 2.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1220 ARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIV-----AHRSARFVVAMLG-VLKAggAYVAL 1293
Cdd:PRK08162    25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLlpnipAMVEAHFGVPMAGaVLNT--LNTRL 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1294 DAGNptqrLAQTLRDCGARLVLCEDDCS-----ALDLMGVQH----ARIDAAQEEAQREQHLRAPHALPAVDPR------ 1358
Cdd:PRK08162   103 DAAS----IAFMLRHGEAKVLIVDTEFAevareALALLPGPKplviDVDDPEYPGGRFIGALDYEAFLASGDPDfawtlp 178
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1888712850 1359 ----SAAYVIYTSGSSGAPKGVVIAH-GALTNYVDAVLA 1392
Cdd:PRK08162   179 adewDAIALNYTSGTTGNPKGVVYHHrGAYLNALSNILA 217
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
1240-1699 2.59e-10

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 65.15  E-value: 2.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLL-ARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLced 1318
Cdd:cd05937      7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI--- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1319 dcsaldlmgvqharidaaqeeaqreqhlraphalpaVDPRSAAYVIYTSGSSGAPKGVVIAHGalTNYVDAVL----ARL 1394
Cdd:cd05937     84 ------------------------------------VDPDDPAILIYTSGTTGLPKAAAISWR--RTLVTSNLlshdLNL 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1395 DPPPRARFAM--VSTIGADLGhtvLFGALASGGALHLIDRdttLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADA 1472
Cdd:cd05937    126 KNGDRTYTCMplYHGTAAFLG---ACNCLMSGGTLALSRK---FSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYD 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1473 LPAHTLVLGGEAtswelldtiaaLRPDC-----------RVHNHYGPTETTVGILTQPAAQACRAAATL--PLGRPLDNN 1539
Cdd:cd05937    200 RDHKVRVAWGNG-----------LRPDIwerfrerfnvpEIGEFYAATEGVFALTNHNVGDFGAGAIGHhgLIRRWKFEN 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1540 ETWLLDEHLN----------------PVGTGGT--GELYLGGAGVALGYLHQPALTAARFVPHPFAAGARLYRSGDRARR 1601
Cdd:cd05937    269 QVVLVKMDPEtddpirdpktgfcvraPVGEPGEmlGRVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQ 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1602 LADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAV--IVVAG----ARLAAFA---TPQPGASLDAAALKRA 1672
Cdd:cd05937    349 DADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGhdgrAGCAAITleeSSAVPTEFTKSLLASL 428
                          490       500
                   ....*....|....*....|....*..
gi 1888712850 1673 LAALLPDYMVPSVLRVIDALPLNRNGK 1699
Cdd:cd05937    429 ARKNLPSYAVPLFLRLTEEVATTDNHK 455
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
1218-1604 2.91e-10

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 65.67  E-value: 2.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1218 RVARHADTQPDAPAVI-----DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYV- 1291
Cdd:PRK08180    44 RLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAp 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1292 -----ALDAGNPTqRLAQTLRDCGARLVLCED-----------DCSALDLMGVQHARIDAA----QEEAQREQHLRAPHA 1351
Cdd:PRK08180   124 vspaySLVSQDFG-KLRHVLELLTPGLVFADDgaafaralaavVPADVEVVAVRGAVPGRAatpfAALLATPPTAAVDAA 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1352 LPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVS------TIGadlGHTVLFGALASGG 1425
Cdd:PRK08180   203 HAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVDwlpwnhTFG---GNHNLGIVLYNGG 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1426 ALHLIDRDTTldADRFAQTLAAARI---DVLKIVPGHLHALLQAERAADALPAH------TLVLGGEATS---WELLDTI 1493
Cdd:PRK08180   280 TLYIDDGKPT--PGGFDETLRNLREispTVYFNVPKGWEMLVPALERDAALRRRffsrlkLLFYAGAALSqdvWDRLDRV 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1494 AALRPDCRVH--NHYGPTEttvgilTQPAAQACRAAATLP--LGRPLDNNETWLldehlnpVGTGGTGELYLGGAGVALG 1569
Cdd:PRK08180   358 AEATCGERIRmmTGLGMTE------TAPSATFTTGPLSRAgnIGLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPG 424
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1888712850 1570 YLHQPALTAARFVPHPFaagarlYRSGDrARRLAD 1604
Cdd:PRK08180   425 YWRAPELTAEAFDEEGY------YRSGD-AVRFVD 452
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
1238-1380 3.97e-10

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 65.01  E-value: 3.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1238 RMSYAELDARAAHVAQWLLA-RDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLC 1316
Cdd:cd05938      5 TYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1317 --------EDDCSALDLMGVQ---------HARIDAAQEEAQREQHLRAPHALPA-VDPRSAAYVIYTSGSSGAPKGVVI 1378
Cdd:cd05938     85 apelqeavEEVLPALRADGVSvwylshtsnTEGVISLLDKVDAASDEPVPASLRAhVTIKSPALYIYTSGTTGLPKAARI 164

                   ..
gi 1888712850 1379 AH 1380
Cdd:cd05938    165 SH 166
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
32-586 6.78e-10

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 64.52  E-value: 6.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   32 QQRPEATALIVIDADGDT--RYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAVPVYPPE 108
Cdd:cd17634     64 RENGDRTAIIYEGDDTSQsrTISYRELHREVCRFAGTLLDLGvKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  109 SKREqhlarLRGIARDAGVRYVLTTAALHERH---------ADAWSMLAPGADVVAV------------------DTLDA 161
Cdd:cd17634    144 APEA-----VAGRIIDSSSRLLITADGGVRAGrsvplkknvDDALNPNVTSVEHVIVlkrtgsdidwqegrdlwwRDLIA 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  162 RDTPSDAPLhPVRADDLAFLQYTSGSTGSPKGVMVSHGN-LLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPV 240
Cdd:cd17634    219 KASPEHQPE-AMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPL 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  241 FSGIPLVLMSPQYFLERPLRWLDAIARHRGTISGAPDFAYRLCAERiNDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVA 320
Cdd:cd17634    298 ACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAA-GDDAIEGTDRSSLRILGSVGEPINPEAYEWYWK 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  321 RFapaGFDAAALYPCYGLAEATLFVTGGVRGAglvshafssAALSAGRAEAARADEAATVLvgcgavqaghrvaivaraa 400
Cdd:cd17634    377 KI---GKEKCPVVDTWWQTETGGFMITPLPGA---------IELKAGSATRPVFGVQPAVV------------------- 425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  401 aeshesheaDVETETSRAGerlADGRIGeIHVSGPSVAHGYWQRADASAQAFVdapRHADGSgparWLrTGDLGFV-HDG 479
Cdd:cd17634    426 ---------DNEGHPQPGG---TEGNLV-ITDPWPGQTRTLFGDHERFEQTYF---STFKGM----YF-SGDGARRdEDG 484
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  480 QLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFAR----------KGRVIAFGATLGGGETLGLALeiaprmkkrfaAA 549
Cdd:cd17634    485 YYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEaavvgiphaiKGQAPYAYVVLNHGVEPSPEL-----------YA 553
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 1888712850  550 QIVETLRRiafdACGETPAAIALLNPGALPKTSSGKL 586
Cdd:cd17634    554 ELRNWVRK----EIGPLATPDVVHWVDSLPKTRSGKI 586
PRK09274 PRK09274
peptide synthase; Provisional
1219-1618 8.09e-10

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 64.15  E-value: 8.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARH----ADTQPDAPAVIDGALR----------MSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVL 1284
Cdd:PRK09274     8 IARHlpraAQERPDQLAVAVPGGRgadgklaydeLSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1285 KAGGAYVALDAGNPTQRLAQTLRDCG------------ARLVLCEDDCSALDLMGVQHARIDAAQEEAQREQHLR-APHA 1351
Cdd:PRK09274    88 KAGAVPVLVDPGMGIKNLKQCLAEAQpdafigipkahlARRLFGWGKPSVRRLVTVGGRLLWGGTTLATLLRDGAaAPFP 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1352 LPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVlarldpppRARFAMVSTiGADLgHT----VLFGaLASGGAL 1427
Cdd:PRK09274   168 MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEAL--------REDYGIEPG-EIDL-PTfplfALFG-PALGMTS 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1428 HLIDRD----TTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAAD-ALPAHTLVLGGEAT----SWELLDTIaaLRP 1498
Cdd:PRK09274   237 VIPDMDptrpATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGiKLPSLRRVISAGAPvpiaVIERFRAM--LPP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1499 DCRVHNHYGPTE----TTVG---ILTQPAAQACRAAATLpLGRPLDNNE------------TWllDEHLnPVGTGGTGEL 1559
Cdd:PRK09274   315 DAEILTPYGATEalpiSSIEsreILFATRAATDNGAGIC-VGRPVDGVEvriiaisdapipEW--DDAL-RLATGEIGEI 390
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850 1560 YLGGAGVALGYLHQPALTAARFVPHPfaAGARLYRSGDRARRLADGSLEYLGRIDDQVK 1618
Cdd:PRK09274   391 VVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
1244-1705 9.17e-10

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 63.55  E-value: 9.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1244 LDARAAHVAQWLLARDLQGGEPVAIVAHRSARfVVAMLGVLKAGGAYVALDAGNPT-QRLAQTLR--DCGARLVLCEDDC 1320
Cdd:cd05929      1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNAR-AAAAEGVWIADGVYIYLINSILTvFAAAAAWKcgACPAYKSSRAPRA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1321 SALDLMGVQHA----RIDAAQEEAQREQHLRAPHAL----PAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLA 1392
Cdd:cd05929     80 EACAIIEIKAAalvcGLFTGGGALDGLEDYEAAEGGspetPIEDEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1393 RLD---PPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRdttLDADRFAQTLAAARIDVLKIVPGHLHALL---QA 1466
Cdd:cd05929    160 AALgfgPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEK---FDPEEFLRLIERYRVTFAQFVPTMFVRLLklpEA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1467 ERAA-DALPAHTLVLGGEATSWELLDTIAALRPDcRVHNHYGPTETtVGI--------LTQPAAqacraaatlpLGRPLD 1537
Cdd:cd05929    237 VRNAyDLSSLKRVIHAAAPCPPWVKEQWIDWGGP-IIWEYYGGTEG-QGLtiingeewLTHPGS----------VGRAVL 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1538 NnETWLLDEHLNPVGTGGTGELYLGGAGvALGYLHQPALTAARFVPHPFAAgarlyrSGDRARRLADGSLEYLGRIDDQV 1617
Cdd:cd05929    305 G-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWST------LGDVGYLDEDGYLYLTDRRSDMI 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1618 KIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALA---ALLPDYMVPSVLRVID 1690
Cdd:cd05929    377 ISGGVNIYPQEIENALIAHPKVLDAAVVGVPdeelGQRVHAVVQPAPGADAGTALAEELIAflrDRLSRYKCPRSIEFVA 456
                          490
                   ....*....|....*
gi 1888712850 1691 ALPLNRNGKLDRQAL 1705
Cdd:cd05929    457 ELPRDDTGKLYRRLL 471
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
469-588 1.09e-09

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 63.24  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  469 RTGDLGFVHDGQ----------LYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAFGAtlGGGETLGLALEI 538
Cdd:COG1541    298 RTGDLTRLLPEPcpcgrthpriGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDRE--GGLDELTVRVEL 375
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1888712850  539 APRMKKRFAAAQIVETLRriafDACGeTPAAIALLNPGALPKtSSGKLQR 588
Cdd:COG1541    376 APGASLEALAEAIAAALK----AVLG-LRAEVELVEPGSLPR-SEGKAKR 419
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
79-509 1.65e-09

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 62.79  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   79 ILMDSGVDYVSAFFGCLYAGVVAVPV---YPPEskreqhlaRLRGIARDAGVRYVLTTAALHERHADAwsmLAPGADVVA 155
Cdd:PRK12406    41 LLMRNDFAFFEAAYAAMRLGAYAVPVnwhFKPE--------EIAYILEDSGARVLIAHADLLHGLASA---LPAGVTVLS 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  156 VDT---------LDARDT-----------------PSDAPLHPVRADdlafLQYTSGSTGSPKGVMVSHGN---LLANEI 206
Cdd:PRK12406   110 VPTppeiaaayrISPALLtppagaidwegwlaqqePYDGPPVPQPQS----MIYTSGTTGHPKGVRRAAPTpeqAAAAEQ 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  207 AIQAGLGVRPDDVFVSWLPLYHD----MGLIGSLLqpvfsGIPLVLMsPQYfleRPLRWLDAIARHR-GTISGAPDFAYR 281
Cdd:PRK12406   186 MRALIYGLKPGIRALLTGPLYHSapnaYGLRAGRL-----GGVLVLQ-PRF---DPEELLQLIERHRiTHMHMVPTMFIR 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  282 LCaeRINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPagfdaaALYPCYGLAEatlfvtggvrgAGLVSHAFSS 361
Cdd:PRK12406   257 LL--KLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGP------VIYEYYGSTE-----------SGAVTFATSE 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  362 AALSagraeaaradEAATVlvgcGAVQAGhrvaivaraaaeshesheADVETeTSRAGERLADGRIGEIHVSGPSVAH-G 440
Cdd:PRK12406   318 DALS----------HPGTV----GKAAPG------------------AELRF-VDEDGRPLPQGEIGEIYSRIAGNPDfT 364
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  441 YWQRADASAQAfvdaprhadgsGPARWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEA 509
Cdd:PRK12406   365 YHNKPEKRAEI-----------DRGGFITSGDVGYLDaDGYLFLCDRKRDMVISGGVNIYPAEIEAVLHA 423
PRK07638 PRK07638
acyl-CoA synthetase; Validated
418-592 2.26e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 62.49  E-value: 2.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  418 AGERLADGRIGEIHVSGPSVAHGYWQRADAsaqafvdaPRHADGSGparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGR 496
Cdd:PRK07638   324 AGEEVQKGEIGTVYVKSPQFFMGYIIGGVL--------ARELNADG---WMTVRDVGYEdEEGFIYIVGREKNMILFGGI 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  497 NLYPQDVEQAVEAHAEFArkgRVIAFG-----------ATLGGGETlglALEIAPRMKKRFAAAQIvetlrriafdacge 565
Cdd:PRK07638   393 NIFPEEIESVLHEHPAVD---EIVVIGvpdsywgekpvAIIKGSAT---KQQLKSFCLQRLSSFKI-------------- 452
                          170       180
                   ....*....|....*....|....*..
gi 1888712850  566 tPAAIALLNpgALPKTSSGKLQRAATR 592
Cdd:PRK07638   453 -PKEWHFVD--EIPYTNSGKIARMEAK 476
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
48-322 2.89e-09

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 62.06  E-value: 2.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   48 DTRYDYAQLDRRARALAARFARDG-AAAERALILMDSGVDYVSAFFGCLYAGVVAvPVYPPESKREQHLarlrgiardag 126
Cdd:cd05939      1 DRHWTFRELNEYSNKVANFFQAQGyRSGDVVALFMENRLEFVALWLGLAKIGVET-ALINSNLRLESLL----------- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  127 vrYVLTTAalherhadawsmlapGADVVAVDTLDARDTpsDAPLHPVRADDLAFLQ-----YTSGSTGSPKGVMVSHGNL 201
Cdd:cd05939     69 --HCITVS---------------KAKALIFNLLDPLLT--QSSTEPPSQDDVNFRDklfyiYTSGTTGLPKAAVIVHSRY 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  202 LANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVL---MSPQYFlerplrWLDAIaRHRGTISG--AP 276
Cdd:cd05939    130 YRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIrkkFSASNF------WDDCV-KYNCTIVQyiGE 202
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1888712850  277 DFAYRLCAERINDETRAKLdlsswRLAFSGSepVRRDTLDDFVARF 322
Cdd:cd05939    203 ICRYLLAQPPSEEEQKHNV-----RLAVGNG--LRPQIWEQFVRRF 241
PRK09192 PRK09192
fatty acyl-AMP ligase;
1241-1383 2.98e-09

