|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-2557 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1882.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 8 LTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEGEE-----LEPRLHLTeykyYP 82
Cdd:PRK12467 52 LSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEgfrqvIDASLSLT----IP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 83 LRIIDFSNVEMIE--IEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMK- 159
Cdd:PRK12467 128 LDDLANEQGRAREsqIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSq 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 160 -KKDPLPDQP---------EPSYLSYIEKESQYlqspRFAKDRLFWTQT-FEHPLEYHSLAdqtslqKQSTSASRDTIIL 228
Cdd:PRK12467 208 gREPSLPALPiqyadyaiwQRSWLEAGERERQL----AYWQEQLGGEHTvLELPTDRPRPA------VPSYRGARLRVDL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 229 SPDLEQTIRIFCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSF 308
Cdd:PRK12467 278 PQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLEL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 309 VRTIGREQLSVMRHQRFPYNLLVNELRNEQKDLHN-LIGISMQYQplqwHNADDFDYETALYFSGYTANELSVQIQE-RI 386
Cdd:PRK12467 358 LQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSpLFQVMFNHQ----NTATGGRDREGAQLPGLTVEELSWARHTaQF 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 387 D--------NGTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHPHSFIKELDMTNTREKQKLLCEFNKTEAVSPKAf 458
Cdd:PRK12467 434 DlaldtyesAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPD- 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL 538
Cdd:PRK12467 513 CVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAYPKERLSYMLKDSGASLLLTQPGCSAPnfsgETLEVDMTSLA--------SEKAENHEFTPADGGSLAYVIYTSGST 610
Cdd:PRK12467 593 DPEYPQDRLAYMLDDSGVRLLLTQSHLLAQ----LPVPAGLRSLCldepadllCGYSGHNPEVALDPDNLAYVIYTSGST 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 611 GQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENV 690
Cdd:PRK12467 669 GQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGV 748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 691 TTAHFIPAMLNSFLDQAEIERLsdrTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPErDRD 770
Cdd:PRK12467 749 TVLKIVPSHLQALLQASRVALP---RPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDE-ERD 824
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 771 RLRIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYP-GERMYKTGDVARWLPDG 849
Cdd:PRK12467 825 FGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADG 904
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 850 NVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGLQ----------RNEVRAQLERLL 919
Cdd:PRK12467 905 VIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAvadgaehqatRDELKAQLRQVL 984
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 920 PGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKA 999
Cdd:PRK12467 985 PDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLA 1064
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1000 TALVSRIAKEFDVQVPLKDVFAHPTVEGLATVIREGTDSPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAV 1079
Cdd:PRK12467 1065 TQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQA 1144
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1080 LELEGKLNPERMERAFKELIKRHESLRTSFEQDaGGDPVQRIHDEVPFTL-QTTVLGERTEQEAAAAFI-----KPFDLS 1153
Cdd:PRK12467 1145 LRLKGPLDIEALERSFDALVARHESLRTTFVQE-DGRTRQVIHPVGSLTLeEPLLLAADKDEAQLKVYVeaearQPFDLE 1223
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1154 QAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRN------LPALRIQYKDYAVWREGFKTGDAYKT 1227
Cdd:PRK12467 1224 QGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSqgqslqLPALPIQYADYAVWQRQWMDAGERAR 1303
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1228 QEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDII 1307
Cdd:PRK12467 1304 QLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIR 1383
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1308 VGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNPVFDAM 1387
Cdd:PRK12467 1384 VGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVM 1463
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1388 FILQNVEKQDI-DLREIKVRPANFAHHISLFDITLIATEINGSICCEMEFSTEVFLKATIERWADHFIEFLHAALSTPET 1466
Cdd:PRK12467 1464 FNHQRDDHQAQaQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPER 1543
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1467 SLAQINILSDKEKQKIVFEFNKTQVEFAQKDVpFHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-G 1545
Cdd:PRK12467 1544 RLGELDLLDEAERRQILEGWNATHTGYPLARL-VHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGvG 1622
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1546 PKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQqelKHLISNLPESE-MSHICLDDE 1624
Cdd:PRK12467 1623 PEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ---SHLQARLPLPDgLRSLVLDQE 1699
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1625 SSYEEN--SCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVrLLQIASFSFDVFSGDLA 1702
Cdd:PRK12467 1700 DDWLEGysDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADV-VLQFTSFAFDVSVWELF 1778
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1703 RTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQfKLPDLDILILGSDMVKAQDFKTLTDR 1782
Cdd:PRK12467 1779 WPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVE-HPLSLRRVVCGGEALEVEALRPWLER 1857
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1783 FGQSmRIINSYGVTEATIDSSFYETSMGGEGTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKP 1862
Cdd:PRK12467 1858 LPDT-GLFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRP 1936
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1863 DLTQMKFTKNPF-VSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQ 1941
Cdd:PRK12467 1937 ALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGK 2016
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1942 AgLAAYIVPSD-----------VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVPN-NVLSRPYTAPV 2009
Cdd:PRK12467 2017 Q-LVAYVVPTDpglvdddeaqvALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDaSELQQAYVAPQ 2095
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2010 NDIQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARLAAEGWSMTIRDLFRYSTIQELCG--HITPLASQADQG 2087
Cdd:PRK12467 2096 SELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAvaQEGDGTVSIDQG 2175
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2088 PAEGEAELTPIQRRFFGQVHAFHNHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFqRDQNGHVIQFNRGINHKD 2167
Cdd:PRK12467 2176 PVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGF-VQEDGGWSAMHRAPEQER 2254
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2168 HELFglyisdWTKASLERTHLdEKLAAEEtviQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLA 2246
Cdd:PRK12467 2255 RPLL------WQVVVADKEEL-EALCEQA---QRSLDLEEGPLLRAVLATLPDGSQrLLLVIHHLVVDGVSWRILLEDLQ 2324
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2247 AAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDIenvPDRLQMNSDAAAFV--LS 2324
Cdd:PRK12467 2325 TAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELPCDH---PQGGLQRRHAASVTthLD 2401
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2325 GDWTEKLLFETQQAYGTDANELLLTALGMALSEWAGHDQIVISTEGHGREGHVPNIDISRTVGWFTSIYPILLdmgIPEP 2404
Cdd:PRK12467 2402 SEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKL---SPTA 2478
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2405 fedQLAYRIKTTKDMLRRVPNKGTGYGLLTHIG--ELRHK-----EPEVSFNYLGQFSEEKEAETFQLsyYQPSYEIAG- 2476
Cdd:PRK12467 2479 ---SLATSIKTIKEQLRAVPNKGLGFGVLRYLGseAARQTlqalpVPRITFNYLGQFDGSFDAEKQAL--FVPSGEFSGa 2553
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2477 EREREYELD----INALITDGRLQVKAVY-TQVFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDFSNKELTLS-- 2549
Cdd:PRK12467 2554 EQSEEAPLGnwlsINGQVYGGELNLGWTFsQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEql 2633
|
2650
....*....|...
gi 363747658 2550 -----ALSSIEDL 2557
Cdd:PRK12467 2634 drlpvAVGDIEDI 2646
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-2557 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1638.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 6 YSLTHAQRRVWFTELLEPNTS--ICNLTACVkfkGNIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTEYKY-YP 82
Cdd:PRK12316 1557 YPLSPMQQGMLFHSLYEQEAGdyINQLRVDV---QGLDPDRFRAAWQATVDRHEILRSGFLWQDGLEQPLQVIHKQVeLP 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 83 LRIIDFSNVEMIE--IEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMkk 160
Cdd:PRK12316 1634 FAELDWRGREDLGqaLDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQ-- 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 161 kdpLPDQPEPSYLSYIekesQYLQSPRFAKDRLFWTQTFEHPLEYHSLADQTSLQKQSTSASRDTIILSPDLEQTIRIFC 240
Cdd:PRK12316 1712 ---PVAAPGGRYRDYI----AWLQRQDAAASEAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFA 1784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 241 EEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAE--KEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQLS 318
Cdd:PRK12316 1785 RAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPgiEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLA 1864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 319 VMRHQRFPY----------------NLLVNELRNEQKDLHNLIGISMQYQPLqwHNADDFDYETALyfsgytanelSVQI 382
Cdd:PRK12316 1865 LREHEHTPLydiqrwagqggealfdSLLVFENYPVAEALKQGAPAGLVFGRV--SNHEQTNYPLTL----------AVTL 1932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 383 QERIdngTIQLNFDYQNtlFSLEDIKRIQSHLLTILENALHHPHSFIKELDMTNTREKQKLLCEFNKTEAVSPKAFTLHG 462
Cdd:PRK12316 1933 GETL---SLQYSYDRGH--FDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQ 2007
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAY 542
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 543 PKERLSYMLKDSGASLLLTQPGCSA---PNFSGETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVE 619
Cdd:PRK12316 2088 PAERLAYMLEDSGAALLLTQRHLLErlpLPAGVARLPLDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVS 2167
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 620 HRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAyLLPPGWEKDSALIVQAIHQENVTTAHFIPAM 699
Cdd:PRK12316 2168 HGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDFPPVY 2246
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 700 LNSFLDQAEIERlsDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIGKP 779
Cdd:PRK12316 2247 LQQLAEHAERDG--RPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRA 2324
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 780 VPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVEFLGRTD 858
Cdd:PRK12316 2325 LGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRID 2404
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 859 DQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEG-----LQRNEVRAQLERLLPGYMVPAYMIEMEQ 933
Cdd:PRK12316 2405 HQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPddaaeDLLAELRAWLAARLPAYMVPAHWVVLER 2484
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 934 WPVTPSGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRIAKEFDVQ 1013
Cdd:PRK12316 2485 LPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLE 2564
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1014 VPLKDVFAHPTVEGLATVIREGTDSPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMER 1093
Cdd:PRK12316 2565 VPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQ 2644
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1094 AFKELIKRHESLRTSFEQDAGGdPVQRIHDEVPFTLQ----TTVLGERTEQEAAAAFIKPFDLSQAPLFRAQIVKISDER 1169
Cdd:PRK12316 2645 AFDALVLRHETLRTRFVEVGEQ-TRQVILPNMSLRIVledcAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQE 2723
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1170 HLLLVDMHHIISDGVSVNILIREFGELYNNRN------LPALRIQYKDYAVWREGFKTGDAYKTQEAYWLKQLEGELPVL 1243
Cdd:PRK12316 2724 HVLVITQHHIVSDGWSMQVMVDELVQAYAGARrgeqptLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVL 2803
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1244 DLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPI 1323
Cdd:PRK12316 2804 ELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERL 2883
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1324 LGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNPVFDAMFILQNVEKQDIDLREI 1403
Cdd:PRK12316 2884 IGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGL 2963
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1404 KVRPANFAHHISLFDITLIATEINGSICCEMEFSTEVFLKATIERWADHFIEFLHAALSTPETSLAQINILSDKEKQKIV 1483
Cdd:PRK12316 2964 HIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLL 3043
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1484 FEFNKTQVEFAqKDVPFHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIV 1562
Cdd:PRK12316 3044 EAWNATAAEYP-LERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGvGPDVLVGVAVERSLEMVV 3122
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1563 GVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQELKhlisnLPESEMSHICLDDESSYEENSCNLNLSPAPEE 1642
Cdd:PRK12316 3123 GLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLR-----LPLAQGVQVLDLDRGDENYAEANPAIRTMPEN 3197
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1643 PVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEP 1722
Cdd:PRK12316 3198 LAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGD-RVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDP 3276
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1723 AEIYKIMNSQRITVMESTPALIIPVMEYVyrNQFKLPDLDILILGSDMVKAQdfktLTDRFGQSMRIINSYGVTEATIDS 1802
Cdd:PRK12316 3277 ALLVELINSEGVDVLHAYPSMLQAFLEEE--DAHRCTSLKRIVCGGEALPAD----LQQQVFAGLPLYNLYGPTEATITV 3350
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1803 SFYETSMGGEGTgdnVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYR 1882
Cdd:PRK12316 3351 THWQCVEEGKDA---VPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYR 3427
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1883 TGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAvqhDKNGQAgLAAYIVPSDVNTN---ALR 1959
Cdd:PRK12316 3428 TGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL---AVDGRQ-LVAYVVPEDEAGDlreALK 3503
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1960 AALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVPNNVLSR-PYTAPVNDIQKTMAYIWEDVLSMSRVGIHDSFFEL 2038
Cdd:PRK12316 3504 AHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQqDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFEL 3583
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2039 GGDSIKALQVAARLAAEGWSMTIRDLFRYSTIQELCGHITPLASQA-DQGPAEGEAELTPIQRRFFGQVHAFHNHYNQSV 2117
Cdd:PRK12316 3584 GGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAvDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSL 3663
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2118 MLFSEKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQfnrginHKDHELFGLYIsdWtKASLERTHLDEKLAAEet 2197
Cdd:PRK12316 3664 LLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAE------HLPVELGGALL--W-RAELDDAEELERLGEE-- 3732
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2198 vIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQ 2276
Cdd:PRK12316 3733 -AQRSLDLADGPLLRALLATLADGSQrLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQE 3811
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2277 IAESKQLLSEKTYWQTILDAHTAFLPKDienVPDRLQMNSDAAAFV--LSGDWTEKLLFETQQAYGTDANELLLTALGMA 2354
Cdd:PRK12316 3812 HARGEALKAELAYWQEQLQGVSSELPCD---HPQGALQNRHAASVQtrLDRELTRRLLQQAPAAYRTQVNDLLLTALARV 3888
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2355 LSEWAGHDQIVISTEGHGREGHVPNIDISRTVGWFTSIYPILLDMGIpepfedQLAYRIKTTKDMLRRVPNKGTGYGLLT 2434
Cdd:PRK12316 3889 VCRWTGEASALVQLEGHGREDLFADIDLSRTVGWFTSLFPVRLSPVE------DLGASIKAIKEQLRAIPNKGIGFGLLR 3962
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2435 HIGELRHKE-------PEVSFNYLGQFSEEKEAETfqlSYYQPSYEIAG-EREREYELD----INALITDGRLQVKAVYT 2502
Cdd:PRK12316 3963 YLGDEESRRtlaglpvPRITFNYLGQFDGSFDEEM---ALFVPAGESAGaEQSPDAPLDnwlsLNGRVYGGELSLDWTFS 4039
|
2570 2580 2590 2600 2610 2620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363747658 2503 -QVFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDFSNKELTLS-------ALSSIEDL 2557
Cdd:PRK12316 4040 rEMFEEATIQRLADDYAAELTALVEHCCDAERHGVTPSDFPLAGLDQArldalplPLGEIEDI 4102
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
11-2557 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1613.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 11 AQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEgEELEPRLHLTEYKYYPLRIIDFSN 90
Cdd:PRK05691 681 AQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYE-RDGVALQRIDAQGEFALQRIDLSD 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 91 VEMIEIE----QWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMKKKDPLPD 166
Cdd:PRK05691 760 LPEAEREaraaQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAEL 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 167 QPEP-SYLSYIEKESQYLQSPRFAKDRLFWTQTF--EHP-LEYHSlaDQTSLQKQSTSASRDTIILSPDLEQTIRIFCEE 242
Cdd:PRK05691 840 APLPlGYADYGAWQRQWLAQGEAARQLAYWKAQLgdEQPvLELAT--DHPRSARQAHSAARYSLRVDASLSEALRGLAQA 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 243 HKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQLSVMRH 322
Cdd:PRK05691 918 HQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAH 997
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 323 QRFPYNLLVNEL-------------RNEQKDLHNLIGI-SMQYQPLQWHNAD-DFDyetalyfsgytanelsVQIQERID 387
Cdd:PRK05691 998 QDLPFEQLVEALpqareqglfqvmfNHQQRDLSALRRLpGLLAEELPWHSREaKFD----------------LQLHSEED 1061
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 388 -NGTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHPHSFIKELDMTNTREKQKLLCEfnKTEAVSPKAFTLHGLFER 466
Cdd:PRK05691 1062 rNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQW--GQAPCAPAQAWLPELLNE 1139
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 467 QAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKER 546
Cdd:PRK05691 1140 QARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 547 LSYMLKDSGASLLLTQPGCSA--PNFSGetleVDMTSLASEKAENHEFTPA----DGGSLAYVIYTSGSTGQPKGVAVEH 620
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSHLLErlPQAEG----VSAIALDSLHLDSWPSQAPglhlHGDNLAYVIYTSGSTGQPKGVGNTH 1295
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 621 RQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAML 700
Cdd:PRK05691 1296 AALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLL 1375
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 701 NSFLDQAeieRLSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPErdrDRLRIPIGKPV 780
Cdd:PRK05691 1376 QLFIDEP---LAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAE---DGERSPIGRPL 1449
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 781 PGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVEFLGRTDD 859
Cdd:PRK05691 1450 GNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQ 1529
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 860 QVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGL-----QRNEVRAQLERLLPGYMVPAYMIEMEQW 934
Cdd:PRK05691 1530 QVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEagqeaEAERLKAALAAELPEYMVPAQLIRLDQM 1609
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 935 PVTPSGKLDRNALPAPGGaaDAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRIAKEFDVQV 1014
Cdd:PRK05691 1610 PLGPSGKLDRRALPEPVW--QQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVEL 1687
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1015 PLKDVFAHPTVEGLATVIR----EGTDSPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPER 1090
Cdd:PRK05691 1688 PLRALFEASELGAFAEQVAriqaAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDR 1767
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1091 MERAFKELIKRHESLRTSFEQDaGGDPVQRIHDEVPF--------TLQTTVLGERTEQEAAAAFIKPFDLSQAPLFRAQI 1162
Cdd:PRK05691 1768 FEAALQALILRHETLRTTFPSV-DGVPVQQVAEDSGLrmdwqdfsALPADARQQRLQQLADSEAHQPFDLERGPLLRACL 1846
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1163 VKISDERHLLLVDMHHIISDGVSVNILIREFGELY----NNRNLP--ALRIQYKDYAVWREGFKTGDAYKTQEAYWLKQL 1236
Cdd:PRK05691 1847 VKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYeaflDDRESPlePLPVQYLDYSVWQRQWLESGERQRQLDYWKAQL 1926
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1237 EGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRP 1316
Cdd:PRK05691 1927 GNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRI 2006
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1317 HKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNPVFDAMFILQNVE-K 1395
Cdd:PRK05691 2007 RPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEfQ 2086
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1396 QDIDLREIKVR-PANFAHHISlFDITLIATEINGSICCEMEFSTEVFLKATIERWADHFIEFLHAALSTPETSLAQINIL 1474
Cdd:PRK05691 2087 QSRQLAGMTVEyLVNDARATK-FDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLL 2165
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1475 SDKEKQKIVFEFNKTQVEFAQkDVPFHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVL 1553
Cdd:PRK05691 2166 AAAEQQQLLDSLAGEAGEARL-DQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGvGPQVRVGLA 2244
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1554 AKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQELKHLISNLPeSEMSHICLDDES----SYEE 1629
Cdd:PRK05691 2245 LERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELP-AGVARWCLEDDAaalaAYSD 2323
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1630 NSC-NLNLspaPEEPVYIIYTSGTTGAPKGVIVtyrnfTHAALAWRQIYELDRKPVRL----LQIASFSFDVFSGDLART 1704
Cdd:PRK05691 2324 APLpFLSL---PQHQAYLIYTSGSTGKPKGVVV-----SHGEIAMHCQAVIERFGMRAddceLHFYSINFDAASERLLVP 2395
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1705 LTNGGTlIVCPDETRLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPdLDILILGSDMVKAQDFKTLTDRFg 1784
Cdd:PRK05691 2396 LLCGAR-VVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLP-VRMCITGGEALTGEHLQRIRQAF- 2472
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1785 QSMRIINSYGVTEATI---DSSFYETSMGGEGTgdnVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQK 1861
Cdd:PRK05691 2473 APQLFFNAYGPTETVVmplACLAPEQLEEGAAS---VPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDR 2549
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1862 PDLTQMKFTKNPFVS-GERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVaVQHDKNG 1940
Cdd:PRK05691 2550 PGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVV-LALDTPS 2628
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1941 QAGLAAYIV-----PSDVNTNALRAA----LTKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVPNNVLSRP-YTAPVN 2010
Cdd:PRK05691 2629 GKQLAGYLVsavagQDDEAQAALREAlkahLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQaYQAPRS 2708
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2011 DIQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARLAAEGWSMTIRDLFRYSTIQELCGHITPL-ASQADQGPA 2089
Cdd:PRK05691 2709 ELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSeAAQAEQGPL 2788
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2090 EGEAELTPIQRRFFGQVHAFHNHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFqRDQNGHvIQFNRGINHKDHE 2169
Cdd:PRK05691 2789 QGASGLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRF-SQADGR-WQAEYRAVTAQEL 2866
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2170 LFGLYISDWTKAslerthldeklAAEETVIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAA 2248
Cdd:PRK05691 2867 LWQVTVADFAEC-----------AALFADAQRSLDLQQGPLLRALLVDGPQGQQrLLLAIHHLVVDGVSWRVLLEDLQAL 2935
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2249 YQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDIENvPDRLQMNSDAAAFVLSGDWT 2328
Cdd:PRK05691 2936 YRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQ-GGNLNRHAQTVSVRLDAERT 3014
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2329 EKLLFETQQAYGTDANELLLTALGMALSEWAGHDQIVISTEGHGREGHVPNIDISRTVGWFTSIYPILLDmgiPEPFEDQ 2408
Cdd:PRK05691 3015 RQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLT---PAPGDDA 3091
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2409 -LAYRIKTTKDMLRRVPNKGTGYGLLTHIGELRHKE-------PEVSFNYLGQFSEEKEAETFqlsyYQPSYEIAGERER 2480
Cdd:PRK05691 3092 aRGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREamaalpqAPITFNYLGQFDQSFASDAL----FRPLDEPAGPAHD 3167
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2481 EY-----ELDINALITDGRLQVKAVYT-QVFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDFSNKELT---LSAL 2551
Cdd:PRK05691 3168 PDaplpnELSVDGQVYGGELVLRWTYSaERYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTqaqLDAL 3247
|
2650
....*....|
gi 363747658 2552 ----SSIEDL 2557
Cdd:PRK05691 3248 pvpaAEIEDV 3257
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1005-2557 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1142.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1005 RIAKEFdVQVPLKD--VFahptvegLATVIREGTD----SPYEAIKPAEKQetyPVSSAQKRIYVLQQLEDGGTGYNMPA 1078
Cdd:PRK12316 8 KLARRF-IELPLEKrrVF-------LATLRGEGVDfslfPIPAGVSSAERD---RLSYAQQRMWFLWQLEPQSGAYNLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1079 VLELEGKLNPERMERAFKELIKRHESLRTSFEQdAGGDPVQRIHDEVPFTLQ--------TTVLGERTEQEAAAAFIKPF 1150
Cdd:PRK12316 77 AVRLNGPLDRQALERAFASLVQRHETLRTVFPR-GADDSLAQVPLDRPLEVEfedcsglpEAEQEARLRDEAQRESLQPF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1151 DLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLPALRIQYKDYAVWREGFKTGDA 1224
Cdd:PRK12316 156 DLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYatgaepGLPALPIQYADYALWQRSWLEAGE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1225 YKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQE 1304
Cdd:PRK12316 236 QERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1305 DIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNPVF 1384
Cdd:PRK12316 316 DIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1385 DAMFILQNVeKQDIDLRE----IKVRPANFAHHISLFDITLIATEINGSICCEMEFSTEVFLKATIERWADHFIEFLHAA 1460
Cdd:PRK12316 396 QVMYNHQPL-VADIEALDtvagLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGM 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1461 LSTPETSLAQINILSDKEKQKIVFEFNKTQVEFA-QKDVpfHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLART 1539
Cdd:PRK12316 475 VENPQARVDELPMLDAEERGQLVEGWNATAAEYPlQRGV--HRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1540 LQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQelkHLISNLP-ESEMS 1617
Cdd:PRK12316 553 LIERGvGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS---HLGRKLPlAAGVQ 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1618 HICLDDESSYEEN--SCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPvRLLQIASFSFD 1695
Cdd:PRK12316 630 VLDLDRPAAWLEGysEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGD-TVLQKTPFSFD 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1696 VFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALIipvmeyvyrnQFKLPD--------LDILILG 1767
Cdd:PRK12316 709 VSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSML----------QAFLQDedvasctsLRRIVCS 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1768 SDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSfYETSMggEGTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGEL 1847
Cdd:PRK12316 779 GEALPADAQEQVFAKLPQA-GLYNLYGPTEAAIDVT-HWTCV--EEGGDSVPIGRPIANLACYILDANLEPVPVGVLGEL 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1848 CIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLV 1927
Cdd:PRK12316 855 YLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1928 REAAVAVQHDKNgqagLAAYIVPSDVNTN---ALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVPN-NVLSR 2003
Cdd:PRK12316 935 REAAVLAVDGKQ----LVGYVVLESEGGDwreALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEaSVAQQ 1010
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2004 PYTAPVNDIQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARLAAEGWSMTIRDLFRYSTIQELCGHIT-PLAS 2082
Cdd:PRK12316 1011 GYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAKaGQAT 1090
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2083 QADQGPAEGEAELTPIQRRFFGQVHAFHNHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFqRDQNGHVIQfnrg 2162
Cdd:PRK12316 1091 AADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRF-REEDGGWQQ---- 1165
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2163 inhkdhelfgLYISDWTKASLERTHL--DEKLAAEETVIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWR 2239
Cdd:PRK12316 1166 ----------AYAAPQAGEVLWQRQAasEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQrLLLVIHHLVVDGVSWR 1235
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2240 ILLEDLAAAYQQALEKkeiqLPPKTDSYLSYADGLTQIAESkqLLSEKTYWQTILDAHTAFLPKDienVPD--RLQMNSD 2317
Cdd:PRK12316 1236 ILLEDLQRAYADLDAD----LPARTSSYQAWARRLHEHAGA--RAEELDYWQAQLEDAPHELPCE---NPDgaLENRHER 1306
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2318 AAAFVLSGDWTEKLLFETQQAYGTDANELLLTALGMALSEWAGHDQIVISTEGHGREGHVPNIDISRTVGWFTSIYPILL 2397
Cdd:PRK12316 1307 KLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSRTVGWFTSLFPVRL 1386
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2398 dmgipEPfEDQLAYRIKTTKDMLRRVPNKGTGYGLLTHIG--ELRHK-----EPEVSFNYLGQFSEE-KEAETFqlsyyQ 2469
Cdd:PRK12316 1387 -----TP-AADLGESIKAIKEQLRAVPDKGIGYGLLRYLAgeEAAARlaalpQPRITFNYLGQFDRQfDEAALF-----V 1455
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2470 PSYEIAGEREREYE-----LDINALITDGRLQVKAVYTQ-VFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDFSN 2543
Cdd:PRK12316 1456 PATESAGAAQDPCAplanwLSIEGQVYGGELSLHWSFSReMFAEATVQRLADDYARELQALIEHCCDERNRGVTPSDFPL 1535
|
1610 1620
....*....|....*....|.
gi 363747658 2544 KELT---LSALS----SIEDL 2557
Cdd:PRK12316 1536 AGLSqaqLDALPlpagEIADI 1556
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1041-2355 |
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: 980.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1041 EAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGgDPVQR 1120
Cdd:COG1020 7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG-RPVQV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1121 IHDEVPFTLQTTVL--------GERTEQEAAAAFIKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIRE 1192
Cdd:COG1020 86 IQPVVAAPLPVVVLlvdlealaEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1193 FGELYN------NRNLPALRIQYKDYAVWREGFKTGDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTL 1266
Cdd:COG1020 166 LLRLYLaayagaPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1267 DQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQY 1346
Cdd:COG1020 246 PAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAEL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1347 LQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNPVFDAMFILQNVEKQDIDLREIKVRPANFAHHISLFDITLIATEI 1426
Cdd:COG1020 326 LARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVET 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1427 NGSICCEMEFSTEVFLKATIERWADHFIEFLHAALSTPETSLAQINILSDKEKQKIVFEFNKTQVEFAQkDVPFHRIFEA 1506
Cdd:COG1020 406 GDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPA-DATLHELFEA 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1507 KAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKA 1584
Cdd:COG1020 485 QAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRAL-GVGPgdLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1585 RIEYILRDSGADILLLQQelkHLISNLPESEMSHICLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYR 1664
Cdd:COG1020 564 RLAYMLEDAGARLVLTQS---ALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1665 NFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALI 1744
Cdd:COG1020 641 ALVNLLAWMQRRYGLGPGD-RVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLL 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1745 IPVMEYVYRNqfkLPDLDILILGSDMVKAQDFKTLTDRFGQsMRIINSYGVTEATIDSSFYETSmGGEGTGDNVPIGSPL 1824
Cdd:COG1020 720 RALLDAAPEA---LPSLRLVLVGGEALPPELVRRWRARLPG-ARLVNLYGPTETTVDSTYYEVT-PPDADGGSVPIGRPI 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1825 PNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPF-VSGERLYRTGDRACWLPNGTIRLLGRMDY 1903
Cdd:COG1020 795 ANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADD 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1904 QVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVP---SDVNTNALRAALTKELPAYMIPAHLIPLEN 1980
Cdd:COG1020 875 QVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPeagAAAAAALLRLALALLLPPYMVPAAVVLLLP 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1981 MPLTLNGKLDRNALPVPNNVLSRPYTAPVNDIQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARLAAEGWSMT 2060
Cdd:COG1020 955 LPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLL 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2061 IRDLFRYSTIQELCGHITPLASQADQGPAEGEAELTPIQRRFFGQVHAFHNHYNQSVMLFSEKGFNANALHLALRKITEH 2140
Cdd:COG1020 1035 LLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLL 1114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2141 HDAIRMIFQRDQNGHVIQFNRGINHKDHELFGLYISDWTKASLERTHLDEKLAAEETVIQSKMNVEKGPLLQAGLFKTAE 2220
Cdd:COG1020 1115 LALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLL 1194
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2221 GDHLLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAF 2300
Cdd:COG1020 1195 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLL 1274
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 2301 LPKDIENVPDRLQMNSDAAAFVLSGDWTEKLLFETQQAYGTDANELLLTALGMAL 2355
Cdd:COG1020 1275 ALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
95-1292 |
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: 933.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 95 EIEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMKKKDPLPDQPEP-SYL 173
Cdd:COG1020 110 AAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPiQYA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 174 SYIEKESQYLQSPRFAKDRLFWTQTFEHPLEYHSL-ADQTSLQKQSTSASRDTIILSPDLEQTIRIFCEEHKINIISLFM 252
Cdd:COG1020 190 DYALWQREWLQGEELARQLAYWRQQLAGLPPLLELpTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 253 ASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQLSVMRHQRFPYNLLVN 332
Cdd:COG1020 270 AAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 333 ELRNEQKDLHNL---IGISMQYQPLQWHNADDFDYETALYFSGYTANELSVQIQERidNGTIQLNFDYQNTLFSLEDIKR 409
Cdd:COG1020 350 ELQPERDLSRNPlfqVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVET--GDGLRLTLEYNTDLFDAATIER 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 410 IQSHLLTILENALHHPHSFIKELDMTNTREKQKLLCEFNKTEAVSPKAFTLHGLFERQAAFTPERLAIRFSGGSLTYAEL 489
Cdd:COG1020 428 MAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAEL 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 490 DMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQPGCSA-- 567
Cdd:COG1020 508 NARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAArl 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 568 PNFSGETLEVDMTSLASEKAENHEfTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTS 647
Cdd:COG1020 588 PELGVPVLALDALALAAEPATNPP-VPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFAS 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 648 FSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAeierLSDRTSLKRVFAGGEP 727
Cdd:COG1020 667 LSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAA----PEALPSLRLVLVGGEA 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 728 LAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPErDRDRLRIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAG 807
Cdd:COG1020 743 LPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPP-DADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGG 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 808 AGVARGYLNRPALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREA 886
Cdd:COG1020 822 AGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREA 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 887 AVTVRTD-SGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPgGAADAETYT 960
Cdd:COG1020 902 VVVAREDaPGDKRLVAYVvpeagAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAP-AAAAAAAAA 980
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 961 APRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLATVIREGTDSPY 1040
Cdd:COG1020 981 APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAA 1060
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1041 EAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSF-----EQDAGG 1115
Cdd:COG1020 1061 APLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRavrqeGPRLRL 1140
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1116 DPVQRIHDEVPFTLQTTVLGERTEQEAAAAFIKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGE 1195
Cdd:COG1020 1141 LVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1220
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1196 LY------NNRNLPALRIQYKDYAVWREGFKTGDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQE 1269
Cdd:COG1020 1221 LLllaaaaAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLL 1300
|
1210 1220
....*....|....*....|...
