|
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
|
|
| |