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 62.33  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1241 YAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAgnPT---------QRLAQTLRDCGA 1311
Cdd:PRK09192    52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPL--PMgfggresyiAQLRGMLASAQP 129
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850 1312 RLVLCEDDCSALDLMGVQHARIDAAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGAL 1383
Cdd:PRK09192   130 AAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
35-521 4.35e-09

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 61.26  E-value: 4.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   35 PEATALIvidaDGDTRYDYAQLDRRARALAARFARDGA--AAERALILMDSGVDYVSAFFGCLYAGVVAVPV---YPPEs 109
Cdd:cd17648      1 PDRVAVV----YGDKRLTYRELNERANRLAHYLLSVAEirPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIdpsYPDE- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  110 kreqhlaRLRGIARDAGVRYVLTTAAlherhadawsmlapgadvvavdtldardtpsdaplhpvradDLAFLQYTSGSTG 189
Cdd:cd17648     76 -------RIQFILEDTGARVVITNST-----------------------------------------DLAYAIYTSGTTG 107
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  190 SPKGVMVSHGNLLANEIAIQAGLGVR-PDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLMSPQyFLERPLRWLDAIARH 268
Cdd:cd17648    108 KPKGVLVEHGSVVNLRTSLSERYFGRdNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDE-MRFDPDRFYAYINRE 186
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  269 RGT-ISGAPDFAYRLCAERINDETRakLDLSSWRLAFSGSEPVRrdtlddfvARFApagfdaAALYPCYGLAEATlfVTG 347
Cdd:cd17648    187 KVTyLSGTPSVLQQYDLARLPHLKR--VDAAGEEFTAPVFEKLR--------SRFA------GLIINAYGPTETT--VTN 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  348 GVRGAgLVSHAFSSAalsagraeaaradeaatvlVGCGaVQAGHRVAIvaraaaeshesheadvetetSRAGERLADGRI 427
Cdd:cd17648    249 HKRFF-PGDQRFDKS-------------------LGRP-VRNTKCYVL--------------------NDAMKRVPVGAV 287
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  428 GEIHVSGPSVAHGYWQRADASAQAFVDAPRHADG----SGPARWLRTGDLG-FVHDGQLYIAGRVKDLVIVRGRNLYPQD 502
Cdd:cd17648    288 GELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerarGRNARLYKTGDLVrWLPSGELEYLGRNDFQVKIRGQRIEPGE 367
                          490
                   ....*....|....*....
gi 1888712850  503 VEQAVEAHAEfARKGRVIA 521
Cdd:cd17648    368 VEAALASYPG-VRECAVVA 385
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
1235-1660 5.17e-09

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 61.30  E-value: 5.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1235 GALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLV 1314
Cdd:cd05914      4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1315 LCEddcsaldlmgvqharidaaqeeaqreqhlraphalpavDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARL 1394
Cdd:cd05914     84 FVS--------------------------------------DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVV 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1395 DPPPRARfaMVSTIgaDLGHT--VLFG---ALASGGALHLIDRDTT--LDADRFAQ------------------------ 1443
Cdd:cd05914    126 LLGKGDK--ILSIL--PLHHIypLTFTlllPLLNGAHVVFLDKIPSakIIALAFAQvtptlgvpvplviekifkmdiipk 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1444 -TLA------AARIDVLKIvpghLHALLQAerAADALPAH--TLVLGGEATSWELLDTIAALR-PDCRvhnHYGPTETTV 1513
Cdd:cd05914    202 lTLKkfkfklAKKINNRKI----RKLAFKK--VHEAFGGNikEFVIGGAKINPDVEEFLRTIGfPYTI---GYGMTETAP 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1514 GILTQPAAQACRAAAtlplGRPLDNNETWLLDehlnPVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarlY 1593
Cdd:cd05914    273 IISYSPPNRIRLGSA----GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------F 338
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1888712850 1594 RSGDRARRLADGSLEYLGRIDDQ-VKIRGYRVEPGEIAARLKALDGVRDAAVIVVAGaRLAAFATPQP 1660
Cdd:cd05914    339 HTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEK-KLVALAYIDP 405
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
1240-1705 5.73e-09

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 61.15  E-value: 5.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYvalDAGNPT---QRLAQTLRDCGARLVLC 1316
Cdd:PLN02330    57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVF---SGANPTaleSEIKKQAEAAGAKLIVT 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1317 ED--------------------DCSALDLMGVQHARIDAAQEEAQREQHLRAPHALPavdprsaayviYTSGSSGAPKGV 1376
Cdd:PLN02330   134 NDtnygkvkglglpvivlgeekIEGAVNWKELLEAADRAGDTSDNEEILQTDLCALP-----------FSSGTTGISKGV 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1377 VIAHGALTNYVDAVLARLDPpprARFAMVSTIG-ADLGHT-----VLFGALASGGALHLIDRdttLDADRFAQTLAAARI 1450
Cdd:PLN02330   203 MLTHRNLVANLCSSLFSVGP---EMIGQVVTLGlIPFFHIygitgICCATLRNKGKVVVMSR---FELRTFLNALITQEV 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1451 DVLKIVPGHLHALLQ----AERAADALPAHTLVLGGEATSWELLDTIAALRPDCRVHNHYGPTETTVGILTQ--PAAQAC 1524
Cdd:PLN02330   277 SFAPIVPPIILNLVKnpivEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHgdPEKGHG 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1525 RAAATlPLGRPLDNNETWLLDEHLN---PVGTggTGELYLGGAGVALGYLHQPALTAarfvpHPFAAGARLYrSGDRARR 1601
Cdd:PLN02330   357 IAKKN-SVGFILPNLEVKFIDPDTGrslPKNT--PGELCVRSQCVMQGYYNNKEETD-----RTIDEDGWLH-TGDIGYI 427
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1602 LADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV----AGARLAAFATPQPGASLDAAALKRALAALL 1677
Cdd:PLN02330   428 DDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLpdeeAGEIPAACVVINPKAKESEEDILNFVAANV 507
                          490       500
                   ....*....|....*....|....*...
gi 1888712850 1678 PDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:PLN02330   508 AHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
1228-1705 6.10e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 61.32  E-value: 6.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1228 DAPAVIDGALRMSYAELDARAAHVAQWLLAR-DLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALdagNP--TQR-LA 1303
Cdd:PRK05677    39 DKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNT---NPlyTAReME 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1304 QTLRDCGARLVLCEDDCS-----ALDLMGVQH---------------ARIDAAQEEAQR---EQHLraPHALP------- 1353
Cdd:PRK05677   116 HQFNDSGAKALVCLANMAhlaekVLPKTGVKHvivtevadmlpplkrLLINAVVKHVKKmvpAYHL--PQAVKfndalak 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1354 -------AVDPRSA--AYVIYTSGSSGAPKGVVIAHgalTNYVDAVLarldpppRARFAMVSTIGAdlGHTVLFGALA-- 1422
Cdd:PRK05677   194 gagqpvtEANPQADdvAVLQYTGGTTGVAKGAMLTH---RNLVANML-------QCRALMGSNLNE--GCEILIAPLPly 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1423 -------SGGALHLIDRDTTL-----DADRFAQTLAAARIDVLKIVPGHLHALLQAE--RAADALPAHTLVLGGEAtswe 1488
Cdd:PRK05677   262 hiyaftfHCMAMMLIGNHNILisnprDLPAMVKELGKWKFSGFVGLNTLFVALCNNEafRKLDFSALKLTLSGGMA---- 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1489 lLDTIAALR----PDCRVHNHYGPTETTVGILTQPAAQACRAAatlpLGRPLDNNETWLLDEHLNPVGTGGTGELYLGGA 1564
Cdd:PRK05677   338 -LQLATAERwkevTGCAICEGYGMTETSPVVSVNPSQAIQVGT----IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1565 GVALGYLHQPALTAARFVPHPFaagarlYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAV 1644
Cdd:PRK05677   413 QVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAA 486
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850 1645 IVV----AGARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:PRK05677   487 IGVpdekSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
47-356 6.41e-09

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 61.15  E-value: 6.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   47 GDTRYDYAQLDRRA--RALAARFARDGAAAERALILMDSGVDYVSAFFGCLYAGVVAVPVypPESKREQHLARlrgIARD 124
Cdd:cd05938      2 EGETYTYRDVDRRSnqAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFL--NTNIRSKSLLH---CFRC 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  125 AGVRYVLTTAALHER--------HADA--WSMLAPGADVVAVDTL-DARDTPSDAPL-----HPVRADDLAFLQYTSGST 188
Cdd:cd05938     77 CGAKVLVVAPELQEAveevlpalRADGvsVWYLSHTSNTEGVISLlDKVDAASDEPVpaslrAHVTIKSPALYIYTSGTT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  189 GSPKGVMVSHGNLLANEiAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVL---MSPQYFlerplrWLDAi 265
Cdd:cd05938    157 GLPKAARISHLRVLQCS-GFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLkpkFSASQF------WDDC- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  266 ARHRGTIsgapdFAY------RLC--AERINDETRAKldlsswRLAF-SGsepVRRDTLDDFVARFAPagfdaAALYPCY 336
Cdd:cd05938    229 RKHNVTV-----IQYigellrYLCnqPQSPNDRDHKV------RLAIgNG---LRADVWREFLRRFGP-----IRIREFY 289
                          330       340
                   ....*....|....*....|...
gi 1888712850  337 GLAEATL-FV--TGGVRGAGLVS 356
Cdd:cd05938    290 GSTEGNIgFFnyTGKIGAVGRVS 312
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
914-1437 6.42e-09

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 61.81  E-value: 6.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  914 AWQRRWLASDAAARQLAywrAALADDAPPLALPYDHTATDTASENADPRAAARVAFALPAPLAQAVRASAARHRATPFVV 993
Cdd:COG3321    867 PFQREDAAAALLAAALA---AALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALL 943
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  994 LLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVLHSDCEAATPLASLFSQLRQRTLDAQANQALPFDVL 1073
Cdd:COG3321    944 ALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLA 1023
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1074 VEHLRPARDAQHGPLFETSFNYLSDDYPALARWPGARAERVEIAETHVKVPLALDLRESRDGSMRAYFTYASARFDAASV 1153
Cdd:COG3321   1024 LAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALA 1103
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1154 ERMAAQYLRAVEAFAHALGDRSADMTDAAAPTLATLDLLDADERARVSAASVARRTPPGEPIHLRVARHADTQPDAPAVI 1233
Cdd:COG3321   1104 AALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAA 1183
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1234 DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARL 1313
Cdd:COG3321   1184 ALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALA 1263
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1314 VLcEDDCSALDLMGVQHARIDAAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLAR 1393
Cdd:COG3321   1264 LL-AAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALA 1342
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1888712850 1394 LDPPPRARFAMVSTIGADLGHTVLFGALASGGALHLIDRDTTLD 1437
Cdd:COG3321   1343 LAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
PLN03051 PLN03051
acyl-activating enzyme; Provisional
1315-1648 6.48e-09

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 60.99  E-value: 6.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1315 LCEDDCSALDLMGVqharidAAQEEAQREQHLRaPHALPAVDPRSaayVIYTSGSSGAPKGVVIAHGALTNYVDAVLARL 1394
Cdd:PLN03051    86 LREQDLSWCDFLGV------AAAQGSVGGNEYS-PVYAPVESVTN---ILFSSGTTGEPKAIPWTHLSPLRCASDGWAHM 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1395 DPPPRARFAMVSTIGADLGHTVLFGALASGGALHL-----IDRDttldadrFAQTLAAARIDVLKIVPghlhALLQAERA 1469
Cdd:PLN03051   156 DIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALyggapLGRG-------FGKFVQDAGVTVLGLVP----SIVKAWRH 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1470 ADALPAHTL--------VLGGEATSWELLDTIAALRPDCR-VHNHYGPTETT----VGILTQPAAQACRAAATLPLGRPL 1536
Cdd:PLN03051   225 TGAFAMEGLdwsklrvfASTGEASAVDDVLWLSSVRGYYKpVIEYCGGTELAsgyiSSTLLQPQAPGAFSTASLGTRFVL 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1537 DNNETWLLDEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAArfVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQ 1616
Cdd:PLN03051   305 LNDNGVPYPDDQPCVGEVALAPPMLGASDRLLNADHDKVYYKG--MPMYGSKGMPLRRHGDIMKRTPGGYFCVQGRADDT 382
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1888712850 1617 VKIRGYRVEPGEIA-ARLKALDGVRDAAVIVVA 1648
Cdd:PLN03051   383 MNLGGIKTSSVEIErACDRAVAGIAETAAVGVA 415
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
183-510 8.39e-09

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 59.62  E-value: 8.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  183 YTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHdmglIGSLlqpvFSGIPLVLMS-PQYFLER--PL 259
Cdd:cd17636      7 YTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFH----IGTL----MFTLATFHAGgTNVFVRRvdAE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  260 RWLDAIARHRGTisgapdFAYRLCA-----ERINDETRakLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGfdaaalyp 334
Cdd:cd17636     79 EVLELIEAERCT------HAFLLPPtidqiVELNADGL--YDLSSLRSSPAAPEWNDMATVDTSPWGRKPGG-------- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  335 cYGLAEATLFVT------GGVRGAGLVSHAFSSAALSAgraeaaradeaatvlvgcgavqaghrvaivaraaaesheshe 408
Cdd:cd17636    143 -YGQTEVMGLATfaalggGAIGGAGRPSPLVQVRILDE------------------------------------------ 179
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  409 advetetsrAGERLADGRIGEIHVSGPSVAHGYWQRADASAQafvdapRHADGsgparWLRTGDLGFVH-DGQLYIAGRV 487
Cdd:cd17636    180 ---------DGREVPDGEVGEIVARGPTVMAGYWNRPEVNAR------RTRGG-----WHHTNDLGRREpDGSLSFVGPK 239
                          330       340
                   ....*....|....*....|...
gi 1888712850  488 KDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:cd17636    240 TRMIKSGAENIYPAEVERCLRQH 262
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
1240-1655 1.03e-08