gi 363747658 1270 VASGLHKLARENGSTLYMVLLAA 1292
Cdd:COG1020 1301 LALLLLLALALALLLLLLLLLAL 1323
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
459-2304 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 886.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGS------LTYAELDMYASRLAAHLAARGITNESIVgVLSERSPEMLIAVLAVLKAG 532
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 533 GAYLPldpAYP--------KERLSYMLKDSGASLLLT---------QPGCSAPNFSGETLEVDmtSLASEKAENHEFTPA 595
Cdd:PRK05691 89 VIAVP---AYPpesarrhhQERLLSIIADAEPRLLLTvadlrdsllQMEELAAANAPELLCVD--TLDPALAEAWQEPAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 596 DGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQF--PLSEDDIVMVKTSFSFDAS-VWQLFWWSLSGASAYLLPP 672
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFgiDLNPDDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 673 GWEKDSAL-IVQAIHQENVTTA---HFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVLPQV----- 743
Cdd:PRK05691 244 AYFLERPLrWLEAISEYGGTISggpDFAYRLCSERVSESALERL-DLSRWRVAYSGSEPIRQDSLERFAEKFAACgfdpd 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 744 SLIHGYGPTEATV-----------------DAAFYVLDPERDRDRLRIPIGKPVPGARLYVLDP-HLAVQPSGVAGELYI 805
Cdd:PRK05691 323 SFFASYGLAEATLfvsggrrgqgipaleldAEALARNRAEPGTGSVLMSCGRSQPGHAVLIVDPqSLEVLGDNRVGEIWA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 806 AGAGVARGYLNRPALTEERFLEdpfYPGERMYKTGDVArWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAAL-RSIEGVR 884
Cdd:PRK05691 403 SGPSIAHGYWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVeREVEVVR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 885 EAAVTV--RTDSGEPELCAYVE---GLQR-----------NEVRAQLERLLPGYMVpayMIEMEQWPVTPSGKLDRNA-- 946
Cdd:PRK05691 479 KGRVAAfaVNHQGEEGIGIAAEisrSVQKilppqaliksiRQAVAEACQEAPSVVL---LLNPGALPKTSSGKLQRSAcr 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 947 -------------LPAPGGAADAETYTAPRNVTEMkLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRIAKEFDVQ 1013
Cdd:PRK05691 556 lrladgsldsyalFPALQAVEAAQTAASGDELQAR-IAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGID 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1014 VPLKDVFAHPTVEG----LATVIREGTDSPyEAIKPAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPE 1089
Cdd:PRK05691 635 LNLRQLFEAPTLAAfsaaVARQLAGGGAAQ-AAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEA 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1090 RMERAFKELIKRHESLRTSF-EQDagGDPVQRIHDEVPFTLQTTVLGE--RTEQEAAAAFIK------PFDLSQAPLFRA 1160
Cdd:PRK05691 714 ALRASFQRLVERHESLRTRFyERD--GVALQRIDAQGEFALQRIDLSDlpEAEREARAAQIReeearqPFDLEKGPLLRV 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1161 QIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLPALRIQYKDYAVW-REGFKTGDAYKtQEAYWL 1233
Cdd:PRK05691 792 TLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYADYGAWqRQWLAQGEAAR-QLAYWK 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1234 KQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIA 1313
Cdd:PRK05691 871 AQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNA 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1314 GRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSrnpVFDAMFilqnv 1393
Cdd:PRK05691 951 NRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQG---LFQVMF----- 1022
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1394 EKQDIDLREIKVRPANFAHHI------SLFDITLIATE-INGSICCEMEFSTEVFLKATIERWADHFIEFLHAALSTPET 1466
Cdd:PRK05691 1023 NHQQRDLSALRRLPGLLAEELpwhsreAKFDLQLHSEEdRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQR 1102
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1467 SLAQINILSDKEKQKIVfEFNKTQVEFAQKDVPfhRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-G 1545
Cdd:PRK05691 1103 ALGDVQLLDAAERAQLA-QWGQAPCAPAQAWLP--ELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGvG 1179
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1546 PKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQqelKHLISNLPESE-MSHICLD-- 1622
Cdd:PRK05691 1180 PDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQ---SHLLERLPQAEgVSAIALDsl 1256
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1623 DESSYEENSCNLNLSpaPEEPVYIIYTSGTTGAPKGVIVtyrnfTHAALA----WRQ-IYELDRKPVrLLQIASFSFDVF 1697
Cdd:PRK05691 1257 HLDSWPSQAPGLHLH--GDNLAYVIYTSGSTGQPKGVGN-----THAALAerlqWMQaTYALDDSDV-LMQKAPISFDVS 1328
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1698 SGDLARTLTNGGTLIVC-PDETRlEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKlpDLDILILGSDMVKAQdf 1776
Cdd:PRK05691 1329 VWECFWPLITGCRLVLAgPGEHR-DPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACT--SLRRLFSGGEALPAE-- 1403
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1777 ktLTDRFGQSM---RIINSYGVTEATIDSSFYETSMggeGTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAG 1853
Cdd:PRK05691 1404 --LRNRVLQRLpqvQLHNRYGPTETAINVTHWQCQA---EDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAG 1478
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1854 VAKGYHQKPDLTQMKFTKNPFV-SGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV 1932
Cdd:PRK05691 1479 LARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAV 1558
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1933 AVQHDKNGQAGLAAYIVP--SDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVPnNVLSRPYTAPVN 2010
Cdd:PRK05691 1559 LVREGAAGAQLVGYYTGEagQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEP-VWQQREHVEPRT 1637
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2011 DIQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARL-AAEGWSMTIRDLFRYSTIQELCGHITPLASQAD---Q 2086
Cdd:PRK05691 1638 ELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTrQACDVELPLRALFEASELGAFAEQVARIQAAGErnsQ 1717
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2087 GPAEGEAELTPI-----QRR--FFGQVHAFHNHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDqNGHVIQf 2159
Cdd:PRK05691 1718 GAIARVDRSQPVplsysQQRmwFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSV-DGVPVQ- 1795
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2160 nrginhKDHELFGLYIsDWT-----KASLERTHLdEKLAAEETviQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVI 2233
Cdd:PRK05691 1796 ------QVAEDSGLRM-DWQdfsalPADARQQRL-QQLADSEA--HQPFDLERGPLLRACLVKAAEREHyFVLTLHHIVT 1865
|
1930 1940 1950 1960 1970 1980 1990
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363747658 2234 DGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTIL-DAHTAF-LPKD 2304
Cdd:PRK05691 1866 EGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLgNEHPLLeLPAD 1938
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1050-2294 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 877.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1050 ETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGdPVQRIHDEVPFTL 1129
Cdd:PRK12467 48 ERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEG-FRQVIDASLSLTI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1130 QTTVLGE---RTEQEAAAAFI-----KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR- 1200
Cdd:PRK12467 127 PLDDLANeqgRARESQIEAYIneevaRPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYs 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1201 -----NLPALRIQYKDYAVWREGFKTGDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLH 1275
Cdd:PRK12467 207 qgrepSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1276 KLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETAL 1355
Cdd:PRK12467 287 ALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTAL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1356 EAFEHQDYPFEELVDKLELTRDMSRNPVFDAMFILQNV-----EKQDIDLREIKVRPANFAHHISLFDITLIATEINGSI 1430
Cdd:PRK12467 367 GAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTatggrDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1431 CCEMEFSTEVFLKATIERWADHFIEFLHAALSTPETSLAQINILSDKEKQKIVFEFNKTQVEFAQKDVpfHRIFEAKAEE 1510
Cdd:PRK12467 447 WAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCV--HQLIEAQARQ 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1511 IPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYI 1589
Cdd:PRK12467 525 HPERPALVFGEQVLSYAELNRQANRLAHVLIAAGvGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYM 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1590 LRDSGADILLLQQELKHLIsNLPESeMSHICLDDESSYEENSCNLNLSPA--PEEPVYIIYTSGTTGAPKGVIVTYR--- 1664
Cdd:PRK12467 605 LDDSGVRLLLTQSHLLAQL-PVPAG-LRSLCLDEPADLLCGYSGHNPEVAldPDNLAYVIYTSGSTGQPKGVAISHGala 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1665 NFTHAALAWRQIYELDrkpvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALI 1744
Cdd:PRK12467 683 NYVCVIAERLQLAADD----SMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHL 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1745 IPVMeyvyrnQFKLPDLDI----LILGSDMVkAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGEGTGdNVPI 1820
Cdd:PRK12467 759 QALL------QASRVALPRpqraLVCGGEAL-QVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFG-NVPI 830
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1821 GSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPF-VSGERLYRTGDRACWLPNGTIRLLG 1899
Cdd:PRK12467 831 GQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLG 910
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1900 RMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQhDKNGQAGLAAYIVPSDVNTNA--------LRAALTKELPAYMI 1971
Cdd:PRK12467 911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ-PGDAGLQLVAYLVPAAVADGAehqatrdeLKAQLRQVLPDYMV 989
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1972 PAHLIPLENMPLTLNGKLDRNALPVPN-NVLSRPYTAPVNDIQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAA 2050
Cdd:PRK12467 990 PAHLLLLDSLPLTPNGKLDRKALPKPDaSAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVIS 1069
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2051 RL-AAEGWSMTIRDLFRYSTiqeLCGHITPLASQAD-------QGPAEGEAELTPIQRR--FFGQVHAFHNHYNQSVMLF 2120
Cdd:PRK12467 1070 RVrQRLGIQVPLRTLFEHQT---LAGFAQAVAAQQQgaqpalpDVDRDQPLPLSYAQERqwFLWQLEPGSAAYHIPQALR 1146
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2121 SEKGFNANALHLALRKITEHHDAIRMIFqRDQNGHVIQFnrginhkDHELFGLYISDwtKASLERTHLDEKLAAE-ETVI 2199
Cdd:PRK12467 1147 LKGPLDIEALERSFDALVARHESLRTTF-VQEDGRTRQV-------IHPVGSLTLEE--PLLLAADKDEAQLKVYvEAEA 1216
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2200 QSKMNVEKGPLLQAGLFKTAEGDHLLI-ALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIA 2278
Cdd:PRK12467 1217 RQPFDLEQGPLLRVGLLRLAADEHVLVlTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWM 1296
|
1290
....*....|....*.
gi 363747658 2279 ESKQLLSEKTYWQTIL 2294
Cdd:PRK12467 1297 DAGERARQLAYWKAQL 1312
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-1339 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 814.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 8 LTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIR--FQLLEGEELeprLHLTEYKYYPLRI 85
Cdd:PRK12316 52 LSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRtvFPRGADDSL---AQVPLDRPLEVEF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 86 IDFSNVEMIEIEQWIQDQAS----IPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMKKK 161
Cdd:PRK12316 129 EDCSGLPEAEQEARLRDEAQreslQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 162 -----DPLPDQpepsYLSYIEKESQYLQSPRFAKDRLFWTQTF--EHP-LEYHSlaDQTSLQKQSTSASRDTIILSPDLE 233
Cdd:PRK12316 209 aepglPALPIQ----YADYALWQRSWLEAGEQERQLEYWRAQLgeEHPvLELPT--DHPRPAVPSYRGSRYEFSIDPALA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 234 QTIRIFCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIG 313
Cdd:PRK12316 283 EALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 314 REQLSVMRHQRFPYNLLVNELRNEQKDLHN-LIGISMQYQPLQwhnADDFDYETA-------LYFSGYTAN-ELSVQIQE 384
Cdd:PRK12316 363 DTVLGAQAHQDLPFERLVEALKVERSLSHSpLFQVMYNHQPLV---ADIEALDTVaglefgqLEWKSRTTQfDLTLDTYE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 385 RidNGTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHPHSFIKELDMTNTREKQKLLCEFNKTEAVSPKAFTLHGLF 464
Cdd:PRK12316 440 K--GGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLF 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 465 ERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPK 544
Cdd:PRK12316 518 EEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPA 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 545 ERLSYMLKDSGASLLLTQpgcsapNFSGETLEVDM----------TSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPK 614
Cdd:PRK12316 598 ERLAYMLEDSGVQLLLSQ------SHLGRKLPLAAgvqvldldrpAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPK 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 615 GVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAH 694
Cdd:PRK12316 672 GAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLH 751
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 695 FIPAMLNSFLDQaeiERLSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLdpeRDRDRLRI 774
Cdd:PRK12316 752 FVPSMLQAFLQD---EDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGGDSV 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 775 PIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFL 854
Cdd:PRK12316 826 PIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYA 905
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 855 GRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVrtdSGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMI 929
Cdd:PRK12316 906 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGKQLVGYVvleseGGDWREALKAHLAASLPEYMVPAQWL 982
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 930 EMEQWPVTPSGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRiAKE 1009
Cdd:PRK12316 983 ALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSR-ARQ 1061
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1010 FDVQVPLKDVFAHPTVEGLATVIREGTDSPYEAiKPAEKQetYPVSSAQKRIYvlQQLEDGGTGYNMPAVLELEGKLNPE 1089
Cdd:PRK12316 1062 AGIQLSPRDLFQHQTIRSLALVAKAGQATAADQ-GPASGE--VALAPVQRWFF--EQAIPQRQHWNQSLLLQARQPLDPD 1136
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1090 RMERAFKELIKRHESLRTSFEQDAGGdpVQRIHDEvpfTLQTTVLGERT--EQEAAAAFI----KPFDLSQAPLFRAQIV 1163
Cdd:PRK12316 1137 RLGRALERLVAHHDALRLRFREEDGG--WQQAYAA---PQAGEVLWQRQaaSEEELLALCeeaqRSLDLEQGPLLRALLV 1211
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1164 KISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR--NLPALRIQYKDYAVWREGFKTGDAykTQEAYWLKQLEGELP 1241
Cdd:PRK12316 1212 DMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLdaDLPARTSSYQAWARRLHEHAGARA--EELDYWQAQLEDAPH 1289
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1242 vlDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLA----RENGSTLymvLLAAYTAFLSRLSGQEDIIVGSPIAGRPH 1317
Cdd:PRK12316 1290 --ELPCENPDGALENRHERKLELRLDAERTRQLLQEApaayRTQVNDL---LLTALARVTCRWSGQASVLVQLEGHGRED 1364
|
1370 1380
....*....|....*....|....*.
gi 363747658 1318 K----DLEPILGMFVNTLALRTRPEG 1339
Cdd:PRK12316 1365 LfediDLSRTVGWFTSLFPVRLTPAA 1390
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1512-1994 |
0e+00 |
|
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: 782.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYIL 1590
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGvAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1591 RDSGADILLLQqelkhlisnlpesemshiclddessyeenscnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAA 1670
Cdd:cd17650 81 EDSGAKLLLTQ--------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1671 LAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALIIPVMEY 1750
Cdd:cd17650 123 HAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1751 VYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGEGTGDNVPIGSPLPNVHMY 1830
Cdd:cd17650 203 VYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1831 VLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGY 1910
Cdd:cd17650 283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1911 RIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD-VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKL 1989
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAAtLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
....*
gi 363747658 1990 DRNAL 1994
Cdd:cd17650 443 DRRAL 447
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
8-1037 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 689.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 8 LTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTEYKYYPLRIID 87
Cdd:PRK10252 10 LVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLPEIID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 88 FSnvemieiEQ---------WIQDQASIPFKLINS-PLYQFYLLRI-DSHEVWlFAKFHHIIMDGISLNVMGNQIIDLYQ 156
Cdd:PRK10252 90 LR-------TQpdphaaaqaLMQADLQQDLRVDSGkPLVFHQLIQLgDNRWYW-YQRYHHLLVDGFSFPAITRRIAAIYC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 157 KMKKKDPLPDQPEPSYLSYIEKESQYLQSPRFAKDRLFWTQTF-EHPlEYHSLADQ-TSLQKQSTSASRDTiiLSPDLEQ 234
Cdd:PRK10252 162 AWLRGEPTPASPFTPFADVVEEYQRYRASEAWQRDAAFWAEQRrQLP-PPASLSPApLPGRSASADILRLK--LEFTDGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 235 TIRIFCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNR-GSKAEKeMLGMFVSSLPIRITVDPDTDFLSFVRTIG 313
Cdd:PRK10252 239 FRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlGSAALT-ATGPVLNVLPLRVHIAAQETLPELATRLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 314 REQLSVMRHQRFPYNLLVNELrNEQKDLHNLIGISMQYQPlqwhnaddFDYEtaLYFSGYTAN--ELS------VQIQER 385
Cdd:PRK10252 318 AQLKKMRRHQRYDAEQIVRDS-GRAAGDEPLFGPVLNIKV--------FDYQ--LDFPGVQAQthTLAtgpvndLELALF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 386 ID-NGTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHPHSFIKELDMTNTREKQKLlCEFNKTEAVSPKAfTLHGLF 464
Cdd:PRK10252 387 PDeHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQL-AQVNATAVEIPET-TLSALV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 465 ERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPK 544
Cdd:PRK10252 465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 545 ERLSYMLKDSGASLLLTQPGcSAPNFSG----ETLEVDMTSLASEKAENHEFTPADggsLAYVIYTSGSTGQPKGVAVEH 620
Cdd:PRK10252 545 DRLKMMLEDARPSLLITTAD-QLPRFADvpdlTSLCYNAPLAPQGAAPLQLSQPHH---TAYIIFTSGSTGRPKGVMVGQ 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 621 RQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAML 700
Cdd:PRK10252 621 TAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSML 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 701 NSFLDQAEIERLSDRT-SLKRVFAGGEPLAPRTAARFASvLPQVSLIHGYGPTEATVDAAFYVLDPErDRDRLR---IPI 776
Cdd:PRK10252 701 AAFVASLTPEGARQSCaSLRQVFCSGEALPADLCREWQQ-LTGAPLHNLYGPTEAAVDVSWYPAFGE-ELAAVRgssVPI 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 777 GKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGR 856
Cdd:PRK10252 779 GYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGR 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 857 TDDQVKIRGYRIEPGEIEAALRSIEGVREAAV-------TVRTDSGEPELCAYV-----EGLQRNEVRAQLERLLPGYMV 924
Cdd:PRK10252 859 SDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacvinqAAATGGDARQLVGYLvsqsgLPLDTSALQAQLRERLPPHMV 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 925 PAYMIEMEQWPVTPSGKLDRNALPAPGGAADAETyTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVS 1004
Cdd:PRK10252 939 PVVLLQLDQLPLSANGKLDRKALPLPELKAQVPG-RAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAA 1017
|
1050 1060 1070
....*....|....*....|....*....|...
gi 363747658 1005 RIAKEFDVQVPLKDVFAHPTVEGLATVIREGTD 1037
Cdd:PRK10252 1018 QLSRQFARQVTPGQVMVASTVAKLATLLDAEED 1050
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
999-2410 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 683.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 999 ATALVSRIAKEFDVQvpLKDVFAH----------PTVEGLATVIREGTDSpyEAIKPAEKQETYPVSSAQKRIYVLQQLE 1068
Cdd:PRK12316 1498 AEATVQRLADDYARE--LQALIEHccdernrgvtPSDFPLAGLSQAQLDA--LPLPAGEIADIYPLSPMQQGMLFHSLYE 1573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1069 DGGTGYNMPAVLELEGkLNPERMERAFKELIKRHESLRTSF-EQDAGGDPVQRIHDEV--PFTLQTTV----LGERTEQE 1141
Cdd:PRK12316 1574 QEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFlWQDGLEQPLQVIHKQVelPFAELDWRgredLGQALDAL 1652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1142 AAAAFIKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRNLPALRIQYKDYAVWREGFKT 1221
Cdd:PRK12316 1653 AQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQDA 1732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1222 GDAyktqEAYWLKQLeGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLS 1301
Cdd:PRK12316 1733 AAS----EAFWKEQL-AALEEPTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYT 1807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1302 GQEDIIVGSPIAGRPHK--DLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEElvdkLELTRDMS 1379
Cdd:PRK12316 1808 GQETVAFGATVAGRPAElpGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYD----IQRWAGQG 1883
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1380 RNPVFDAMFILQNVE-----KQDIDLREIKVRPANfaHHISLFDITLiATEINGSICCEMEFSTEVFLKATIERWADHFI 1454
Cdd:PRK12316 1884 GEALFDSLLVFENYPvaealKQGAPAGLVFGRVSN--HEQTNYPLTL-AVTLGETLSLQYSYDRGHFDAAAIERLDRHLL 1960
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1455 EFLHAALSTPETSLAQINILSDKEKQKIVFEFNKTQvEFAQKDVPFHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERAN 1534
Cdd:PRK12316 1961 HLLEQMAEDAQAALGELALLDAGERQRILADWDRTP-EAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRAN 2039
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1535 RLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQqelKHLISNLP- 1612
Cdd:PRK12316 2040 RLAHRLRARGvGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQ---RHLLERLPl 2116
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1613 ESEMSHICLDDESSYEEN-SCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVtyrnfTHAALAWR-----QIYELDRKPvRL 1686
Cdd:PRK12316 2117 PAGVARLPLDRDAEWADYpDTAPAVQLAGENLAYVIYTSGSTGLPKGVAV-----SHGALVAHcqaagERYELSPAD-CE 2190
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1687 LQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLePAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQfKLPDLDILIL 1766
Cdd:PRK12316 2191 LQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWD-PEQLYDEMERHGVTILDFPPVYLQQLAEHAERDG-RPPAVRVYCF 2268
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1767 GSDMVKAQDFkTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGEGTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGE 1846
Cdd:PRK12316 2269 GGEAVPAASL-RLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGE 2347
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1847 LCIGGAGVAKGYHQKPDLTQMKFTKNPF-VSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTG 1925
Cdd:PRK12316 2348 LYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHP 2427
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1926 LVREAAVAVQHDKNGQAgLAAYIVPSDVNTN---ALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVPN-NVL 2001
Cdd:PRK12316 2428 AVREAVVVAQDGASGKQ-LVAYVVPDDAAEDllaELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDvSQL 2506
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2002 SRPYTAPVNDIQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARL-AAEGWSMTIRDLFRYSTIQELCGHITPL 2080
Cdd:PRK12316 2507 RQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVrQDLGLEVPLRILFERPTLAAFAASLESG 2586
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2081 -ASQA-DQGPAEGEAEL----TPIQRRFFGQVHAFHNHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFqRDQNG 2154
Cdd:PRK12316 2587 qTSRApVLQKVTRVQPLplshAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRF-VEVGE 2665
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2155 HVIQFNRGINHKDHELFglyisdWTKASLERThLDEKLAAEetvIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVI 2233
Cdd:PRK12316 2666 QTRQVILPNMSLRIVLE------DCAGVADAA-IRQRVAEE---IQRPFDLARGPLLRVRLLALDGQEHvLVITQHHIVS 2735
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2234 DGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDIENVPDRLQ 2313
Cdd:PRK12316 2736 DGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQ 2815
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2314 MNSDAAAFVLSGDWTEKLLFETQQAYGTDANELLLTALGMALSEWAGHDQIVISTEGHGREghvpNIDISRTVGWFTSIY 2393
Cdd:PRK12316 2816 SHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN----RAETERLIGFFVNTQ 2891
|
1450
....*....|....*..
gi 363747658 2394 PILLDMGIPEPFEDQLA 2410
Cdd:PRK12316 2892 VLRAQVDAQLAFRDLLG 2908
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1045-2099 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 669.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1045 PAEKQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGkLNPERMERAFKELIKRHESLRTSF-EQDAGGDPVQRIHD 1123
Cdd:PRK12316 4096 LGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvWQGELGRPLQVVHK 4174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1124 --EVPFTLQ----TTVLGERTEQEAAAAFIKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELY 1197
Cdd:PRK12316 4175 qvSLPFAELdwrgRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY 4254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1198 NNRNLPALRIQYKDYAVWregFKTGDAYKTqEAYWLKQLEGELPVLDLPADHARPPVRSFAG-DKVSFTLDQEVASGLHK 1276
Cdd:PRK12316 4255 SGRPPAQPGGRYRDYIAW---LQRQDAAAS-EAFWREQLAALDEPTRLAQAIARADLRSANGyGEHVRELDATATARLRE 4330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1277 LARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETA 1354
Cdd:PRK12316 4331 FARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAelPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQN 4410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1355 LEAFEHQDYPFEELvdklELTRDMSRNPVFDAMFILQN------VEKQ-DIDLREIKVRpanfAHHISLFDITLiATEIN 1427
Cdd:PRK12316 4411 LALREHEHTPLYEI----QRWAGQGGEALFDSLLVFENypvseaLQQGaPGGLRFGEVT----NHEQTNYPLTL-AVGLG 4481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1428 GSICCEMEFSTEVFLKATIERWADHFIEFLHAALSTPETSLAQINILSDKEKQKIVFEFNKTQVEF-AQKDVpfHRIFEA 1506
Cdd:PRK12316 4482 ETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYpATRCV--HQLVAE 4559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1507 KAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKAR 1585
Cdd:PRK12316 4560 RARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGvGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER 4639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1586 IEYILRDSGADILLLQqelKHLISNLPESE-MSHICLDDESSYEENSCNLNLSP-APEEPVYIIYTSGTTGAPKGVIVTY 1663
Cdd:PRK12316 4640 LAYMMEDSGAALLLTQ---SHLLQRLPIPDgLASLALDRDEDWEGFPAHDPAVRlHPDNLAYVIYTSGSTGRPKGVAVSH 4716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1664 RNFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLePAEIYKIMNSQRITVMESTPAL 1743
Cdd:PRK12316 4717 GSLVNHLHATGERYELTPDD-RVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWD-PERLYAEIHEHRVTVLVFPPVY 4794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1744 IIPVMEYvYRNQFKLPDLDILILGSDMVkAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGEGTGDNVPIGSP 1823
Cdd:PRK12316 4795 LQQLAEH-AERDGEPPSLRVYCFGGEAV-AQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTP 4872
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1824 LPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPF-VSGERLYRTGDRACWLPNGTIRLLGRMD 1902
Cdd:PRK12316 4873 LGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVD 4952
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1903 YQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAgLAAYIVPSDVN-----------TNALRAALTKELPAYMI 1971
Cdd:PRK12316 4953 HQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQ-LVGYVVPQDPAladadeaqaelRDELKAALRERLPEYMV 5031
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1972 PAHLIPLENMPLTLNGKLDRNALPVPN-NVLSRPYTAPVNDIQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAA 2050
Cdd:PRK12316 5032 PAHLVFLARMPLTPNGKLDRKALPQPDaSLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTS 5111
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 363747658 2051 RLAAE-GWSMTIRDLFRYSTIQELcghiTPLASQADQGPAEGEAELTPIQ 2099
Cdd:PRK12316 5112 RIQLElGLELPLRELFQTPTLAAF----VELAAAAGSGDDEKFDDLEELL 5157
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-1215 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 668.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 3 EHTYSLTHAQRRVWFTELLEPNTSICNLTACVKFKGnIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTeYKY-- 80
Cdd:PRK12467 2644 EDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQVV-YKQar 2721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 81 YPLRIIDFSN--VEMIEIEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISlnvmGNQII-DLYQK 157
Cdd:PRK12467 2722 LPFSRLDWRDraDLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWS----GSQLLgEVLQR 2797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 158 MKKKDPLPdqPEPSYLSYIekesQYLQSPRFAKDRLFWTQTFEHPLEYHSLADQTSLQKQSTSASRDTIILSPDLEQTIR 237
Cdd:PRK12467 2798 YFGQPPPA--REGRYRDYI----AWLQAQDAEASEAFWKEQLAALEEPTRLARALYPAPAEAVAGHGAHYLHLDATQTRQ 2871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 238 I--FCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNR--GSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIG 313
Cdd:PRK12467 2872 LieFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRpaQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQ 2951
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 314 REQLSVMRHQRFPY----------------NLLVNELRNEQKDLHNLIGISMQYQPLqwHNADDFDYetalyfsgytANE 377
Cdd:PRK12467 2952 AQNLALREFEHTPLadiqrwagqggealfdSILVFENYPISEALKQGAPSGLRFGAV--SSREQTNY----------PLT 3019
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 378 LSVQIQEridngTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHPHSFIKELDMTNTREKQKLLCEFNKTEAVSPKA 457
Cdd:PRK12467 3020 LAVGLGD-----TLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSE 3094
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 458 FTLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLP 537
Cdd:PRK12467 3095 RLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 538 LDPAYPKERLSYMLKDSGASLLLTQPGC----SAPNfSGETLEVDMTSLASEkAENHEFTPADGGSLAYVIYTSGSTGQP 613
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLTQAHLleqlPAPA-GDTALTLDRLDLNGY-SENNPSTRVMGENLAYVIYTSGSTGKP 3252
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 614 KGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGAsAYLLPPGWEKDSALIVQAIHQENVTTA 693
Cdd:PRK12467 3253 KGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGG-CLVVRDNDLWDPEELWQAIHAHRISIA 3331
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 694 HFIPAMLNSFLDQAEIerlSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRLR 773
Cdd:PRK12467 3332 CFPPAYLQQFAEDAGG---ADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPY 3408
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 774 IPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFY-PGERMYKTGDVARWLPDGNVE 852
Cdd:PRK12467 3409 APIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIE 3488
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 853 FLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAY 927
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVvpadpQGDWRETLRDHLAASLPDYMVPAQ 3568
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 928 MIEMEQWPVTPSGKLDRNALPAPgGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRIA 1007
Cdd:PRK12467 3569 LLVLAAMPLGPNGKVDRKALPDP-DAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIR 3647
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1008 KEFDVQVPLKDVFAHPTVEGLATVIREGTdspyeaikpaekqetypvssaqkriyvlqqledggtgynmpavLELEGKLN 1087
Cdd:PRK12467 3648 QSLGLKLSLRDLMSAPTIAELAGYSPLGD-------------------------------------------VPVNLLLD 3684
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1088 PERMERAFKELIKRHESLRTSFEqdagGDPVQRIHDEvpftlqttvlgerteqeaaaafikpfdlsqaplfraqivkisd 1167
Cdd:PRK12467 3685 LNRLETGFPALFCRHEGLGTVFD----YEPLAVILEG------------------------------------------- 3717
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*...