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 60.51  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCEDD 1319
Cdd:cd17641     13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDE 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1320 ---------------------CSALDLMGVQHAR-IDAAQ-EEAQREQHLRAP----HALPAVDPRSAAYVIYTSGSSGA 1372
Cdd:cd17641     93 eqvdklleiadripsvryviyCDPRGMRKYDDPRlISFEDvVALGRALDRRDPglyeREVAAGKGEDVAVLCTTSGTTGK 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1373 PKGVVIAHGALTNYvDAVLARLDP--PPRARFAMVST--IGADLghTVLFGALASGGALHLIDRDTTLDAD------RFa 1442
Cdd:cd17641    173 PKLAMLSHGNFLGH-CAAYLAADPlgPGDEYVSVLPLpwIGEQM--YSVGQALVCGFIVNFPEEPETMMEDlreigpTF- 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1443 qTLAAARI--DVLKIVPGHL------------HALLQAERAADA-LPAHTLVLGGEATSW--------ELLDTI------ 1493
Cdd:cd17641    249 -VLLPPRVweGIAADVRARMmdatpfkrfmfeLGMKLGLRALDRgKRGRPVSLWLRLASWladallfrPLRDRLgfsrlr 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1494 ------AALRPDCRVHNH---------YGPTETTVGILTQPAAQACRAAatlpLGRPLDNNEtwlldehlnpVGTGGTGE 1558
Cdd:cd17641    328 saatggAALGPDTFRFFHaigvplkqlYGQTELAGAYTVHRDGDVDPDT----VGVPFPGTE----------VRIDEVGE 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1559 LYLGGAGVALGYLHQPALTAARFVPHPFaagarlYRSGDRARRLADGSLEYLGRIDDQVKI-RGYRVEPGEIAARLKALD 1637
Cdd:cd17641    394 ILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSP 467
                          490
                   ....*....|....*...
gi 1888712850 1638 GVRDAAVIVVAGARLAAF 1655
Cdd:cd17641    468 YIAEAVVLGAGRPYLTAF 485
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
2054-2295 1.22e-08

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 60.85  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2054 FWRGYLaDAPALLPLSTDRARPTRVSHAGAARHFRLDAtlgarvRTLAQAHGMTPFAVLLASFQWFLHRHTGADDLVIGT 2133
Cdd:TIGR03443    1 RWSERL-DNPTLSVLPHDYLRPANNRLVEATYSLQLPS------AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2134 D--VDGRE---RAELEALIGFFvnvvPLRSRIAADGANLASFDawldaarqstwdaldhrALPFDRIVDALALKRRRDAN 2208
Cdd:TIGR03443   74 SsnKSGRPfvlRLNITPELSFL----QLYAKVSEEEKEGASDI-----------------GVPFDELSEHIQAAKKLERT 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2209 PlvqVLFVLR--DLPRGNtrvpglavelLRPPTTQSKFDMALFVEAVDGGYDIEWVYASALFDAATIERAFDAWRATLDA 2286
Cdd:TIGR03443  133 P---PLFRLAfqDAPDNQ----------QTTYSTGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSA 199

                   ....*....
gi 1888712850 2287 VSADPRAPL 2295
Cdd:TIGR03443  200 ASSNPDEPI 208
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
31-514 1.41e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 59.70  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   31 AQQRPEATALIVidADGDTRYDYAQLDRRARALAARFARDGAA-AERALILMDSGVDYVSAFFGCLYAGVVAVPVyppes 109
Cdd:PRK13391     7 AQTTPDKPAVIM--ASTGEVVTYRELDERSNRLAHLFRSLGLKrGDHVAIFMENNLRYLEVCWAAERSGLYYTCV----- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  110 krEQHL--ARLRGIARDAGVRYVLTTAAlherHADAWSMLA---PGA----DVVAVDTLDARDTPSDA----PLHPVRAD 176
Cdd:PRK13391    80 --NSHLtpAEAAYIVDDSGARALITSAA----KLDVARALLkqcPGVrhrlVLDGDGELEGFVGYAEAvaglPATPIADE 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  177 DL-AFLQYTSGSTGSPKGVMvshGNLLANEIAIQAGL--------GVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLV 247
Cdd:PRK13391   154 SLgTDMLYSSGTTGRPKGIK---RPLPEQPPDTPLPLtaflqrlwGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIV 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  248 lmspqyfLER--PLRWLDAIARHRGTISG-APDFAYRLCaeRINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAP 324
Cdd:PRK13391   231 -------MEHfdAEQYLALIEEYGVTHTQlVPTMFSRML--KLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGP 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  325 agfdaaALYPCYGLAEATLFVtgGVRGAGLVSHAFSSAalsagraeaaradeaaTVLVGcgavqaghrvaivaraaaesh 404
Cdd:PRK13391   302 ------IIHEYYAATEGLGFT--ACDSEEWLAHPGTVG----------------RAMFG--------------------- 336
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  405 ESHEADvetetsRAGERLADGRIGEIHVSGPSvAHGYWQRADASAQAfvdapRHADGSgparWLRTGDLGFVH-DGQLYI 483
Cdd:PRK13391   337 DLHILD------DDGAELPPGEPGTIWFEGGR-PFEYLNDPAKTAEA-----RHPDGT----WSTVGDIGYVDeDGYLYL 400
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1888712850  484 AGRVKDLVIVRGRNLYPQDVEQAVEAHAEFA 514
Cdd:PRK13391   401 TDRAAFMIISGGVNIYPQEAENLLITHPKVA 431
PLN03102 PLN03102
acyl-activating enzyme; Provisional
408-593 1.46e-08

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 60.03  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  408 EADVE-TETSRAGERlaDGR-IGEIHVSGPSVAHGYWQRADASAQAFvdapRHAdgsgparWLRTGDLGFVH-DGQLYIA 484
Cdd:PLN03102   373 DVDVKnKETQESVPR--DGKtMGEIVIKGSSIMKGYLKNPKATSEAF----KHG-------WLNTGDVGVIHpDGHVEIK 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  485 GRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGrVIAFGATLgGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDACG 564
Cdd:PLN03102   440 DRSKDIIISGGENISSVEVENVLYKYPKVLETA-VVAMPHPT-WGETPCAFVVLEKGETTKEDRVDKLVTRERDLIEYCR 517
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1888712850  565 ET------PAAIALLNpgALPKTSSGKLQRAATRE 593
Cdd:PLN03102   518 ENlphfmcPRKVVFLQ--ELPKNGNGKILKPKLRD 550
PRK05857 PRK05857
fatty acid--CoA ligase;
1218-1712 1.64e-08

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 59.64  E-value: 1.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1218 RVARHADTQPDAPAV--IDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDA 1295
Cdd:PRK05857    19 RVFEQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADG 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1296 GNPTQRLAQTLRDCGARLVL----CEDDCSALDLMGVQHARIDAAQEEAQREQHLRAPHALPAVDPRSAA----YVIYTS 1367
Cdd:PRK05857    99 NLPIAAIERFCQITDPAAALvapgSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSedplAMIFTS 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1368 GSSGAPKGVVIAHGAL-----------TNYVDAVLAR--LDPPPRARFAMVSTIGADLGHtvlfGALASGGALHLIDRDT 1434
Cdd:PRK05857   179 GTTGEPKAVLLANRTFfavpdilqkegLNWVTWVVGEttYSPLPATHIGGLWWILTCLMH----GGLCVTGGENTTSLLE 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1435 TLDADRFAQTLaaaridvlkIVPGHLHALLQAERAADAL--PAHTLVLGGEATSWELLDTIAAlrPDCRVHNHYGPTETT 1512
Cdd:PRK05857   255 ILTTNAVATTC---------LVPTLLSKLVSELKSANATvpSLRLVGYGGSRAIAADVRFIEA--TGVRTAQVYGLSETG 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1513 VGILTQPAAQACRAAATL-PLGRPLDNNETWLLDEHLNPVGTGGTGE------LYLGGAGVALGYLHQPALTAARFVPHp 1585
Cdd:PRK05857   324 CTALCLPTDDGSIVKIEAgAVGRPYPGVDVYLAATDGIGPTAPGAGPsasfgtLWIKSPANMLGYWNNPERTAEVLIDG- 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1586 faagarLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVI---------VVAGARLAAFA 1656
Cdd:PRK05857   403 ------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYeipdeefgaLVGLAVVASAE 476
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1888712850 1657 TPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSALARPA 1712
Cdd:PRK05857   477 LDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATAD 532
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
162-310 1.76e-08

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 59.95  E-value: 1.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  162 RDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVM-VSHGNLLANEIAIQAGLGVRPDDVF-----VSWLPlYHDMGLIGS 235
Cdd:TIGR02188  223 AKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLhTTGGYLLYAAMTMKYVFDIKDGDIFwctadVGWIT-GHSYIVYGP 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  236 LL----QPVFSGIPlvlMSPQyflerPLRWLDAIARHRGTI-SGAPDfAYRLCAeRINDETRAKLDLSSWRLAFSGSEPV 310
Cdd:TIGR02188  302 LAngatTVMFEGVP---TYPD-----PGRFWEIIEKHKVTIfYTAPT-AIRALM-RLGDEWVKKHDLSSLRLLGSVGEPI 371
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1730-1804 1.91e-08

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 52.57  E-value: 1.91e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850 1730 ALAQCWAALLDpsngtdnatdnataTPSLTIARDDSFFALGGHSLAAMRLASRVRSRWSVELPLREIFASPTLAA 1804
Cdd:pfam00550    2 RLRELLAEVLG--------------VPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK08162 PRK08162
acyl-CoA synthetase; Validated
423-600 1.96e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 59.58  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  423 ADGR-IGEIHVSGPSVAHGYWQRADASAQAFvdaprhADGsgparWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYP 500
Cdd:PRK08162   383 ADGEtIGEIMFRGNIVMKGYLKNPKATEEAF------AGG-----WFHTGDLAVLHpDGYIKIKDRSKDIIISGGENISS 451
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  501 QDVEQAVEAHAEfarkgrvIAFGATLGG-----GETLGLALEIAPRMKKRfaAAQIVETLRriAFDACGETPAAIALlnp 575
Cdd:PRK08162   452 IEVEDVLYRHPA-------VLVAAVVAKpdpkwGEVPCAFVELKDGASAT--EEEIIAHCR--EHLAGFKVPKAVVF--- 517
                          170       180
                   ....*....|....*....|....*
gi 1888712850  576 GALPKTSSGKLQRAATREgwRARTL 600
Cdd:PRK08162   518 GELPKTSTGKIQKFVLRE--QAKSL 540
PRK08315 PRK08315
AMP-binding domain protein; Validated
1220-1699 2.35e-08

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 59.44  E-value: 2.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1220 ARHADTQPDAPAVI--DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALdagN 1297
Cdd:PRK08315    23 DRTAARYPDREALVyrDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTI---N 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 PTQRLAQTlrdcgaRLVLCEDDCSALDLMG----------VQHARIDAAQEEAQREQHLRAPH----------------- 1350
Cdd:PRK08315   100 PAYRLSEL------EYALNQSGCKALIAADgfkdsdyvamLYELAPELATCEPGQLQSARLPElrrviflgdekhpgmln 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1351 -----------ALPAVDPRSAAY----VI---YTSGSSGAPKGVVIAHGALTN--YVDAVLARLDPPPRAR--------F 1402
Cdd:PRK08315   174 fdellalgravDDAELAARQATLdpddPIniqYTSGTTGFPKGATLTHRNILNngYFIGEAMKLTEEDRLCipvplyhcF 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1403 AMVstigadLGhtVLfGALASGGALHLIdrdttldADRF--AQTLAAA---RIDVLKIVPGHLHALLqaeraadALPaht 1477
Cdd:PRK08315   254 GMV------LG--NL-ACVTHGATMVYP-------GEGFdpLATLAAVeeeRCTALYGVPTMFIAEL-------DHP--- 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1478 lvlggEATSWEL--LDT-IAALRPdC------RVHN--H-------YGPTETTVGIlTQPAAQACRAAATLPLGRPLDNN 1539
Cdd:PRK08315   308 -----DFARFDLssLRTgIMAGSP-CpievmkRVIDkmHmsevtiaYGMTETSPVS-TQTRTDDPLEKRVTTVGRALPHL 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1540 ETWLLDEHLN-PVGTGGTGELYLGGAGVALGYLHQPALTAARFVPhpfaagARLYRSGDRARRLADGSLEYLGRIDDQVk 1618
Cdd:PRK08315   381 EVKIVDPETGeTVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDA------DGWMHTGDLAVMDEEGYVNIVGRIKDMI- 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1619 IRG----YrvePGEIAARLKALDGVRDAAVIVVAGAR----LAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVID 1690
Cdd:PRK08315   454 IRGgeniY---PREIEEFLYTHPKIQDVQVVGVPDEKygeeVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVD 530

                   ....*....
gi 1888712850 1691 ALPLNRNGK 1699
Cdd:PRK08315   531 EFPMTVTGK 539
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
421-509 2.54e-08

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 58.85  E-value: 2.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  421 RLADGRIGEIHVSGPSVAHGYWQradasaqAFVDAPRHadgsgparwLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLY 499
Cdd:PRK07445   295 TIPANQTGNITIQAQSLALGYYP-------QILDSQGI---------FETDDLGYLdAQGYLHILGRNSQKIITGGENVY 358
                           90
                   ....*....|
gi 1888712850  500 PQDVEQAVEA 509
Cdd:PRK07445   359 PAEVEAAILA 368
PRK07798 PRK07798
acyl-CoA synthetase; Validated
20-269 2.74e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 59.13  E-value: 2.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   20 AHGLAARLRALAQQRPEATALIVidadGDTRYDYAQLDRRARALAARFARDGA-AAERALILMDSGVDYVSAFFGCLYAG 98
Cdd:PRK07798     2 AWNIADLFEAVADAVPDRVALVC----GDRRLTYAELEERANRLAHYLIAQGLgPGDHVGIYARNRIEYVEAMLGAFKAR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   99 VVAVPVYPPESKREqhlarLRGIARDAGVRYVLTTAALHERHADAWSMLaPGADVV--------------AVDTLDARDT 164
Cdd:PRK07798    78 AVPVNVNYRYVEDE-----LRYLLDDSDAVALVYEREFAPRVAEVLPRL-PKLRTLvvvedgsgndllpgAVDYEDALAA 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  165 PSDAPLHPVR-ADDLAFLqYTSGSTGSPKGVMVSH---------------GNLLANEIAIQAGLGVRPDDVFVSWLPLYH 228
Cdd:PRK07798   152 GSPERDFGERsPDDLYLL-YTGGTTGMPKGVMWRQedifrvllggrdfatGEPIEDEEELAKRAAAGPGMRRFPAPPLMH 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1888712850  229 DMGLIGSlLQPVFSGIPLVLMSPQYFleRPLRWLDAIARHR 269
Cdd:PRK07798   231 GAGQWAA-FAALFSGQTVVLLPDVRF--DADEVWRTIEREK 268
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
1197-1709 3.83e-08

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 59.17  E-value: 3.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1197 RARV---SAASVARRTPPGEPIHLRVARHADTQPDAPAVID-GALRMSYAELDARAAHVAQwLLARDLQGGEPVAIVAHR 1272
Cdd:PRK08633   596 KQAVfelSFDSWKSRKEALPPLAEAWIDTAKRNWSRLAVADsTGGELSYGKALTGALALAR-LLKRELKDEENVGILLPP 674
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1273 SARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCG-----------ARLVLCEDDCSALDLMGVQHarIDAAQEEAQ 1341
Cdd:PRK08633   675 SVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQiktvitsrkflEKLKNKGFDLELPENVKVIY--LEDLKAKIS 752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1342 REQHLRA-------PHAL------PAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLdpPPRARFAMVST- 1407
Cdd:PRK08633   753 KVDKLTAllaarllPARLlkrlygPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVF--NLRNDDVILSSl 830
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1408 -IGADLGHTV-LFGALASG-GALHLIDrdtTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPA--HTLVLGG 1482
Cdd:PRK08633   831 pFFHSFGLTVtLWLPLLEGiKVVYHPD---PTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFAslRLVVAGA 907
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1483 EATSWELLDTIAaLRPDCRVHNHYGPTETT------------VGILTQPAAQACRaaatlpLGRPLDNNETWLLD-EHLN 1549
Cdd:PRK08633   908 EKLKPEVADAFE-EKFGIRILEGYGATETSpvasvnlpdvlaADFKRQTGSKEGS------VGMPLPGVAVRIVDpETFE 980
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1550 PVGTGGTGELYLGGAGVALGYLHQPALTAARFVPhpfAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGY-----RV 1624
Cdd:PRK08633   981 ELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEmvplgAV 1057
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1625 EPgEIAARLKALDGVrdaaVIVVA------GARLAAFATPqpGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNG 1698
Cdd:PRK08633  1058 EE-ELAKALGGEEVV----FAVTAvpdekkGEKLVVLHTC--GAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSG 1130
                          570
                   ....*....|.
gi 1888712850 1699 KLDRQALSALA 1709
Cdd:PRK08633  1131 KLDLKGLKELA 1141
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
1240-1654 4.38e-08

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 58.25  E-value: 4.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVAL--DAGNPTQRLAQTLRDCGARLVLCE 1317
Cdd:cd05932      8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLypTLNPDTIRYVLEHSESKALFVGKL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1318 DDCSAL------DLMGVQHARIDAAQEEAQREQhLRAPHAL----PAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYV 1387
Cdd:cd05932     88 DDWKAMapgvpeGLISISLPPPSAANCQYQWDD-LIAQHPPleerPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1388 DAVLARLDPPPRARfaMVSTIgaDLGHT-----VLFGALASGGALHLIDrdttlDADRFAQTLAAARIDVLKIVPgHLHA 1462
Cdd:cd05932    167 QAGIEHIGTEENDR--MLSYL--PLAHVtervfVEGGSLYGGVLVAFAE-----SLDTFVEDVQRARPTLFFSVP-RLWT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1463 LLQaERAADALPAHTL---------------------------VLGGEAT--SWELLDTIAALRPDcrVHNHYGPTET-T 1512
Cdd:cd05932    237 KFQ-QGVQDKIPQQKLnlllkipvvnslvkrkvlkglgldqcrLAGCGSApvPPALLEWYRSLGLN--ILEAYGMTENfA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1513 VGILTQPaaqacRAAATLPLGRPLDNNEtwlldehlnpVGTGGTGELYLGGAGVALGYLHQPALTAARFVPHPFaagarl 1592
Cdd:cd05932    314 YSHLNYP-----GRDKIGTVGNAGPGVE----------VRISEDGEILVRSPALMMGYYKDPEATAEAFTADGF------ 372
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1888712850 1593 YRSGDRARRLADGSLEYLGRIDDQVKI-RGYRVEPGEIAARLKALDGVRdaaVIVVAGARLAA 1654
Cdd:cd05932    373 LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVE---MVCVIGSGLPA 432
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
1452-1709 4.77e-08

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 58.08  E-value: 4.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1452 VLKIVPGHLHALLQaeRAADALPAHTLVLGGEATSW-ELLDTIAALRpdCRVHNHYGPTETTVGILTQpaaqacraaatL 1530
Cdd:PRK07445   210 FLSLVPTQLQRLLQ--LRPQWLAQFRTILLGGAPAWpSLLEQARQLQ--LRLAPTYGMTETASQIATL-----------K 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1531 P---------LGRPLdnnetwlldEHLN-PVGTGGTGELYLGGAGVALGYlhqpaltaarfVPHPFAAgARLYRSGDRAR 1600
Cdd:PRK07445   275 PddflagnnsSGQVL---------PHAQiTIPANQTGNITIQAQSLALGY-----------YPQILDS-QGIFETDDLGY 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1601 RLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAAL 1676
Cdd:PRK07445   334 LDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPdphwGEVVTAIYVPKDPSISLEELKTAIKDQL 413
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1888712850 1677 LPdYMVPSVLRVIDALPLNRNGKLDRQALSALA 1709
Cdd:PRK07445   414 SP-FKQPKHWIPVPQLPRNPQGKINRQQLQQIA 445
PRK07529 PRK07529
AMP-binding domain protein; Validated
1184-1709 5.40e-08

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 58.04  E-value: 5.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1184 PTLATLDLLDADERARVSAASVARRTppgepiHLRVARHADTQPDAPAVI--------DGALRMSYAELDARAAHVAQWL 1255
Cdd:PRK07529     2 PAFATLADIEAIEAVPLAARDLPAST------YELLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1256 LARDLQGGEPVAIVAHRSARFVVAMLG---------------------VLKAGGAYVALDAGnPT------QRLAQTLRD 1308
Cdd:PRK07529    76 HSLGVGPGDVVAFLLPNLPETHFALWGgeaagianpinpllepeqiaeLLRAAGAKVLVTLG-PFpgtdiwQKVAEVLAA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1309 C----------GARLVLCEDDCSALDLMGVQHARIDAAQEEAQREQHLRAPHALPAVDPRSAAYViYTSGSSGAPKGVVI 1378
Cdd:PRK07529   155 LpelrtvvevdLARYLPGPKRLAVPLIRRKAHARILDFDAELARQPGDRLFSGRPIGPDDVAAYF-HTGGTTGMPKLAQH 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1379 AHGALTnyVDAvlarldppprarFAMVSTIGADLGHTVLFG---------------ALASGGALHLID----RDTTLdAD 1439
Cdd:PRK07529   234 THGNEV--ANA------------WLGALLLGLGPGDTVFCGlplfhvnallvtglaPLARGAHVVLATpqgyRGPGV-IA 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1440 RFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAHTLVLGGEAT-SWELLDTIAAlRPDCRVHNHYGPTETTVGILTQ 1518
Cdd:PRK07529   299 NFWKIVERYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPlPVEVFRRFEA-ATGVRIVEGYGLTEATCVSSVN 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1519 PAAQACRAAA---TLPLGR----PLDNNETWLLDehlnpVGTGGTGELYLGGAGVALGYLhqpalTAARfvPHPFAAGAR 1591
Cdd:PRK07529   378 PPDGERRIGSvglRLPYQRvrvvILDDAGRYLRD-----CAVDEVGVLCIAGPNVFSGYL-----EAAH--NKGLWLEDG 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1592 LYRSGDRARRLADGSLEYLGRIDDQVkIR-GYRVEPGEIAARLKALDGVRDAAVI----VVAGARLAAFATPQPGASLDA 1666
Cdd:PRK07529   446 WLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVgrpdAHAGELPVAYVQLKPGASATE 524
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1888712850 1667 AALKRALAALLPD-YMVPSVLRVIDALPLNRNGKLDRQALSALA 1709
Cdd:PRK07529   525 AELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPALRRDA 568
PLN02246 PLN02246
4-coumarate--CoA ligase
1214-1383 6.96e-08

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 57.68  E-value: 6.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1214 PIHLRVARHADTQPDAPAVIDGAL--RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYV 1291
Cdd:PLN02246    24 PLHDYCFERLSEFSDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1292 AldaGNP---TQRLAQTLRDCGARLVLCEDdCSALDLMGVQHAR------IDAAQEEAQREQHLRAP--HALPAVD--PR 1358
Cdd:PLN02246   104 T---ANPfytPAEIAKQAKASGAKLIITQS-CYVDKLKGLAEDDgvtvvtIDDPPEGCLHFSELTQAdeNELPEVEisPD 179
                          170       180
                   ....*....|....*....|....*
gi 1888712850 1359 SAAYVIYTSGSSGAPKGVVIAHGAL 1383
Cdd:PLN02246   180 DVVALPYSSGTTGLPKGVMLTHKGL 204
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1358-1709 9.44e-08

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 56.72  E-value: 9.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1358 RSAAYvIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRArfamVSTIGADLGH-----TVLFGALASGGALHLID- 1431
Cdd:cd05944      3 DVAAY-FHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDD----VLLCGLPLFHvngsvVTLLTPLASGAHVVLAGp 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1432 ---RDTTLdADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAAlRPDCRVHNHYGP 1508
Cdd:cd05944     78 agyRNPGL-FDNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFED-ATGLPVVEGYGL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1509 TETTVGI-LTQPAAQACRAAATLPLgrPLDNNETWLLD---EHLNPVGTGGTGELYLGGAGVALGYLHQPALTAArfvph 1584
Cdd:cd05944    156 TEATCLVaVNPPDGPKRPGSVGLRL--PYARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNA----- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1585 pfAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVI----VVAGARLAAFATPQP 1660
Cdd:cd05944    229 --FVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVgqpdAHAGELPVAYVQLKP 306
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1661 GASLDAAALKRALAALLPDY-MVPSVLRVIDALPLNRNGKLDRQALSALA 1709
Cdd:cd05944    307 GAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADA 356
PRK05857 PRK05857
fatty acid--CoA ligase;
26-590 1.23e-07

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 56.94  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   26 RLRALAQQRPEATALIviDADGDTRYDYAQLDRRARALAARFARDGAA-AERALILMDSGVDYVSAFFGCLYAGVVAVPV 104
Cdd:PRK05857    19 RVFEQARQQPEAIALR--RCDGTSALRYRELVAEVGGLAADLRAQSVSrGSRVLVISDNGPETYLSVLACAKLGAIAVMA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  105 ---YPPESkreqhLARLRGIARDAGV-----RYVLTTAALHERHADAWSMLAPGADVVAVDTLDARDTPSDAPlhPVRAD 176
Cdd:PRK05857    97 dgnLPIAA-----IERFCQITDPAAAlvapgSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA--DQGSE 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  177 DLAFLQYTSGSTGSPKGVMVSHGNLLA-NEIAIQAGLGvrpddvFVSW---------LPLYHdMGLIGSLLQPVFSGIPL 246
Cdd:PRK05857   170 DPLAMIFTSGTTGEPKAVLLANRTFFAvPDILQKEGLN------WVTWvvgettyspLPATH-IGGLWWILTCLMHGGLC 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  247 VLMSPQYFLERPLRWLDAIArhrgTISGAPDFAYRLCAE-RINDETRAKLDLsswrLAFSGSEPVRRDTlddfvaRFAPA 325
Cdd:PRK05857   243 VTGGENTTSLLEILTTNAVA----TTCLVPTLLSKLVSElKSANATVPSLRL----VGYGGSRAIAADV------RFIEA 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  326 -GFDAAALypcYGLAEAtlfvtgGVRGAGLVSHAFSSAALSAGraeaaradeaatvlvGCGAVQAGhrvaivaraaAESH 404
Cdd:PRK05857   309 tGVRTAQV---YGLSET------GCTALCLPTDDGSIVKIEAG---------------AVGRPYPG----------VDVY 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  405 ESHEADVETETSRAGErlaDGRIGEIHVSGPSVAHGYWQRADASAQAFVDAprhadgsgparWLRTGDLGFVH-DGQLYI 483
Cdd:PRK05857   355 LAATDGIGPTAPGAGP---SASFGTLWIKSPANMLGYWNNPERTAEVLIDG-----------WVNTGDLLERReDGFFYI 420
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  484 AGRVKDLVIVRGRNLYPQDVEQAVEA-------------HAEF-ARKGRVIAFGATLGGGETLGLALEIAPRMKKRfaaa 549
Cdd:PRK05857   421 KGRSSEMIICGGVNIAPDEVDRIAEGvsgvreaacyeipDEEFgALVGLAVVASAELDESAARALKHTIAARFRRE---- 496
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1888712850  550 qiVETLRRiafdacgetPAAIALLNPgaLPKTSSGKLQRAA 590
Cdd:PRK05857   497 --SEPMAR---------PSTIVIVTD--IPRTQSGKVMRAS 524
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1237-1612 1.77e-07

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 56.31  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1237 LRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQtlrdcgarlvlC 1316
Cdd:cd05910      1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQ-----------C 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1317 EDDCSALDLMGVQHARIDAAqeeaqreqhlraphalpavdprsaayVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDP 1396
Cdd:cd05910     70 LQEAEPDAFIGIPKADEPAA--------------------------ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1397 PPRAR----FAMVSTIGADLGHTVLFGALASggalhliDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQA-ERAAD 1471
Cdd:cd05910    124 RPGEVdlatFPLFALFGPALGLTSVIPDMDP-------TRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYcAQHGI 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1472 ALPAHTLVL-GGEATSWELLDTI-AALRPDCRVHNHYGPTE----TTVG---ILTQPAAQACRAAATLpLGRPLDNNE-- 1540
Cdd:cd05910    197 TLPSLRRVLsAGAPVPIALAARLrKMLSDEAEILTPYGATEalpvSSIGsreLLATTTAATSGGAGTC-VGRPIPGVRvr 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1541 ----------TWLLDEHLNPvgtGGTGELYLGGAGVALGYLHQPALTAARFVPHPfaAGARLYRSGDRARRLADGSLEYL 1610
Cdd:cd05910    276 iieiddepiaEWDDTLELPR---GEIGEITVTGPTVTPTYVNRPVATALAKIDDN--SEGFWHRMGDLGYLDDEGRLWFC 350

                   ..
gi 1888712850 1611 GR 1612
Cdd:cd05910    351 GR 352
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
159-512 1.87e-07

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 56.33  E-value: 1.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  159 LDARDTPSDAPLHPvrADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQA--GLGVRPDDVFVSWLPLYHDMGLiGSL 236
Cdd:PRK05620   166 LDGRSTVYDWPELD--ETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTtdSLAVTHGESFLCCVPIYHVLSW-GVP 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  237 LQPVFSGIPLVLMSPQYFLERpLRWLDAIARHRgTISGAPDFAYRLCAERINDETRAKldlsSWRLAFSGSEPVRRDTLD 316
Cdd:PRK05620   243 LAAFMSGTPLVFPGPDLSAPT-LAKIIATAMPR-VAHGVPTLWIQLMVHYLKNPPERM----SLQEIYVGGSAVPPILIK 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  317 DFVARFapaGFDaaaLYPCYGLAEatlfvTGGVrgaGLVSHAFSSAAlsagraeaaradeaatvlvgcGAVQAGHrvaiv 396
Cdd:PRK05620   317 AWEERY---GVD---VVHVWGMTE-----TSPV---GTVARPPSGVS---------------------GEARWAY----- 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  397 araaAESHESHEADVETETSRAGERLA--DGRIGEIHVSGPSVAHGYW----QRADASAQAFVDaprHADGSGPAR---- 466
Cdd:PRK05620   357 ----RVSQGRFPASLEYRIVNDGQVMEstDRNEGEIQVRGNWVTASYYhsptEEGGGAASTFRG---EDVEDANDRftad 429
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1888712850  467 -WLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAE 512
Cdd:PRK05620   430 gWLRTGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPE 477
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
634-691 1.92e-07