gi 363747658 1168 ERHLLLVDMHHIISDGvsvnilirefgelYNNRNLPALRIQYKDYAVW 1215
Cdd:PRK12467 3718 DRHVLGLTCRHLLDDG-------------WQDTSLQAMAVQYADYILW 3752
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
472-947 |
0e+00 |
|
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: 667.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQPGcsapnfsgetlevdmtslasekaenheftpadggSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQ 631
Cdd:cd05930 81 EDSGAKLVLTDPD----------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 632 HQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIER 711
Cdd:cd05930 127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 712 LsdrTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRlRIPIGKPVPGARLYVLDPH 791
Cdd:cd05930 207 L---PSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDG-RVPIGRPIPNTRVYVLDEN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 792 LAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPG 871
Cdd:cd05930 283 LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 872 EIEAALRSIEGVREAAVTVRTD-SGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRN 945
Cdd:cd05930 363 EIEAALLAHPGVREAAVVAREDgDGEKRLVAYVvpdegGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
..
gi 363747658 946 AL 947
Cdd:cd05930 443 AL 444
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-1025 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 658.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 3 EHTYSLTHAQRRVWFTELLEPNTSICNLTACVKFKGnIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTEYKY-Y 81
Cdd:PRK12316 4100 EDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGELGRPLQVVHKQVsL 4178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 82 PLRIIDFSNVEMIE--IEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMK 159
Cdd:PRK12316 4179 PFAELDWRGRADLQaaLDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGRP 4258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 160 kkdplPDQPEPSYLSYIekesQYLQSPRFAKDRLFWTQTFEHPLEYHSLADQTSLQKQSTSASRDTIILSPDLEQTIRI- 238
Cdd:PRK12316 4259 -----PAQPGGRYRDYI----AWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRSANGYGEHVRELDATATARLr 4329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 239 -FCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGS--KAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIGRE 315
Cdd:PRK12316 4330 eFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAelPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQ 4409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 316 QLSVMRHQRFPynlLVNELRNEQKDLHNLIGISMQYQPLQWHNADDFDYETALYFSGYTANE-------LSVQIQEridn 388
Cdd:PRK12316 4410 NLALREHEHTP---LYEIQRWAGQGGEALFDSLLVFENYPVSEALQQGAPGGLRFGEVTNHEqtnypltLAVGLGE---- 4482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 389 gTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHPHSFIKELDMTNTREKQKLLCEFNKTEAVSPKAFTLHGLFERQA 468
Cdd:PRK12316 4483 -TLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERA 4561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 469 AFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLS 548
Cdd:PRK12316 4562 RMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLA 4641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 549 YMLKDSGASLLLTQPGCSA--PNFSG-ETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVS 625
Cdd:PRK12316 4642 YMMEDSGAALLLTQSHLLQrlPIPDGlASLALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN 4721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 626 FLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPG-WekDSALIVQAIHQENVTTAHFIPAMLNSFL 704
Cdd:PRK12316 4722 HLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSlW--DPERLYAEIHEHRVTVLVFPPVYLQQLA 4799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 705 DQAeiERLSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIGKPVPGAR 784
Cdd:PRK12316 4800 EHA--ERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRS 4877
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 785 LYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVEFLGRTDDQVKI 863
Cdd:PRK12316 4878 GYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKI 4957
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 864 RGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYV-------------EGLQRNEVRAQLERLLPGYMVPAYMIE 930
Cdd:PRK12316 4958 RGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVvpqdpaladadeaQAELRDELKAALRERLPEYMVPAHLVF 5037
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 931 MEQWPVTPSGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRIAKEF 1010
Cdd:PRK12316 5038 LARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLEL 5117
|
1050
....*....|....*
gi 363747658 1011 DVQVPLKDVFAHPTV 1025
Cdd:PRK12316 5118 GLELPLRELFQTPTL 5132
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
461-947 |
0e+00 |
|
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: 634.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 461 HGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDP 540
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 541 AYPKERLSYMLKDSGASLLLTQPGCSAPnFSGETL--EVDMTSLASEKAENHEfTPADGGSLAYVIYTSGSTGQPKGVAV 618
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAAR-LPAGGDvaLLGDEALAAPPATPPL-VPPRPDNLAYVIYTSGSTGRPKGVMV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 619 EHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPA 698
Cdd:cd17646 159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 699 MLNSFLDQAEIERLsdrTSLKRVFAGGEPLAPRTAARFASvLPQVSLIHGYGPTEATVDAAFYVLDPerDRDRLRIPIGK 778
Cdd:cd17646 239 MLRVFLAEPAAGSC---ASLRRVFCSGEALPPELAARFLA-LPGAELHNLYGPTEAAIDVTHWPVRG--PAETPSVPIGR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 779 PVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTD 858
Cdd:cd17646 313 PVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 859 DQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV------EGLQRNEVRAQLERLLPGYMVPAYMIEM 931
Cdd:cd17646 393 DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAApAGAARLVGYVvpaagaAGPDTAALRAHLAERLPEYMVPAAFVVL 472
|
490
....*....|....*.
gi 363747658 932 EQWPVTPSGKLDRNAL 947
Cdd:cd17646 473 DALPLTANGKLDRAAL 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1042-2101 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 628.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1042 AIKPAEKQETYPVSSAQKRIyVLQQLEDGGTG-YNMPAVLELEGkLNPERMERAFKELIKRHESLRTSF-EQDAGGDPVQ 1119
Cdd:PRK12467 2637 PVAVGDIEDIYPLSPMQQGM-LFHTLYEGGAGdYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFlWDGELEEPLQ 2714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1120 RIHD--EVPFTL----QTTVLGERTEQEAAAAFIKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREF 1193
Cdd:PRK12467 2715 VVYKqaRLPFSRldwrDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEV 2794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1194 GELYNNRNLPALRIQYKDYAVWregFKTGDAyKTQEAYWLKQL----EGELPVLDLPADHARPpvRSFAGDKvSFTLDQE 1269
Cdd:PRK12467 2795 LQRYFGQPPPAREGRYRDYIAW---LQAQDA-EASEAFWKEQLaaleEPTRLARALYPAPAEA--VAGHGAH-YLHLDAT 2867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1270 VASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGKPFVQYL 1347
Cdd:PRK12467 2868 QTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAqlRGAEQQLGLFINTLPVIASPRAEQTVSDWL 2947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1348 QEVRETALEAFEHQDYPFeelvdkLELTRDMSR--NPVFDAMFILQNV-------EKQDIDLREIKVRpanfAHHISLFD 1418
Cdd:PRK12467 2948 QQVQAQNLALREFEHTPL------ADIQRWAGQggEALFDSILVFENYpisealkQGAPSGLRFGAVS----SREQTNYP 3017
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1419 ITLiATEINGSICCEMEFSTEVFLKATIERWADHFIEFLHAALSTPETSLAQINILSDKEKQKIVFEFNKTQVEFAQkDV 1498
Cdd:PRK12467 3018 LTL-AVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPS-ER 3095
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1499 PFHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLA-RTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPI 1577
Cdd:PRK12467 3096 LVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAhRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPL 3175
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1578 DSHYPKARIEYILRDSGADILLLQQelkHLISNLPESEMSH---ICLDDESSYEENscNLNLSPAPEEPVYIIYTSGTTG 1654
Cdd:PRK12467 3176 DPEYPRERLAYMIEDSGVKLLLTQA---HLLEQLPAPAGDTaltLDRLDLNGYSEN--NPSTRVMGENLAYVIYTSGSTG 3250
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1655 APKGVIVTYRNFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRlEPAEIYKIMNSQRI 1734
Cdd:PRK12467 3251 KPKGVGVRHGALANHLCWIAEAYELDAND-RVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLW-DPEELWQAIHAHRI 3328
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1735 TVMESTPALIIPVMEYVYRNQfkLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGEGT 1814
Cdd:PRK12467 3329 SIACFPPAYLQQFAEDAGGAD--CASLDIYVFGGEAVPPAAFEQVKRKLKPR-GLTNGYGPTEAVVTVTLWKCGGDAVCE 3405
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1815 GDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPF-VSGERLYRTGDRACWLPNG 1893
Cdd:PRK12467 3406 APYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsGSGGRLYRTGDLARYRADG 3485
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1894 TIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAgLAAYIVPSDVNTN---ALRAALTKELPAYM 1970
Cdd:PRK12467 3486 VIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQ-LVAYVVPADPQGDwreTLRDHLAASLPDYM 3564
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1971 IPAHLIPLENMPLTLNGKLDRNALPVPNNVLSRPYTAPVNDIQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAA 2050
Cdd:PRK12467 3565 VPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLS 3644
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|..
gi 363747658 2051 RL-AAEGWSMTIRDLFRYSTIQELCGHItplasqadQGPAEGEAELTPIQRR 2101
Cdd:PRK12467 3645 RIrQSLGLKLSLRDLMSAPTIAELAGYS--------PLGDVPVNLLLDLNRL 3688
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1051-1464 |
0e+00 |
|
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: 588.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1051 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGdPVQRIHDEVPFTLQ 1130
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGE-PVQVILPPLPLPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1131 TTVLGERTE-------QEAAAAFI-KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR-- 1200
Cdd:cd19531 80 VVDLSGLPEaereaeaQRLAREEArRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFla 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1201 ----NLPALRIQYKDYAVWREGFKTGDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHK 1276
Cdd:cd19531 160 grpsPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1277 LARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALE 1356
Cdd:cd19531 240 LARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1357 AFEHQDYPFEELVDKLELTRDMSRNPVFDAMFILQNVEKQDIDLREIKVRPANFAHHISLFDITLIATEINGSICCEMEF 1436
Cdd:cd19531 320 AYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEY 399
|
410 420
....*....|....*....|....*...
gi 363747658 1437 STEVFLKATIERWADHFIEFLHAALSTP 1464
Cdd:cd19531 400 NTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
463-947 |
0e+00 |
|
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: 574.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAY 542
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 543 PKERLSYMLKDSGASLLLTQPGCSAPNFSGETLEVDMTSLASEKAENHEfTPADGGSLAYVIYTSGSTGQPKGVAVEHRQ 622
Cdd:cd12117 82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPA-VPVSPDDLAYVMYTSGSTGRPKGVAVTHRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 623 AVSFLTGMQHqFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNS 702
Cdd:cd12117 161 VVRLVKNTNY-VTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 703 FLDQAEiERLSdrtSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRlRIPIGKPVPG 782
Cdd:cd12117 240 LADEDP-ECFA---GLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAG-SIPIGRPIAN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 783 ARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVK 862
Cdd:cd12117 315 TRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 863 IRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTP 938
Cdd:cd12117 395 IRGFRIELGEIEAALRAHPGVREAVVVVREDaGGDKRLVAYVvaeGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTA 474
|
....*....
gi 363747658 939 SGKLDRNAL 947
Cdd:cd12117 475 NGKVDRRAL 483
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
8-1340 |
1.41e-180 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 622.19 E-value: 1.41e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 8 LTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIR--FQLLEGeelEPRLHLTEYKYYPLRI 85
Cdd:PRK05691 1731 LSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRttFPSVDG---VPVQQVAEDSGLRMDW 1807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 86 IDFSNVEMIEIEQWIQ----DQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMKKK 161
Cdd:PRK05691 1808 QDFSALPADARQQRLQqladSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDD 1887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 162 DPLPDQPEP-SYLSYIEKESQYLQSPRFAKDRLFWTQTF--EHPLeYHSLADQTSLQKQSTSASRDTIILSPDLEQTIRI 238
Cdd:PRK05691 1888 RESPLEPLPvQYLDYSVWQRQWLESGERQRQLDYWKAQLgnEHPL-LELPADRPRPPVQSHRGELYRFDLSPELAARVRA 1966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 239 FCEEHKiniISLFM---ASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPD---TDFLSFVRTI 312
Cdd:PRK05691 1967 FNAQRG---LTLFMtmtATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQmsvSELLEQVRQT 2043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 313 GREQLSvmrHQRFPYNLLVNELRNEQKDLHN-LIGISMQYQPLQWHNADDFDYETALYF---SGYTANELSVQIQERidN 388
Cdd:PRK05691 2044 VIEGQS---HQDLPFDHLVEALQPPRSAAYNpLFQVMCNVQRWEFQQSRQLAGMTVEYLvndARATKFDLNLEVTDL--D 2118
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 389 GTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHPHSFIKELDMTNTREKQKLLCEFNKTEAVSPKAFTLHGLFERQA 468
Cdd:PRK05691 2119 GRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQA 2198
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 469 AFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLS 548
Cdd:PRK05691 2199 ARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLH 2278
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 549 YMLKDSGASLLLTQpgcsAPNFS--GE--------TLEVDMTSLASEKAenhefTPADGGSL----AYVIYTSGSTGQPK 614
Cdd:PRK05691 2279 YMIEDSGIGLLLSD----RALFEalGElpagvarwCLEDDAAALAAYSD-----APLPFLSLpqhqAYLIYTSGSTGKPK 2349
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 615 GVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPG-WekDSALIVQAIHQENVTTA 693
Cdd:PRK05691 2350 GVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGqW--GAEEICQLIREQQVSIL 2427
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 694 HFIPAMlNSFLDQAEIERlSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEaTVDAAFYVLDPER-DRDRL 772
Cdd:PRK05691 2428 GFTPSY-GSQLAQWLAGQ-GEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTE-TVVMPLACLAPEQlEEGAA 2504
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 773 RIPIGKPVpGARL-YVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYP-GERMYKTGDVARWLPDGN 850
Cdd:PRK05691 2505 SVPIGRVV-GARVaYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGL 2583
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 851 VEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGLQ-----------RNEVRAQLERLL 919
Cdd:PRK05691 2584 VEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVagqddeaqaalREALKAHLKQQL 2663
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 920 PGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKA 999
Cdd:PRK05691 2664 PDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILS 2743
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1000 TALVSRiAKEFDVQVPLKDVFAHPTVEGLATVIregTDSPYEAIKPAEKQETYPVSSAQKRIYVLQQLEDggTGYNMPAV 1079
Cdd:PRK05691 2744 IQVVSR-ARQLGIHFSPRDLFQHQTVQTLAAVA---THSEAAQAEQGPLQGASGLTPIQHWFFDSPVPQP--QHWNQALL 2817
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1080 LELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGDPVQ-RIHDEVPFTLQTTVLGERTEQEAAAAFIKPFDLSQAPLF 1158
Cdd:PRK05691 2818 LEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEyRAVTAQELLWQVTVADFAECAALFADAQRSLDLQQGPLL 2897
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1159 RAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRN------LPALRIQYKDYAVWREGFKTGDAYKTQEAYW 1232
Cdd:PRK05691 2898 RALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSagaepaLPAKTSAFRDWAARLQAYAGSESLREELGWW 2977
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1233 LKQLEGelPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGST-LYMVLLAAYTAFLSRLSGQEDIIVGSP 1311
Cdd:PRK05691 2978 QAQLGG--PRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTqVNDLLLTALARVLCRWSGQPSVLVQLE 3055
|
1370 1380 1390
....*....|....*....|....*....|...
gi 363747658 1312 IAGRPHK----DLEPILGMFVNTLALRTRPEGG 1340
Cdd:PRK05691 3056 GHGREALfddiDLTRSVGWFTSAYPLRLTPAPG 3088
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
463-950 |
3.49e-179 |
|
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: 558.48 E-value: 3.49e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAY 542
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 543 PKERLSYMLKDSGASLLLTQPGCSAP-NFSGETLEVDMTSLASEKAENHEfTPADGGSLAYVIYTSGSTGQPKGVAVEHR 621
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPiAFIGLIDLLDEDTIYHEESENLE-PVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 622 QAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLN 701
Cdd:cd17655 161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 702 sFLDQAeieRLSDRTSLKRVFAGGEPLAPRTAARF-ASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRdRLRIPIGKPV 780
Cdd:cd17655 241 -LLDAA---DDSEGLSLKHLIVGGEALSTELAKKIiELFGTNPTITNAYGPTETTVDASIYQYEPETDQ-QVSVPIGKPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 781 PGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQ 860
Cdd:cd17655 316 GNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 861 VKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPV 936
Cdd:cd17655 396 VKIRGYRIELGEIEARLLQHPDIKEAVVIARKDeQGQNYLCAYIvseKELPVAQLREFLARELPDYMIPSYFIKLDEIPL 475
|
490
....*....|....
gi 363747658 937 TPSGKLDRNALPAP 950
Cdd:cd17655 476 TPNGKVDRKALPEP 489
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
5-425 |
1.55e-175 |
|
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: 545.04 E-value: 1.55e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 5 TYSLTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEgEELEPRLHLTEYKYYPLR 84
Cdd:cd19533 1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTE-EEGEPYQWIDPYTPVPIR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 85 IIDFS--NVEMIEIEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMKKKD 162
Cdd:cd19533 80 HIDLSgdPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 163 PLPDQPEPSYLSYIEKESQYLQSPRFAKDRLFWTQTFEHPLEYHSLADQTSlqKQSTSASRDTIILSPDLEQTIRIFCEE 242
Cdd:cd19533 160 PAPPAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAP--GRSLAFLRRTAELPPELTRTLLEAAEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 243 HKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQLSVMRH 322
Cdd:cd19533 238 HGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 323 QRFPYNLLVNELRNEQkDLHNLIGISMQYQPLQWHNADDF-DYETALYFSGYTaNELSVQIQERIDNGTIQLNFDYQNTL 401
Cdd:cd19533 318 QRYRYEDLRRDLGLTG-ELHPLFGPTVNYMPFDYGLDFGGvVGLTHNLSSGPT-NDLSIFVYDRDDESGLRIDFDANPAL 395
|
410 420
....*....|....*....|....
gi 363747658 402 FSLEDIKRIQSHLLTILENALHHP 425
Cdd:cd19533 396 YSGEDLARHQERLLRLLEEAAADP 419
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1512-1994 |
5.67e-175 |
|
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: 544.82 E-value: 5.67e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQnRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYI 1589
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLR-ERGVGPGdlVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1590 LRDSGADILLLQqelkhlisnlpesemshiclddessyeenscnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYRNFTHA 1669
Cdd:cd05930 80 LEDSGAKLVLTD--------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1670 ALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALIIPVME 1749
Cdd:cd05930 122 LLWMQEAYPLTPGD-RVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1750 YVYRNQFklPDLDILILGSDMVKAQDFKTLTDRFGQsMRIINSYGVTEATIDSSFYETSMGGEgTGDNVPIGSPLPNVHM 1829
Cdd:cd05930 201 ELELAAL--PSLRLVLVGGEALPPDLVRRWRELLPG-ARLVNLYGPTEATVDATYYRVPPDDE-EDGRVPIGRPIPNTRV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1830 YVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKING 1909
Cdd:cd05930 277 YVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1910 YRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPLTLN 1986
Cdd:cd05930 357 YRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggeLDEEELRAHLAERLPDYMVPSAFVVLDALPLTPN 436
|
....*...
gi 363747658 1987 GKLDRNAL 1994
Cdd:cd05930 437 GKVDRKAL 444
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1048-1483 |
7.60e-175 |
|
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: 544.62 E-value: 7.60e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1048 KQETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGDPVQRIHDEVPF 1127
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1128 TLQTTVLG---ERTEQEAAAAFI-----KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELY-- 1197
Cdd:pfam00668 81 ELEIIDISdlsESEEEEAIEAFIqrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYqq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1198 --NNRNLPALRIQ-YKDYAVWREGFKTGDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGL 1274
Cdd:pfam00668 161 llKGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1275 HKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETA 1354
Cdd:pfam00668 241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1355 LEAFEHQDYPFEELVDKLELTRDMSRNPVFDAMFILQNVEKQDI-----DLREIKVRPANFAHHISLFDITLIATEINGS 1429
Cdd:pfam00668 321 LSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSqeeefQLSELDLSVSSVIEEEAKYDLSLTASERGGG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 363747658 1430 ICCEMEFSTEVFLKATIERWADHFIEFLHAALSTPETSLAQINILSDKEKQKIV 1483
Cdd:pfam00668 401 LTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
485-888 |
7.69e-172 |
|
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: 534.54 E-value: 7.69e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 485 TYAELDMYASRLAAHL-AARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQP 563
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 564 GcSAPNFSGETLEVDM------TSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLS 637
Cdd:TIGR01733 81 A-LASRLAGLVLPVILldplelAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 638 EDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSA-LIVQAIHQENVTTAHFIPAMLNSFLDQAEierlSDRT 716
Cdd:TIGR01733 160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAaLLAALIAEHPVTVLNLTPSLLALLAAALP----PALA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 717 SLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIGKPVPGARLYVLDPHLAVQP 796
Cdd:TIGR01733 236 SLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 797 SGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYP--GERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIE 874
Cdd:TIGR01733 316 VGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395
|
410
....*....|....
gi 363747658 875 AALRSIEGVREAAV 888
Cdd:TIGR01733 396 AALLRHPGVREAVV 409
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
464-948 |
1.32e-170 |
|
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: 534.62 E-value: 1.32e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 464 FERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYP 543
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 544 KERLSYMLKDSGASLLLTQPGcSAPNFSGET---LEVDMTSLASEkAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEH 620
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPA-LAGELAVELvavTLLDQPGAAAG-ADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 621 RQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAML 700
Cdd:cd17651 159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 701 NSFLDQAEieRLSDR-TSLKRVFAGGEPLAPRTA-ARFASVLPQVSLIHGYGPTEATVdAAFYVLDPERDRDRLRIPIGK 778
Cdd:cd17651 239 RALAEHGR--PLGVRlAALRYLLTGGEQLVLTEDlREFCAGLPGLRLHNHYGPTETHV-VTALSLPGDPAAWPAPPPIGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 779 PVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTD 858
Cdd:cd17651 316 PIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 859 DQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYVEGLQRN-----EVRAQLERLLPGYMVPAYMIEME 932
Cdd:cd17651 396 DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDrPGEKRLVAYVVGDPEApvdaaELRAALATHLPEYMVPSAFVLLD 475
|
490
....*....|....*.
gi 363747658 933 QWPVTPSGKLDRNALP 948
Cdd:cd17651 476 ALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1502-1997 |
3.64e-163 |
|
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: 513.41 E-value: 3.64e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1502 RIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQnRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDS 1579
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLR-EKGVGPdtIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1580 HYPKARIEYILRDSGADILLLQQELKHLISNLPESEMshicLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGV 1659
Cdd:cd17655 80 DYPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDL----LDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1660 IVTYRNFTHAALAWRQIYELDRKpVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMES 1739
Cdd:cd17655 156 MIEHRGVVNLVEWANKVIYQGEH-LRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1740 TPALiipVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSmGGEGTGDNVP 1819
Cdd:cd17655 235 TPAH---LKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYE-PETDQQVSVP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1820 IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLPNGTIRLLG 1899
Cdd:cd17655 311 IGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1900 RMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPS-DVNTNALRAALTKELPAYMIPAHLIPL 1978
Cdd:cd17655 391 RIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEkELPVAQLREFLARELPDYMIPSYFIKL 470
|
490
....*....|....*....
gi 363747658 1979 ENMPLTLNGKLDRNALPVP 1997
Cdd:cd17655 471 DEIPLTPNGKVDRKALPEP 489
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2092-2528 |
3.79e-163 |
|
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: 510.64 E-value: 3.79e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2092 EAELTPIQRRFFGQVHAFHNHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDqNGHVIQFNRGInhkDHELF 2171
Cdd:cd19534 1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRRE-DGGWQQRIRGD---VEELF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2172 GLYISDWTKASLErthldEKLAAEETVIQSKMNVEKGPLLQAGLFK-TAEGDHLLIALHHLVIDGVSWRILLEDLAAAYQ 2250
Cdd:cd19534 77 RLEVVDLSSLAQA-----AAIEALAAEAQSSLDLEEGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2251 QALEKKEIQLPPKTdSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDienvPDRLQMNSDAAAFVLSGDWTEK 2330
Cdd:cd19534 152 QALAGEPIPLPSKT-SFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKD----PEQTYGDARTVSFTLDEEETEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2331 LLFETQQAYGTDANELLLTALGMALSEWAGHDQIVISTEGHGREGHVPNIDISRTVGWFTSIYPILLDMGIPEPFEDQla 2410
Cdd:cd19534 227 LLQEANAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEASEDLGDT-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2411 yrIKTTKDMLRRVPNKGTGYGLLTHIGELR------HKEPEVSFNYLGQFSEEKEAETFQLSYY-QPSYEIAGEREREYE 2483
Cdd:cd19534 305 --LKRVKEQLRRIPNKGIGYGILRYLTPEGtkrlafHPQPEISFNYLGQFDQGERDDALFVSAVgGGGSDIGPDTPRFAL 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 363747658 2484 LDINALITDGRLQVKAVY-TQVFSKHSIECFMDRFHRHLIETIEHC 2528
Cdd:cd19534 383 LDINAVVEGGQLVITVSYsRNMYHEETIQQLADSYKEALEALIEHC 428
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
472-947 |
4.46e-162 |
|
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: 508.77 E-value: 4.46e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQPGcsapnfsgetlevdmtslasekaenheftpadggSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQ 631
Cdd:cd17643 81 ADSGPSLLLTDPD----------------------------------DLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 632 HQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAmlnSF--LDQAEI 709
Cdd:cd17643 127 RWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPS---AFyqLVEAAD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 710 ERLSDRTSLKRVFAGGEPLAPRTAARFAS--VLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIGKPVPGARLYV 787
Cdd:cd17643 204 RDGRDPLALRYVIFGGEALEAAMLRPWAGrfGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLRVYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 788 LDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFY-PGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGY 866
Cdd:cd17643 284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 867 RIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSG 940
Cdd:cd17643 364 RIELGEIEAALATHPSVRDAAVIVREDEpGDTRLVAYVvaddgAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443
|
....*..
gi 363747658 941 KLDRNAL 947
Cdd:cd17643 444 KLDRAAL 450
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
472-948 |
1.17e-161 |
|
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: 507.29 E-value: 1.17e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQpgcsapnfsgetlevdmtslasekaenheftpaDGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQ 631
Cdd:cd17649 81 EDSGAGLLLTH---------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 632 HQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIER 711
Cdd:cd17649 128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 712 LSDRTSLKRVFAGGEPLAPRTAARFASVlpQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIGKPVPGARLYVLDPH 791
Cdd:cd17649 208 DGRPPSLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDAD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 792 LAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFY-PGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEP 870
Cdd:cd17649 286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGaPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 871 GEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGLQ-------RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLD 943
Cdd:cd17649 366 GEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAaaaqpelRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445
|
....*
gi 363747658 944 RNALP 948
Cdd:cd17649 446 RKALP 450
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
472-948 |
4.65e-160 |
|
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: 502.17 E-value: 4.65e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQPGcsapnfsgetlevdmtslasekaenheftpadggSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQ 631
Cdd:cd17652 81 ADARPALLLTTPD----------------------------------NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 632 HQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSfLDQAEIer 711
Cdd:cd17652 127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA-LPPDDL-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 712 LSDRTslkrVFAGGEPLAPRTAARFAsvlPQVSLIHGYGPTEATVDAAFYVLDPERDRdrlrIPIGKPVPGARLYVLDPH 791
Cdd:cd17652 204 PDLRT----LVVAGEACPAELVDRWA---PGRRMINAYGPTETTVCATMAGPLPGGGV----PPIGRPVPGTRVYVLDAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 792 LAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPF-YPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEP 870
Cdd:cd17652 273 LRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 871 GEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 944
Cdd:cd17652 353 GEVEAALTEHPGVAEAVVVVRDDrPGDKRLVAYVvpapgAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
....
gi 363747658 945 NALP 948
Cdd:cd17652 433 RALP 436
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
472-947 |
2.33e-155 |
|
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: 490.27 E-value: 2.33e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQPGCSAPnFSGETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQ 631
Cdd:cd12116 81 EDAEPALVLTDDALPDR-LPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 632 HQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEier 711
Cdd:cd12116 160 ERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGW--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 712 lSDRTSLkRVFAGGEPLAPRTAARFASvlPQVSLIHGYGPTEATVDAAFYVLDPERDrdrlRIPIGKPVPGARLYVLDPH 791
Cdd:cd12116 237 -QGRAGL-TALCGGEALPPDLAARLLS--RVGSLWNLYGPTETTIWSTAARVTAAAG----PIPIGRPLANTQVYVLDAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 792 LAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFY-PGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEP 870
Cdd:cd12116 309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 871 GEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEG-----LQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRN 945
Cdd:cd12116 389 GEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLkagaaPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468
|
..
gi 363747658 946 AL 947
Cdd:cd12116 469 AL 470
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
460-947 |
3.32e-153 |
|
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: 483.36 E-value: 3.32e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 460 LHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLD 539
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 540 PAYPKERLSYMLKDSGASLLLTQPGcsapnfsgetlevdmtslasekaenheftpadggSLAYVIYTSGSTGQPKGVAVE 619
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTDPD----------------------------------DLAYVIYTSGSTGRPKGVAIE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 620 HRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLppgwEKDSALIVQAIHQEnVTTAHFIPAM 699
Cdd:cd12115 127 HRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA----DNVLALPDLPAAAE-VTLINTVPSA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 700 LNSFLDQAEIErlsdrTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRDrlrIPIGKP 779
Cdd:cd12115 202 AAELLRHDALP-----ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGE---VSIGRP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 780 VPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDD 859
Cdd:cd12115 274 LANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 860 QVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQ 933
Cdd:cd12115 354 QVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAaGERRLVAYIvaepgAAGLVEDLRRHLGTRLPAYMVPSRFVRLDA 433
|
490
....*....|....