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 49.87  E-value: 1.92e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850  634 SALAALWCEALD-ARLALAPDAHFFASGGSSLSAARLVALIGARLGRRVALAQIFETPT 691
Cdd:pfam00550    1 ERLRELLAEVLGvPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPT 59
PRK07788 PRK07788
acyl-CoA synthetase; Validated
22-512 1.95e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 56.47  E-value: 1.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   22 GLAARLRAL-AQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGV 99
Cdd:PRK07788    49 GPFAGLVAHaARRAPDRAALI----DERGTLTYAELDEQSNALARGLLALGVRAGDGVaVLARNHRGFVLALYAAGKVGA 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  100 VAVpVYPPESKREQhlarLRGIARDAGVRYVLT----TAALHERHAD-----AWSMLAPGADVVA--VDTLD---ARDTP 165
Cdd:PRK07788   125 RII-LLNTGFSGPQ----LAEVAAREGVKALVYddefTDLLSALPPDlgrlrAWGGNPDDDEPSGstDETLDdliAGSST 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  166 SDAPLHPVRAddlAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLiGSLLQPVFSGIP 245
Cdd:PRK07788   200 APLPKPPKPG---GIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGW-AHLTLAMALGST 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  246 LVLMspQYFleRPLRWLDAIARHRGT-ISGAPDFAYRLCAerINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAP 324
Cdd:PRK07788   276 VVLR--RRF--DPEATLEDIAKHKATaLVVVPVMLSRILD--LGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGP 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  325 AgfdaaaLYPCYGLAEAtlfvtggvrgaglvshafSSAALSAGRAEAARADEAATVLVGCgavqaghrvaivaraaaesh 404
Cdd:PRK07788   350 V------LYNLYGSTEV------------------AFATIATPEDLAEAPGTVGRPPKGV-------------------- 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  405 esheaDVETETSRaGERLADGRIGEIHVSGPSVAHGYwqradasaqafvdaprhADGSGPAR---WLRTGDLG-FVHDGQ 480
Cdd:PRK07788   386 -----TVKILDEN-GNEVPRGVVGRIFVGNGFPFEGY-----------------TDGRDKQIidgLLSSGDVGyFDEDGL 442
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1888712850  481 LYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAE 512
Cdd:PRK07788   443 LFVDGRDDDMIVSGGENVFPAEVEDLLAGHPD 474
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
176-514 1.98e-07

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 55.90  E-value: 1.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  176 DDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGIPLVLmSPQYFL 255
Cdd:cd05937     87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLAL-SRKFSA 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  256 ERplRWLDAIArhrgtiSGAPDFAY--RLCAERINDETRAKLDLSSWRLAFSGSepVRRDTLDDFVARFApagfdAAALY 333
Cdd:cd05937    166 SQ--FWKDVRD------SGATIIQYvgELCRYLLSTPPSPYDRDHKVRVAWGNG--LRPDIWERFRERFN-----VPEIG 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  334 PCYGLAEATL---------FVTGGVRGAGLVSHAFSSAALsagraeaaradeaatVLVgcgavqaghrvaivaraaaesh 404
Cdd:cd05937    231 EFYAATEGVFaltnhnvgdFGAGAIGHHGLIRRWKFENQV---------------VLV---------------------- 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  405 eshEADVETET----SRAG--ERLADGRIGEIHVSGP----SVAHGYWQRADASAQAFV-DAPRHADGsgparWLRTGD- 472
Cdd:cd05937    274 ---KMDPETDDpirdPKTGfcVRAPVGEPGEMLGRVPfknrEAFQGYLHNEDATESKLVrDVFRKGDI-----YFRTGDl 345
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1888712850  473 LGFVHDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFA 514
Cdd:cd05937    346 LRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIA 387
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
79-515 2.71e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 55.80  E-value: 2.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   79 ILMDSGVDYVSAFFGCLYAGVVAVPVYPpeSKREQHLARlrgIARDAGVRYVLTTAALHERHADawsMLAPGADVVAVDT 158
Cdd:PRK13388    57 VLLGNTPEMLFWLAAAALGGYVLVGLNT--TRRGAALAA---DIRRADCQLLVTDAEHRPLLDG---LDLPGVRVLDVDT 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  159 LDARDTPSDAP-LHPVR---ADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIG 234
Cdd:PRK13388   129 PAYAELVAAAGaLTPHRevdAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMA 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  235 SLLQPVFSGIPLVLmsPQYFleRPLRWLDAIARHRGTI---SGAPdFAYRLCAERINDETRAKLdlsswRLAFsGSEPVR 311
Cdd:PRK13388   209 GWAPAVASGAAVAL--PAKF--SASGFLDDVRRYGATYfnyVGKP-LAYILATPERPDDADNPL-----RVAF-GNEASP 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  312 RDtLDDFVARFapagfdAAALYPCYGLAEatlfvtggvrGAGLVSHAFSSAALSAGRAEaaradeaatvlVGCGAVqagh 391
Cdd:PRK13388   278 RD-IAEFSRRF------GCQVEDGYGSSE----------GAVIVVREPGTPPGSIGRGA-----------PGVAIY---- 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  392 rvaivaraaaeshesheaDVETETSRAGERL-ADGR-------IGEI-HVSGPSVAHGYWQRADAsaqafvDAPRHADGs 462
Cdd:PRK13388   326 ------------------NPETLTECAVARFdAHGAllnadeaIGELvNTAGAGFFEGYYNNPEA------TAERMRHG- 380
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1888712850  463 gparWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFAR 515
Cdd:PRK13388   381 ----MYWSGDLAYRDaDGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINR 430
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
1628-1699 5.06e-07

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 49.08  E-value: 5.06e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1888712850 1628 EIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGK 1699
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPdelkGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
162-310 5.23e-07

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 54.87  E-value: 5.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  162 RDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSH-GNLLANEIAIQAGLGVRPDDVF-----VSWLPlYHDMGLIGS 235
Cdd:cd05966    217 AKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTgGYLLYAATTFKYVFDYHPDDIYwctadIGWIT-GHSYIVYGP 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  236 LL----QPVFSGIPLVlmsPQyflerPLRWLDAIARHRGTI-SGAPDfAYRLCAeRINDETRAKLDLSSWRLAFSGSEPV 310
Cdd:cd05966    296 LAngatTVMFEGTPTY---PD-----PGRYWDIVEKHKVTIfYTAPT-AIRALM-KFGDEWVKKHDLSSLRVLGSVGEPI 365
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
1239-1618 6.19e-07

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 54.53  E-value: 6.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1239 MSYAELDARAAHVAQWLLARdlqGGEP-----VAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARL 1313
Cdd:cd05927      6 ISYKEVAERADNIGSALRSL---GGKPapasfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1314 VLCEDDCSALDLmgvqharidaAQEEAQREQHlRAPHALPavDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLAR 1393
Cdd:cd05927     83 VFCDAGVKVYSL----------EEFEKLGKKN-KVPPPPP--KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKI 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1394 LD--PPPRARFAMVSTIgaDLGHT----VLFGALASGGALHLIDRDTTLDADrfaqTLAAARIDVLKIVP---GHLHALL 1464
Cdd:cd05927    150 LEilNKINPTDVYISYL--PLAHIfervVEALFLYHGAKIGFYSGDIRLLLD----DIKALKPTVFPGVPrvlNRIYDKI 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1465 QAERAADALPAHTL------------------------------------------VLGGEATSWELLDTIAALrPDCRV 1502
Cdd:cd05927    224 FNKVQAKGPLKRKLfnfalnyklaelrsgvvraspfwdklvfnkikqalggnvrlmLTGSAPLSPEVLEFLRVA-LGCPV 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1503 HNHYGPTETTVGI-LTQPAAQACRAaatlpLGRPLDNNETWLLD-EHLN--PVGTGGTGELYLGGAGVALGYLHQPALTA 1578
Cdd:cd05927    303 LEGYGQTECTAGAtLTLPGDTSVGH-----VGGPLPCAEVKLVDvPEMNydAKDPNPRGEVCIRGPNVFSGYYKDPEKTA 377
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1888712850 1579 ARFVPHPFaagarlYRSGDRARRLADGSLeylgRIDDQVK 1618
Cdd:cd05927    378 EALDEDGW------LHTGDIGEWLPNGTL----KIIDRKK 407
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
1238-1647 6.20e-07

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 54.77  E-value: 6.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1238 RMSYAELDARAAHVAQWLLARDLQGGepVAIVAHRSARFVVAMLGVLKAGGAyVALDAG-----NPTQRLAQTLRDC--- 1309
Cdd:PRK05851    31 RHPWPEVHGRAENVAARLLDRDRPGA--VGLVGEPTVELVAAIQGAWLAGAA-VSILPGpvrgaDDGRWADATLTRFagi 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1310 GARLVLCEDdcSALDLMGVQHARIdaAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDA 1389
Cdd:PRK05851   108 GVRTVLSHG--SHLERLRAVDSSV--TVHDLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRG 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1390 VLARLD-PPPRARFAMVSTIGADLGHTVLFGALASGGALHLI------------------DRDTTLDADRFAQTLAAARI 1450
Cdd:PRK05851   184 LNARVGlDAATDVGCSWLPLYHDMGLAFLLTAALAGAPLWLApttafsaspfrwlswlsdSRATLTAAPNFAYNLIGKYA 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1451 DVLKIVpgHLHALLQAERAADALPAHTLVLGGEATSWELLDTIAALrpdcrvhNHYGPTETTVGILT-QPAAQACRAAAT 1529
Cdd:PRK05851   264 RRVSDV--DLGALRVALNGGEPVDCDGFERFATAMAPFGFDAGAAA-------PSYGLAESTCAVTVpVPGIGLRVDEVT 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1530 LP----------LGRPLDNNETWLL-DEHLNPVGTGGTGELYLGGAGVALGYLHQPALTAARFvphpFAAGARLYrsgdr 1598
Cdd:PRK05851   335 TDdgsgarrhavLGNPIPGMEVRISpGDGAAGVAGREIGEIEIRGASMMSGYLGQAPIDPDDW----FPTGDLGY----- 405
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1888712850 1599 arrLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVIVV 1647
Cdd:PRK05851   406 ---LVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAV 451
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
20-605 6.24e-07

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 54.80  E-value: 6.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   20 AHGLAARLRALAQQRPeatALIVIDADGDTR-YDYAQLDRRARALAARFARDGAA-AERALILMDSGVDYVSAFFGCLYA 97
Cdd:cd05968     63 VEQLLDKWLADTRTRP---ALRWEGEDGTSRtLTYGELLYEVKRLANGLRALGVGkGDRVGIYLPMIPEIVPAFLAVARI 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   98 GVVAVPVYppeSKREQHLARLRgiARDAGVRYVLTTAALHER--------HADAWSMLAPGADVVAVdtldARDTPSDAP 169
Cdd:cd05968    140 GGIVVPIF---SGFGKEAAATR--LQDAEAKALITADGFTRRgrevnlkeEADKACAQCPTVEKVVV----VRHLGNDFT 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  170 LHPVR-------------------ADDLAFLQYTSGSTGSPKGVMVSHGNL-LANEIAIQAGLGVRPDDVfVSWLPlyhD 229
Cdd:cd05968    211 PAKGRdlsydeeketagdgaerteSEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDL-LTWFT---D 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  230 MG-LIGSLLqpVFSGIplvLMSPQYFL-------ERPLRWLDAIARHRGTISGAPDFAYRLCAERiNDETRAKLDLSSWR 301
Cdd:cd05968    287 LGwMMGPWL--IFGGL---ILGATMVLydgapdhPKADRLWRMVEDHEITHLGLSPTLIRALKPR-GDAPVNAHDLSSLR 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  302 LAFSGSEPVRRDTLDDFvarFAPAGFDAAALYPCYGLAEatlfVTGGVRGAGLVS--HAFSSAALSAGRaeaaradeaat 379
Cdd:cd05968    361 VLGSTGEPWNPEPWNWL---FETVGKGRNPIINYSGGTE----ISGGILGNVLIKpiKPSSFNGPVPGM----------- 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  380 vlvgcgavqaghrvaivaraaaesheshEADVETETSRAgerlADGRIGEIHVSGP--SVAHGYWQRADASAQAFVDapr 457
Cdd:cd05968    423 ----------------------------KADVLDESGKP----ARPEVGELVLLAPwpGMTRGFWRDEDRYLETYWS--- 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  458 hadgSGPARWLRtGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFAR----------KGRVIAFGATL 526
Cdd:cd05968    468 ----RFDNVWVH-GDFAYYdEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLEsaaigvphpvKGEAIVCFVVL 542
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  527 GGGETLGLALEiaprmkkrfaaaqivETLRRIAFDACGETPAAIALLNPGALPKTSSGKLQRAATREGWRARTL-DLYAL 605
Cdd:cd05968    543 KPGVTPTEALA---------------EELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELgDLSSL 607
PLN02654 PLN02654
acetate-CoA ligase
1238-1709 8.01e-07

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 54.52  E-value: 8.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1238 RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCe 1317
Cdd:PLN02654   120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT- 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1318 ddCSALDlMGVQ----HARIDAAQEEAQRE-----------------------QHLRA----------PHALPA--VDPR 1358
Cdd:PLN02654   199 --CNAVK-RGPKtinlKDIVDAALDESAKNgvsvgicltyenqlamkredtkwQEGRDvwwqdvvpnyPTKCEVewVDAE 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1359 SAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLAR-LDPPPRARFAMVSTIGADLGHT-VLFGALASGGALHLIDRDTTL 1436
Cdd:PLN02654   276 DPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYaFDYKPTDVYWCTADCGWITGHSyVTYGPMLNGATVLVFEGAPNY 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1437 -DADRFAQTLAAARIDVLKIVPGHLHALLQA--ERAADALPAHTLVLG--GEA---TSWE-LLDTIAALRpdCRVHNHYG 1507
Cdd:PLN02654   356 pDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDgdEYVTRHSRKSLRVLGsvGEPinpSAWRwFFNVVGDSR--CPISDTWW 433
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1508 PTETTvGILTQPaaqacraaatLPLGRPLDNNETWLLDEHLNPV-----GTGGTGEL--YLGGAGVALGYLHQPALTAAR 1580
Cdd:PLN02654   434 QTETG-GFMITP----------LPGAWPQKPGSATFPFFGVQPVivdekGKEIEGECsgYLCVKKSWPGAFRTLYGDHER 502
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1581 FVPHPFAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVI----VVAGARLAAFA 1656
Cdd:PLN02654   503 YETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVgiehEVKGQGIYAFV 582
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1888712850 1657 TPQPGASLDAAALKRALAALLPD---YMVPSVLRVIDALPLNRNGKLDRQALSALA 1709
Cdd:PLN02654   583 TLVEGVPYSEELRKSLILTVRNQigaFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 638
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
145-592 8.33e-07