gi 363747658 934 WPVTPSGKLDRNAL 947
Cdd:cd12115 434 LPLTPNGKIDRSAL 447
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
3-444 |
5.82e-148 |
|
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: 468.35 E-value: 5.82e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 3 EHTYSLTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTEYKYYP 82
Cdd:pfam00668 2 QDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 83 LRIIDFSNVEMIE----IEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKM 158
Cdd:pfam00668 82 LEIIDISDLSESEeeeaIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 159 KKKDPLPDQPEPSYLSYIEKESQYLQSPRFAKDRLFWTQTFEHPLEYHSLA-DQTSLQKQSTSASRDTIILSPDLEQTIR 237
Cdd:pfam00668 162 LKGEPLPLPPKTPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPkDYARPADRSFKGDRLSFTLDEDTEELLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 238 IFCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQL 317
Cdd:pfam00668 242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 318 SVMRHQRFPYNLLVNELRNEQKDL-HNLIGISMQYQPLQWHnaddFDYETALYFSGYTAN-----------ELSVQIQER 385
Cdd:pfam00668 322 SAEPHQGYPFGDLVNDLRLPRDLSrHPLFDPMFSFQNYLGQ----DSQEEEFQLSELDLSvssvieeeakyDLSLTASER 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 386 idNGTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHPHSFIKELDMTNTREKQKLL 444
Cdd:pfam00668 398 --GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1053-2091 |
7.40e-148 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 497.64 E-value: 7.40e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1053 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGdPVQRIHDEVPF-TLQT 1131
Cdd:PRK10252 9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGE-VWQWVDPALTFpLPEI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1132 TVLGERTEQEAAAAFIKPFDLSQA-------PLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRN--- 1201
Cdd:PRK10252 88 IDLRTQPDPHAAAQALMQADLQQDlrvdsgkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLrge 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1202 ------LPALRIQYKDYAVWREGfktgDAYKTQEAYWLKQLEGELPVLDLPAdhARPPVRSFAGDKVSFTLDQEVASGLH 1275
Cdd:PRK10252 168 ptpaspFTPFADVVEEYQRYRAS----EAWQRDAAFWAEQRRQLPPPASLSP--APLPGRSASADILRLKLEFTDGAFRQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1276 KLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETAL 1355
Cdd:PRK10252 242 LAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1356 EAFEHQDYPFEELVdkleltRDMSR----NPVFDAMFILQNVEKQdIDLREIKVRpanfAHHIS---LFDITL-IATEIN 1427
Cdd:PRK10252 322 KMRRHQRYDAEQIV------RDSGRaagdEPLFGPVLNIKVFDYQ-LDFPGVQAQ----THTLAtgpVNDLELaLFPDEH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1428 GSICCEMEFSTEVFLKATIERWADHFIEFLHAALSTPETSLAQINILSDKEKQKIvFEFNKTQVEFAqkDVPFHRIFEAK 1507
Cdd:PRK10252 391 GGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQL-AQVNATAVEIP--ETTLSALVAQQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARI 1586
Cdd:PRK10252 468 AAKTPDAPALADARYQFSYREMREQVVALANLLRERGvKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1587 EYILRDSGADILLLQQELKHLISNLPESEMshICLDDESSYEENScnLNLSPAPEEPVYIIYTSGTTGAPKGVIVTyrnf 1666
Cdd:PRK10252 548 KMMLEDARPSLLITTADQLPRFADVPDLTS--LCYNAPLAPQGAA--PLQLSQPHHTAYIIFTSGSTGRPKGVMVG---- 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1667 tHAALAWRQIYELDRKPV----RLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMEstpa 1742
Cdd:PRK10252 620 -QTAIVNRLLWMQNHYPLtaddVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTH---- 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1743 lIIPVMEYVYRNQfklPDLDILILGSDMVKaQDFKT-------LTDRFGQ--SMRIINSYGVTEATIDSSFYETS--MGG 1811
Cdd:PRK10252 695 -FVPSMLAAFVAS---LTPEGARQSCASLR-QVFCSgealpadLCREWQQltGAPLHNLYGPTEAAVDVSWYPAFgeELA 769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1812 EGTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLP 1891
Cdd:PRK10252 770 AVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLD 849
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1892 NGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAA----VAVQHDKNGQAG--LAAYIVPSD---VNTNALRAAL 1962
Cdd:PRK10252 850 DGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGGDArqLVGYLVSQSglpLDTSALQAQL 929
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1963 TKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVPNNVLSRPYTAPVNDIQKTMAYIWEDVLSMSRVGIHDSFFELGGDS 2042
Cdd:PRK10252 930 RERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHS 1009
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 363747658 2043 IKALQVAARLAAE-GWSMTIRDLFRYSTIQELCghiTPLASQADQGPAEG 2091
Cdd:PRK10252 1010 LLAMKLAAQLSRQfARQVTPGQVMVASTVAKLA---TLLDAEEDESRRLG 1056
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
459-948 |
7.60e-148 |
|
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: 468.84 E-value: 7.60e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL 538
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAYPKERLSYMLKDSGASLLLTQPgcsapnfsgetlevdmtslasekaENheftpadggsLAYVIYTSGSTGQPKGVAV 618
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLTQP------------------------EN----------LAYVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 619 EHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPA 698
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 699 MLNSFLDQAEIERLSDRTSLKRVFAGGEPLAPRTAARFASVL-PQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIG 777
Cdd:cd17644 207 YWHLLVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINVYGPTEATIAATVCRLTQLTERNITSVPIG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 778 KPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFY--PGERMYKTGDVARWLPDGNVEFLG 855
Cdd:cd17644 287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYLG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 856 RTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMI 929
Cdd:cd17644 367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDqPGNKRLVAYIvphyeESPSTVELRQFLKAKLPDYMIPSAFV 446
|
490
....*....|....*....
gi 363747658 930 EMEQWPVTPSGKLDRNALP 948
Cdd:cd17644 447 VLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
472-947 |
6.04e-145 |
|
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: 459.63 E-value: 6.04e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQPGcsapnfsgetlevdmtslasekaenheftpadggSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQ 631
Cdd:cd17650 81 EDSGAKLLLTQPE----------------------------------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 632 HQFPLSEDDIVMVK-TSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIE 710
Cdd:cd17650 127 REYELDSFPVRLLQmASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 711 RLsDRTSLKRVFAGGEPLAPR----TAARFasvLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIGKPVPGARLY 786
Cdd:cd17650 207 GL-DLSAMRLLIVGSDGCKAQdfktLAARF---GQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 787 VLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGY 866
Cdd:cd17650 283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 867 RIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKL 942
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVAVREDKgGEARLCAYVvaaATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
....*
gi 363747658 943 DRNAL 947
Cdd:cd17650 443 DRRAL 447
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1502-1994 |
4.85e-141 |
|
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: 449.73 E-value: 4.85e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1502 RIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQnRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDS 1579
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLR-AAGVGPgdVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1580 HYPKARIEYILRDSGADILLLQQELKHLISNLPESEMShicldDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGV 1659
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVI-----DEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1660 IVTYRNFTHAAL--AWRQIYELDRkpvrLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVM 1737
Cdd:cd12117 155 AVTHRGVVRLVKntNYVTLGPDDR----VLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1738 ESTPALIipvmeyvyrNQfkLPDLDI--------LILGSDMVKAQDFKTLTDRFGqSMRIINSYGVTEATIDSSFYETSm 1809
Cdd:cd12117 231 WLTAALF---------NQ--LADEDPecfaglreLLTGGEVVSPPHVRRVLAACP-GLRLVNGYGPTENTTFTTSHVVT- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1810 GGEGTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACW 1889
Cdd:cd12117 298 ELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARW 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1890 LPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPS-DVNTNALRAALTKELPA 1968
Cdd:cd12117 378 LPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEgALDAAELRAFLRERLPA 457
|
490 500
....*....|....*....|....*.
gi 363747658 1969 YMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd12117 458 YMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1042-2084 |
2.98e-137 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 484.29 E-value: 2.98e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1042 AIKPAEKQETYPVSSAQKRIyVLQQLEDGGTG-YNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGDPVQR 1120
Cdd:PRK05691 3248 PVPAAEIEDVYPLTPMQEGL-LLHTLLEPGTGlYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQV 3326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1121 IHD--EVPFTLQT-TVLGERTEQEAAAAFIKP-----FDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIRE 1192
Cdd:PRK05691 3327 IHKpgRTPIDYLDwRGLPEDGQEQRLQALHKQereagFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMND 3406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1193 FGELYN------NRNLPALRiQYKDYAVW--REGFKTGdayktqEAYWLKQLEG-ELPVLdLPADhaRPPVRSFAGDKVS 1263
Cdd:PRK05691 3407 FFEIYTalgegrEAQLPVPP-RYRDYIGWlqRQDLAQA------RQWWQDNLRGfERPTP-IPSD--RPFLREHAGDSGG 3476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1264 FT-------LDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRP--HKDLEPILGMFVNTLALR 1334
Cdd:PRK05691 3477 MVvgdcytrLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPvsMPQMQRTVGLFINSIALR 3556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1335 TR-PEGGKP--FVQYLQEVRETALEAFEHQDYPfeeLVDKLELTRDMSRNPVFDAMFILQN--VEKQDID-LREIKVRPA 1408
Cdd:PRK05691 3557 VQlPAAGQRcsVRQWLQGLLDSNMELREYEYLP---LVAIQECSELPKGQPLFDSLFVFENapVEVSVLDrAQSLNASSD 3633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1409 NFAHHISlFDITLIATEiNGSICCEMEFSTEVFLKATIERWADHFIEFLHAALSTPETSLAQINILSDKEKQKIVFEFNK 1488
Cdd:PRK05691 3634 SGRTHTN-FPLTAVCYP-GDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNR 3711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1489 TQVEFAQkDVPFHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTL-QNRKGPKPTVAVLAKRSIDAIVGVLAV 1567
Cdd:PRK05691 3712 SERDYPL-EQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALrAAGVGVDQPVALLAERGLDLLGMIVGS 3790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1568 MKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQELKH----LISNLPESEMSHICL-DDESSYEENSCNLNLSPAPEE 1642
Cdd:PRK05691 3791 FKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREqaraLLDELGCANRPRLLVwEEVQAGEVASHNPGIYSGPDN 3870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1643 PVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVrLLQIASFSFDV----FsgdLARTLTnGGTLIVCPDET 1718
Cdd:PRK05691 3871 LAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADV-IAQTASQSFDIsvwqF---LAAPLF-GARVEIVPNAI 3945
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1719 RLEPAEIYKIMNSQRITVMESTPALIIPVMEyvyRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQsMRIINSYGVTEA 1798
Cdd:PRK05691 3946 AHDPQGLLAHVQAQGITVLESVPSLIQGMLA---EDRQALDGLRWMLPTGEAMPPELARQWLQRYPQ-IGLVNAYGPAEC 4021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1799 TIDSSFYETSMGGEgTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPF-VSG 1877
Cdd:PRK05691 4022 SDDVAFFRVDLAST-RGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPG 4100
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1878 ERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAgLAAYIVPSDVNTN- 1956
Cdd:PRK05691 4101 ERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKH-LVGYLVPHQTVLAq 4179
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1957 -----ALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVPN--NVLSRPYTAPVNDIQKTMAYIWEDVLSMSRV 2029
Cdd:PRK05691 4180 galleRIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDigQLQSQAYLAPRNELEQTLATIWADVLKVERV 4259
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 2030 GIHDSFFELGGDSIKALQVAARL-AAEGWSMTIRDLFRYSTIQELCGHITPLASQA 2084
Cdd:PRK05691 4260 GVHDNFFELGGHSLLATQIASRVqKALQRNVPLRAMFECSTVEELAEYIEGLAGSA 4315
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1512-1995 |
3.22e-137 |
|
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: 437.07 E-value: 3.22e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYIL 1590
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGvGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1591 RDSGADILLLQqelkhlisnlpesemshiclddessyeenscnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYRNFthAA 1670
Cdd:cd17652 81 ADARPALLLTT--------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGL--AN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1671 LAWRQIYELDRKP-VRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALI--IPV 1747
Cdd:cd17652 121 LAAAQIAAFDVGPgSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALaaLPP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1748 MEyvyrnqfkLPDLDILILGSDMVKAQdfktLTDRFGQSMRIINSYGVTEATIDSsfyeTSMGGEGTGDNVPIGSPLPNV 1827
Cdd:cd17652 201 DD--------LPDLRTLVVAGEACPAE----LVDRWAPGRRMINAYGPTETTVCA----TMAGPLPGGGVPPIGRPVPGT 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1828 HMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPF-VSGERLYRTGDRACWLPNGTIRLLGRMDYQVK 1906
Cdd:cd17652 265 RVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1907 INGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPL 1983
Cdd:cd17652 345 IRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPgaaPTAAELRAHLAERLPGYMVPAAFVVLDALPL 424
|
490
....*....|..
gi 363747658 1984 TLNGKLDRNALP 1995
Cdd:cd17652 425 TPNGKLDRRALP 436
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
461-948 |
6.29e-137 |
|
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: 436.22 E-value: 6.29e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 461 HGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDP 540
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 541 AYPKERLSYMLKDSGASLLLTQPGcsapnfsgetlevdmtslasekaenheftpadggSLAYVIYTSGSTGQPKGVAVEH 620
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNPD----------------------------------DLAYVIYTSGSTGLPKGVMIEH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 621 RQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAhFIPAML 700
Cdd:cd17645 127 HNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIS-FLPTGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 701 nsfldqAEIERLSDRTSLKRVFAGGEPLAprtaarfASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRdrlrIPIGKPV 780
Cdd:cd17645 206 ------AEQFMQLDNQSLRVLLTGGDKLK-------KIERKGYKLVNNYGPTENTVVATSFEIDKPYAN----IPIGKPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 781 PGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQ 860
Cdd:cd17645 269 DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 861 VKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPV 936
Cdd:cd17645 349 VKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDAdGRKYLVAYVtapEEIPHEELREWLKNDLPDYMIPTYFVHLKALPL 428
|
490
....*....|..
gi 363747658 937 TPSGKLDRNALP 948
Cdd:cd17645 429 TANGKVDRKALP 440
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
472-947 |
3.45e-135 |
|
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: 432.85 E-value: 3.45e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQPGCSAPNFSGETLEVDMTSLASEKAENHEfTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQ 631
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPP-VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 632 HQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIER 711
Cdd:cd12114 160 RRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 712 LSDRtSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPErDRDRLRIPIGKPVPGARLYVLDPH 791
Cdd:cd12114 240 ALLP-SLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEV-PPDWRSIPYGRPLANQRYRVLDPR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 792 LAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPfyPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPG 871
Cdd:cd12114 318 GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 872 EIEAALRSIEGVREAAVTVRTDSGEPELCAYVE------GLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRN 945
Cdd:cd12114 396 EIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVpdndgtPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
..
gi 363747658 946 AL 947
Cdd:cd12114 476 AL 477
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1504-1995 |
4.88e-135 |
|
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: 432.92 E-value: 4.88e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1504 FEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNR-KGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYP 1582
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARgVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1583 KARIEYILRDSGADILLLQQELKHLisnLPESEMSHICLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVT 1662
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGE---LAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1663 YRNFTHAaLAW-RQIYELDRkPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTP 1741
Cdd:cd17651 158 HRSLANL-VAWqARASSLGP-GARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1742 ALIIPVMEYVYRNQFKLPDL-DILILGSDMVKAQDFKTLTDRFGqSMRIINSYGVTEATIDSSfYETSMGGEGTGDNVPI 1820
Cdd:cd17651 236 VALRALAEHGRPLGVRLAALrYLLTGGEQLVLTEDLREFCAGLP-GLRLHNHYGPTETHVVTA-LSLPGDPAAWPAPPPI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1821 GSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLPNGTIRLLGR 1900
Cdd:cd17651 314 GRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1901 MDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVP---SDVNTNALRAALTKELPAYMIPAHLIP 1977
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGdpeAPVDAAELRAALATHLPEYMVPSAFVL 473
|
490
....*....|....*...
gi 363747658 1978 LENMPLTLNGKLDRNALP 1995
Cdd:cd17651 474 LDALPLTPNGKLDRRALP 491
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
2090-2547 |
7.25e-134 |
|
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: 427.91 E-value: 7.25e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2090 EGEAELTPIQRR--FFGQVHAFHNHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQFNRgiNHKD 2167
Cdd:pfam00668 2 QDEYPLSPAQKRmwFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVIL--EERP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2168 HELFGLYISDWTKASLERThldEKLAAEETvIQSKMNVEKGPLLQAGLFK-TAEGDHLLIALHHLVIDGVSWRILLEDLA 2246
Cdd:pfam00668 80 FELEIIDISDLSESEEEEA---IEAFIQRD-LQSPFDLEKGPLFRAGLFRiAENRHHLLLSMHHIIVDGVSLGILLRDLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2247 AAYQQALEKKEIQLPPKTDsYLSYADGLTQIAESKQLLSEKTYWQTILD---AHTAFLPKDIENVPDRLQMNSDAAAFvl 2323
Cdd:pfam00668 156 DLYQQLLKGEPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQLEgelPVLQLPKDYARPADRSFKGDRLSFTL-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2324 sGDWTEKLLFETQQAYGTDANELLLTALGMALSEWAGHDQIVISTEGHGReghvPNIDISRTVGWFTSIYPILLDMGIPE 2403
Cdd:pfam00668 233 -DEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR----PSPDIERMVGMFVNTLPLRIDPKGGK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2404 PFedqlAYRIKTTKDMLRRV-PNKGTGYGLLTHIGELRHKE-------PEVSF-NYLGQFSEEkeaETFQLSYYQPSYEI 2474
Cdd:pfam00668 308 TF----SELIKRVQEDLLSAePHQGYPFGDLVNDLRLPRDLsrhplfdPMFSFqNYLGQDSQE---EEFQLSELDLSVSS 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 2475 AGEREREYELDINALITDGRLQVKAVY-TQVFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDFSNKELT 2547
Cdd:pfam00668 381 VIEEEAKYDLSLTASERGGGLTIKIDYnTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1512-1994 |
5.39e-131 |
|
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: 419.79 E-value: 5.39e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYIL 1590
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGvGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1591 RDSGADILLLQqelkhlisnlpesemshiclddessyeenscnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAA 1670
Cdd:cd17643 81 ADSGPSLLLTD--------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1671 LAWRQIYELDRKPVRLLqIASFSFDvFS-GDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALIIPVME 1749
Cdd:cd17643 123 AATQRWFGFNEDDVWTL-FHSYAFD-FSvWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1750 YVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFG-QSMRIINSYGVTEATIDSSFYETSMGGEGTGDNVPIGSPLPNVH 1828
Cdd:cd17643 201 AADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGlDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1829 MYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVS-GERLYRTGDRACWLPNGTIRLLGRMDYQVKI 1907
Cdd:cd17643 281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1908 NGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPLT 1984
Cdd:cd17643 361 RGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDgaaADIAELRALLKELLPDYMVPARYVPLDALPLT 440
|
490
....*....|
gi 363747658 1985 LNGKLDRNAL 1994
Cdd:cd17643 441 VNGKLDRAAL 450
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
471-948 |
5.99e-131 |
|
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: 420.73 E-value: 5.99e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 471 TPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYM 550
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 551 LKDSGASLLLTQPGC-SAPNFSGETLEVDMTSLASEKAENHEFTPADGgSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTG 629
Cdd:cd17656 81 MLDSGVRVVLTQRHLkSKLSFNKSTILLEDPSISQEDTSNIDYINNSD-DLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 630 MQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAE- 708
Cdd:cd17656 160 EREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREf 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 709 IERLSDrtSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAfYVLDPErDRDRLRIPIGKPVPGARLYVL 788
Cdd:cd17656 240 INRFPT--CVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTT-YTINPE-AEIPELPPIGKPISNTWIYIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 789 DPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRI 868
Cdd:cd17656 316 DQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 869 EPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYVEGLQR---NEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 944
Cdd:cd17656 396 ELGEIEAQLLNHPGVSEAVVLDKADDkGEKYLCAYFVMEQElniSQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDR 475
|
....
gi 363747658 945 NALP 948
Cdd:cd17656 476 KALP 479
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-1033 |
9.75e-131 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 463.10 E-value: 9.75e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 3 EHTYSLTHAQRRVWFTELLEPNTSICNLTAcvKFKGNIELDT--LEGALNHSISRNDAIR--FQLLEGEELEPRLHltey 78
Cdd:PRK05691 3255 EDVYPLTPMQEGLLLHTLLEPGTGLYYMQD--RYRINSALDPerFAQAWQAVVARHEALRasFSWNAGETMLQVIH---- 3328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 79 KYYPLRI--IDFSNVEMIEIEQWIQ----DQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQII 152
Cdd:PRK05691 3329 KPGRTPIdyLDWRGLPEDGQEQRLQalhkQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFF 3408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 153 DLYQKMKKKDPLPDQPEPSYLSYIekesQYLQSPRFAKDRLFWTQT---FEHPLeyhSLADQTSLQKQSTSASRDTII-- 227
Cdd:PRK05691 3409 EIYTALGEGREAQLPVPPRYRDYI----GWLQRQDLAQARQWWQDNlrgFERPT---PIPSDRPFLREHAGDSGGMVVgd 3481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 228 ----LSPDLEQTIRIFCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNR--GSKAEKEMLGMFVSSLPIRITVDP 301
Cdd:PRK05691 3482 cytrLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIALRVQLPA 3561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 302 DTDFLSFVRTIGREQLSVMRHQRFPYNLLVNelRNEQKDLHnligismQYQPLqwhnaddFDyetALYFSGYTANELSV- 380
Cdd:PRK05691 3562 AGQRCSVRQWLQGLLDSNMELREYEYLPLVA--IQECSELP-------KGQPL-------FD---SLFVFENAPVEVSVl 3622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 381 ----QIQERIDNGTIQLNF----------------DYQNTLFSLEDIKRIQSHLLTILENALHHPHSFIKELDMTNTREK 440
Cdd:PRK05691 3623 draqSLNASSDSGRTHTNFpltavcypgddlglhlSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQER 3702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 441 QKLLCEFNKTEAVSPKAFTLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPE 520
Cdd:PRK05691 3703 DFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLD 3782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 521 MLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQPGC--SAPNFSGETLEVDMTSL-------ASEKAENHE 591
Cdd:PRK05691 3783 LLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACreQARALLDELGCANRPRLlvweevqAGEVASHNP 3862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 592 FTPADGGSLAYVIYTSGSTGQPKGVAVEHRqavSFLTGMQHQFP---LSEDDIVMVKTSFSFDASVWQLFWWSLSGASAY 668
Cdd:PRK05691 3863 GIYSGPDNLAYVIYTSGSTGLPKGVMVEQR---GMLNNQLSKVPylaLSEADVIAQTASQSFDISVWQFLAAPLFGARVE 3939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 669 LLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERlsdrTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHG 748
Cdd:PRK05691 3940 IVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQAL----DGLRWMLPTGEAMPPELARQWLQRYPQIGLVNA 4015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 749 YGPTEATVDAAFYVLDPERDRDRLrIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLED 828
Cdd:PRK05691 4016 YGPAECSDDVAFFRVDLASTRGSY-LPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPH 4094
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 829 PF-YPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYV---- 903
Cdd:PRK05691 4095 PFgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLvphq 4174
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 904 ----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPG-GAADAETYTAPRNVTEMKLSQLWEDVL 978
Cdd:PRK05691 4175 tvlaQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDiGQLQSQAYLAPRNELEQTLATIWADVL 4254
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 979 KNGPVGIHDNFFDRGGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLATVIR 1033
Cdd:PRK05691 4255 KVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIE 4309
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1512-1995 |
3.91e-130 |
|
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: 417.15 E-value: 3.91e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYIL 1590
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGvGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1591 RDSGADILLLQqelkhlisnlpesemshiclddessyeenscnlnlspAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAA 1670
Cdd:cd17649 81 EDSGAGLLLTH-------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHC 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1671 LAWRQIYELdRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPAliipvmey 1750
Cdd:cd17649 124 QATAERYGL-TPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPA-------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1751 vYRNQFKL----------PDLDILILGSDmvkAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGEGTGDNVPI 1820
Cdd:cd17649 195 -YLQQLAEeadrtgdgrpPSLRLYIFGGE---ALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1821 GSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPF-VSGERLYRTGDRACWLPNGTIRLLG 1899
Cdd:cd17649 271 GRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1900 RMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQhDKNGQAGLAAYIVPSDVNTNA-----LRAALTKELPAYMIPAH 1974
Cdd:cd17649 351 RVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPelraqLRTALRASLPDYMVPAH 429
|
490 500
....*....|....*....|.
gi 363747658 1975 LIPLENMPLTLNGKLDRNALP 1995
Cdd:cd17649 430 LVFLARLPLTPNGKLDRKALP 450
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1525-1932 |
2.56e-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: 413.20 E-value: 2.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1525 SYRFLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQ 1602
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPgdRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1603 ELKHLisnLPESEMSHICLD-DESSYEENSCNLNLS---PAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYE 1678
Cdd:TIGR01733 81 ALASR---LAGLVLPVILLDpLELAALDDAPAPPPPdapSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1679 LDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQR-ITVMESTPALIIPVMEyvyRNQFK 1757
Cdd:TIGR01733 158 LDPDD-RVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAA---ALPPA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1758 LPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGEGTGDNVPIGSPLPNVHMYVLSQTDQ 1837
Cdd:TIGR01733 234 LASLRLVILGGEALTPALVDRWRARGPGA-RLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1838 IQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFV--SGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETE 1915
Cdd:TIGR01733 313 PVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELG 392
|
410
....*....|....*..
gi 363747658 1916 EIESVLLQTGLVREAAV 1932
Cdd:TIGR01733 393 EIEAALLRHPGVREAVV 409
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1501-1994 |
9.13e-129 |
|
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: 414.75 E-value: 9.13e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1501 HRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDS 1579
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGvGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1580 HYPKARIEYILRDSGADILLLQQELKHLISNLPEsemsHICLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGV 1659
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGD----VALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1660 IVTyrnftHAALAWRQIYELDRKPV----RLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRIT 1735
Cdd:cd17646 157 MVT-----HAGIVNRLLWMQDEYPLgpgdRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1736 VMESTPALIIPVMEYVYRNQfkLPDLDILILGSDMVKAQdfktLTDRFGQ--SMRIINSYGVTEATIDSSFYETSmgGEG 1813
Cdd:cd17646 232 TCHFVPSMLRVFLAEPAAGS--CASLRRVFCSGEALPPE----LAARFLAlpGAELHNLYGPTEAAIDVTHWPVR--GPA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1814 TGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLPNG 1893
Cdd:cd17646 304 ETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1894 TIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPS----DVNTNALRAALTKELPAY 1969
Cdd:cd17646 384 ALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAagaaGPDTAALRAHLAERLPEY 463
|
490 500
....*....|....*....|....*
gi 363747658 1970 MIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd17646 464 MVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1501-1995 |
6.68e-125 |
|
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: 402.58 E-value: 6.68e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1501 HRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDS 1579
Cdd:cd17644 3 HQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGvKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1580 HYPKARIEYILRDSGADILLLQQElkhlisnlpesemshiclddessyeenscnlNLSpapeepvYIIYTSGTTGAPKGV 1659
Cdd:cd17644 83 NYPQERLTYILEDAQISVLLTQPE-------------------------------NLA-------YVIYTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1660 IVTYR---NFTHAALAWRQIYELDRkpvrLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITV 1736
Cdd:cd17644 125 MIEHQslvNLSHGLIKEYGITSSDR----VLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1737 MESTPALIIPVMEYVYRNQFKLPD-LDILILGSDMVKAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGEGTG 1815
Cdd:cd17644 201 LSLPPAYWHLLVLELLLSTIDLPSsLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1816 DNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVS--GERLYRTGDRACWLPNG 1893
Cdd:cd17644 281 TSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1894 TIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVP---SDVNTNALRAALTKELPAYM 1970
Cdd:cd17644 361 NIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPhyeESPSTVELRQFLKAKLPDYM 440
|
490 500
....*....|....*....|....*
gi 363747658 1971 IPAHLIPLENMPLTLNGKLDRNALP 1995
Cdd:cd17644 441 IPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1512-1994 |
4.25e-124 |
|
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: 400.51 E-value: 4.25e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNR-KGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYIL 1590
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARgVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1591 RDSGADILLLQQELKH-LISNLPESEmsHICLDDESSYEenscNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHA 1669
Cdd:cd12116 81 EDAEPALVLTDDALPDrLPAGLPVLL--LALAAAAAAPA----APRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1670 ALAWRQiyELDRKPV-RLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALIIPVM 1748
Cdd:cd12116 155 LHSMRE--RLGLGPGdRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1749 EYVYRNqfkLPDLDILILGsdmvKAQDfKTLTDRF-GQSMRIINSYGVTEATIDSSFYETSMGGEGtgdnVPIGSPLPNV 1827
Cdd:cd12116 233 DAGWQG---RAGLTALCGG----EALP-PDLAARLlSRVGSLWNLYGPTETTIWSTAARVTAAAGP----IPIGRPLANT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1828 HMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFV-SGERLYRTGDRACWLPNGTIRLLGRMDYQVK 1906
Cdd:cd12116 301 QVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1907 INGYRIETEEIESVLLQTGLVREAAVAVQHDkNGQAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPL 1983
Cdd:cd12116 381 IRGHRIELGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAgaaPDAAALRAHLRATLPAYMVPSAFVRLDALPL 459
|
490
....*....|.
gi 363747658 1984 TLNGKLDRNAL 1994
Cdd:cd12116 460 TANGKLDRKAL 470
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1512-1995 |
4.42e-123 |
|
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: 398.00 E-value: 4.42e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYIL 1590
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGvKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1591 RDSGADILLLQQELKhlisNLPESEMSHICLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAa 1670
Cdd:cd17656 82 LDSGVRVVLTQRHLK----SKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNL- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1671 LAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALIIPVM-E 1749
Cdd:cd17656 157 LHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFsE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1750 YVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMRiiNSYGVTEATIDSSfYETSMGGEgTGDNVPIGSPLPNVHM 1829
Cdd:cd17656 237 REFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLH--NHYGPSETHVVTT-YTINPEAE-IPELPPIGKPISNTWI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1830 YVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKING 1909
Cdd:cd17656 313 YILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1910 YRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVP-SDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGK 1988
Cdd:cd17656 393 YRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMeQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472
|
....*..
gi 363747658 1989 LDRNALP 1995
Cdd:cd17656 473 VDRKALP 479
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
472-948 |
5.90e-123 |
|
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: 396.77 E-value: 5.90e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGGSLTYAELDMYASRLAAHLAARG-ITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYM 550
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 551 LKDSGASLLLTqpgcsapnfsgetlevdmtslasekaenhefTPADggsLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGM 630
Cdd:cd17648 81 LEDTGARVVIT-------------------------------NSTD---LAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 631 QHQFPLS--EDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFldqae 708
Cdd:cd17648 127 SERYFGRdnGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY----- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 709 ieRLSDRTSLKRVFAGGEPLaprTAARFASVLPQVS--LIHGYGPTEATVDAafyVLDPERDRDRLRIPIGKPVPGARLY 786
Cdd:cd17648 202 --DLARLPHLKRVDAAGEEF---TAPVFEKLRSRFAglIINAYGPTETTVTN---HKRFFPGDQRFDKSLGRPVRNTKCY 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 787 VLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFY-PGE-------RMYKTGDVARWLPDGNVEFLGRTD 858
Cdd:cd17648 274 VLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQtEQErargrnaRLYKTGDLVRWLPSGELEYLGRND 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 859 DQVKIRGYRIEPGEIEAALRSIEGVREAAVTVR---TDSGEPE----LCAYV---EGLQRNEVRAQLERLLPGYMVPAYM 928
Cdd:cd17648 354 FQVKIRGQRIEPGEVEAALASYPGVRECAVVAKedaSQAQSRIqkylVGYYLpepGHVPESDLLSFLRAKLPRYMVPARL 433
|
490 500
....*....|....*....|
gi 363747658 929 IEMEQWPVTPSGKLDRNALP 948
Cdd:cd17648 434 VRLEGIPVTINGKLDVRALP 453
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1053-1464 |
1.17e-122 |
|
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: 394.87 E-value: 1.17e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1053 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGdPVQRIHD--EVPFTLQ 1130
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGG-PYQVVLPaaEARPDLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1131 TTVLGERTEQEAAAAFI-KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLP 1203
Cdd:cd19540 82 VVDVTEDELAARLAEAArRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARragrapDWA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1204 ALRIQYKDYAVW-REGFktGDA------YKTQEAYWLKQLEGeLP-VLDLPADHARPPVRSFAGDKVSFTLDQEVASGLH 1275
Cdd:cd19540 162 PLPVQYADYALWqRELL--GDEddpdslAARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1276 KLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETAL 1355
Cdd:cd19540 239 ALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1356 EAFEHQDYPFEELVDKLELTRDMSRNPVFDAMFILQNVEKQDIDLREIKVRPANFAHHISLFDITLIATE------INGS 1429
Cdd:cd19540 319 AAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTErrdadgAPAG 398
|
410 420 430
....*....|....*....|....*....|....*
gi 363747658 1430 ICCEMEFSTEVFLKATIERWADHFIEFLHAALSTP 1464
Cdd:cd19540 399 LTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
460-958 |
5.10e-122 |
|
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: 393.79 E-value: 5.10e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 460 LHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLD 539
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 540 PAYPKERLSYMLKDSGASLLLTqpgcsapnfsgetlevdmtslasekaenheftpadggslAYVIYTSGSTGQPKGVAVE 619
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 620 HRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSL-SGASAYLLPpgwEKDSALIVQAIHQENVTTAHFIPA 698
Cdd:COG0318 122 HRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLlAGATLVLLP---RFDPERVLELIERERVTVLFGVPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 699 MLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVLpQVSLIHGYGPTEATVDAAFyvlDPERDRDRLRIPIGK 778
Cdd:COG0318 199 MLARLLRHPEFARY-DLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTV---NPEDPGERRPGSVGR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 779 PVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFlEDPFYpgermyKTGDVARWLPDGNVEFLGRTD 858
Cdd:COG0318 274 PLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWL------RTGDLGRLDEDGYLYIVGRKK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 859 DQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD--SGEpELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEM 931
Cdd:COG0318 347 DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDekWGE-RVVAFVvlrpgAELDAEELRAFLRERLARYKVPRRVEFV 425
|
490 500
....*....|....*....|....*..
gi 363747658 932 EQWPVTPSGKLDRNALPAPGGAADAET 958
Cdd:COG0318 426 DELPRTASGKIDRRALRERYAAGALEA 452
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
460-947 |
1.33e-121 |
|
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: 393.83 E-value: 1.33e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 460 LHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLD 539
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 540 PAYPKERLSYMLKDSGASLLLtqpgCSAPNfsgetlevdmtslasekaenheftpadggSLAYVIYTSGSTGQPKGVAVE 619
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVL----TSSPS-----------------------------DAAYVIFTSGSTGKPKGVVIE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 620 HRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAyLLPPGWEKDSALiVQAIHQENVTTAHFIPAM 699
Cdd:cd05918 128 HRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCL-CIPSEEDRLNDL-AGFINRLRVTWAFLTPSV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 700 LnSFLDQAEIerlsdrTSLKRVFAGGEPLAPRTAARFASvlpQVSLIHGYGPTEATVDAAFY-VLDPERDRDrlripIGK 778
Cdd:cd05918 206 A-RLLDPEDV------PSLRTLVLGGEALTQSDVDTWAD---RVRLINAYGPAECTIAATVSpVVPSTDPRN-----IGR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 779 PVpGARLYVLDP--HLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFY-------PGERMYKTGDVARWLPDG 849
Cdd:cd05918 271 PL-GATCWVVDPdnHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWlkqegsgRGRRLYRTGDLVRYNPDG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 850 NVEFLGRTDDQVKIRGYRIEPGEIEAALRS-IEGVREAAVTV---RTDSGEPELCAYVEG-------------------- 905
Cdd:cd05918 350 SLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVvkpKDGSSSPQLVAFVVLdgsssgsgdgdslflepsde 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 363747658 906 LQRN--EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05918 430 FRALvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
464-864 |
7.32e-120 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 386.28 E-value: 7.32e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 464 FERQAAFTPERLAIRFSGG-SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAY 542
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGrRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 543 PKERLSYMLKDSGASLLLTQPGCSAPNF---------SGETLEVDMTSLASEKAENHEF----------TPADGGSLAYV 603
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELlealgklevVKLVLVLDRDPVLKEEPLPEEAkpadvpppppPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 604 IYTSGSTGQPKGVAVEHRQAVSFLTGM----QHQFPLSEDDIVMVKTSFSFDASV-WQLFWWSLSGASAYLLPPGWEKDS 678
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 679 ALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVLPQVsLIHGYGPTEATVda 758
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRA-LLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTG-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 759 AFYVLDPERDRDRLRIPIGKPVPGARLYVLDPH-LAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDpfypgeRMY 837
Cdd:pfam00501 317 VVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------GWY 390
|
410 420
....*....|....*....|....*..
gi 363747658 838 KTGDVARWLPDGNVEFLGRTDDQVKIR 864
Cdd:pfam00501 391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
463-947 |
4.54e-119 |
|
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: 384.74 E-value: 4.54e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAY 542
Cdd:cd17653 2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 543 PKERLSYMLKDSGASLLLTQPgcsapnfsgetlevdmtslasekaenhefTPADggsLAYVIYTSGSTGQPKGVAVEHRQ 622
Cdd:cd17653 82 PSARIQAILRTSGATLLLTTD-----------------------------SPDD---LAYIIFTSGSTGIPKGVMVPHRG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 623 AVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLlppgweKDSALIVQAIHQEnVTTAHFIPAMLNS 702
Cdd:cd17653 130 VLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDPFAHVART-VDALMSTPSILST 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 703 FldqaeieRLSDRTSLKRVFAGGEPLAPRTAARFAsvlPQVSLIHGYGPTEATVDAAFYVLDPERdrdrlRIPIGKPVPG 782
Cdd:cd17653 203 L-------SPQDFPNLKTIFLGGEAVPPSLLDRWS---PGRRLYNAYGPTECTISSTMTELLPGQ-----PVTIGKPIPN 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 783 ARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVK 862
Cdd:cd17653 268 STCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVK 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 863 IRGYRIEPGEIEA-ALRSIEGVREAAVTVRTDSgepeLCAYV--EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPS 939
Cdd:cd17653 348 VRGFRINLEEIEEvVLQSQPEVTQAAAIVVNGR----LVAFVtpETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTAN 423
|
....*...
gi 363747658 940 GKLDRNAL 947
Cdd:cd17653 424 GKVDRKAL 431
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
468-947 |
4.90e-119 |
|
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: 385.06 E-value: 4.90e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 468 AAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERL 547
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 548 SYMLKDSGASLLLtqpgcsapnfsgetlevdmtslasekaenheftpADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFL 627
Cdd:cd05945 81 REILDAAKPALLI----------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 628 TGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPamlnSFLDQA 707
Cdd:cd05945 127 NWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTP----SFAAMC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 708 EIERLSDRT---SLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIGKPVPGAR 784
Cdd:cd05945 203 LLSPTFTPEslpSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYAKPGAK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 785 LYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDpfyPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIR 864
Cdd:cd05945 283 LVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 865 GYRIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYVEG------LQRNEVRAQLERLLPGYMVPAYMIEMEQWPVT 937
Cdd:cd05945 360 GYRIELEEIEAALRQVPGVKEAVVVPKYKGeKVTELIAFVVPkpgaeaGLTKAIKAELAERLPPYMIPRRFVYLDELPLN 439
|
490
....*....|
gi 363747658 938 PSGKLDRNAL 947
Cdd:cd05945 440 ANGKIDRKAL 449
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1501-1995 |
2.67e-116 |
|
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: 376.89 E-value: 2.67e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1501 HRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNrKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPID 1578
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRG-KGVKPddQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1579 SHYPKARIEYILRDSGADILLLQqelkhlisnlpesemshiclddessyeenscnlnlspaPEEPVYIIYTSGTTGAPKG 1658
Cdd:cd17645 80 PDYPGERIAYMLADSSAKILLTN--------------------------------------PDDLAYVIYTSGSTGLPKG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1659 VIVTYRNFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVme 1738
Cdd:cd17645 122 VMIEHHNLVNLCEWHRPYFGVTPAD-KSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITI-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1739 stPALIIPVMEyvyrnQFKLPD---LDILILGSDMVKAQDFKtltdrfgqSMRIINSYGVTEATIDSSFYETsmggEGTG 1815
Cdd:cd17645 199 --SFLPTGAAE-----QFMQLDnqsLRVLLTGGDKLKKIERK--------GYKLVNNYGPTENTVVATSFEI----DKPY 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1816 DNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLPNGTI 1895
Cdd:cd17645 260 ANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1896 RLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV-PSDVNTNALRAALTKELPAYMIPAH 1974
Cdd:cd17645 340 EFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTaPEEIPHEELREWLKNDLPDYMIPTY 419
|
490 500
....*....|....*....|.
gi 363747658 1975 LIPLENMPLTLNGKLDRNALP 1995
Cdd:cd17645 420 FVHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1512-1995 |
7.22e-111 |
|
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: 361.72 E-value: 7.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYI 1589
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDdlVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1590 LRDSGADILLlqqelkhlisnlpesemshiclddessyeENSCNLnlspapeepVYIIYTSGTTGAPKGVIVTYRNFTHA 1669
Cdd:cd17648 81 LEDTGARVVI-----------------------------TNSTDL---------AYAIYTSGTTGKPKGVLVEHGSVVNL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1670 ALAWRQIYEL-DRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALIipvM 1748
Cdd:cd17648 123 RTSLSERYFGrDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVL---Q 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1749 EYVYRnqfKLPDLDILILGSDMVKAQDFKTLTDRFGQsmRIINSYGVTEATIDS--SFYETSMGGEGTgdnvpIGSPLPN 1826
Cdd:cd17648 200 QYDLA---RLPHLKRVDAAGEEFTAPVFEKLRSRFAG--LIINAYGPTETTVTNhkRFFPGDQRFDKS-----LGRPVRN 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1827 VHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGE--------RLYRTGDRACWLPNGTIRLL 1898
Cdd:cd17648 270 TKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1899 GRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKN-----GQAGLAAYIVPSD--VNTNALRAALTKELPAYMI 1971
Cdd:cd17648 350 GRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPghVPESDLLSFLRAKLPRYMV 429
|
490 500
....*....|....*....|....
gi 363747658 1972 PAHLIPLENMPLTLNGKLDRNALP 1995
Cdd:cd17648 430 PARLVRLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1501-1994 |
3.40e-109 |
|
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: 358.01 E-value: 3.40e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1501 HRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDS 1579
Cdd:cd05918 2 HDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGvGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1580 HYPKARIEYILRDSGADILLlqqelkhlisnlpesemshiclddeSSyeenscnlnlspAPEEPVYIIYTSGTTGAPKGV 1659
Cdd:cd05918 82 SHPLQRLQEILQDTGAKVVL-------------------------TS------------SPSDAAYVIFTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1660 IVTYRNFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEpaEIYKIMNSQRITVMES 1739
Cdd:cd05918 125 VIEHRALSTSALAHGRALGLTSES-RVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1740 TP---ALIIPVmeyvyrnqfKLPDLDILILGSDMVKAQDfktlTDRFGQSMRIINSYGVTEATIDSSFYETSMGGEGTgd 1816
Cdd:cd05918 202 TPsvaRLLDPE---------DVPSLRTLVLGGEALTQSD----VDTWADRVRLINAYGPAECTIAATVSPVVPSTDPR-- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1817 NvpIGSPLPnVHMYVLSQ--TDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNP-------FVSGERLYRTGDRA 1887
Cdd:cd05918 267 N--IGRPLG-ATCWVVDPdnHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1888 CWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQ---TGLVREAAVAVQHDKNGQAGLAAYIVPSDVNTN-------- 1956
Cdd:cd05918 344 RYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQslpGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGsgdgdslf 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 363747658 1957 ------------ALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05918 424 lepsdefralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1512-1994 |
1.81e-108 |
|
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: 355.81 E-value: 1.81e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQ-NRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYIL 1590
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKaAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1591 RDSGADILLLQQELKHLisNLPESEMSHICLDDESSYEENScnlNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAA 1670
Cdd:cd12114 81 ADAGARLVLTDGPDAQL--DVAVFDVLILDLDALAAPAPPP---PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1671 LAWRQIYELDRKPvRLLQIASFSFD--VFsgDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPALIIPVM 1748
Cdd:cd12114 156 LDINRRFAVGPDD-RVLALSSLSFDlsVY--DIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1749 EYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGEGTGdNVPIGSPLPNVH 1828
Cdd:cd12114 233 DVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDA-RLISLGGATEASIWSIYHPIDEVPPDWR-SIPYGRPLANQR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1829 MYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPfvSGERLYRTGDRACWLPNGTIRLLGRMDYQVKIN 1908
Cdd:cd12114 311 YRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1909 GYRIETEEIESVLLQTGLVReAAVAVQHDKNGQAGLAAYIVP-SDVNT---NALRAALTKELPAYMIPAHLIPLENMPLT 1984
Cdd:cd12114 389 GYRIELGEIEAALQAHPGVA-RAVVVVLGDPGGKRLAAFVVPdNDGTPiapDALRAFLAQTLPAYMIPSRVIALEALPLT 467
|
490
....*....|
gi 363747658 1985 LNGKLDRNAL 1994
Cdd:cd12114 468 ANGKVDRAAL 477
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1053-1464 |
7.69e-108 |
|
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: 352.34 E-value: 7.69e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1053 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGgDPVQRIHDEVPFTL--- 1129
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDG-VPYQLILEEDEATPkle 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1130 QTTVLGERTEQEAAAAFIKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLP 1203
Cdd:cd19538 82 IKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARckgeapELA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1204 ALRIQYKDYAVWREGFKTGDAYKT-----QEAYWLKQLEGeLPV-LDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKL 1277
Cdd:cd19538 162 PLPVQYADYALWQQELLGDESDPDsliarQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1278 ARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEA 1357
Cdd:cd19538 241 AKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1358 FEHQDYPFEELVDKLELTRDMSRNPVFDAMFILQNVEKQDIDLREIkvrPANFAHH---ISLFDITLIATEIN-----GS 1429
Cdd:cd19538 321 YEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGL---EAKLELRtvgSAKFDLTFELREQYndgtpNG 397
|
410 420 430
....*....|....*....|....*....|....*
gi 363747658 1430 ICCEMEFSTEVFLKATIERWADHFIEFLHAALSTP 1464
Cdd:cd19538 398 IEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1502-1994 |
9.86e-107 |
|
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: 349.30 E-value: 9.86e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1502 RIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTL-QNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSH 1580
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLlQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1581 YPKARIEYILRDSGADILLlqqelkhlisnlpesemshiclddessyeensCNlnlsPAPEEPVYIIYTSGTTGAPKGVI 1660
Cdd:cd17653 81 LPSARIQAILRTSGATLLL--------------------------------TT----DSPDDLAYIIFTSGSTGIPKGVM 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1661 VTYRNFTHAALAWRqiYELDRKP-VRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAeiykimnSQRITVMES 1739
Cdd:cd17653 125 VPHRGVLNYVSQPP--ARLDVGPgSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHV-------ARTVDALMS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1740 TPALI--IPVMEYvyrnqfklPDLDILILGSDMVKAqdfkTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGgegtgDN 1817
Cdd:cd17653 196 TPSILstLSPQDF--------PNLKTIFLGGEAVPP----SLLDRWSPGRRLYNAYGPTECTISSTMTELLPG-----QP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1818 VPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLPNGTIRL 1897
Cdd:cd17653 259 VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1898 LGRMDYQVKINGYRIETEEIESVLLQT-GLVREAAvAVQHDKNgqagLAAYIVPSDVNTNALRAALTKELPAYMIPAHLI 1976
Cdd:cd17653 339 LGREDNQVKVRGFRINLEEIEEVVLQSqPEVTQAA-AIVVNGR----LVAFVTPETVDVDGLRSELAKHLPSYAVPDRII 413
|
490
....*....|....*...
gi 363747658 1977 PLENMPLTLNGKLDRNAL 1994
Cdd:cd17653 414 ALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1501-1994 |
1.03e-105 |
|
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: 346.61 E-value: 1.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1501 HRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDS 1579
Cdd:cd12115 2 HDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGvGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1580 HYPKARIEYILRDSGADILLLQqelkhlisnlpesemshiclddessyeenscnlnlspaPEEPVYIIYTSGTTGAPKGV 1659
Cdd:cd12115 82 AYPPERLRFILEDAQARLVLTD--------------------------------------PDDLAYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1660 IVTYRNfTHAALAW-RQIYELDrKPVRLLQIASFSFD--VFsgDLARTLTNGGTLIVCPDETRL--EPAEiykimnsQRI 1734
Cdd:cd12115 124 AIEHRN-AAAFLQWaAAAFSAE-ELAGVLASTSICFDlsVF--ELFGPLATGGKVVLADNVLALpdLPAA-------AEV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1735 TVMESTPALIIPVMEyvyrnQFKLP-DLDILILGSDMVKAQDFKTLTDRfGQSMRIINSYGVTEATIDSSFYETSMGGEG 1813
Cdd:cd12115 193 TLINTVPSAAAELLR-----HDALPaSVRVVNLAGEPLPRDLVQRLYAR-LQVERVVNLYGPSEDTTYSTVAPVPPGASG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1814 TgdnVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLPNG 1893
Cdd:cd12115 267 E---VSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1894 TIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VNTNALRAALTKELPAYM 1970
Cdd:cd12115 344 LLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPgaaGLVEDLRRHLGTRLPAYM 423
|
490 500
....*....|....*....|....
gi 363747658 1971 IPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd12115 424 VPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1508-1994 |
1.72e-102 |
|
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: 337.68 E-value: 1.72e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRKGPKPT-VAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARI 1586
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDpVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1587 EYILRDSGADILLLqqelkhlisnlpesemshiclddessyeenscnlnlspAPEEPVYIIYTSGTTGAPKGVIVTYRNF 1666
Cdd:cd05945 81 REILDAAKPALLIA--------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1667 tHAALAWrqiyELDRKPV----RLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPA 1742
Cdd:cd05945 123 -VSFTNW----MLSDFPLgpgdVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPS 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1743 LIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYE---TSMGGEGTgdnVP 1819
Cdd:cd05945 198 FAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDA-RIYNTYGPTEATVAVTYIEvtpEVLDGYDR---LP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1820 IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPfvsGERLYRTGDRACWLPNGTIRLLG 1899
Cdd:cd05945 274 IGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1900 RMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD----VNTNALRAALTKELPAYMIPAHL 1975
Cdd:cd05945 351 RLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPgaeaGLTKAIKAELAERLPPYMIPRRF 430
|
490
....*....|....*....
gi 363747658 1976 IPLENMPLTLNGKLDRNAL 1994
Cdd:cd05945 431 VYLDELPLNANGKIDRKAL 449
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1500-1994 |
5.21e-98 |
|
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: 324.84 E-value: 5.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1500 FHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPI 1577
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRAL-GVGPgdRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1578 DSHYPKARIEYILRDSGADILLLqqelkhlisnlpesemshiclddessyeenscnlnlspapeepVYIIYTSGTTGAPK 1657
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT-------------------------------------------ALILYTSGTTGRPK 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1658 GVIVTYRNFTHAALAWRQIYELDRKPvRLLQIASFSFDV-FSGDLARTLTNGGTLIVCPdetRLEPAEIYKIMNSQRITV 1736
Cdd:COG0318 117 GVMLTHRNLLANAAAIAAALGLTPGD-VVLVALPLFHVFgLTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1737 MESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATIDSSFYETSMGGEGTGd 1816
Cdd:COG0318 193 LFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG--VRIVEGYGLTETSPVVTVNPEDPGERRPG- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1817 nvPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTknpfvsgERLYRTGDRACWLPNGTIR 1896
Cdd:COG0318 270 --SVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1897 LLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---SDVNTNALRAALTKELPAYMIP 1972
Cdd:COG0318 341 IVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVvGVPDEKWGER-VVAFVVLrpgAELDAEELRAFLRERLARYKVP 419
|
490 500
....*....|....*....|..
gi 363747658 1973 AHLIPLENMPLTLNGKLDRNAL 1994
Cdd:COG0318 420 RRVEFVDELPRTASGKIDRRAL 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1504-1907 |
1.19e-89 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 299.23 E-value: 1.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1504 FEAKAEEIPEHIAVIDNEIE-ISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHY 1581
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGvGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1582 PKARIEYILRDSGADILLLQQELK--HLISNLPESEM--SHICLDDESSYEENSCNLNLS-----------PAPEEPVYI 1646
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKleELLEALGKLEVvkLVLVLDRDPVLKEEPLPEEAKpadvpppppppPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1647 IYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPV---RLLQIASFSFDV-FSGDLARTLTNGGTLIVCPDETRLEP 1722
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpddRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1723 AEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQsmRIINSYGVTEATIDS 1802
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG--ALVNGYGLTETTGVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1803 SFYETSMGGEGTGDnvPIGSPLPNVHMYVLSQ-TDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKnpfvsgERLY 1881
Cdd:pfam00501 319 TTPLPLDEDLRSLG--SVGRPLPGTEVKIVDDeTGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWY 390
|
410 420
....*....|....*....|....*.
gi 363747658 1882 RTGDRACWLPNGTIRLLGRMDYQVKI 1907
Cdd:pfam00501 391 RTGDLGRRDEDGYLEIVGRKKDQIKL 416
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1053-1464 |
2.80e-89 |
|
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: 298.52 E-value: 2.80e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1053 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGDPVQRI----------H 1122
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEIlppgpaplevR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1123 DEVPFTLQTTVLGERTEQEAAAafiKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR-- 1200
Cdd:cd19539 83 DLSDPDSDRERRLEELLRERES---RGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARrk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1201 ----NLPALRIQYKDYAVWREGFKTGDAYKTQEAYWLKQLEGeLPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHK 1276
Cdd:cd19539 160 gpaaPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1277 LARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALE 1356
Cdd:cd19539 239 LAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1357 AFEHQDYPFEELVDKLELTRDMSRNPVFDAMFILQNVEKQDIDLR-EIKVRPANFAHHISLFDITLIATEINGSICCEME 1435
Cdd:cd19539 319 AQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAgGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLG 398
|
410 420
....*....|....*....|....*....
gi 363747658 1436 FSTEVFLKATIERWADHFIEFLHAALSTP 1464
Cdd:cd19539 399 YATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1501-1994 |
1.06e-88 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 299.89 E-value: 1.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1501 HRIFEAkAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRKGPKPT-VAVLAKRSIDAIVGVLAVMKAGGVYIPIDS 1579
Cdd:PRK04813 6 ETIEEF-AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSpIIVFGHMSPEMLATFLGAVKAGHAYIPVDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1580 HYPKARIEYILRDSGADILLLQQELKHLISNLPEsemshICLDD--ESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPK 1657
Cdd:PRK04813 85 SSPAERIEMIIEVAKPSLIIATEELPLEILGIPV-----ITLDElkDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1658 GVIVTYRN---FTHAALawrQIYELDRKPVRLLQiASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRI 1734
Cdd:PRK04813 160 GVQISHDNlvsFTNWML---EDFALPEGPQFLNQ-APYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1735 TVMESTPALI-IPVMEYVYrNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGEG 1813
Cdd:PRK04813 236 NVWVSTPSFAdMCLLDPSF-NEEHLPNLTHFLFCGEELPHKTAKKLLERFPSA-TIYNTYGPTEATVAVTSIEITDEMLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1814 TGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTknpFVSGERLYRTGDRAcWLPNG 1893
Cdd:PRK04813 314 QYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGDAG-YLEDG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1894 TIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREaAVAVQHDKNGQA-GLAAYIVPSDVN-------TNALRAALTKE 1965
Cdd:PRK04813 390 LLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVES-AVVVPYNKDHKVqYLIAYVVPKEEDferefelTKAIKKELKER 468
|
490 500
....*....|....*....|....*....
gi 363747658 1966 LPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK04813 469 LMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
1501-1994 |
8.11e-86 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 291.28 E-value: 8.11e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1501 HRIFEAkAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRKGP-KPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDS 1579
Cdd:TIGR01734 4 EAIQAF-AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPkKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1580 HYPKARIEYILRDSGADILLLQQELKhliSNLPESEMSHICLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGV 1659
Cdd:TIGR01734 83 SIPSERIEMIIEAAGPELVIHTAELS---IDAVGTQIITLSALEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1660 IVTYRN---FTHaalaWrqIYELDRKP--VRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRI 1734
Cdd:TIGR01734 160 QISHDNlvsFTN----W--MLADFPLSegKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1735 TVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFgQSMRIINSYGVTEATIDSSFYETSMGGEGT 1814
Cdd:TIGR01734 234 NVWVSTPSFVDMCLLDPNFNQENYPHLTHFLFCGEELPVKTAKALLERF-PKATIYNTYGPTEATVAVTSVKITQEILDQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1815 GDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTknpFVSGERLYRTGDRACwLPNGT 1894
Cdd:TIGR01734 313 YPRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1895 IRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQ-AGLAAYIVPSDVN-------TNALRAALTKEL 1966
Cdd:TIGR01734 389 LFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAIVPETEDfekefqlTKAIKKELKKSL 468
|
490 500
....*....|....*....|....*...
gi 363747658 1967 PAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:TIGR01734 469 PAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
465-947 |
1.14e-84 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 288.19 E-value: 1.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 465 ERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPK 544
Cdd:TIGR01734 7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 545 ERLSYMLKDSGASLLLTQPGCSAPNFSGETLEVDMTSLASEKAENHEFT-PADGGSLAYVIYTSGSTGQPKGVAVEHRQA 623
Cdd:TIGR01734 87 ERIEMIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAETSGGPVSFDhAVKGDDNYYIIYTSGSTGNPKGVQISHDNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 624 VSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQEN----VTTAHFIP-A 698
Cdd:TIGR01734 167 VSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGlnvwVSTPSFVDmC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 699 MLNSFLDQAEIERLSdrtslkRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIGK 778
Cdd:TIGR01734 247 LLDPNFNQENYPHLT------HFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEILDQYPRLPIGF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 779 PVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLedpFYPGERMYKTGDVARwLPDGNVEFLGRTD 858
Cdd:TIGR01734 321 AKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQLFYQGRLD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 859 DQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEP--ELCAYV---------EGLQRNEVRAQLERLLPGYMVPAY 927
Cdd:TIGR01734 397 FQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKveYLIAAIvpetedfekEFQLTKAIKKELKKSLPAYMIPRK 476
|
490 500
....*....|....*....|
gi 363747658 928 MIEMEQWPVTPSGKLDRNAL 947
Cdd:TIGR01734 477 FIYRDQLPLTANGKIDRKAL 496
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
249-1049 |
2.79e-83 |
|
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: 303.52 E-value: 2.79e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 249 SLFMASFYICISRITSKKDLAIGTyygnRGSKAEKEMLgmfvsslpIRITVDPDTDFLSFVRTIGREQLSVMRHQRFPYN 328
Cdd:TIGR03443 50 IILLAAFAALVYRLTGDEDIVLGT----SSNKSGRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 329 LLVNELRNEQKDLHNLIGISMQYQplqwhNADDFDYETalYFSGYTAnELSVQIQEriDNGTIQLNFDYQNTLFSLEDIK 408
Cdd:TIGR03443 118 ELSEHIQAAKKLERTPPLFRLAFQ-----DAPDNQQTT--YSTGSTT-DLTVFLTP--SSPELELSIYYNSLLFSSDRIT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 409 RIQSHLLTILENALHHPHSFIKELDMTNTREKQKL--------LCEFNKTeavspkaftLHGLFERQAAFTPERLAI--- 477
Cdd:TIGR03443 188 IVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLpdptkdldWSGFRGA---------IHDIFADNAEKHPDRTCVvet 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 478 -RFSGGS-----LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:TIGR03443 259 pSFLDPSsktrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSG--ASLLLTQPGCSAP---NFSGETLEV----------DMTSL---ASEKAENHEFTPADG--GSLAYVI------- 604
Cdd:TIGR03443 339 SVAKprALIVIEKAGTLDQlvrDYIDKELELrteipalalqDDGSLvggSLEGGETDVLAPYQAlkDTPTGVVvgpdsnp 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 605 ---YTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASaYLLP-------PG- 673
Cdd:TIGR03443 419 tlsFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQ-LLVPtaddigtPGr 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 674 ---WEKDSAlivqaihqenVTTAHFIPAMLNSFLDQAEierlSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYG 750
Cdd:TIGR03443 498 laeWMAKYG----------ATVTHLTPAMGQLLSAQAT----TPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 751 PTEaTVDAAFYVLDPERDRD-----RLR--IPIGKPVPGARLYVLDPHLAVQPSGVA--GELYIAGAGVARGYLNRPALT 821
Cdd:TIGR03443 564 TTE-TQRAVSYFEIPSRSSDstflkNLKdvMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELN 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 822 EERFL--------------------EDPFY--PGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRS 879
Cdd:TIGR03443 643 AEKFVnnwfvdpshwidldkennkpEREFWlgPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQ 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 880 IEGVREAAVTVRTD-SGEPELCAY--------------------------VEGLQR-----NEVRAQLERLLPGYMVPAY 927
Cdd:TIGR03443 723 HPLVRENVTLVRRDkDEEPTLVSYivpqdksdeleefksevddeessdpvVKGLIKyrkliKDIREYLKKKLPSYAIPTV 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 928 MIEMEQWPVTPSGKLDRNALP----------APGGAADAETYTAprNVTEMKLSQLWEDVLKNGP--VGIHDNFFDRGGH 995
Cdd:TIGR03443 803 IVPLKKLPLNPNGKVDKPALPfpdtaqlaavAKNRSASAADEEF--TETEREIRDLWLELLPNRPatISPDDSFFDLGGH 880
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 996 SLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLATVIR-----EGTDSPYEAIKPAEKQ 1049
Cdd:TIGR03443 881 SILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDrlkkgEELADEGDSEIEEEET 939
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1054-1286 |
3.43e-80 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 264.98 E-value: 3.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1054 VSSAQKRIYVLqqlEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDaGGDPVQRIHDEVPFTLQTTV 1133
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEE-DGEPVQRIDPDADLPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1134 LG--------ERTEQEAAAAFIKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR----- 1200
Cdd:COG4908 77 LSalpepereAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALlegep 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1201 -NLPALRIQYKDYAVWREGFKTGDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLAR 1279
Cdd:COG4908 157 pPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236
|
....*..
gi 363747658 1280 ENGSTLY 1286
Cdd:COG4908 237 AHGATVN 243
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
471-947 |
1.18e-78 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 270.61 E-value: 1.18e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 471 TPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYM 550
Cdd:PRK04813 15 QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 551 LKDSGASLLLtqpgcSAPNFSGETLEVDMTSLASEKAENHEFTPAD------GGSLAYVIYTSGSTGQPKGVAVEHRQAV 624
Cdd:PRK04813 95 IEVAKPSLII-----ATEELPLEILGIPVITLDELKDIFATGNPYDfdhavkGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 625 SFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQEN----VTTAHFIP-AM 699
Cdd:PRK04813 170 SFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPinvwVSTPSFADmCL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 700 LNSFLDQaeiERLSDrtsLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPE--RDRDRLriPIG 777
Cdd:PRK04813 250 LDPSFNE---EHLPN---LTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEITDEmlDQYKRL--PIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 778 KPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEdpfYPGERMYKTGDVARwLPDGNVEFLGRT 857
Cdd:PRK04813 322 YAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY-LEDGLLFYQGRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 858 DDQVKIRGYRIEPGEIEAALRSIEGVREA-AVTVRTDSGEPELCAYV---EGLQRNE------VRAQLERLLPGYMVPAY 927
Cdd:PRK04813 398 DFQIKLNGYRIELEEIEQNLRQSSYVESAvVVPYNKDHKVQYLIAYVvpkEEDFEREfeltkaIKKELKERLMEYMIPRK 477
|
490 500
....*....|....*....|
gi 363747658 928 MIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK04813 478 FIYRDSLPLTPNGKIDRKAL 497
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
600-943 |
1.21e-77 |
|
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: 261.45 E-value: 1.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 600 LAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGwekDSA 679
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 680 LIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASvLPQVSLIHGYGPTEATVDAA 759
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGY-DLSSLRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 760 FYVLDperDRDRLRIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFledpfypGERMYKT 839
Cdd:cd04433 157 TGPPD---DDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 840 GDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYVE-----GLQRNEVR 912
Cdd:cd04433 227 GDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPewGE-RVVAVVVlrpgaDLDAEELR 305
|
330 340 350
....*....|....*....|....*....|.