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 54.24  E-value: 8.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  145 SMLAPGADVvavDTLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMV-SHGNLLANEIAIQAGLGVRPDDVF--- 220
Cdd:cd05967    202 DLTKPGRDL---DWSELLAKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRdNGGHAVALNWSMRNIYGIKPGDVWwaa 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  221 --VSWLpLYHDMGLIGSLLQpvfsGIPLVLmspqyFLERPLRWLDA------IARHRGT-ISGAPDfAYRLCAERINDET 291
Cdd:cd05967    279 sdVGWV-VGHSYIVYGPLLH----GATTVL-----YEGKPVGTPDPgafwrvIEKYQVNaLFTAPT-AIRAIRKEDPDGK 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  292 RAKL-DLSSWRLAFSGSEPvrrdtLDdfvarfapagfdaaalYPCYGLAEATLfvtggvrGAGLVSHAF---SSAALSAG 367
Cdd:cd05967    348 YIKKyDLSSLRTLFLAGER-----LD----------------PPTLEWAENTL-------GVPVIDHWWqteTGWPITAN 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  368 RaeaaradeaatVLVGCGAVQAGHRVAIVAraaaesheSHEADVETETsraGERLADGRIGEIHVSGP---SVAHGYWQR 444
Cdd:cd05967    400 P-----------VGLEPLPIKAGSPGKPVP--------GYQVQVLDED---GEPVGPNELGNIVIKLPlppGCLLTLWKN 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  445 ADASAQAFVDaprHADGsgparWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH---AEFArkgrVI 520
Cdd:cd05967    458 DERFKKLYLS---KFPG-----YYDTGDAGYKdEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHpavAECA----VV 525
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850  521 AFGATLGGGETLGLALeiaPRMKKRFAAAQIVETLRRIAFDACGETPAAIALLNPGALPKTSSGKLQRAATR 592
Cdd:cd05967    526 GVRDELKGQVPLGLVV---LKEGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
1208-1392 1.41e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 53.58  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1208 RTPPGEPIHLRVARHADTQPDAPA--------VIDGALR-MSYAELDARAAHVAqwllARDLQGGEP---VAIVAHRSAR 1275
Cdd:PRK07769    16 RFPPNTNLVRHVERWAKVRGDKLAyrfldfstERDGVARdLTWSQFGARNRAVG----ARLQQVTKPgdrVAILAPQNLD 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1276 FVVAMLGVLKAGGAYVAL-DAGNP--TQRLAQTLRDCGARLVLCEDDCSA------LDLMGVQHARI---DAAQEEaqre 1343
Cdd:PRK07769    92 YLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEgvrkffRARPAKERPRViavDAVPDE---- 167
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1344 qhLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGAL-TNYVDAVLA 1392
Cdd:PRK07769   168 --VGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLpTNVLQVIDA 215
PRK05691 PRK05691
peptide synthase; Validated
48-691 1.79e-06

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 53.63  E-value: 1.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   48 DTRYDYAQLDRRARALAARFARDGAAAERAL-ILMDSGVDYVSAFFGCLYAGVVAVPVYPPESkreqhLARLRGIARDAG 126
Cdd:PRK05691  3743 DQQWSYAELNRAANRLGHALRAAGVGVDQPVaLLAERGLDLLGMIVGSFKAGAGYLPLDPGLP-----AQRLQRIIELSR 3817
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  127 VRYVLTTAALHERHADAWSML--APGADVVAVDTLDARDTPSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLAN 204
Cdd:PRK05691  3818 TPVLVCSAACREQARALLDELgcANRPRLLVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNN 3897
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  205 EIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFSGipLVLMSPQYFLERPLRWLDAIARHRGTI-SGAPDFAYRLC 283
Cdd:PRK05691  3898 QLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGA--RVEIVPNAIAHDPQGLLAHVQAQGITVlESVPSLIQGML 3975
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  284 AerindETRAKLDLSSWRLAFSGSEPvrRDTLDDFVARFAPAGfdaaaLYPCYGLAEATLFVtggvrgaglvshAFSSAA 363
Cdd:PRK05691  3976 A-----EDRQALDGLRWMLPTGEAMP--PELARQWLQRYPQIG-----LVNAYGPAECSDDV------------AFFRVD 4031
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  364 LsagraeaaradeaatvlvgcgavqaghrvaivaraaaESHESHEADVETETSRAGERLAD--------GRIGEIHVSGP 435
Cdd:PRK05691  4032 L-------------------------------------ASTRGSYLPIGSPTDNNRLYLLDealelvplGAVGELCVAGT 4074
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  436 SVAHGYWQRADASAQAFVDAPRHADGSgpaRWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFa 514
Cdd:PRK05691  4075 GVGRGYVGDPLRTALAFVPHPFGAPGE---RLYRTGDLARRRsDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEV- 4150
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  515 RKGRVIAFGATLG--------GGETLGLALEIAPRMKKRFaAAQIVETLrriafdacgeTPAAIALLNpgALPKTSSGKL 586
Cdd:PRK05691  4151 REAAVAVQEGVNGkhlvgylvPHQTVLAQGALLERIKQRL-RAELPDYM----------VPLHWLWLD--RLPLNANGKL 4217
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  587 QRAATregwraRTLDLYALWEQgafviggdddaarapDAPAALDARESALAALWCEALDARLALAPDaHFFASGGSSLSA 666
Cdd:PRK05691  4218 DRKAL------PALDIGQLQSQ---------------AYLAPRNELEQTLATIWADVLKVERVGVHD-NFFELGGHSLLA 4275
                          650       660
                   ....*....|....*....|....*
gi 1888712850  667 ARLVALIGARLGRRVALAQIFETPT 691
Cdd:PRK05691  4276 TQIASRVQKALQRNVPLRAMFECST 4300
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
469-588 2.04e-06

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 52.63  E-value: 2.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  469 RTGDLGFVHDGQ----------LYIAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAfgATLGGGETLGLALEI 538
Cdd:cd05913    294 RTRDITRLLPGPcpcgrthrriDRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLIL--TRQEHLDELTIKVEV 371
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1888712850  539 AP---RMKKRFAAAQIVETLRRiafDACGETPaAIALLNPGALPKtSSGKLQR 588
Cdd:cd05913    372 RPeadDDEKLEALKQRLERHIK---SVLGVTV-EVELVEPGSLPR-SEGKAKR 419
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
421-510 2.49e-06

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 52.57  E-value: 2.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  421 RLADGrigEIHVSGPSVAHGYWQraDASAQAFVDAprhaDGsgparWLRTGDLGFVHDGQLYIAGRVKDLVIVRGRNLYP 500
Cdd:PRK09029   301 KLVDG---EIWLRGASLALGYWR--QGQLVPLVND----EG-----WFATRDRGEWQNGELTILGRLDNLFFSGGEGIQP 366
                           90
                   ....*....|
gi 1888712850  501 QDVEQAVEAH 510
Cdd:PRK09029   367 EEIERVINQH 376
PLN02479 PLN02479
acetate-CoA ligase
423-593 2.55e-06

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 52.54  E-value: 2.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  423 ADGR-IGEIHVSGPSVAHGYWQRADASAQAFvdaprhADGsgparWLRTGDLGFVH-DGQLYIAGRVKDLVIVRGRNLYP 500
Cdd:PLN02479   397 ADGKtMGEIVMRGNMVMKGYLKNPKANEEAF------ANG-----WFHSGDLGVKHpDGYIEIKDRSKDIIISGGENISS 465
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  501 QDVEQAVEAHAEFArKGRVIAfGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRriafdACGE------TPAAIALln 574
Cdd:PLN02479   466 LEVENVVYTHPAVL-EASVVA-RPDERWGESPCAFVTLKPGVDKSDEAALAEDIMK-----FCRErlpaywVPKSVVF-- 536
                          170       180
                   ....*....|....*....|...
gi 1888712850  575 pGALPKTSSGKLQ----RAATRE 593
Cdd:PLN02479   537 -GPLPKTATGKIQkhvlRAKAKE 558
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
421-590 2.92e-06

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 51.97  E-value: 2.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  421 RLADGRIgeiHVSGPSVAHGYwqradasaqafVDAPRHADGSGPArWLRTGDLGFVHDGQLYIAGRVKDLVIVRGRNLYP 500
Cdd:PRK07824   204 RVEDGRI---ALGGPTLAKGY-----------RNPVDPDPFAEPG-WFRTDDLGALDDGVLTVLGRADDAISTGGLTVLP 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  501 QDVEQAVEAHAEFArkgrviafgatlgGGETLGLAleiAPRMKKRFAAA--------QIVETLRRIAFDACGETPAAIAL 572
Cdd:PRK07824   269 QVVEAALATHPAVA-------------DCAVFGLP---DDRLGQRVVAAvvgdggpaPTLEALRAHVARTLDRTAAPREL 332
                          170
                   ....*....|....*...
gi 1888712850  573 LNPGALPKTSSGKLQRAA 590
Cdd:PRK07824   333 HVVDELPRRGIGKVDRRA 350
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
1221-1709 8.06e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 51.29  E-value: 8.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1221 RHADTQPDAPAVI----DGAL--RMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALD 1294
Cdd:PRK00174    75 RHLKTRGDKVAIIwegdDPGDsrKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVF 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1295 AGNPTQRLAQTLRDCGARLVLCED---------------DcSALDLMG-------VQHARIDAAQEE-----------AQ 1341
Cdd:PRK00174   155 GGFSAEALADRIIDAGAKLVITADegvrggkpiplkanvD-EALANCPsvekvivVRRTGGDVDWVEgrdlwwhelvaGA 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1342 REQHlrAPHALPAVDPrsaAYVIYTSGSSGAPKGVV------IAHGALTN-YVdavlarLDPPPRARFAMVSTIGADLGH 1414
Cdd:PRK00174   234 SDEC--EPEPMDAEDP---LFILYTSGSTGKPKGVLhttggyLVYAAMTMkYV------FDYKDGDVYWCTADVGWVTGH 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1415 T-VLFGALASGGalhlidrdTTL---------DADRFAQTLAAARIDVLKIVPGHLHALLqaeRAADALPAHT----L-V 1479
Cdd:PRK00174   303 SyIVYGPLANGA--------TTLmfegvpnypDPGRFWEVIDKHKVTIFYTAPTAIRALM---KEGDEHPKKYdlssLrL 371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1480 LG--GE-----ATSWelldtiaalrpdcrVHNHYG----P-------TETTvGILTQPaaqacraaatLP---------L 1532
Cdd:PRK00174   372 LGsvGEpinpeAWEW--------------YYKVVGgercPivdtwwqTETG-GIMITP----------LPgatplkpgsA 426
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1533 GRPLDNNETWLLDEHLNPVGtggtgelylGGAGvalGYL----------------HQpaltaaRFVPHPFAAGARLYRSG 1596
Cdd:PRK00174   427 TRPLPGIQPAVVDEEGNPLE---------GGEG---GNLvikdpwpgmmrtiygdHE------RFVKTYFSTFKGMYFTG 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1597 DRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVI----VVAGARLAAFATPQPGASLDaaalkra 1672
Cdd:PRK00174   489 DGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVgrpdDIKGQGIYAFVTLKGGEEPS------- 561
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1888712850 1673 laallpDYMV----------------PSVLRVIDALPLNRNGKLDRQALSALA 1709
Cdd:PRK00174   562 ------DELRkelrnwvrkeigpiakPDVIQFAPGLPKTRSGKIMRRILRKIA 608
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
167-228 9.59e-06

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 51.00  E-value: 9.59e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1888712850  167 DAPLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVR-----PDDVFVSWLPLYH 228
Cdd:PLN02861   211 DCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTdrvatEEDSYFSYLPLAH 277
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
1239-1425 1.28e-05

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 50.53  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1239 MSYAELDARAAHVAQWLLARD-LQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCe 1317
Cdd:cd17632     68 ITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV- 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1318 dDCSALDL----------------------MGVQHARIDAAQEE--------------AQREQHLRAPHAL-PAVDPRSA 1360
Cdd:cd17632    147 -SAEHLDLaveavleggtpprlvvfdhrpeVDAHRAALESARERlaavgipvttltliAVRGRDLPPAPLFrPEPDDDPL 225
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850 1361 AYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRA----RFAMVSTIGadlGHTVLFGALASGG 1425
Cdd:cd17632    226 ALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPAsitlNFMPMSHIA---GRISLYGTLARGG 291
PRK05850 PRK05850
acyl-CoA synthetase; Validated
1223-1380 1.29e-05

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 50.33  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1223 ADTQPDAPAV--ID-------GALRMSYAELDARAAHVAQWLlARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVAL 1293
Cdd:PRK05850    11 ASLQPDDAAFtfIDyeqdpagVAETLTWSQLYRRTLNVAEEL-RRHGSTGDRAVILAPQGLEYIVAFLGALQAGLIAVPL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1294 DA---GNPTQRLAQTLRDCGARLVLC----EDDCSA-LDLMGVQHA----RIDAAQEEAQREQHLRaphalpAVDPRSAA 1361
Cdd:PRK05850    90 SVpqgGAHDERVSAVLRDTSPSVVLTtsavVDDVTEyVAPQPGQSAppviEVDLLDLDSPRGSDAR------PRDLPSTA 163
                          170
                   ....*....|....*....
gi 1888712850 1362 YVIYTSGSSGAPKGVVIAH 1380
Cdd:PRK05850   164 YLQYTSGSTRTPAGVMVSH 182
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
147-236 1.57e-05

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 50.15  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  147 LAPGADVVAVDTLDARDTPSDAPLHPVR----ADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDD-VFV 221
Cdd:cd17632    190 LAAVGIPVTTLTLIAVRGRDLPPAPLFRpepdDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPAsITL 269
                           90
                   ....*....|....*...
gi 1888712850  222 SWLPLYHDMG---LIGSL 236
Cdd:cd17632    270 NFMPMSHIAGrisLYGTL 287
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
1236-1392 1.71e-05

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 50.12  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1236 ALRMSYAELDARAAHVAQwLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDA---GNPTQRLAQTLRDCGAR 1312
Cdd:PRK12476    66 AVELTWTQLGVRLRAVGA-RLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFApelPGHAERLDTALRDAEPT 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1313 LVLceddcsaldlmgVQHARIDAAQEEAQREQHLRAPHALpAVD--PRSA--------------AYVIYTSGSSGAPKGV 1376
Cdd:PRK12476   145 VVL------------TTTAAAEAVEGFLRNLPRLRRPRVI-AIDaiPDSAgesfvpveldtddvSHLQYTSGSTRPPVGV 211
                          170
                   ....*....|....*..
gi 1888712850 1377 VIAHGAL-TNYVDAVLA 1392
Cdd:PRK12476   212 EITHRAVgTNLVQMILS 228
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
1222-1376 1.85e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 49.62  E-value: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1222 HADTQPDAPAVI--DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPT 1299
Cdd:PRK13390     6 HAQIAPDRPAVIvaETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1300 QRLAQTLRDCGARLVlceddcsaldlmgVQHARIDAAQEEAQREQHLRAP------------HALPAVDPRSA-----AY 1362
Cdd:PRK13390    86 PEADYIVGDSGARVL-------------VASAALDGLAAKVGADLPLRLSfggeidgfgsfeAALAGAGPRLTeqpcgAV 152
                          170
                   ....*....|....
gi 1888712850 1363 VIYTSGSSGAPKGV 1376
Cdd:PRK13390   153 MLYSSGTTGFPKGI 166
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
1213-1705 1.93e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 50.03  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1213 EPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVA 1292
Cdd:PRK06710    24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1293 LDAGNPTQRLAQTLRDCGARLVLCEDDC--------SALDLMGVQHARI--------DAAQEEAQREQ------------ 1344
Cdd:PRK06710   104 TNPLYTERELEYQLHDSGAKVILCLDLVfprvtnvqSATKIEHVIVTRIadflpfpkNLLYPFVQKKQsnlvvkvseset 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1345 -HL-------RAPHALPAVDPRS-AAYVIYTSGSSGAPKGVVIAHGALT-----------NYVDAVLARLDPPPrarFAM 1404
Cdd:PRK06710   184 iHLwnsvekeVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNLVsntlmgvqwlyNCKEGEEVVLGVLP---FFH 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1405 VSTIGADLGHTVLfgalaSGGALHLIDRdttLDADRFAQTLAAARIDVLKIVPGHLHALLQAE--RAADALPAHTLVLGG 1482
Cdd:PRK06710   261 VYGMTAVMNLSIM-----QGYKMVLIPK---FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPllKEYDISSIRACISGS 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1483 EATSWELLDTIAALRPDCRVHNhYGPTETTvgiltqPAAQACRA-AATLP--LGRPLDNNETWLLD----EHLNPvgtGG 1555
Cdd:PRK06710   333 APLPVEVQEKFETVTGGKLVEG-YGLTESS------PVTHSNFLwEKRVPgsIGVPWPDTEAMIMSletgEALPP---GE 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1556 TGELYLGGAGVALGYLHQPALTAArfvphpfAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKA 1635
Cdd:PRK06710   403 IGEIVVKGPQIMKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYE 475
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1888712850 1636 LDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQAL 1705
Cdd:PRK06710   476 HEKVQEVVTIGVPdpyrGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1219-1629 2.00e-05

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 49.67  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTqpdaPAVIDGALRMSYAELDARAAHVAQWLLAR-DLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALdagN 1297
Cdd:PRK08974    33 VARYADQ----PAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNV---N 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1298 P--TQR-LAQTLRDCGAR-LVLCEDDCSALD--------------LMGVQHAR-----IDAAQEEAQR---EQHLraPHA 1351
Cdd:PRK08974   106 PlyTPReLEHQLNDSGAKaIVIVSNFAHTLEkvvfktpvkhviltRMGDQLSTakgtlVNFVVKYIKRlvpKYHL--PDA 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1352 L----------------PAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVST------IG 1409
Cdd:PRK08974   184 IsfrsalhkgrrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELVVTalplyhIF 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1410 ADLGHTVLFGALASGGALHLIDRDTtldaDRFAQTLAAARIDVLKIVPGHLHALLQAERAADA-LPAHTLVLGGE----- 1483
Cdd:PRK08974   264 ALTVNCLLFIELGGQNLLITNPRDI----PGFVKELKKYPFTAITGVNTLFNALLNNEEFQELdFSSLKLSVGGGmavqq 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1484 --ATSWELLDtiaalrpDCRVHNHYGPTETTVGILTQPAAQACRAAAtlpLGRPLDNNETWLLDEHLNPVGTGGTGELYL 1561
Cdd:PRK08974   340 avAERWVKLT-------GQYLLEGYGLTECSPLVSVNPYDLDYYSGS---IGLPVPSTEIKLVDDDGNEVPPGEPGELWV 409
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1888712850 1562 GGAGVALGYLHQPALTAARFVPHPFAagarlyrSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEI 1629
Cdd:PRK08974   410 KGPQVMLGYWQRPEATDEVIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEI 470
PRK13382 PRK13382
bile acid CoA ligase;
169-514 2.66e-05

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 49.37  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  169 PLHPVRADDLAFLqyTSGSTGSPKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGligsllqpvFSGIPLVL 248
Cdd:PRK13382   191 PEPTGRKGRVILL--TSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWG---------FSQLVLAA 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  249 MSPQYFLER----PLRWLDAIARHRGT-ISGAPDFAYRLCaeRINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFA 323
Cdd:PRK13382   260 SLACTIVTRrrfdPEATLDLIDRHRATgLAVVPVMFDRIM--DLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFG 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  324 PAgfdaaaLYPCYGLAEATLFVTGgvrgaglvshafSSAALSAGRAEAARADEAATVLVgcgavqaghrvaivarAAAES 403
Cdd:PRK13382   338 DV------IYNNYNATEAGMIATA------------TPADLRAAPDTAGRPAEGTEIRI----------------LDQDF 383
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  404 HEsheadvetetsragerLADGRIGEIHVSGPSVAHGYwqrADASAQAFVDAprhadgsgparWLRTGDLGFVHD-GQLY 482
Cdd:PRK13382   384 RE----------------VPTGEVGTIFVRNDTQFDGY---TSGSTKDFHDG-----------FMASGDVGYLDEnGRLF 433
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1888712850  483 IAGRVKDLVIVRGRNLYPQDVEQAVEAHAEFA 514
Cdd:PRK13382   434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVA 465
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1344-1429 2.72e-05

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 49.32  E-value: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1344 QHLRAPH-ALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDPPPRARFAMVSTIGADLGHTV-LFGAL 1421
Cdd:PRK08043   350 AHLLMPRlAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVgLFTPL 429

                   ....*...
gi 1888712850 1422 ASGGALHL 1429
Cdd:PRK08043   430 LTGAEVFL 437
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
27-514 3.07e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 49.22  E-value: 3.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   27 LRALAQQRPEATALIvidaDGDTRYDYAQLDRRARALAARFARDGAAAERALILM-DSGVDYVSAFFGCLYAGVVAVPVy 105
Cdd:PRK13383    41 LAVTAARWPGRTAII----DDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMcRNGRGFVTAVFAVGLLGADVVPI- 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  106 ppesKREQHLARLRGIARDAGVRYVLTTAALHERHAdawsmlAPGADVVAVD--TLDARDTPSdaplHPVRADDLAFLQY 183
Cdd:PRK13383   116 ----STEFRSDALAAALRAHHISTVVADNEFAERIA------GADDAVAVIDpaTAGAEESGG----RPAVAAPGRIVLL 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  184 TSGSTGSPKGVmvshgnllANEIAIQAGLGV----------RPDDVFVSWLPLYHDMGLIGSLLQPVFSGIplVLMSPQY 253
Cdd:PRK13383   182 TSGTTGKPKGV--------PRAPQLRSAVGVwvtildrtrlRTGSRISVAMPMFHGLGLGMLMLTIALGGT--VLTHRHF 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  254 FLERPLRwldAIARHRG-TISGAPDFAYRLCaeRINDETRAKLDLSSWRLAFSGSepvrrDTLDDFVA-RFAPAGFDAaa 331
Cdd:PRK13383   252 DAEAALA---QASLHRAdAFTAVPVVLARIL--ELPPRVRARNPLPQLRVVMSSG-----DRLDPTLGqRFMDTYGDI-- 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  332 LYPCYGLAEATLfvtggvrgaglvshafssAALSAGRAEAARADEAATVLVGCGAvqaghrvaivaraaaeshesheadv 411
Cdd:PRK13383   320 LYNGYGSTEVGI------------------GALATPADLRDAPETVGKPVAGCPV------------------------- 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  412 eTETSRAGERLADGRIGEIHVSGPSVAHGYwqrADASAQAFVDAprhadgsgparWLRTGDLGFVHD-GQLYIAGRVKDL 490
Cdd:PRK13383   357 -RILDRNNRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVVDG-----------MTSTGDMGYLDNaGRLFIVGREDDM 421
                          490       500
                   ....*....|....*....|....
gi 1888712850  491 VIVRGRNLYPQDVEQAVEAHAEFA 514
Cdd:PRK13383   422 IISGGENVYPRAVENALAAHPAVA 445
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1716-1812 4.03e-05

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 44.16  E-value: 4.03e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  1716 REAARAAPQGETETALAQCWAALLDpsngtdnatdnatATPSLTIARDDSFFALGGHSLAAMRLASRVRSRWSVELPLRE 1795
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLG-------------HAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATL 68
                            90
                    ....*....|....*..
gi 1888712850  1796 IFASPTLAALAARIEAQ 1812
Cdd:smart00823   69 VFDHPTPAALAEHLAAE 85
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
1240-1448 7.52e-05

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 48.19  E-value: 7.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLC--- 1316
Cdd:PLN02387   108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICdsk 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1317 -----------------------EDDCSALDLMGVQHARIDAAQEEAQREQHLRAPHALPAvdPRSAAYVIYTSGSSGAP 1373
Cdd:PLN02387   188 qlkklidissqletvkrviymddEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPS--PNDIAVIMYTSGSTGLP 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1374 KGVVIAHGaltNYVdavlarldppprARFAMVSTIGADLGH-------------------TVLFGALAS---GGALHLID 1431
Cdd:PLN02387   266 KGVMMTHG---NIV------------ATVAGVMTVVPKLGKndvylaylplahilelaaeSVMAAVGAAigyGSPLTLTD 330
                          250       260
                   ....*....|....*....|...
gi 1888712850 1432 ------RDTTLDADRFAQTLAAA 1448
Cdd:PLN02387   331 tsnkikKGTKGDASALKPTLMTA 353
PLN02479 PLN02479
acetate-CoA ligase
1550-1718 7.88e-05

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 47.92  E-value: 7.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1550 PVGTGGT--GELYLGGAGVALGYLHQPALTAarfvpHPFAAGarLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPG 1627
Cdd:PLN02479   394 PVPADGKtmGEIVMRGNMVMKGYLKNPKANE-----EAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSL 466
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1628 EIAARLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRAL-----AALLPDYMVP-SVlrVIDALPLNRN 1697
Cdd:PLN02479   467 EVENVVYTHPAVLEASVVARPderwGESPCAFVTLKPGVDKSDEAALAEDimkfcRERLPAYWVPkSV--VFGPLPKTAT 544
                          170       180
                   ....*....|....*....|.
gi 1888712850 1698 GKLDRQALSALARPAAPHREA 1718
Cdd:PLN02479   545 GKIQKHVLRAKAKEMGPVKKS 565
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
251-768 8.30e-05

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 48.33  E-value: 8.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  251 PQYFLERPLRWLDAIARHRGTISGAPDFAYRLCAERINDETRAKLDLSSWRLAFSGSEPVRRDTLDDFVARFAPAGFDAA 330
Cdd:COG3321    864 PTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALL 943
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  331 ALYPCYGLAEATLFVTGGVRGAGLVSHAFSSAALSAGRAEAARADEAATVLVGCGAVQAGHRVAIVARAAAESHESHEAD 410
Cdd:COG3321    944 ALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLA 1023
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  411 VETETSRAGERLADGRIGEIHVSGP-----SVAHGYWQRADASAQAFVDAPRHADGSGPARWLRTGDLGFVHDGQLYIAG 485
Cdd:COG3321   1024 LAALLAAAAAALAAAAAAAAAAAALaalaaAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALA 1103
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  486 RVKDLVIVRGRNLYPQDVEQAVEAHAEFARKGRVIAFGATLGGGETLGLALEIAPRMKKRFAAAQIVETLRRIAFDACGE 565
Cdd:COG3321   1104 AALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAA 1183
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  566 TPAAIALLNPGALPKTSSGKLQRAATREGWRARTLDLYALWEQGAFVIGGDDDAARAPDAPAALDARESALAALWCEALD 645
Cdd:COG3321   1184 ALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALA 1263
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  646 ARLALAPDAHFFASGGSSLSAARLVALIGARLGRRVALAQIFETPTLAAMAAALAEPESVEEAQDDAQDEAQDNAPIEPA 725
Cdd:COG3321   1264 LLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALAL 1343
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1888712850  726 EEAVISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALR 768
Cdd:COG3321   1344 AAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
1363-1645 8.85e-05

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 47.46  E-value: 8.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1363 VIYTSGSSGAPKGVVIAHGALTNYVdAVLAR--LDPPPRARFAMVSTIG-ADLGHTVLFGALASGGAL--HLIDRdttLD 1437
Cdd:cd05928    179 IYFTSGTTGSPKMAEHSHSSLGLGL-KVNGRywLDLTASDIMWNTSDTGwIKSAWSSLFEPWIQGACVfvHHLPR---FD 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1438 ADRFAQTLAAARIDVLKIVPGHLHALLQAERAADALPA--HTLVlGGEATSWELLDTIAAlRPDCRVHNHYGPTETTV-- 1513
Cdd:cd05928    255 PLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSlqHCVT-GGEPLNPEVLEKWKA-QTGLDIYEGYGQTETGLic 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1514 ----GILTQPAAqacraaatlpLGRPLDNNETWLLDEHLNPVGTGGTGELYL-----GGAGVALGYLHQPALTAARFVph 1584
Cdd:cd05928    333 anfkGMKIKPGS----------MGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIR-- 400
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1888712850 1585 pfaagARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVI 1645
Cdd:cd05928    401 -----GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVV 456
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
162-228 8.90e-05

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 47.89  E-value: 8.90e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850  162 RDTPSDapLHPVRADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAI-----QAGLGVRPDDVFVSWLPLYH 228
Cdd:PLN02430   208 KENPSE--TNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlfmeQFEDKMTHDDVYLSFLPLAH 277
prpE PRK10524
propionyl-CoA synthetase; Provisional
1219-1709 8.99e-05

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 47.64  E-value: 8.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1219 VARHADTQPDAPAVI------DGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVA 1292
Cdd:PRK10524    59 VDRHLAKRPEQLALIavstetDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSV 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1293 LDAGNPTQRLAQTLRDCGARLVLCEDDCS--------------ALDLMGVQHAR-------IDAAQEEAQREQH---LRA 1348
Cdd:PRK10524   139 VFGGFASHSLAARIDDAKPVLIVSADAGSrggkvvpykplldeAIALAQHKPRHvllvdrgLAPMARVAGRDVDyatLRA 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1349 PHA--------LPAVDPrsaAYVIYTSGSSGAPKGVVIAHG----ALTNYVDAVLarlDPPPRARFAMVSTIGADLGHT- 1415
Cdd:PRK10524   219 QHLgarvpvewLESNEP---SYILYTSGTTGKPKGVQRDTGgyavALATSMDTIF---GGKAGETFFCASDIGWVVGHSy 292
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1416 VLFGALASGGALHLIDRDTTL-DA-------DRFAQTL---AAARIDVLKIVPghlHALLqaeRAADALPAHTLVLGGE- 1483
Cdd:PRK10524   293 IVYAPLLAGMATIMYEGLPTRpDAgiwwrivEKYKVNRmfsAPTAIRVLKKQD---PALL---RKHDLSSLRALFLAGEp 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1484 ----ATSWeLLDTIAalRPdcrVHNHYGPTETTVGILT-QPAAQACRAAATLPlGRPLDNNETWLLDEHL-NPVGTGGTG 1557
Cdd:PRK10524   367 ldepTASW-ISEALG--VP---VIDNYWQTETGWPILAiARGVEDRPTRLGSP-GVPMYGYNVKLLNEVTgEPCGPNEKG 439
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1558 ELylggagVALGYLHQPALTA-----ARFVPHPFAAGARL-YRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAA 1631
Cdd:PRK10524   440 VL------VIEGPLPPGCMQTvwgddDRFVKTYWSLFGRQvYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEE 513
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1632 RLKALDGVRDAAVIVVA----GARLAAFATPQPGASLDAAALKRALAAllpDYMV-----------PSVLRVIDALPLNR 1696
Cdd:PRK10524   514 SISSHPAVAEVAVVGVKdalkGQVAVAFVVPKDSDSLADREARLALEK---EIMAlvdsqlgavarPARVWFVSALPKTR 590
                          570
                   ....*....|...
gi 1888712850 1697 NGKLDRQALSALA 1709
Cdd:PRK10524   591 SGKLLRRAIQAIA 603
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1345-1395 2.03e-04

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 46.88  E-value: 2.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1888712850 1345 HLRAPH-ALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLD 1395
Cdd:PRK06814   779 AGRFPLvYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID 830
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
165-276 2.19e-04

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 46.27  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  165 PSDAPLHPVRADDLAFLQYTSGSTGSPKGVMVSH--GNLLANEIAIQAGLGVRPDDVFVSWLPLYHDMGLIGSLLQPVFS 242
Cdd:cd05915    142 GEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHraLVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVG 221
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1888712850  243 GIPLVLMSpqyfLERPLRWLDAIARHRGT-ISGAP 276
Cdd:cd05915    222 AKQVLPGP----RLDPASLVELFDGEGVTfTAGVP 252
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
179-228 3.33e-04