gi 363747658 913 AQLERLLPGYMVPAYMIEMEQWPVTPSGKLD 943
Cdd:cd04433 306 AHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1232-2097 |
2.09e-76 |
|
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: 281.57 E-value: 2.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1232 WLKQLEGeLPVLDLPADHARPPVRSFAGDKVSFTLDQEVAsglhklARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSp 1311
Cdd:TIGR03443 2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSAEV------TAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1312 iagRPHKDLEPilgmfvntLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNPVFdamFILQ 1391
Cdd:TIGR03443 74 ---SSNKSGRP--------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPL---FRLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1392 NVEKQDIDLReikvrpaNFAHHiSLFDITLIATEINGSICCEMEFSTEVFLKATIERWADHFIEFLHAALSTPETSLAQI 1471
Cdd:TIGR03443 140 FQDAPDNQQT-------TYSTG-STTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1472 NILSDKEKQkiVFEFNKTQVEFAQKDVPFHRIFEAKAEEIPEHIAVIDNEI---------EISYRFLNERANRLARTLQN 1542
Cdd:TIGR03443 212 SLITPSQKS--LLPDPTKDLDWSGFRGAIHDIFADNAEKHPDRTCVVETPSfldpssktrSFTYKQINEASNILAHYLLK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1543 rKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKAR-IEYI----------LRDSGAdillLQQELKHLIS 1609
Cdd:TIGR03443 290 -TGIKRgdVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqTIYLsvakpralivIEKAGT----LDQLVRDYID 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1610 NLPE--SEMSHICLDDESSYE----ENSCNLNLSP-------------APEEPVYIIYTSGTTGAPKGVIvtYRNFTHAA 1670
Cdd:TIGR03443 365 KELElrTEIPALALQDDGSLVggslEGGETDVLAPyqalkdtptgvvvGPDSNPTLSFTSGSEGIPKGVL--GRHFSLAY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1671 -LAWR-QIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPAL----- 1743
Cdd:TIGR03443 443 yFPWMaKRFGLSEND-KFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMgqlls 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1744 -----IIPVMeyvyRNQFKLPDldILIlGSDMVKAQdfkTLtdrfGQSMRIINSYGVTEATIDSSFYE-TSMGGEGT--- 1814
Cdd:TIGR03443 522 aqattPIPSL----HHAFFVGD--ILT-KRDCLRLQ---TL----AENVCIVNMYGTTETQRAVSYFEiPSRSSDSTflk 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1815 --GDNVPIGSPLPNVHMYVLSQTDQIQPIGVA--GELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGE------------ 1878
Cdd:TIGR03443 588 nlKDVMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldkennkp 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1879 ----------RLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYI 1948
Cdd:TIGR03443 668 erefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYI 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1949 VP-----------SDVNTNA------------------LRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVPNN 1999
Cdd:TIGR03443 748 VPqdksdeleefkSEVDDEEssdpvvkglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDT 827
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2000 V-------LSRPYTAP--VNDIQKTMAYIWEDVLSM--SRVGIHDSFFELGGDSI----------KALQVAARLAAegws 2058
Cdd:TIGR03443 828 AqlaavakNRSASAADeeFTETEREIRDLWLELLPNrpATISPDDSFFDLGGHSIlatrmifelrKKLNVELPLGL---- 903
|
970 980 990 1000
....*....|....*....|....*....|....*....|..
gi 363747658 2059 mtirdLFRYSTIQELCGHITPLAS---QADQGPAEGEAELTP 2097
Cdd:TIGR03443 904 -----IFKSPTIKGFAKEVDRLKKgeeLADEGDSEIEEEETV 940
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1051-1388 |
6.52e-74 |
|
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: 253.92 E-value: 6.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1051 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAG-GDPVQRIHDEVPFTL 1129
Cdd:cd19532 1 TEPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEdGEPMQGVLASSPLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1130 QT-TVlgeRTEQEAAAAFIK----PFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRNLPA 1204
Cdd:cd19532 81 EHvQI---SDEAEVEEEFERlknhVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1205 LRIQYKDYAVW-REGFKTGdAYKTQEAYWLKQLEGE---LPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARE 1280
Cdd:cd19532 158 PPLQYLDFAARqRQDYESG-ALDEDLAYWKSEFSTLpepLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1281 NGSTLYMVLLAAYTAFLSRLSGQEDIIVGspI--AGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAF 1358
Cdd:cd19532 237 LRVTPFHFYLAALQVLLARLLDVDDICIG--IadANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAAL 314
|
330 340 350
....*....|....*....|....*....|
gi 363747658 1359 EHQDYPFEELVDKLELTRDMSRNPVFDAMF 1388
Cdd:cd19532 315 AHSRVPFDVLLDELGVPRSATHSPLFQVFI 344
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1052-1457 |
1.36e-73 |
|
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: 253.10 E-value: 1.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1052 YPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGgDPVQRIHDEVP-FTLQ 1130
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAG-RYEQVVLDKTVrFRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1131 TTVLGERTEQEA------AAAFIKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYN-----N 1199
Cdd:cd19066 81 IIDLRNLADPEArlleliDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDaaerqK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1200 RNLPALRIQYKDYAVWREGFKTGDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLAR 1279
Cdd:cd19066 161 PTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1280 ENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFE 1359
Cdd:cd19066 241 ESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1360 HQDYPFEELVDKLELTRDMSRNPVFDAMFILQNVEKQDIDLREIKVRPANFAHHI-SLFDITLIATE-INGSICCEMEFS 1437
Cdd:cd19066 321 HQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVYTSSEgTVFDLDLEASEdPDGDLLLRLEYS 400
|
410 420
....*....|....*....|
gi 363747658 1438 TEVFLKATIERWADHFIEFL 1457
Cdd:cd19066 401 RGVYDERTIDRFAERYMTAL 420
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1053-1462 |
9.98e-71 |
|
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: 244.86 E-value: 9.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1053 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDaGGDPVQRIHDEVPFTLQTT 1132
Cdd:cd20483 3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEG-DDFGEQQVLDDPSFHLIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1133 VLGERTEQEAA------AAFIKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNN------- 1199
Cdd:cd20483 82 DLSEAADPEAAldqlvrNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDAlragrdl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1200 RNLPALRIQYKDYAVWREGFKTGDAYKTQEAYWLKQLEGELPVLD-LP-ADHARPPVRSFAGDKVSFTLDQEVASGLHKL 1277
Cdd:cd20483 162 ATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKlLPfAKAERPPVKDYERSTVEATLDKELLARMKRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1278 ARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEA 1357
Cdd:cd20483 242 CAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1358 FEHQDYPFEELVDKLELTRDMSRNPVFDAMFILQ------NVEKQDIDLREIK---VRPAnfahhislFDITLIATEI-N 1427
Cdd:cd20483 322 YEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvhgkfpEYDTGDFKFTDYDhydIPTA--------CDIALEAEEDpD 393
|
410 420 430
....*....|....*....|....*....|....*
gi 363747658 1428 GSICCEMEFSTEVFLKATIERWADHFIEFLHAALS 1462
Cdd:cd20483 394 GGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIR 428
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
463-947 |
4.28e-70 |
|
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: 244.39 E-value: 4.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAY 542
Cdd:cd05936 4 LLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 543 PKERLSYMLKDSGASLLltqpgcsapnFSGETLEvDMTSLASEKAENHEFTPADggsLAYVIYTSGSTGQPKGVAVEHRQ 622
Cdd:cd05936 84 TPRELEHILNDSGAKAL----------IVAVSFT-DLLAAGAPLGERVALTPED---VAVLQYTSGTTGVPKGAMLTHRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 623 AVSFLTGMQH--QFPLSEDDIVMVKT----SFSFDASVwQLFWwsLSGASAYLLPpgwEKDSALIVQAIHQENVTTAHFI 696
Cdd:cd05936 150 LVANALQIKAwlEDLLEGDDVVLAALplfhVFGLTVAL-LLPL--ALGATIVLIP---RFRPIGVLKEIRKHRVTIFPGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 697 PAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVLpQVSLIHGYGPTEATVDAAFyvlDPERDRDRLRiPI 776
Cdd:cd05936 224 PTMYIALLNAPEFKKR-DFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAV---NPLDGPRKPG-SI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 777 GKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLGR 856
Cdd:cd05936 298 GIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVDR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 857 TDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT--VRTDSGEpELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMI 929
Cdd:cd05936 371 KKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgvPDPYSGE-AVKAFVvlkegASLTEEEIIAFCREQLAGYKVPRQVE 449
|
490
....*....|....*...
gi 363747658 930 EMEQWPVTPSGKLDRNAL 947
Cdd:cd05936 450 FRDELPKSAVGKILRREL 467
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1051-1464 |
7.02e-70 |
|
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: 242.61 E-value: 7.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1051 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGdPVQRIHDEVPFTLQ 1130
Cdd:cd20484 1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGV-PFQKIEPSKPLSFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1131 TTVLGERTEQEAAAaFI-----KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELY-------N 1198
Cdd:cd20484 80 EEDISSLKESEIIA-YLrekakEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYqallqgkQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1199 NRNLPALRIqYKDYAVWREGFKTGDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLA 1278
Cdd:cd20484 159 PTLASSPAS-YYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1279 RENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAF 1358
Cdd:cd20484 238 RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1359 EHQDYPFEELVDKLELTRDMSRNPVFDAMFILQNVeKQDIDLREIKVRPANF--------AHHISLFDITLIATEINGSI 1430
Cdd:cd20484 318 DHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNF-LQSTSLQQFLAEYQDVlsiefvegIHQEGEYELVLEVYEQEDRF 396
|
410 420 430
....*....|....*....|....*....|....
gi 363747658 1431 CCEMEFSTEVFLKATIERWADHFIEFLHAALSTP 1464
Cdd:cd20484 397 TLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1052-1464 |
1.05e-68 |
|
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: 239.03 E-value: 1.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1052 YPVSSAQKRIYvLQQLEDGGTG-YNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGDPVQRIHDEVPFTLQ 1130
Cdd:cd19543 2 YPLSPMQEGML-FHSLLDPGSGaYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1131 TTVLGERTEQEAAAAF--------IKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYN---- 1198
Cdd:cd19543 81 ELDLSHLSEAEQEAELealaeedrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalge 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1199 --NRNLPALRiQYKDYAVWREGFKTGDAyktqEAYWLKQLEG--ELPVldLPADHARPPVRSFAGDKVSFTLDQEVASGL 1274
Cdd:cd19543 161 gqPPSLPPVR-PYRDYIAWLQRQDKEAA----EAYWREYLAGfeEPTP--LPKELPADADGSYEPGEVSFELSAELTARL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1275 HKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRE 1352
Cdd:cd19543 234 QELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAelPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1353 TALEAFEHQDYPFEELVdklelTRDMSRNPVFDAMFILQN--------VEKQDIDLREIKVRPANFAHhislFDITLIAT 1424
Cdd:cd19543 314 QQLELREHEYVPLYEIQ-----AWSEGKQALFDHLLVFENypvdesleEEQDEDGLRITDVSAEEQTN----YPLTVVAI 384
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 363747658 1425 EiNGSICCEMEFSTEVFLKATIERWADHFIEFLHAALSTP 1464
Cdd:cd19543 385 P-GEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
459-949 |
5.45e-68 |
|
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: 240.07 E-value: 5.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL 538
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAYPKERLSYMLKDSGASLLLTQ-----------PGCSAPNFSGETLEVDMTSLASEKAENHEF----------TPADG 597
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSserldllhpalPGCHDLRTLIIVGDPAHASEGHPGEEPASWpkllalgdadPPHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 598 --GSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASA----YLLP 671
Cdd:TIGR03098 161 idSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVvlhdYLLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 672 pgweKDsalIVQAIHQENVTTAHFIPAMlnsFLDQAEIE-RLSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYG 750
Cdd:TIGR03098 241 ----RD---VLKALEKHGITGLAAVPPL---WAQLAQLDwPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 751 PTEAtVDAAFyvLDPERdRDRLRIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPF 830
Cdd:TIGR03098 311 LTEA-FRSTY--LPPEE-VDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 831 YPG-----ERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAA--------------VTVR 891
Cdd:TIGR03098 387 FPGelhlpELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVafgvpdptlgqaivLVVT 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 892 TDSGEPelcayvegLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPA 949
Cdd:TIGR03098 467 PPGGEE--------LDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
463-947 |
1.06e-64 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 231.92 E-value: 1.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAFTPERLAIRFSG-----GSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLP 537
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 538 LDPAYPKERLSYMLKDSGASLLLTQPGC------------------SAPN------FSGETLEVDMT------SLASEKA 587
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITADGGlrggkvidlkekvdealeELPSlehvivVGRTGADVPMEgdldwdELLAAAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 588 ENHEFTPADGGSLAYVIYTSGSTGQPKGVavEHRQA---VSFLTGMQHQFPLSEDDIVmvktsFSFdASV-WQLFWWS-- 661
Cdd:COG0365 174 AEFEPEPTDADDPLFILYTSGTTGKPKGV--VHTHGgylVHAATTAKYVLDLKPGDVF-----WCT-ADIgWATGHSYiv 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 662 ----LSGASAYLLP--PGWeKDSALIVQAIHQENVTTAHFIPAMLNSFLdQAEIERLS--DRTSLKRVFAGGEPLAPRTA 733
Cdd:COG0365 246 ygplLNGATVVLYEgrPDF-PDPGRLWELIEKYGVTVFFTAPTAIRALM-KAGDEPLKkyDLSSLRLLGSAGEPLNPEVW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 734 ARFASVLpQVSLIHGYGPTEAT-VDAAFYVLDPERdrdrlriP--IGKPVPGARLYVLDPHLAVQPSGVAGELYIAGA-- 808
Cdd:COG0365 324 EWWYEAV-GVPIVDGWGQTETGgIFISNLPGLPVK-------PgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwp 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 809 GVARGYLNRPALTEERFLEDpfYPGerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 888
Cdd:COG0365 396 GMFRGYWNDPERYRETYFGR--FPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 889 TVRTDS--GEpELCAYV---EGLQ-----RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:COG0365 472 VGVPDEirGQ-VVKAFVvlkPGVEpsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
464-944 |
1.11e-64 |
|
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: 227.49 E-value: 1.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 464 FERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYP 543
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 544 KERLSYMLKDSGASLLLtqpgcsapnfsgetlevdmtslasekaenheftpadgGSLAYVIYTSGSTGQPKGVAVEHR-- 621
Cdd:cd17631 81 PPEVAYILADSGAKVLF-------------------------------------DDLALLMYTSGTTGRPKGAMLTHRnl 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 622 --QAVSFLTGmqhqFPLSEDD--IVMVKTSFSFDASVWQLFWWsLSGASAYLLPpGWEKDSALivQAIHQENVTTAHFIP 697
Cdd:cd17631 124 lwNAVNALAA----LDLGPDDvlLVVAPLFHIGGLGVFTLPTL-LRGGTVVILR-KFDPETVL--DLIERHRVTSFFLVP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 698 AMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVlpQVSLIHGYGPTEATVDAAFyvLDPERDRDRLRiPIG 777
Cdd:cd17631 196 TMIQALLQHPRFATT-DLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTF--LSPEDHRRKLG-SAG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 778 KPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLGRT 857
Cdd:cd17631 270 RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 858 DDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EG--LQRNEVRAQLERLLPGYMVPAYMIE 930
Cdd:cd17631 343 KDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEkwGE-AVVAVVvprPGaeLDEDELIAHCRERLARYKIPKSVEF 421
|
490
....*....|....
gi 363747658 931 MEQWPVTPSGKLDR 944
Cdd:cd17631 422 VDALPRNATGKILK 435
|
|
| NRPS-para261 |
TIGR01720 |
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
2408-2554 |
4.47e-61 |
|
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.
Pssm-ID: 273774 [Multi-domain] Cd Length: 153 Bit Score: 206.36 E-value: 4.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2408 QLAYRIKTTKDMLRRVPNKGTGYGLLTHIGELRHK-----EPEVSFNYLGQFSEEKEAETFQLSYYQPSYEIAGEREREY 2482
Cdd:TIGR01720 1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEKlaaspQPEISFNYLGQFDADSNDELFQPSSYSPGEAISPESPRPY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363747658 2483 ELDINALITDGRLQVKAVY-TQVFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDFSNKELTLSALSSI 2554
Cdd:TIGR01720 81 ALEINAMIEDGELTLTWSYpTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1642-1990 |
1.04e-60 |
|
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: 212.53 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1642 EPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVrLLQIASFSFDVFSGDLARTLTNGGTLIVCPdetRLE 1721
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDV-FLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1722 PAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATID 1801
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG--IKLVNGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1802 SSFYETSMGGEGTGDnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQmkftknpFVSGERLY 1881
Cdd:cd04433 155 VATGPPDDDARKPGS---VGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATA-------AVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1882 RTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---SDVNTNA 1957
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVvGVPDPEWGER-VVAVVVLrpgADLDAEE 303
|
330 340 350
....*....|....*....|....*....|...
gi 363747658 1958 LRAALTKELPAYMIPAHLIPLENMPLTLNGKLD 1990
Cdd:cd04433 304 LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1051-1464 |
3.00e-59 |
|
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: 211.46 E-value: 3.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1051 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGdPVQRIHDEVPFTLQ 1130
Cdd:cd19533 1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGE-PYQWIDPYTPVPIR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1131 -TTVLGERTEQEAA-----AAFIKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYN----NR 1200
Cdd:cd19533 80 hIDLSGDPDPEGAAqqwmqEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTallkGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1201 NLPA------LRIQYKDYAvwregFKTGDAYKTQEAYWLKQLEGELPVLDLpADHARPPVRSFAGDKVSFTLDQEVAsgL 1274
Cdd:cd19533 160 PAPPapfgsfLDLVEEEQA-----YRQSERFERDRAFWTEQFEDLPEPVSL-ARRAPGRSLAFLRRTAELPPELTRT--L 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1275 HKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETA 1354
Cdd:cd19533 232 LEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSREL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1355 LEAFEHQDYPFEELVDKLELTRDmsRNPVFDamfILQNVEKQDIDLREIKV--RPANFAHHISL-FDITLIATEINGSIC 1431
Cdd:cd19533 312 RSLLRHQRYRYEDLRRDLGLTGE--LHPLFG---PTVNYMPFDYGLDFGGVvgLTHNLSSGPTNdLSIFVYDRDDESGLR 386
|
410 420 430
....*....|....*....|....*....|...
gi 363747658 1432 CEMEFSTEVFLKATIERWADHFIEFLHAALSTP 1464
Cdd:cd19533 387 IDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1500-1994 |
5.58e-59 |
|
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: 213.49 E-value: 5.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1500 FHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRkGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPI 1577
Cdd:TIGR03098 2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGL-GLARGerVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1578 DSHYPKARIEYILRDSGADILLLQQELKHLISNLPES--EMSHICLDDESSY-------EENSC---NLNLSPA------ 1639
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPGchDLRTLIIVGDPAHaseghpgEEPASwpkLLALGDAdpphpv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 -PEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELdRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVcpdET 1718
Cdd:TIGR03098 161 iDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLEN-RPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVL---HD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1719 RLEPAEIYKIMNSQRITVMESTPaliiPVMEYVYRNQFKLPDLDILIL----GSDMVKAQdFKTLTDRFGQSmRIINSYG 1794
Cdd:TIGR03098 237 YLLPRDVLKALEKHGITGLAAVP----PLWAQLAQLDWPESAAPSLRYltnsGGAMPRAT-LSRLRSFLPNA-RLFLMYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1795 VTEAtidssFYETSMGGEGTgDNVP--IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKN 1872
Cdd:TIGR03098 311 LTEA-----FRSTYLPPEEV-DRRPdsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1873 P-FVSGERLYRT----GDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAA 1946
Cdd:TIGR03098 385 PpFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAfGVPDPTLGQA-IVL 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 363747658 1947 YIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:TIGR03098 464 VVTPPGgeeLDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
483-947 |
7.34e-59 |
|
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: 211.18 E-value: 7.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 483 SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQ 562
Cdd:cd17654 16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 563 PgcsapnfsgetlEVDMTSLASEKAENHEFTPADGGsLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIV 642
Cdd:cd17654 96 K------------ELDNAPLSFTPEHRHFNIRTDEC-LAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 643 MVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQEN-VTTAHFIPAMLNSFLDQAEIER-LSDRTSLKR 720
Cdd:cd17654 163 FLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRHrITVLQATPTLFRRFGSQSIKSTvLSATSSLRV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 721 VFAGGEPLAPRTAAR-FASVLPQVSLIHGYGPTEATVDAAFYVLdPERDrdrLRIPIGKPVPGARLYVLDphlaVQPSGV 799
Cdd:cd17654 243 LALGGEPFPSLVILSsWRGKGNRTRIFNIYGITEVSCWALAYKV-PEED---SPVQLGSPLLGTVIEVRD----QNGSEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 800 AGELY---IAGAGVARGYLNRPALTeerfledpfypgerMYKTGDVARwLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAA 876
Cdd:cd17654 315 TGQVFlggLNRVCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQV 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 877 LRSIEGVREAAVTVRTDsgEPELCAYVEGLQRNEVRAQLER-LLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd17654 380 IESCLGVESCAVTLSDQ--QRLIAFIVGESSSSRIHKELQLtLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
472-950 |
2.26e-58 |
|
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: 211.99 E-value: 2.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGG-------SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPK 544
Cdd:cd17647 2 PERTCVVETPSlnssktrSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 545 ERLSYMLkdsgasllltqpGCSAPNfsgetlevdmtSLASEKAENHEFTPADGGSLAYviyTSGSTGQPKGVAVEHRQAV 624
Cdd:cd17647 82 ARQNIYL------------GVAKPR-----------GLIVIRAAGVVVGPDSNPTLSF---TSGSEGIPKGVLGRHFSLA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 625 SFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASayLLPPGWEK--DSALIVQAIHQENVTTAHFIPAMLNS 702
Cdd:cd17647 136 YYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQ--LLVPTQDDigTPGRLAEWMAKYGATVTHLTPAMGQL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 703 FLDQAEierlSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLdPERDRD-----RLR--IP 775
Cdd:cd17647 214 LTAQAT----TPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEV-PSRSSDptflkNLKdvMP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 776 IGKPVPGARLYVLDPHLAVQPSGVA--GELYIAGAGVARGYLNRPALTEERFLED--------------------PFY-- 831
Cdd:cd17647 289 AGRGMLNVQLLVVNRNDRTQICGIGevGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnepwrQFWlg 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 832 PGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD-SGEPELCAY-------- 902
Cdd:cd17647 369 PRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDkDEEPTLVSYivprfdkp 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 903 -------------------VEGLQR-----NEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAP 950
Cdd:cd17647 449 ddesfaqedvpkevstdpiVKGLIGyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
459-947 |
3.60e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 211.20 E-value: 3.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL 538
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAYPKERLSYMLKDSGASLLLTQPG---------------------CSAPNFSGETLEVDMTSLASEKAENHEFTPADG 597
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLVDSEfvpllaailpqlptvrtviveGDGPAAPLAPEVGEYEELLAAASDTFDFPDIDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 598 GSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFsFDASVWqlfWWS----LSGASaYLLPPg 673
Cdd:PRK06187 167 NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAW---GLPylalMAGAK-QVIPR- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 674 wEKDSALIVQAIHQENVTTAHFIPAMLNsFLDQAEIERLSDRTSLKRVFAGGEPLAPRTAARFASVLpQVSLIHGYGPTE 753
Cdd:PRK06187 241 -RFDPENLLDLIETERVTFFFAVPTIWQ-MLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 754 ATVDAAFYVLDPE-RDRDRLRIPIGKPVPGARLYVLDPHLAVQP--SGVAGELYIAGAGVARGYLNRPALTEERFLEDpf 830
Cdd:PRK06187 318 TSPVVSVLPPEDQlPGQWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG-- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 831 ypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTvrtdsGEP------ELCAYV- 903
Cdd:PRK06187 396 -----WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVI-----GVPdekwgeRPVAVVv 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 363747658 904 ----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK06187 466 lkpgATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
480-888 |
1.21e-54 |
|
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: 200.13 E-value: 1.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 480 SGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLL 559
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 560 LTQPGC-------SAPNFSGETLEV------------DMTSLASEKAENHEFTP-ADGGS-LAYVIYTSGSTGQPKGVAV 618
Cdd:cd05911 87 FTDPDGlekvkeaAKELGPKDKIIVlddkpdgvlsieDLLSPTLGEEDEDLPPPlKDGKDdTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 619 EHRQAVSFLTGMQHQFPLSE--DDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPpgwEKDSALIVQAIHQENVTTAHFI 696
Cdd:cd05911 167 SHRNLIANLSQVQTFLYGNDgsNDVILGFLPLYHIYGLFTTLASLLNGATVIIMP---KFDSELFLDLIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 697 PAMLNSFLDQAEI--ERLSdrtSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAfyvLDPERDRDRLRI 774
Cdd:cd05911 244 PPIAAALAKSPLLdkYDLS---SLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILT---VNPDGDDKPGSV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 775 piGKPVPGARLYVLDPHL-AVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEF 853
Cdd:cd05911 318 --GRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWL------HTGDIGYFDEDGYLYI 389
|
410 420 430
....*....|....*....|....*....|....*
gi 363747658 854 LGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 888
Cdd:cd05911 390 VDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAV 424
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
485-948 |
1.73e-54 |
|
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: 197.51 E-value: 1.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 485 TYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTqpg 564
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 565 csapnfsgetlevdmtslasekaenheftpadggSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMV 644
Cdd:cd05934 82 ----------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLT 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 645 KTS-FSFDASVWQLFWWSLSGASAYLLPpgweKDSA-LIVQAIHQENVTTAHFIPAMLNSFLDQAeiERLSDRTSLKRVF 722
Cdd:cd05934 128 VLPlFHINAQAVSVLAALSVGATLVLLP----RFSAsRFWSDVRRYGATVTNYLGAMLSYLLAQP--PSPDDRAHRLRAA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 723 AGGEPLAPRTAA---RFAsvlpqVSLIHGYGPTEATVDAAfyvldpeRDRDRLRIP--IGKPVPGARLYVLDPHLAVQPS 797
Cdd:cd05934 202 YGAPNPPELHEEfeeRFG-----VRLLEGYGMTETIVGVI-------GPRDEPRRPgsIGRPAPGYEVRIVDDDGQELPA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 798 GVAGELYIAGA---GVARGYLNRPALTEERFledpfypGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIE 874
Cdd:cd05934 270 GEPGELVIRGLrgwGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 875 AALRSIEGVREAAV-TVRTDSGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALP 948
Cdd:cd05934 343 RAILRHPAVREAAVvAVPDEVGEDEVKAVVvlrpgETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
485-947 |
5.06e-53 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 193.82 E-value: 5.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 485 TYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQPG 564
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 565 CSAPNFsgETLEVDMTSLASEKAENHEfTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMV 644
Cdd:TIGR01923 81 LEEKDF--QADSLDRIEAAGRYETSLS-ASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 645 KTSFSFDASVWQLFWWSLSGASAYLLppgwEKDSALIvQAIHQENVTTAHFIPAMLNSFLDQaeierLSDRTSLKRVFAG 724
Cdd:TIGR01923 158 SLPLYHISGLSILFRWLIEGATLRIV----DKFNQLL-EMIANERVTHISLVPTQLNRLLDE-----GGHNENLRKILLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 725 GEPLaPRTAARFASVLpQVSLIHGYGPTEATvdAAFYVLDPERDRDRLriPIGKPVPGARLYVLDPHLAVQpsgvaGELY 804
Cdd:TIGR01923 228 GSAI-PAPLIEEAQQY-GLPIYLSYGMTETC--SQVTTATPEMLHARP--DVGRPLAGREIKIKVDNKEGH-----GEIM 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 805 IAGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR 884
Cdd:TIGR01923 297 VKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQ 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 363747658 885 EAAVTVRTDS--GE-PElcAYVEGlqRNEV-RAQLERLLPG----YMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:TIGR01923 370 EAVVVPKPDAewGQvPV--AYIVS--ESDIsQAKLIAYLTEklakYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
1053-1384 |
3.74e-52 |
|
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: 191.54 E-value: 3.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1053 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDaGGDPVQRIHD------EVP 1126
Cdd:cd19546 6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGD-GGDVHQRILDadaarpELP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1127 FTLQT-----TVLGERTEQeaaaafikPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR- 1200
Cdd:cd19546 85 VVPATeeelpALLADRAAH--------LFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1201 --NLP---ALRIQYKDYAVW-REGFKTGDAYKT----QEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEV 1270
Cdd:cd19546 157 egRAPeraPLPLQFADYALWeRELLAGEDDRDSligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1271 ASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPHK-DLEPILGMFVNTLALRTRPEGGKPFVQYLQE 1349
Cdd:cd19546 237 HARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRELLGR 316
|
330 340 350
....*....|....*....|....*....|....*
gi 363747658 1350 VRETALEAFEHQDYPFEELVDKLELTRDMSRNPVF 1384
Cdd:cd19546 317 VREAVREARRHQDVPFERLAELLALPPSADRHPVF 351
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
496-947 |
4.94e-52 |
|
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: 191.50 E-value: 4.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 496 LAAHLAARGITNESIVGVLSERSPEMLIAVlAVLKAGGA----YLPLDPAYPKERLSYMLKDSGASLLLTQPG------- 564
Cdd:cd05922 7 ASALLEAGGVRGERVVLILPNRFTYIELSF-AVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGaadrlrd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 565 -CSAPNFSGETLEVDMTSLASEKAENHEFTPADggsLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVM 643
Cdd:cd05922 86 aLPASPDPGTVLDADGIRAARASAPAHEVSHED---LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 644 VKTSFSFDASVWQLFWWSLSGASAyLLPPGWEKDSAlIVQAIHQENVTTAHFIP---AMLNSF-LDQAEIERLSDRTSlk 719
Cdd:cd05922 163 TVLPLSYDYGLSVLNTHLLRGATL-VLTNDGVLDDA-FWEDLREHGATGLAGVPstyAMLTRLgFDPAKLPSLRYLTQ-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 720 rvfAGGEpLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFyvLDPERDRDRLRiPIGKPVPGARLYVLDPHLAVQPSGV 799
Cdd:cd05922 239 ---AGGR-LPQETIARLRELLPGAQVYVMYGQTEATRRMTY--LPPERILEKPG-SIGLAIPGGEFEILDDDGTPTPPGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 800 AGELYIAGAGVARGYLNRPAlteerFLEDPFYPGERMYkTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRS 879
Cdd:cd05922 312 PGEIVHRGPNVMKGYWNDPP-----YRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 363747658 880 IEGVREAAVTVRTDSGEPELCAYVEGLQRNEVRAQLERL---LPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05922 386 IGLIIEAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLaerLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1502-1994 |
1.41e-51 |
|
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: 190.47 E-value: 1.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1502 RIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSH 1580
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGvQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1581 YPKARIEYILRDSGADILLLQQELKHLISNLPesemshicldDESSYEENScnlnlspaPEEPVYIIYTSGTTGAPKGVI 1660
Cdd:cd05936 83 YTPRELEHILNDSGAKALIVAVSFTDLLAAGA----------PLGERVALT--------PEDVAVLQYTSGTTGVPKGAM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1661 VTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLT--NGGTLIVCPdetRLEPAEIYKIMNSQRITVME 1738
Cdd:cd05936 145 LTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPlaLGATIVLIP---RFRPIGVLKEIRKHRVTIFP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1739 STPALIIPVMEYVYRNQFKLPDLDILILGSD--MVK-AQDFKTLTDrfgqsMRIINSYGVTEATIDSSFyeTSMGGE--- 1812
Cdd:cd05936 222 GVPTMYIALLNAPEFKKRDFSSLRLCISGGAplPVEvAERFEELTG-----VPIVEGYGLTETSPVVAV--NPLDGPrkp 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1813 GTgdnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLtqmkfTKNPFVSGerLYRTGDRACWLPN 1892
Cdd:cd05936 295 GS-----IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEE-----TAEAFVDG--WLRTGDIGYMDED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1893 GTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA-VQHDKNGQAgLAAYIVPSD---VNTNALRAALTKELPA 1968
Cdd:cd05936 363 GYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgVPDPYSGEA-VKAFVVLKEgasLTEEEIIAFCREQLAG 441
|
490 500
....*....|....*....|....*.
gi 363747658 1969 YMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05936 442 YKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
472-947 |
2.31e-51 |
|
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: 190.60 E-value: 2.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:cd05926 3 APALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQPGC------SAPNFSGETLEV--------------DMTSLASEKAENHEFTPADGGSLAYVIYTSGSTG 611
Cdd:cd05926 83 ADLGSKLVLTPKGElgpasrAASKLGLAILELaldvgvlirapsaeSLSNLLADKKNAKSEGVPLPDDLALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 612 QPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTS-FSFDASVWQLFWWSLSGASAyLLPPGWekdSALIV-QAIHQEN 689
Cdd:cd05926 163 RPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPlFHVHGLVASLLSTLAAGGSV-VLPPRF---SASTFwPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 690 VTTAHFIPAMLNSFLDQAEIERLSDRTSLKRVFAGGEPLAPRTAARFASVLpQVSLIHGYGPTEATVDAAFYVLDPERDR 769
Cdd:cd05926 239 ATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAAHQMTSNPLPPGPRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 770 drlriP--IGKPVpGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLP 847
Cdd:cd05926 318 -----PgsVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLDA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 848 DGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EG--LQRNEVRAQLERLLP 920
Cdd:cd05926 386 DGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEkyGE-EVAAAVvlrEGasVTEEELRAFCRKHLA 464
|
490 500
....*....|....*....|....*..
gi 363747658 921 GYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05926 465 AFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
2095-2528 |
3.33e-50 |
|
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: 185.31 E-value: 3.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2095 LTPIQRRFFgqvhaFHN-------HYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDqNGHVIQFNRGinhkD 2167
Cdd:cd19066 4 LSPMQRGMW-----FLKklatdpsAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEE-AGRYEQVVLD----K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2168 HELFGLYISDWTKASLERTHLDEKLAAeetVIQSKMNVEKGPLLQAGLFKTA-EGDHLLIALHHLVIDGVSWRILLEDLA 2246
Cdd:cd19066 74 TVRFRIEIIDLRNLADPEARLLELIDQ---IQQTIYDLERGPLVRVALFRLAdERDVLVVAIHHIIVDGGSFQILFEDIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2247 AAYQQALEKKEIqLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDIENVPDRLQMNSDAAA-FVLSG 2325
Cdd:cd19066 151 SVYDAAERQKPT-LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLeFFLRS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2326 DWTEKLLfETQQAYGTDANELLLTALGMALSEWAGHDQIVISTEGHGReghvPNIDISRTVGWFTSIYPILLDMGIPEPF 2405
Cdd:cd19066 230 EETKRLR-EVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR----PDEAVEDTIGLFLNLLPLRIDTSPDATF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2406 EdqlaYRIKTTKDMLRRVPNKGTGYG--LLTHIGELR----HKEPEVSFNYLGQFSEEKEAETFQLSyyqpSYEIAGERE 2479
Cdd:cd19066 305 P----ELLKRTKEQSREAIEHQRVPFieLVRHLGVVPeapkHPLFEPVFTFKNNQQQLGKTGGFIFT----TPVYTSSEG 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 363747658 2480 REYELDINALI-TDGRLQVKAVY-TQVFSKHSIECFMDRFHRHLIETIEHC 2528
Cdd:cd19066 377 TVFDLDLEASEdPDGDLLLRLEYsRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
454-947 |
9.72e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 186.26 E-value: 9.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 454 SPKAFTLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGG 533
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 534 AYLPLDPAYPKERLSYMLKDSGASLLLTQ--------PGCSAPNF----------SGETLEVDMTSLAS--EKAENHEFT 593
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAKALFVLglflgvdySATTRLPAlehvviceteEDDPHTEKMKTFTDflAAGDPAERA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 594 PA-DGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSF--------SFDASVwqlfwwsLSG 664
Cdd:PRK07656 161 PEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFfhvfgykaGVNAPL-------MRG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 665 ASAYLLPpgwEKDSALIVQAIHQENVTTAHFIPAMLNSFLD--QAEIERLSdrtSLKRVFAGGEPLAPRTAARFASVLPQ 742
Cdd:PRK07656 234 ATILPLP---VFDPDEVFRLIETERITVLPGPPTMYNSLLQhpDRSAEDLS---SLRLAVTGAASMPVALLERFESELGV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 743 VSLIHGYGPTEAtvdAAFYVLDPeRDRDRLRIP--IGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPAL 820
Cdd:PRK07656 308 DIVLTGYGLSEA---SGVTTFNR-LDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 821 TEERFLEDPFypgerMYkTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD--SGEPe 898
Cdd:PRK07656 384 TAAAIDADGW-----LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDerLGEV- 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 363747658 899 LCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK07656 457 GKAYVvlkpgAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1523-1997 |
4.06e-49 |
|
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: 184.64 E-value: 4.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1523 EISYRFLNERANRLARTLQN---RKGPkpTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILL 1599
Cdd:cd17647 20 SFTYRDINEASNIVAHYLIKtgiKRGD--VVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1600 LQQELKHLISnlPESemshiclddessyeenscNLNLSpapeepvyiiYTSGTTGAPKGVIvtYRNFTHAA-LAW-RQIY 1677
Cdd:cd17647 98 VIRAAGVVVG--PDS------------------NPTLS----------FTSGSEGIPKGVL--GRHFSLAYyFPWmAKRF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1678 ELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPAliipvMEYVYRNQF- 1756
Cdd:cd17647 146 NLSEND-KFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPA-----MGQLLTAQAt 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1757 -KLPDLDILILGSDMVKAQDFKTLtDRFGQSMRIINSYGVTEATIDSSFYETSMGGEGTG------DNVPIGSPLPNVHM 1829
Cdd:cd17647 220 tPFPKLHHAFFVGDILTKRDCLRL-QTLAENVRIVNMYGTTETQRAVSYFEVPSRSSDPTflknlkDVMPAGRGMLNVQL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1830 YVLSQTD--QIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGE----------------------RLYRTGD 1885
Cdd:cd17647 299 LVVNRNDrtQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprdRLYRTGD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1886 RACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSDVN----------- 1954
Cdd:cd17647 379 LGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKpddesfaqedv 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 1955 -------------------TNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVP 1997
Cdd:cd17647 459 pkevstdpivkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
466-947 |
4.95e-49 |
|
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: 182.28 E-value: 4.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 466 RQAAFTPERlairfsggSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKE 545
Cdd:cd05919 1 KTAFYAADR--------SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 546 RLSYMLKDSGASLLLTqpgcsapnfsgetlevdmtslasekaenheftpaDGGSLAYVIYTSGSTGQPKGVAVEHRQAVS 625
Cdd:cd05919 73 DYAYIARDCEARLVVT----------------------------------SADDIAYLLYSSGTTGPPKGVMHAHRDPLL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 626 FLTGMQHQ-FPLSEDDIVMV--KTSFSFDA--SVWqlFWWSlSGASAyLLPPGW-EKDSALIVQAIHQENVTTAhfIPAM 699
Cdd:cd05919 119 FADAMAREaLGLTPGDRVFSsaKMFFGYGLgnSLW--FPLA-VGASA-VLNPGWpTAERVLATLARFRPTVLYG--VPTF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 700 LNSFLDQAEIERLSDRtSLKRVFAGGEPLaPRTAARFASVLPQVSLIHGYGPTEAtvdaaFYVLDPERDrDRLRI-PIGK 778
Cdd:cd05919 193 YANLLDSCAGSPDALR-SLRLCVSAGEAL-PRGLGERWMEHFGGPILDGIGATEV-----GHIFLSNRP-GAWRLgSTGR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 779 PVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTD 858
Cdd:cd05919 265 PVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRAD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 859 DQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV---------EGLQRNEVRAQLERlLPGYMVPAYM 928
Cdd:cd05919 338 DMLKVGGQWVSPVEVESLIIQHPAVAEAAVVaVPESTGLSRLTAFVvlkspaapqESLARDIHRHLLER-LSAHKVPRRI 416
|
490
....*....|....*....
gi 363747658 929 IEMEQWPVTPSGKLDRNAL 947
Cdd:cd05919 417 AFVDELPRTATGKLQRFKL 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1508-1994 |
5.18e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 181.26 E-value: 5.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEIEISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKA 1584
Cdd:PRK07656 15 ARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAAlgiGKGDR--VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1585 RIEYILRDSGADILLLQQEL----KHLISNLPESEMSHICLDDESSYEENSC-----------NLNLSPA--PEEPVYII 1647
Cdd:PRK07656 93 EAAYILARGDAKALFVLGLFlgvdYSATTRLPALEHVVICETEEDDPHTEKMktftdflaagdPAERAPEvdPDDVADIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1648 YTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPvRLLQIASFsFDVF---SGDLArTLTNGGTLIVCPdetRLEPAE 1724
Cdd:PRK07656 173 FTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGD-RYLAANPF-FHVFgykAGVNA-PLMRGATILPLP---VFDPDE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1725 IYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMrIINSYGVTEAtidSSF 1804
Cdd:PRK07656 247 VFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDI-VLTGYGLSEA---SGV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1805 yeTSMGGEGTG-DNVP--IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerLY 1881
Cdd:PRK07656 323 --TTFNRLDDDrKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW-----LH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1882 rTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGlAAYIVP---SDVNTNA 1957
Cdd:PRK07656 396 -TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAViGVPDERLGEVG-KAYVVLkpgAELTEEE 473
|
490 500 510
....*....|....*....|....*....|....*..
gi 363747658 1958 LRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK07656 474 LIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1052-1397 |
9.77e-48 |
|
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: 177.64 E-value: 9.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1052 YPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGDPVQRIH--------- 1122
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHrqaqvpvte 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1123 -DEVPFTLQTTVLGERTEQEaaaaFIKPFDLSQAPLFRAQIVKISDERHLLLV-DMHHIISDGVSVNILIREFGELYNNR 1200
Cdd:cd19536 82 lDLTPLEEQLDPLRAYKEET----KIRRFDLGRAPLVRAALVRKDERERFLLViSDHHSILDGWSLYLLVKEILAVYNQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1201 -------NLPALriQYKDYAVWREGFKTGDAYktqEAYWLKQLEG-ELPVLdlpadharPPVRSFAGDKVSFTLDQEVAS 1272
Cdd:cd19536 158 leykplsLPPAQ--PYRDFVAHERASIQQAAS---ERYWREYLAGaTLATL--------PALSEAVGGGPEQDSELLVSV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1273 GL----HKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGkPFVQY 1346
Cdd:cd19536 225 PLpvrsRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTLSEE-TVEDL 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 363747658 1347 LQEVRETALEAFEHQDYPFEelvdklELTRDMSRNPVFDAMFILQNVEKQD 1397
Cdd:cd19536 304 LKRAQEQELESLSHEQVPLA------DIQRCSEGEPLFDSIVNFRHFDLDF 348
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
473-947 |
1.19e-47 |
|
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: 178.25 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 473 ERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNE-SIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRgDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLtqpgcsapnfsgetlevdmtslasekaenheftpadggSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQ 631
Cdd:cd05941 81 TDSEPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 632 HQFPLSEDD-IVMVKTSFS----FDASVWQLFwwslSGASAYLLPpgweKDSALIV-QAIHQENVTTAHFIPAMLNSFLD 705
Cdd:cd05941 123 DAWRWTEDDvLLHVLPLHHvhglVNALLCPLF----AGASVEFLP----KFDPKEVaISRLMPSITVFMGVPTIYTRLLQ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 706 QAEIERLSDRTSLKRVFA-------GGEPLAPRTAARFASVLPQVsLIHGYGPTEaTVDAAFYVLDPERdrdrlrIP--I 776
Cdd:cd05941 195 YYEAHFTDPQFARAAAAErlrlmvsGSAALPVPTLEEWEAITGHT-LLERYGMTE-IGMALSNPLDGER------RPgtV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 777 GKPVPGARLYVLDPHLA-VQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLG 855
Cdd:cd05941 267 GMPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWF------KTGDLGVVDEDGYYWILG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 856 RT-DDQVKIRGYRIEPGEIEAALRSIEGVREAAVTvrtdsGEPE------LCAYV------EGLQRNEVRAQLERLLPGY 922
Cdd:cd05941 341 RSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVI-----GVPDpdwgerVVAVVvlragaAALSLEELKEWAKQRLAPY 415
|
490 500
....*....|....*....|....*
gi 363747658 923 MVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05941 416 KRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1512-1991 |
2.95e-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: 2.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNR-KGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYIL 1590
Cdd:cd17631 9 PDRTALVFGGRSLTYAELDERVNRLAHALRALgVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1591 RDSGADILLlqqelkhlisnlpesemshiclddessyeenscnlnlspapEEPVYIIYTSGTTGAPKGVIVTYRNFTHAA 1670
Cdd:cd17631 89 ADSGAKVLF-----------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1671 LAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPdetRLEPAEIYKIMNSQRITVMESTPALIIPVMEY 1750
Cdd:cd17631 128 VNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPTMIQALLQH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1751 VYRNQFKLPDLDILILGSDMVKAQDFKTLTDRfgqSMRIINSYGVTEATIDSSFyetsMGGEGTGDNV-PIGSPLPNVHM 1829
Cdd:cd17631 205 PRFATTDLSSLRAVIYGGAPMPERLLRALQAR---GVKFVQGYGMTETSPGVTF----LSPEDHRRKLgSAGRPVFFVEV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1830 YVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlyRTGDRACWLPNGTIRLLGRMDYQVKING 1909
Cdd:cd17631 278 RIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRKKDMIISGG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1910 YRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAyIVPSDVNT---NALRAALTKELPAYMIPAHLIPLENMPLTL 1985
Cdd:cd17631 351 ENVYPAEVEDVLYEHPAVAEVAViGVPDEKWGEAVVAV-VVPRPGAEldeDELIAHCRERLARYKIPKSVEFVDALPRNA 429
|
....*.
gi 363747658 1986 NGKLDR 1991
Cdd:cd17631 430 TGKILK 435
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
483-942 |
9.20e-47 |
|
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: 175.65 E-value: 9.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 483 SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTq 562
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 563 PGcsapnfsgetlevdmtslaSEKAENHEftpADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIV 642
Cdd:cd05903 80 PE-------------------RFRQFDPA---AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 643 MVKTSFS-FDASVWQLFWWSLSGASAYLLPPgWEKDSALivQAIHQENVTTAHFIPAMLNSFLDQAEI--ERLSDrtsLK 719
Cdd:cd05903 138 LVASPMAhQTGFVYGFTLPLLLGAPVVLQDI-WDPDKAL--ALMREHGVTFMMGATPFLTDLLNAVEEagEPLSR---LR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 720 RVFAGGEPLaPRTAARFASVLPQVSLIHGYGPTEatVDAAFYVLDPERDRDRLRIPiGKPVPGARLYVLDPHLAVQPSGV 799
Cdd:cd05903 212 TFVCGGATV-PRSLARRAAELLGAKVCSAYGSTE--CPGAVTSITPAPEDRRLYTD-GRPLPGVEIKVVDDTGATLAPGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 800 AGELYIAGAGVARGYLNRPALTEErfledpFYPgERMYKTGDVARWLPDGNVEFLGRTDDqVKIR-GYRIEPGEIEAALR 878
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRPDLTAD------AAP-EGWFRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVEDLLL 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 879 SIEGVREAAVTVRTDS--GEpELCAYV---EG--LQRNEVRAQLERL-LPGYMVPAYMIEMEQWPVTPSGKL 942
Cdd:cd05903 360 GHPGVIEAAVVALPDErlGE-RACAVVvtkSGalLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1506-2410 |
4.83e-46 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 184.60 E-value: 4.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1506 AKAEEIPEHIAVI------DNEIEISYRFLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIds 1579
Cdd:PRK05691 17 RRAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPA-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1580 hYP--------KARIEYILRDSGADILL--------LQQELKHLISNLPESemshICLDD-ESSYEENSCNLNLspAPEE 1642
Cdd:PRK05691 95 -YPpesarrhhQERLLSIIADAEPRLLLtvadlrdsLLQMEELAAANAPEL----LCVDTlDPALAEAWQEPAL--QPDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1643 PVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKP----VRLLQ-------IASFSFDVFSGD----------L 1701
Cdd:PRK05691 168 IAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPddviVSWLPlyhdmglIGGLLQPIFSGVpcvlmspayfL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1702 ARTL-------TNGGTLIVCPDETrlepaeiYKIMnSQRItvmeSTPALiipvmeyvyrNQFKLPDLDILILGSDMVKAQ 1774
Cdd:PRK05691 248 ERPLrwleaisEYGGTISGGPDFA-------YRLC-SERV----SESAL----------ERLDLSRWRVAYSGSEPIRQD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1775 DFKTLTDRFG----QSMRIINSYGVTEATIdssFYETSMGGEGT-----------------GDNVPI---GSPLPNVHMY 1830
Cdd:PRK05691 306 SLERFAEKFAacgfDPDSFFASYGLAEATL---FVSGGRRGQGIpaleldaealarnraepGTGSVLmscGRSQPGHAVL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1831 VLS-QTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNpfvSGERLYRTGDRAcWLPNGTIRLLGRMDYQVKING 1909
Cdd:PRK05691 383 IVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH---DGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1910 YRIETEEIESVL------LQTGlvREAAVAVQHDKNGQAGLAAYI-------VPSDVNTNALRAALT---KELPAYMIpa 1973
Cdd:PRK05691 459 HNLYPQDIEKTVerevevVRKG--RVAAFAVNHQGEEGIGIAAEIsrsvqkiLPPQALIKSIRQAVAeacQEAPSVVL-- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1974 hLIPLENMPLTLNGKLDRNA---------------LPVPNNVLSRPYTAPVNDIQKTMAYIWEDVLSMSRVGIHDSFFEL 2038
Cdd:PRK05691 535 -LLNPGALPKTSSGKLQRSAcrlrladgsldsyalFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLL 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2039 GGDSIKALQVAARLAAE-GWSMTIRDLFRYSTIQELCGHITplASQADQGPAEGEAELTP---------IQRR--FFGQV 2106
Cdd:PRK05691 614 GGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAAFSAAVA--RQLAGGGAAQAAIARLPrgqalpqslAQNRlwLLWQL 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2107 HAFHNHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQrDQNGHVIQfnRGINHKDHELFGLYISDWTKAslERT 2186
Cdd:PRK05691 692 DPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFY-ERDGVALQ--RIDAQGEFALQRIDLSDLPEA--ERE 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2187 HLDEKLAAEETviQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPKTD 2265
Cdd:PRK05691 767 ARAAQIREEEA--RQPFDLEKGPLLRVTLVRLDDEEHqLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPL 844
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2266 SYLSYADGLTQIAESKQLLSEKTYWQTIL-DAHTAF-LPKDienVPDRLQMNSDAAAFVLS-GDWTEKLLFETQQAYGTD 2342
Cdd:PRK05691 845 GYADYGAWQRQWLAQGEAARQLAYWKAQLgDEQPVLeLATD---HPRSARQAHSAARYSLRvDASLSEALRGLAQAHQAT 921
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 2343 ANELLLTALGMALSEWAGHDQIVISTEGHGReghvPNIDISRTVGWFTSIYPILLDMGIPEPFEDQLA 2410
Cdd:PRK05691 922 LFMVLLAAFQALLHRYSGQGDIRIGVPNANR----PRLETQGLVGFFINTQVLRAQLDGRLPFTALLA 985
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
484-947 |
5.32e-46 |
|
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: 172.91 E-value: 5.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQp 563
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 564 gcsapnfsgetlEVDMtslasekaenheftpadggslAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVm 643
Cdd:cd05972 80 ------------AEDP---------------------ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIH- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 644 vktsFSFDASVWQLFWWS------LSGAsAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNsFLDQAEIERLsDRTS 717
Cdd:cd05972 126 ----WNIADPGWAKGAWSsffgpwLLGA-TVFVYEGPRFDAERILELLERYGVTSFCGPPTAYR-MLIKQDLSSY-KFSH 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 718 LKRVFAGGEPLAPRTAARF--ASVLPqvslIH-GYGPTEATVDAAFYVLDPERdrdrlriP--IGKPVPGARLYVLDPHL 792
Cdd:cd05972 199 LRLVVSAGEPLNPEVIEWWraATGLP----IRdGYGQTETGLTVGNFPDMPVK-------PgsMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 793 AVQPSGVAGELYI--AGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEP 870
Cdd:cd05972 268 RELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGP 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 871 GEIEAALRSIEGVREAAVTVRTD--------------SGEPELCAYVEGLQrNEVRAQLERllpgYMVPaYMIEM-EQWP 935
Cdd:cd05972 341 FEVESALLEHPAVAEAAVVGSPDpvrgevvkafvvltSGYEPSEELAEELQ-GHVKKVLAP----YKYP-REIEFvEELP 414
|
490
....*....|..
gi 363747658 936 VTPSGKLDRNAL 947
Cdd:cd05972 415 KTISGKIRRVEL 426
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1524-1994 |
5.83e-46 |
|
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: 173.43 E-value: 5.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQNRKGPKP-TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQ 1602
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEErAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1603 ELKHL-ISNLPESEMSHICLDdessyeENSCnlnlspapeepvYIIYTSGTTGAPKGVIVTYR----NFTHAALawrqiy 1677
Cdd:cd17654 97 ELDNApLSFTPEHRHFNIRTD------ECLA------------YVIHTSGTTGTPKIVAVPHKcilpNIQHFRS------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1678 ELDRKPVRLLQIASF-SFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNS-QRITVMESTPALI--IPVMEYVYR 1753
Cdd:cd17654 153 LFNITSEDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKrHRITVLQATPTLFrrFGSQSIKST 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1754 NQFKLPDLDILILG-----SDMVkaqdFKTLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGEGtgdnVPIGSPLPNVH 1828
Cdd:cd17654 233 VLSATSSLRVLALGgepfpSLVI----LSSWRGKGNRT-RIFNIYGITEVSCWALAYKVPEEDSP----VQLGSPLLGTV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1829 MYVLSQTDQIQpigvAGELCIGGagVAKGYHQKPDLTQMKFTknpfvsgerLYRTGDRaCWLPNGTIRLLGRMDYQVKIN 1908
Cdd:cd17654 304 IEVRDQNGSEG----TGQVFLGG--LNRVCILDDEVTVPKGT---------MRATGDF-VTVKDGELFFLGRKDSQIKRR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1909 GYRIETEEIESVLLQTGLVREAAVAVQHDKNgqagLAAYIVPSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGK 1988
Cdd:cd17654 368 GKRINLDLIQQVIESCLGVESCAVTLSDQQR----LIAFIVGESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGK 443
|
....*.
gi 363747658 1989 LDRNAL 1994
Cdd:cd17654 444 VDKSEL 449
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
466-946 |
7.24e-46 |
|
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: 175.50 E-value: 7.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 466 RQAAFTPERLAIRF------SGGSLTYAELDMYASRLAAHLAARGITNESiVGVLSERSPEMLIAVLAVLKAGG----AY 535
Cdd:cd05931 1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAiavpLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 536 LPlDPAYPKERLSYMLKDSGASLLLTQPG--------CSAPNFSGETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTS 607
Cdd:cd05931 80 PP-TPGRHAERLAAILADAGPRVVLTTAAalaavrafAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 608 GSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVmvktsfsfdASvW---------QLFWWS--LSGASAYLLPP---- 672
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVV---------VS-WlplyhdmglIGGLLTplYSGGPSVLMSPaafl 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 673 ----GWekdsaliVQAIHQENVTTAhfipAMLNSFLDQA-------EIERLsDRTSLKRVFAGGEPLAPRT----AARFA 737
Cdd:cd05931 229 rrplRW-------LRLISRYRATIS----AAPNFAYDLCvrrvrdeDLEGL-DLSSWRVALNGAEPVRPATlrrfAEAFA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 738 SV-LPQVSLIHGYGPTEATV------DAAFYVLDpERDRDRLRIPI----------------GKPVPGARLYVLDP-HLA 793
Cdd:cd05931 297 PFgFRPEAFRPSYGLAEATLfvsggpPGTGPVVL-RVDRDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPeTGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 794 VQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYPGERMYKTGDVARwLPDGNVEFLGRTDDQVKIRGYRIEPGEI 873
Cdd:cd05931 376 ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 874 EAALRSIEGV----REAAVTVRTDSGEP-----ELCAYVEGLQ----RNEVRAQLER---------LLpgymVPAYMIem 931
Cdd:cd05931 455 EATAEEAHPAlrpgCVAAFSVPDDGEERlvvvaEVERGADPADlaaiAAAIRAAVARehgvapadvVL----VRPGSI-- 528
|
570
....*....|....*
gi 363747658 932 eqwPVTPSGKLDRNA 946
Cdd:cd05931 529 ---PRTSSGKIQRRA 540
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1515-1994 |
7.82e-46 |
|
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: 172.86 E-value: 7.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1515 IAVIDNEIEISYRFLNERANRLARTLQNRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRD 1592
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGKDLRGdrVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1593 SGADILLlqqelkhlisnlpesemshiclddessyeenscnlnlspapeEPVYIIYTSGTTGAPKGVIVTYRNFTH--AA 1670
Cdd:cd05941 83 SEPSLVL------------------------------------------DPALILYTSGTTGRPKGVVLTHANLAAnvRA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1671 L--AWRQiyeldRKPVRLLQIASFsFDV---FSGDLArTLTNGGTLIVCPdetRLEPAEIYKIMNSQRITVMESTPALII 1745
Cdd:cd05941 121 LvdAWRW-----TEDDVLLHVLPL-HHVhglVNALLC-PLFAGASVEFLP---KFDPKEVAISRLMPSITVFMGVPTIYT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1746 PVMEYvYRNQFKLPDLDI---------LILGSDMVKAQDFKTLTDRFGQsmRIINSYGVTEATIDSSfyetsmgGEGTGD 1816
Cdd:cd05941 191 RLLQY-YEAHFTDPQFARaaaaerlrlMVSGSAALPVPTLEEWEAITGH--TLLERYGMTEIGMALS-------NPLDGE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1817 NVP--IGSPLPNVHMYVLSQ-TDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACWLPNG 1893
Cdd:cd05941 261 RRPgtVGMPLPGVQARIVDEeTGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1894 TIRLLGRM-DYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVPSD----VNTNALRAALTKELP 1967
Cdd:cd05941 335 YYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAViGVPDPDWGER-VVAVVVLRAgaaaLSLEELKEWAKQRLA 413
|
490 500
....*....|....*....|....*..
gi 363747658 1968 AYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05941 414 PYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
463-947 |
3.11e-45 |
|
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: 173.20 E-value: 3.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAFTPERLAIRFSGGS----LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL 538
Cdd:cd12119 1 LLEHAARLHGDREIVSRTHEGevhrYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAYPKERLSYMLKDSGASLLLTQP------------------------GCSAPNFSGETLEvDMTSLASEKAENHEFTP 594
Cdd:cd12119 81 NPRLFPEQIAYIINHAEDRVVFVDRdflplleaiaprlptvehvvvmtdDAAMPEPAGVGVL-AYEELLAAESPEYDWPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 595 ADGGSLAYVIYTSGSTGQPKGVAVEHRQAV--SFLTGMQHQFPLSEDDIVMVKTSFsFDASVWQL-FWWSLSGASayLLP 671
Cdd:cd12119 160 FDENTAAAICYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAK--LVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 672 PGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVLpqVSLIHGYGP 751
Cdd:cd12119 237 PGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGR-DLSSLRRVVIGGSAVPRSLIEAFEERG--VRVIHAWGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 752 TE----ATVDA--AFYVLDPERDRDRLRIPIGKPVPGARLYVLDPHLAVQP-SGVA-GELYIAGAGVARGYLNRPALTEE 823
Cdd:cd12119 314 TEtsplGTVARppSEHSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPwDGKAvGELQVRGPWVTKSYYKNDEESEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 824 rFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GE-PELC 900
Cdd:cd12119 394 -LTEDGWL------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPkwGErPLAV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 363747658 901 AYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd12119 467 VVLkegATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
467-947 |
3.26e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 172.07 E-value: 3.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 467 QAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKER 546
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 547 LSYMLKDSGASLLLTQPGCSAPNFSGEtlEVDMTSLASEKAENHEF-TPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVS 625
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAKLIPGI--SVKFAELMNGPKEEAEIqEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHWW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 626 FLTGMQHQFPLSEDDivmvktsfSFDASVwQLFWWS-LS--------GASAYLLppgwEK-DSALIVQAIHQENVTTAHF 695
Cdd:PRK03640 169 SAVGSALNLGLTEDD--------CWLAAV-PIFHISgLSilmrsviyGMRVVLV----EKfDAEKINKLLQTGGVTIISV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 696 IPAMLNSFLDQAEIERLSDrtSLKRVFAGGEPLAPRTAArfASVLPQVSLIHGYGPTEATVDAAfyVLDPERDRDRLRiP 775
Cdd:PRK03640 236 VSTMLQRLLERLGEGTYPS--SFRCMLLGGGPAPKPLLE--QCKEKGIPVYQSYGMTETASQIV--TLSPEDALTKLG-S 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 776 IGKPVPGARLYVLDpHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLG 855
Cdd:PRK03640 309 AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYVLD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 856 RTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTvrtdsGEPEL------CAYV---EGLQRNEVRAQLERLLPGYMVPA 926
Cdd:PRK03640 381 RRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV-----GVPDDkwgqvpVAFVvksGEVTEEELRHFCEEKLAKYKVPK 455
|
490 500
....*....|....*....|.