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 45.90  E-value: 3.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1888712850  179 AFLQYTSGSTGSPKGVMVSH-GNLLANEIAIQAG-LGVRPDDVFVSWLPLYH 228
Cdd:PRK06018   180 AGMCYTSGTTGDPKGVLYSHrSNVLHALMANNGDaLGTSAADTMLPVVPLFH 231
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
1240-1385 4.29e-04

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 45.42  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1240 SYAELDARAAHVAQWLLAR-DLQGGEPVAIVAHRSARFVVAMLGVLKAGGAYVALDAGNPTQRLAQTLRDCGARLVLCED 1318
Cdd:cd05905     16 TWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTVE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1319 DCSALDLMGVQHAR--------------IDAAQEEAQREQHLRAPHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALT 1384
Cdd:cd05905     96 ACLKGLPKKLLKSKtaaeiakkkgwpkiLDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLL 175

                   .
gi 1888712850 1385 N 1385
Cdd:cd05905    176 A 176
PLN02614 PLN02614
long-chain acyl-CoA synthetase
174-228 4.31e-04

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 45.40  E-value: 4.31e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  174 RADDLAFLQYTSGSTGSPKGVMVSHGNLLANEIAIQAGLG-----VRPDDVFVSWLPLYH 228
Cdd:PLN02614   221 KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAH 280
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
1355-1709 5.77e-04

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 45.19  E-value: 5.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1355 VDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVLARLDP----------PPRARFAMVStigadlghTVLFGALAsg 1424
Cdd:PRK06334   180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPkeddvmmsflPPFHAYGFNS--------CTLFPLLS-- 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1425 gALHLIDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQ-AERAADALPAHTL-VLGGEATSWELLDTIAALRPDCRV 1502
Cdd:PRK06334   250 -GVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKtAKKQESCLPSLRFvVIGGDAFKDSLYQEALKTFPHIQL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1503 HNHYGPTE----TTVGILTQPAAQACraaatlpLGRPLDNNETWLLDEHLN-PVGTGGTGELYLGGAGVALGYL----HQ 1573
Cdd:PRK06334   329 RQGYGTTEcspvITINTVNSPKHESC-------VGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLgedfGQ 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1574 PaltaarFVPhpfAAGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEpgeiaarLKALDGV----------RDAA 1643
Cdd:PRK06334   402 G------FVE---LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVS-------LEALESIlmegfgqnaaDHAG 465
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1888712850 1644 VIVVAG-----ARLAAFATpqpGASLDAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSALA 1709
Cdd:PRK06334   466 PLVVCGlpgekVRLCLFTT---FPTSISEVNDILKNSKTSSILKISYHHQVESIPMLGTGKPDYCSLNALA 533
PRK08308 PRK08308
acyl-CoA synthetase; Validated
1588-1707 6.03e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 44.64  E-value: 6.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1588 AGARLYRSGDRARRLADGSLEYLGRIDDQVKIRGYRVEPGEIAARLKALDGVRDAAVI----VVAGARLAAFATPQPGAS 1663
Cdd:PRK08308   288 MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkdPVAGERVKAKVISHEEID 367
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1888712850 1664 ldAAALKRALAALLPDYMVPSVLRVIDALPLNRNGKLDRQALSA 1707
Cdd:PRK08308   368 --PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
COG3903 COG3903
Predicted ATPase [General function prediction only];
634-1018 6.67e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 45.01  E-value: 6.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  634 SALAALWCEALDARLALAPDAHFFASGGSSLSAARLVALIGARLGRRVALAQIFETPTLAAMAAALAEPESVEEAQDDAQ 713
Cdd:COG3903    549 AALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAA 628
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  714 DEAQDNAPIEPAEEAVISHAQQRQLFAWRLDPASRAYHVAAGIRLDGALDREALRQSLDRLCERHAALRTHFVETGDAAH 793
Cdd:COG3903    629 LAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAA 708
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  794 LYAPRTEAAAPLAWAHVDLSDLGDIDEHDRERALRECAQRFADAPFDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGW 873
Cdd:COG3903    709 AALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAA 788
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  874 SMQLLVEELVDGYRAALDGATTHGEAQAKAKTRITYADYAAWQRRWLASDAAARQLAYWRAALADDAPPLALPYDHTATD 953
Cdd:COG3903    789 AAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAA 868
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1888712850  954 TASENADPRAAARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVA 1018
Cdd:COG3903    869 ALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
633-692 8.86e-04

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 40.22  E-value: 8.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1888712850  633 ESALAALWCEALDARLA-LAPDAHFFAS-GGSSLSAARLVALIGARLGRRVALAQIFETPTL 692
Cdd:COG0236      7 EERLAEIIAEVLGVDPEeITPDDSFFEDlGLDSLDAVELIAALEEEFGIELPDTELFEYPTV 68
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
165-309 9.18e-04

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 44.36  E-value: 9.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  165 PSDAPLHPVRADDLAFLQYTSGSTGSPKGVMvsH---GNLLANEIAIQAGLGVRPDDVF-----VSWLPlYHDMGLIGSL 236
Cdd:PRK00174   234 SDECEPEPMDAEDPLFILYTSGSTGKPKGVL--HttgGYLVYAAMTMKYVFDYKDGDVYwctadVGWVT-GHSYIVYGPL 310
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1888712850  237 L----QPVFSGIPlvlMSPQyflerPLRWLDAIARHRGTI-SGAPDfAYR-LCAEriNDETRAKLDLSSWRLAFSGSEP 309
Cdd:PRK00174   311 AngatTLMFEGVP---NYPD-----PGRFWEVIDKHKVTIfYTAPT-AIRaLMKE--GDEHPKKYDLSSLRLLGSVGEP 378
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
35-316 9.51e-04

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 44.00  E-value: 9.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   35 PEATALIVIDADGDTRYDYAQLDRRARALAARFARDGAAAERALIL-MDSGVDYVSAFFGCLYAGVVAVPV---YPPEsk 110
Cdd:cd17654      1 PDRPALIIDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLrCDRGTESPVAILAILFLGAAYAPIdpaSPEQ-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  111 reqhlaRLRGIARDAGVRYVLTTAALHErhadawsmlapgADVVAVDTLDARDTPSDAPLhpvraddlAFLQYTSGSTGS 190
Cdd:cd17654     79 ------RSLTVMKKCHVSYLLQNKELDN------------APLSFTPEHRHFNIRTDECL--------AYVIHTSGTTGT 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  191 PKGVMVSHGNLLANEIAIQAGLGVRPDDVFVSWLPLYHD---MGLIGSLLqpvfSGIPLvLMSPQYFLERPLRWLDAIA- 266
Cdd:cd17654    133 PKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDpsvVEIFLSLS----SGATL-LIVPTSVKVLPSKLADILFk 207
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1888712850  267 RHRGTISGA-PDFAYRLCAERINDETRAKldLSSWRLAFSGSEPVRRDTLD 316
Cdd:cd17654    208 RHRITVLQAtPTLFRRFGSQSIKSTVLSA--TSSLRVLALGGEPFPSLVIL 256
PLN02654 PLN02654
acetate-CoA ligase
165-220 1.79e-03

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 43.35  E-value: 1.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1888712850  165 PSDAPLHPVRADDLAFLQYTSGSTGSPKGVM-VSHGNLLANEIAIQAGLGVRPDDVF 220
Cdd:PLN02654   264 PTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLhTTGGYMVYTATTFKYAFDYKPTDVY 320
COG3903 COG3903
Predicted ATPase [General function prediction only];
599-984 2.83e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 43.08  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  599 TLDLYALWEQGAFVIGGDDDAARAPDAPAALDARESALAALWCEALDARLALAPDAHFFASGGSSLSAARLVALIGARLG 678
Cdd:COG3903    548 AAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLA 627
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  679 RRVALAQIFETPTLAAMAAALAEPESVEEAQDDAQDEAQDNAPIEPAEEAVISHAQQRQLFAWRLDPASRAYHVAAGIRL 758
Cdd:COG3903    628 ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAA 707
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  759 DGALDREALRQSLDRLCERHAALRTHFVETGDAAHLYAPRTEAAAPLAWAHVDLSDLGDIDEHDRERALRECAQRFADAP 838
Cdd:COG3903    708 AAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALA 787
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  839 FDLLRGPLLRAGLVRMSDERHVLMLALHHIATDGWSMQLLVEELVDGYRAALDGATTHGEAQAKAKTRITYADYAAWQRR 918
Cdd:COG3903    788 AAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAA 867
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1888712850  919 WLASDAAARQLAYWRAALADDAPPLALPYDHTATDTASENADPRAAARVAFALPAPLAQAVRASAA 984
Cdd:COG3903    868 AALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
PRK08308 PRK08308
acyl-CoA synthetase; Validated
466-510 3.12e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 42.33  E-value: 3.12e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1888712850  466 RWLRTGDLGFV-HDGQLYIAGRVKDLVIVRGRNLYPQDVEQAVEAH 510
Cdd:PRK08308   291 KEIFTKDLGYKsERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRL 336
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
82-316 3.35e-03

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 42.64  E-value: 3.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850   82 DSGVDYVSAFFGCLYAGVV-AVPVYPPESKREQHLARLRGIArdAGVRYVLTTAALHERHADAWSMLAPGADVVAVDtlD 160
Cdd:cd05943    156 DFGVPGVLDRFGQIEPKVLfAVDAYTYNGKRHDVREKVAELV--KGLPSLLAVVVVPYTVAAGQPDLSKIAKALTLE--D 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  161 ARDTPSDAPLHPVRA--DDLAFLQYTSGSTGSPKGVMVSHGNLLAN---EIAIQAGLgvRPDDVF-----VSWLpLYHdm 230
Cdd:cd05943    232 FLATGAAGELEFEPLpfDHPLYILYSSGTTGLPKCIVHGAGGTLLQhlkEHILHCDL--RPGDRLfyyttCGWM-MWN-- 306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  231 GLIGSLLqpvfSGIPLVLM--SPQYfleRPLRWL-DAIARHRGTISGApDFAYRLCAERINDETRAKLDLSSWRLAFSGS 307
Cdd:cd05943    307 WLVSGLA----VGATIVLYdgSPFY---PDTNALwDLADEEGITVFGT-SAKYLDALEKAGLKPAETHDLSSLRTILSTG 378

                   ....*....
gi 1888712850  308 EPVRRDTLD 316
Cdd:cd05943    379 SPLKPESFD 387
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
1876-2115 5.74e-03

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 41.62  E-value: 5.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1876 LRGPLDAARLQRSLAALIARHEVLRSAFDADDEGDPVLkiaprmevlmpVIEPLAHPdndanshtnshtnsdenARTQAT 1955
Cdd:PRK09294    30 LRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWEL-----------VADDLLHP-----------------GIVVVD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1956 AQALDDAARTPFDLSRAPLVRATLLRFDAAHHVLIVslHHIVADGGSVHILLDELCELY-RAQRDGAPPAL----APLAV 2030
Cdd:PRK09294    82 GDAARPLPELQLDQGVSLLALDVVPDDGGARVTLYI--HHSIADAHHSASLLDELWSRYtDVVTTGDPGPIrpqpAPQSL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 2031 QYADYAHWQRARFTPDAVREAQQFWRGYLADAPALLPLSTdRARPTRVSHagaARHfRLDATLGARVRTLAQAHGMTPFA 2110
Cdd:PRK09294   160 EAVLAQRGIRRQALSGAERFMPAMYAYELPPTPTAAVLAK-PGLPQAVPV---TRC-RLSKAQTSSLAAFGRRHRLTVNA 234

                   ....*
gi 1888712850 2111 VLLAS 2115
Cdd:PRK09294   235 LVSAA 239
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
1357-1390 5.81e-03

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 41.72  E-value: 5.81e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1888712850 1357 PRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAV 1390
Cdd:PLN02430   219 PLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGV 252
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
1344-1647 6.19e-03

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 41.67  E-value: 6.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1344 QHLRA--PHALPAVDPRSAAYVIYTSGSSGAPKGVVIAHGALTNYVDAVlarldppprARFamVSTIGADLGHTV----- 1416
Cdd:COG1541     67 EDLRDnyPFGLFAVPLEEIVRIHASSGTTGKPTVVGYTRKDLDRWAELF---------ARS--LRAAGVRPGDRVqnafg 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1417 --LF--GALASGGALHL---IDRDTTLDADRFAQTLAAARIDVLKIVPGHLHALLQAERAA----DALPAHTLVLGGEAT 1485
Cdd:COG1541    136 ygLFtgGLGLHYGAERLgatVIPAGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEgidpRDLSLKKGIFGGEPW 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1486 SWELLDTIAAlRPDCRVHNHYGPTETTVGIltqpaaqacraaatlplgrpldNNET--------W-------LLD-EHLN 1549
Cdd:COG1541    216 SEEMRKEIEE-RWGIKAYDIYGLTEVGPGV----------------------AYECeaqdglhiWedhflveIIDpETGE 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1550 PVGTGGTGELY---LGGAGvalgylhQPALtaarfvphpfaagaRlYRSGDRARRLADGS--------LEY-LGRIDDQV 1617
Cdd:COG1541    273 PVPEGEEGELVvttLTKEA-------MPLI--------------R-YRTGDLTRLLPEPCpcgrthprIGRiLGRADDML 330
                          330       340       350
                   ....*....|....*....|....*....|
gi 1888712850 1618 KIRGYRVEPGEIAARLKALDGVRDAAVIVV 1647
Cdd:COG1541    331 IIRGVNVFPSQIEEVLLRIPEVGPEYQIVV 360
PLN02736 PLN02736
long-chain acyl-CoA synthetase
1339-1383 8.42e-03

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 41.24  E-value: 8.42e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1888712850 1339 EAQREQHLRAPHAlPAvdPRSAAYVIYTSGSSGAPKGVVIAHGAL 1383
Cdd:PLN02736   205 LAQGRSSPQPFRP-PK--PEDVATICYTSGTTGTPKGVVLTHGNL 246
COG3903 COG3903
Predicted ATPase [General function prediction only];
879-1295 9.79e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 41.16  E-value: 9.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  879 VEELVDGYRAALDGATTHGEAQAKAktRITYADYAAWQRRWLASDAAARQlaywRAALADDAPPLALPYDHTATDTASEN 958
Cdd:COG3903    521 LDAEHDNLRAALRWALAHGDAELAL--RLAAALAPFWFLRGLLREGRRWL----ERALAAAGEAAAALAAAAALAAAAAA 594
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850  959 ADPRAAARVAFALPAPLAQAVRASAARHRATPFVVLLAAYHAWLYRVTGQRAIRTGVPVANRTRPETHDVIGFFVNTLVL 1038
Cdd:COG3903    595 ARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAA 674
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1039 HSDCEAATPLASLFSQLRQRTLDAQANQALPFDVLVEHLRPARDAQHGPLFETSFNYLSDDYPALARWPGARAERVEIAE 1118
Cdd:COG3903    675 AAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAA 754
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1119 THVKVPLALDLRESRDGSMRAYFTYASARFDAASVERMAAQYLRAVEAFAHALGDRSADMTDAAAPTLATLDLLDADERA 1198
Cdd:COG3903    755 AAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAAL 834
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888712850 1199 RVSAASVARRTPPGEPIHLRVARHADTQPDAPAVIDGALRMSYAELDARAAHVAQWLLARDLQGGEPVAIVAHRSARFVV 1278
Cdd:COG3903    835 AAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAA 914
                          410
                   ....*....|....*..
gi 1888712850 1279 AMLGVLKAGGAYVALDA 1295
Cdd:COG3903    915 AALAAAAAAAAAAAAAA 931
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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