gi 363747658 927 YMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK03640 456 RFYFVEELPRNASGKLLRHEL 476
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
472-947 |
3.98e-45 |
|
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: 172.55 E-value: 3.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQPGCsAPNFsGETLEVDMTSL---------ASEKAENH--EFTPADGGSL----------AYVIYTSGST 610
Cdd:cd05959 98 EDSRARVVVVSGEL-APVL-AAALTKSEHTLvvlivsggaGPEAGALLlaELVAAEAEQLkpaathaddpAFWLYSSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 611 GQPKGVAveHRQA---VSFLTGMQHQFPLSEDDIVMvktsfsfdaSVWQLFW---------WSLS-GASAYLLPpgwEKD 677
Cdd:cd05959 176 GRPKGVV--HLHAdiyWTAELYARNVLGIREDDVCF---------SAAKLFFayglgnsltFPLSvGATTVLMP---ERP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 678 S-ALIVQAIHQENVTTAHFIPAMLNSFLDQaeiERLSDR--TSLKRVFAGGEPLAP----RTAARFAsvlpqVSLIHGYG 750
Cdd:cd05959 242 TpAAVFKRIRRYRPTVFFGVPTLYAAMLAA---PNLPSRdlSSLRLCVSAGEALPAevgeRWKARFG-----LDILDGIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 751 PTEAtvdaaFYVLDPERDRDRLRIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLedpf 830
Cdd:cd05959 314 STEM-----LHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ---- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 831 ypGErMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV------ 903
Cdd:cd05959 385 --GE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVgVEDEDGLTKPKAFVvlrpgy 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 363747658 904 --EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05959 462 edSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
483-947 |
6.35e-45 |
|
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: 169.97 E-value: 6.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 483 SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTq 562
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 563 pgcsapnfsGETLEvdmtslasekaenheftpadggSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIV 642
Cdd:cd05935 80 ---------GSELD----------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 643 MVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALivQAIHQENVTTAHFIPAMLNSFLDQAEIERlSDRTSLKRVF 722
Cdd:cd05935 129 LACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETAL--ELIEKYKVTFWTNIPTMLVDLLATPEFKT-RDLSSLKVLT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 723 AGGEPLAPRTAARFASvLPQVSLIHGYGPTEATvdAAFYVLDPERDRdrlRIPIGKPVPGARLYVLDPH-LAVQPSGVAG 801
Cdd:cd05935 206 GGGAPMPPAVAEKLLK-LTGLRFVEGYGLTETM--SQTHTNPPLRPK---LQCLGIP*FGVDARVIDIEtGRELPPNEVG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 802 ELYIAGAGVARGYLNRPALTEERFLEDPfypGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIE 881
Cdd:cd05935 280 EIVVRGPQIFKGYWNRPEETEESFIEIK---GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHP 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 882 GVREAAVTVRTD--SGEpELCAYVegLQRNEVRAQL---------ERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05935 357 AI*EVCVISVPDerVGE-EVKAFI--VLRPEYRGKVteediiewaREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1052-1464 |
8.98e-45 |
|
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: 168.64 E-value: 8.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1052 YPVSSAQKRIyVLQQLEDGGTGYNmPAVLELEGKLNPERMERAFKELIKRHESLRTSF-EQDAGGDPVQRIHDEVPftlq 1130
Cdd:cd19542 2 YPCTPMQEGM-LLSQLRSPGLYFN-HFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQVVLKSLD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1131 TTVLGERTEQEAAAAFIKPFD----LSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRNLPAlR 1206
Cdd:cd19542 76 PPIEEVETDEDSLDALTRDLLddptLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-A 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1207 IQYKDYAVWREGFKTGDAYktqeAYWLKQLEGELPVLDLPADHARPPVRsfagdkvsfTLDQEVASG--LHKLARENGST 1284
Cdd:cd19542 155 PPFSDYISYLQSQSQEESL----QYWRKYLQGASPCAFPSLSPKRPAER---------SLSSTRRSLakLEAFCASLGVT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1285 LYMVLLAAYTAFLSRLSGQEDIIVGSPIAGR--PHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQD 1362
Cdd:cd19542 222 LASLFQAAWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQH 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1363 YPFEELVDKLELTRdmsRNPVFDAMFILQNVE-KQDIDLREIKVRPANFAHHISLFDITLIATEINGSICCEMEFSTEVF 1441
Cdd:cd19542 302 LSLREIQRALGLWP---SGTLFNTLVSYQNFEaSPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVL 378
|
410 420
....*....|....*....|...
gi 363747658 1442 LKATIERWADHFIEFLHAALSTP 1464
Cdd:cd19542 379 SEEQAEELLEQFDDILEALLANP 401
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
8-425 |
1.28e-44 |
|
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: 168.69 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 8 LTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIR--FQLLEGEelePRLHLTEYKYYPLRI 85
Cdd:cd19531 4 LSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRttFVEVDGE---PVQVILPPLPLPLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 86 IDFSNVEMI----EIEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQ--KMK 159
Cdd:cd19531 81 VDLSGLPEAereaEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAafLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 160 KKDPLPDQPePSYLSYIEKESQYLQSPRFAKDRLFWTQTFEHPLEYHSL-ADQTSLQKQSTSASRDTIILSPDLEQTIRI 238
Cdd:cd19531 161 RPSPLPPLP-IQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELpTDRPRPAVQSFRGARVRFTLPAELTAALRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 239 FCEEHKiniISLFM---ASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIgRE 315
Cdd:cd19531 240 LARREG---ATLFMtllAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARV-RE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 316 Q-LSVMRHQRFPYNLLVNELRNEQkdlhnligiSMQYQPL-----QWHNAD--------------DFDYETALYfsgyta 375
Cdd:cd19531 316 TaLEAYAHQDLPFEKLVEALQPER---------DLSRSPLfqvmfVLQNAPaaalelpgltveplEVDSGTAKF------ 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 363747658 376 nELSVQIQERidNGTIQLNFDYqNT-LFSLEDIKRIQSHLLTILENALHHP 425
Cdd:cd19531 381 -DLTLSLTET--DGGLRGSLEY-NTdLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
485-947 |
1.09e-43 |
|
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: 166.45 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 485 TYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTqpg 564
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 565 csapnfsgetlevdmtslasekaenheftpaDGGS-LAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQ--HQ-FPLSEDd 640
Cdd:cd05971 85 -------------------------------DGSDdPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQfpFNlFPRDGD- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 641 ivmvktsfsfdasvwqLFW----WSLSGASAYLLPPGW--------------EKDSALIVQAIHqeNVTTAhFIPAMLNS 702
Cdd:cd05971 133 ----------------LYWtpadWAWIGGLLDVLLPSLyfgvpvlahrmtkfDPKAALDLMSRY--GVTTA-FLPPTALK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 703 FLDQAEIERLSDRTSLKRVFAGGEPLAPRTAArFASVLPQVSLIHGYGPTEAT-VDAAFYVLDPERDRDrlripIGKPVP 781
Cdd:cd05971 194 MMRQQGEQLKHAQVKLRAIATGGESLGEELLG-WAREQFGVEVNEFYGQTECNlVIGNCSALFPIKPGS-----MGKPIP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 782 GARLYVLDPHLAVQPSGVAGELYI--AGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLGRTDD 859
Cdd:cd05971 268 GHRVAIVDDNGTPLPPGEVGEIAVelPDPVAFLGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 860 QVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD--SGEpELCAYV---------EGLQRnEVRAQLERLLPGYMVPAYM 928
Cdd:cd05971 341 VITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDpiRGE-IVKAFVvlnpgetpsDALAR-EIQELVKTRLAAHEYPREI 418
|
490
....*....|....*....
gi 363747658 929 IEMEQWPVTPSGKLDRNAL 947
Cdd:cd05971 419 EFVNELPRTATGKIRRREL 437
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
2095-2344 |
2.53e-43 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 159.05 E-value: 2.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2095 LTPIQRRFFgqvhaFH----NHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFqRDQNGHVIQFNRginhkDHEL 2170
Cdd:COG4908 1 LSPAQKRFL-----FLepgsNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRF-VEEDGEPVQRID-----PDAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2171 FGLYISDWTK-ASLERTHLDEKLAAEEtvIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAA 2248
Cdd:COG4908 70 LPLEVVDLSAlPEPEREAELEELVAEE--ASRPFDLARGPLLRAALIRLGEDEHvLLLTIHHIISDGWSLGILLRELAAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2249 YQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTIL-DAHTAF-LPKDIENvPDRLQMNSDAAAFVLSGD 2326
Cdd:COG4908 148 YAALLEGEPPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLaGAPPVLeLPTDRPR-PAVQTFRGATLSFTLPAE 226
|
250
....*....|....*...
gi 363747658 2327 WTEKLLfETQQAYGTDAN 2344
Cdd:COG4908 227 LTEALK-ALAKAHGATVN 243
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
459-947 |
4.55e-43 |
|
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: 166.86 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGayLPL 538
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DpAYPKER---LSYMLKDSGASLLLT----------------QPGCSAPN---FSGETLE-VDMTSLASEKAENHEFTPa 595
Cdd:COG1021 104 F-ALPAHRraeISHFAEQSEAVAYIIpdrhrgfdyralarelQAEVPSLRhvlVVGDAGEfTSLDALLAAPADLSEPRP- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 596 DGGSLAYVIYTSGSTGQPKGVAVEHrqavsfltgmqhqfplseDDIVmvktsFSFDASVwQLfwWSLSGASAYL--LP-- 671
Cdd:COG1021 182 DPDDVAFFQLSGGTTGLPKLIPRTH------------------DDYL-----YSVRASA-EI--CGLDADTVYLaaLPaa 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 672 -------PGW----------------EKDSALivQAIHQENVTTAHFIPAMLNSFLDQAEIERlSDRTSLKRVFAGGEPL 728
Cdd:COG1021 236 hnfplssPGVlgvlyaggtvvlapdpSPDTAF--PLIERERVTVTALVPPLALLWLDAAERSR-YDLSSLRVLQVGGAKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 729 APRTAARFASVLP----QVslihgYGPTEATV-----DaafyvlDPErdrDRLRIPIGKPV-PGARLYVLDPHLAVQPSG 798
Cdd:COG1021 313 SPELARRVRPALGctlqQV-----FGMAEGLVnytrlD------DPE---EVILTTQGRPIsPDDEVRIVDEDGNPVPPG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 799 VAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVkIR-GYRIEPGEIEAAL 877
Cdd:COG1021 379 EVGELLTRGPYTIRGYYRAPEHNARAFTPDGFY------RTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLL 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 878 RSIEGVREAAVTVRTDS--GEpELCAYV----EGLQRNEVRAQL-ERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:COG1021 452 LAHPAVHDAAVVAMPDEylGE-RSCAFVvprgEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
480-889 |
5.93e-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: 165.87 E-value: 5.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 480 SGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLL 559
Cdd:cd05904 29 TGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 560 LTQPgCSAPNFS---------GETLEVDMTSLASEKAENHEFTPA---DGGSLAYVIYTSGSTGQPKGVAVEHRQAVSfL 627
Cdd:cd05904 109 FTTA-ELAEKLAslalpvvllDSAEFDSLSFSDLLFEADEAEPPVvviKQDDVAALLYSSGTTGRSKGVMLTHRNLIA-M 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 628 TGMQHQF--PLSEDDIVMVKT-----SFSFDASVWQLfwwSLSGASAYLLPpgwEKDSALIVQAIHQENVTTAHFIPAML 700
Cdd:cd05904 187 VAQFVAGegSNSDSEDVFLCVlpmfhIYGLSSFALGL---LRLGATVVVMP---RFDLEELLAAIERYKVTHLPVVPPIV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 701 NSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAfYVLDPERDRDRlRIPIGKPV 780
Cdd:cd05904 261 LALVKSPIVDKY-DLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVA-MCFAPEKDRAK-YGSVGRLV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 781 PGARLYVLDPH-LAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDD 859
Cdd:cd05904 338 PNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW------LHTGDLCYIDEDGYLFIVDRLKE 411
|
410 420 430
....*....|....*....|....*....|
gi 363747658 860 QVKIRGYRIEPGEIEAALRSIEGVREAAVT 889
Cdd:cd05904 412 LIKYKGFQVAPAELEALLLSHPEILDAAVI 441
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
472-950 |
6.99e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 166.31 E-value: 6.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 472 PERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQPGC----------SAPNFS-----GETLE-VDMTSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKG 615
Cdd:PRK06188 106 EDAGISTLIVDPAPfveralallaRVPSLKhvltlGPVPDgVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 616 VAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVwqLFWWSL-SGASAYLLPpGWEKDSALivQAIHQENVTTAH 694
Cdd:PRK06188 186 VMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLlRGGTVIVLA-KFDPAEVL--RAIEEQRITATF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 695 FIPAMLNSFLDQAEIERlSDRTSLKRVFAGGEPLAP-RTA---ARFASVLPQVslihgYGPTEATVdaAFYVLDPE---R 767
Cdd:PRK06188 261 LVPTMIYALLDHPDLRT-RDLSSLETVYYGASPMSPvRLAeaiERFGPIFAQY-----YGQTEAPM--VITYLRKRdhdP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 768 DRDRLRIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGDVARWLP 847
Cdd:PRK06188 333 DDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLH-------TGDVAREDE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 848 DGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EGLQRN--EVRAQLERLLP 920
Cdd:PRK06188 406 DGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEkwGE-AVTAVVvlrPGAAVDaaELQAHVKERKG 484
|
490 500 510
....*....|....*....|....*....|
gi 363747658 921 GYMVPAYMIEMEQWPVTPSGKLDRNALPAP 950
Cdd:PRK06188 485 SVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
8-423 |
8.06e-43 |
|
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: 163.59 E-value: 8.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 8 LTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTEYKYyPLRIID 87
Cdd:cd20483 4 MSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSF-HLIVID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 88 FSNVEMIE--IEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMKKKDPLP 165
Cdd:cd20483 83 LSEAADPEaaLDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 166 DQPEPSYlSYIEK---ESQYLQSPRFAKDRLFWTQTFEHPLEYHSL---ADQTSLQKQSTSASRDTIILSPDLEQTIRIF 239
Cdd:cd20483 163 TVPPPPV-QYIDFtlwHNALLQSPLVQPLLDFWKEKLEGIPDASKLlpfAKAERPPVKDYERSTVEATLDKELLARMKRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 240 CEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQLSV 319
Cdd:cd20483 242 CAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 320 MRHQRFPYNLLVNELRNEQKDLHNLIG-ISMQYQ---PLQWHNADDFDYETALYFSGYTANELSVQIQERIDNGtIQLNF 395
Cdd:cd20483 322 YEHSAVPFDYIVDALDVPRSTSHFPIGqIAVNYQvhgKFPEYDTGDFKFTDYDHYDIPTACDIALEAEEDPDGG-LDLRL 400
|
410 420
....*....|....*....|....*...
gi 363747658 396 DYQNTLFSLEDIKRIQSHLLTILENALH 423
Cdd:cd20483 401 EFSTTLYDSADMERFLDNFVTFLTSVIR 428
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1531-1994 |
2.16e-42 |
|
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: 163.38 E-value: 2.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1531 ERANRLARTLQNRKGPKP--TVAVLAKRSiDAIVGVLAVMKAGG----VYIPIDSHYPKARIEYILRDSGADILLLQQEL 1604
Cdd:cd05922 1 LGVSAAASALLEAGGVRGerVVLILPNRF-TYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1605 K-HLISNLPESEMSHICLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQ---IYELD 1680
Cdd:cd05922 80 AdRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEylgITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1681 RKPVRLlqiaSFSFDVFSGDLARTLTNGGTLIVCPDEtrLEPAEIYKIMNSQRITVMESTPALIiPVMEYVYRNQFKLPD 1760
Cdd:cd05922 160 RALTVL----PLSYDYGLSVLNTHLLRGATLVLTNDG--VLDDAFWEDLREHGATGLAGVPSTY-AMLTRLGFDPAKLPS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1761 LDILILGSDMVKAQDFKTLTDRFgQSMRIINSYGVTEATIDSSFYETSMGGEGTGDnvpIGSPLPNVHMYVLSQTDQIQP 1840
Cdd:cd05922 233 LRYLTQAGGRLPQETIARLRELL-PGAQVYVMYGQTEATRRMTYLPPERILEKPGS---IGLAIPGGEFEILDDDGTPTP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1841 IGVAGELCIGGAGVAKGYHQKPdltqmKFTKNPFVSGERLYrTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESV 1920
Cdd:cd05922 309 PGEPGEIVHRGPNVMKGYWNDP-----PYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAA 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 1921 LLQTGLVREAAVAVQHDKNGQAGLAAYIVPSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05922 383 ARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1500-1994 |
2.67e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 164.59 E-value: 2.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1500 FHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQnRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPI 1577
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALR-ALGVKKgdRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1578 DSHYPKARIEYILRDSGADILLLQQEL-KHLISNLPESEMSH--ICLDDESSYEENSCNLNLS------------PAPEE 1642
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLVDSEFvPLLAAILPQLPTVRtvIVEGDGPAAPLAPEVGEYEellaaasdtfdfPDIDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1643 --PVYIIYTSGTTGAPKGVIVTYRN-FTH--AALAWRQIYELDRKPVRLLQIASFSFDVFsgdLARTLTnGGTLIVcPDe 1717
Cdd:PRK06187 167 ndAAAMLYTSGTTGHPKGVVLSHRNlFLHslAVCAWLKLSRDDVYLVIVPMFHVHAWGLP---YLALMA-GAKQVI-PR- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1718 tRLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILG-SDMVKA--QDFKtltDRFGqsMRIINSYG 1794
Cdd:PRK06187 241 -RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGgAALPPAllREFK---EKFG--IDLVQGYG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1795 VTEA--TIDSSFYETSMGGEGTgdnVPI--GSPLPNVHMYVLSQTDQIQP--IGVAGELCIGGAGVAKGYHQKPDLtqmk 1868
Cdd:PRK06187 315 MTETspVVSVLPPEDQLPGQWT---KRRsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEA---- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1869 fTKNPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAY 1947
Cdd:PRK06187 388 -TAETIDGG--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAViGVPDEKWGERPVAVV 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 363747658 1948 IVPSDVNTNA--LRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK06187 465 VLKPGATLDAkeLRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
465-947 |
6.73e-42 |
|
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: 162.47 E-value: 6.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 465 ERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPK 544
Cdd:cd12118 11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 545 ERLSYMLKDSGASLLLTQpgcsaPNFSGETLevdmtsLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHR--- 621
Cdd:cd12118 91 EEIAFILRHSEAKVLFVD-----REFEYEDL------LAEGDPDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRgay 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 622 -QAVS--FLTGMQHqfplsedDIVMVKTSFSFDASVWqLFWWSLS--GASAYLLPpgwEKDSALIVQAIHQENVTtaHF- 695
Cdd:cd12118 160 lNALAniLEWEMKQ-------HPVYLWTLPMFHCNGW-CFPWTVAavGGTNVCLR---KVDAKAIYDLIEKHKVT--HFc 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 696 -IPAMLNSFLDQAEierlSDRTSLKR---VFAGGEPLAPRTAARFASVLPQVSliHGYGPTEATVDAAFYVLDPERD--- 768
Cdd:cd12118 227 gAPTVLNMLANAPP----SDARPLPHrvhVMTAGAPPPAAVLAKMEELGFDVT--HVYGLTETYGPATVCAWKPEWDelp 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 769 ---RDRLRIPIGKPVPGAR-LYVLDPHL--AVQPSGV-AGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGD 841
Cdd:cd12118 301 teeRARLKARQGVRYVGLEeVDVLDPETmkPVPRDGKtIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFH-------SGD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 842 VARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYVE-----GLQRNEVRAQ 914
Cdd:cd12118 374 LAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEkwGE-VPCAFVElkegaKVTEEEIIAF 452
|
490 500 510
....*....|....*....|....*....|...
gi 363747658 915 LERLLPGYMVPAYMIEMEqWPVTPSGKLDRNAL 947
Cdd:cd12118 453 CREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
459-947 |
1.30e-41 |
|
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: 161.34 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL 538
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAYPKERLSYMLKDSGASLLLTqpgcsapnfSGETLEVDMTSLASEKAENHeftpadgGSLAYVIYTSGSTGQPKGVAV 618
Cdd:cd05920 96 LPSHRRSELSAFCAHAEAVAYIV---------PDRHAGFDHRALARELAESI-------PEVALFLLSGGTTGTPKLIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 619 EHR----------------QAVSFLTGM--QHQFPLSEDDIVMVktsfsfdasvwqlfwwSLSGASAYLLPPGwEKDSAL 680
Cdd:cd05920 160 THNdyaynvrasaevcgldQDTVYLAVLpaAHNFPLACPGVLGT----------------LLAGGRVVLAPDP-SPDAAF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 681 ivQAIHQENVTTAHFIPAMLNSFLDQAEIERlSDRTSLKRVFAGGEPLAPRTAARFASVLpQVSLIHGYGPTEATVDaaF 760
Cdd:cd05920 223 --PLIEREGVTVTALVPALVSLWLDAAASRR-ADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEGLLN--Y 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 761 YVL-DPErdrDRLRIPIGKPV-PGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyK 838
Cdd:cd05920 297 TRLdDPD---EVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFY------R 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 839 TGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV----EGLQRNEVR 912
Cdd:cd05920 368 TGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDEllGE-RSCAFVvlrdPPPSAAQLR 446
|
490 500 510
....*....|....*....|....*....|....*.
gi 363747658 913 AQL-ERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05920 447 RFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
1066-1387 |
2.31e-41 |
|
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: 158.50 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1066 QLEDGGTGYNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGdPVQRIHDEVPFTLQTTVLGERTEqeaaaa 1145
Cdd:cd19537 16 QLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGG-LRRSYSSSPPRVQRVDTLDVWKE------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1146 FIKPFDLSQAPLFRaqiVKISDeRHLLLVdMHHIISDGVSVNILIREFGELYNNRNLPALRIQYKDYAVWRegfKTGDAy 1225
Cdd:cd19537 89 INRPFDLEREDPIR---VFISP-DTLLVV-MSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWS---RPASP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1226 kTQEAYWLKQLEGeLPVLDLPAdhaRPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQED 1305
Cdd:cd19537 160 -EDLDFWSEYLSG-LPLLNLPR---RTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1306 IIVGSPIAGRPHKDLEPILGMFVNTLALRTR--PEGGKPFVQYLQEVRETALEAFEHQdYPFEELVDKLELTRDMSRNPV 1383
Cdd:cd19537 235 IVLGAPYLNRTSEEDMETVGLFLEPLPIRIRfpSSSDASAADFLRAVRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPL 313
|
....
gi 363747658 1384 FDAM 1387
Cdd:cd19537 314 FDVM 317
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
457-943 |
2.74e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 161.59 E-value: 2.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 457 AFTLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYL 536
Cdd:PRK07798 2 AWNIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 537 PLDPAYPKERLSYMLKDSGASLLLTQpGCSAPNF-------------------SGETLE---VDMTSLASEKAENHEFTP 594
Cdd:PRK07798 82 NVNYRYVEDELRYLLDDSDAVALVYE-REFAPRVaevlprlpklrtlvvvedgSGNDLLpgaVDYEDALAAGSPERDFGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 595 ADGGSLaYVIYTSGSTGQPKGVAVEHRQ-------AVSFLTGmqhQFPLSEDDIV-----------MVKTSFSFDASVWQ 656
Cdd:PRK07798 161 RSPDDL-YLLYTGGTTGMPKGVMWRQEDifrvllgGRDFATG---EPIEDEEELAkraaagpgmrrFPAPPLMHGAGQWA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 657 LFWWSLSGASAyLLPPGWEKDSALIVQAIHQENVTTAHFI-PAMLNSFLDQAEIERLSDRTSLKRVFAGGEPLAPRTAAR 735
Cdd:PRK07798 237 AFAALFSGQTV-VLLPDVRFDADEVWRTIEREKVNVITIVgDAMARPLLDALEARGPYDLSSLFAIASGGALFSPSVKEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 736 FASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIgkpvpGARLYVLDPHL-AVQP-SGVAGelYIAGAG-VAR 812
Cdd:PRK07798 316 LLELLPNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTI-----GPRTVVLDEDGnPVEPgSGEIG--WIARRGhIPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 813 GYLNRPALTEERFLEdpfYPGERMYKTGDVARWLPDGNVEFLGRtdDQVKIR--GYRIEPGEIEAALRSIEGVREAAVTV 890
Cdd:PRK07798 389 GYYKDPEKTAETFPT---IDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVADALVVG 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 891 RTDS--GEpELCAYVE-----GLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLD 943
Cdd:PRK07798 464 VPDErwGQ-EVVAVVQlregaRPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
451-963 |
3.32e-41 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 161.85 E-value: 3.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 451 EAVSPKAFTLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLK 530
Cdd:PRK06155 14 DPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 531 AGGAYLPLDPAYPKERLSYMLKDSGASLLLTQPGCSApnfSGETLEVDMTSLAS-----EKAENH--------EFTPAD- 596
Cdd:PRK06155 94 LGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLA---ALEAADPGDLPLPAvwlldAPASVSvpagwstaPLPPLDa 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 597 --------GGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDiVMVKTSFSFDASVWQLFWWS-LSGASA 667
Cdd:PRK06155 171 papaaavqPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD-VLYTTLPLFHTNALNAFFQAlLAGATY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 668 YLLPpgweKDSAL-IVQAIHQENVTTAHFIPAMLNSFLDQAEIErlSDRTSLKRVfaggePLAPRTAARFASVLPQ---V 743
Cdd:PRK06155 250 VLEP----RFSASgFWPAVRRHGATVTYLLGAMVSILLSQPARE--SDRAHRVRV-----ALGPGVPAALHAAFRErfgV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 744 SLIHGYGPTEAtvDAAFYVLDPERDRDRLripiGKPVPGARLYVLDPHLAVQPSGVAGELYIAGA---GVARGYLNRPAL 820
Cdd:PRK06155 319 DLLDGYGSTET--NFVIAVTHGSQRPGSM----GRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 821 TEERFLEDPFYPGERmyktgdVARwLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV-TVRTDSGEPEL 899
Cdd:PRK06155 393 TVEAWRNLWFHTGDR------VVR-DADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVfPVPSELGEDEV 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 900 CAYV---EGLQRN--EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAAD-----AETYTAPR 963
Cdd:PRK06155 466 MAAVvlrDGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTADtwdreAAGVQLPR 539
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
8-247 |
3.43e-41 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 152.89 E-value: 3.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 8 LTHAQRRVWFtelLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIR--FQLLEGEelePRLHLTEYKYYPLRI 85
Cdd:COG4908 1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRtrFVEEDGE---PVQRIDPDADLPLEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 86 IDFSNVEMI----EIEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMKKK 161
Cdd:COG4908 75 VDLSALPEPereaELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 162 DPLPDQPEP-SYLSYIEKESQYLQSPRFAKDRLFWTQTFEHPLEYHSLA-DQTSLQKQSTSASRDTIILSPDLEQTIRIF 239
Cdd:COG4908 155 EPPPLPELPiQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPtDRPRPAVQTFRGATLSFTLPAELTEALKAL 234
|
....*...
gi 363747658 240 CEEHKINI 247
Cdd:COG4908 235 AKAHGATV 242
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
467-947 |
5.06e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 159.97 E-value: 5.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 467 QAAFTPERLAIR--FSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPK 544
Cdd:PRK09088 4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 545 ERLSYMLKDSGASLLLTQPGCSAPNFSGETLEVDMTSLASEKAENHEFTPADGGSLayVIYTSGSTGQPKGVAVEHRQav 624
Cdd:PRK09088 84 SELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPERVSL--ILFTSGTSGQPKGVMLSERN-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 625 sfLTGMQHQFPLSEDdiVMVKTSFSFDASVWQLFWW------SLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPA 698
Cdd:PRK09088 160 --LQQTAHNFGVLGR--VDAHSSFLCDAPMFHIIGLitsvrpVLAVGGSILVSNGFEPKRTLGRLGDPALGITHYFCVPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 699 MLNSFLDQAEIERlSDRTSLKRVFAGGeplAPRTAARFASVLPQ-VSLIHGYGPTEA-TVDAAfyVLDPERDRDRLRiPI 776
Cdd:PRK09088 236 MAQAFRAQPGFDA-AALRHLTALFTGG---APHAAEDILGWLDDgIPMVDGFGMSEAgTVFGM--SVDCDVIRAKAG-AA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 777 GKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGR 856
Cdd:PRK09088 309 GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIARRDADGFFWVVDR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 857 TDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEPELCAYV--EG--LQRNEVRAQLERLLPGYMVPAYMIE 930
Cdd:PRK09088 383 KKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAqwGEVGYLAIVpaDGapLDLERIRSHLSTRLAKYKVPKHLRL 462
|
490
....*....|....*..
gi 363747658 931 MEQWPVTPSGKLDRNAL 947
Cdd:PRK09088 463 VDALPRTASGKLQKARL 479
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1515-1994 |
5.49e-41 |
|
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: 159.79 E-value: 5.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1515 IAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDS 1593
Cdd:cd05926 6 LVVPGSTPALTYADLAELVDDLARQLAALGiKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1594 GADILLLQ-----------QELKHLISNLP-ESEMSHICLDDES-SYEENSCNLNLS---PAPEEPVYIIYTSGTTGAPK 1657
Cdd:cd05926 86 GSKLVLTPkgelgpasraaSKLGLAILELAlDVGVLIRAPSAESlSNLLADKKNAKSegvPLPDDLALILHTSGTTGRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1658 GVIVTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTlIVCPDetRLEPAEIYKIMNSQRITVM 1737
Cdd:cd05926 166 GVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGS-VVLPP--RFSASTFWPDVRDYNATWY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1738 ESTPALI-IPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMriINSYGVTEAT--IDSSFYETSMGGEGT 1814
Cdd:cd05926 243 TAVPTIHqILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPV--LEAYGMTEAAhqMTSNPLPPGPRKPGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1815 gdnVPIGSplpNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACWLPNGT 1894
Cdd:cd05926 321 ---VGKPV---GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLDADGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1895 IRLLGRmdyqVK--IN--GYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---SDVNTNALRAALTKEL 1966
Cdd:cd05926 389 LFLTGR----IKelINrgGEKISPLEVDGVLLSHPAVLEAVAfGVPDEKYGEE-VAAAVVLregASVTEEELRAFCRKHL 463
|
490 500
....*....|....*....|....*...
gi 363747658 1967 PAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05926 464 AAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1508-1994 |
5.81e-41 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 161.43 E-value: 5.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVI-----DNEIEISYRFLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSH 1580
Cdd:COG0365 19 AEGRGDKVALIwegedGEERTLTYAELRREVNRFANALRAL-GVKKgdRVAIYLPNIPEAVIAMLACARIGAVHSPVFPG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1581 Y-PKArIEYILRDSGADILL-------------LQQELKHLISNLPESE--------MSHICLDDESSYEE--NSCNLNL 1636
Cdd:COG0365 98 FgAEA-LADRIEDAEAKVLItadgglrggkvidLKEKVDEALEELPSLEhvivvgrtGADVPMEGDLDWDEllAAASAEF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1637 SPAP---EEPVYIIYTSGTTGAPKGVIVTYRNF-THAALAWRQIYEL---DRkpvrllqIASFSfDVF-----SGDLART 1704
Cdd:COG0365 177 EPEPtdaDDPLFILYTSGTTGKPKGVVHTHGGYlVHAATTAKYVLDLkpgDV-------FWCTA-DIGwatghSYIVYGP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1705 LTNGGTLIVCPD-ETRLEPAEIYKIMNSQRITVMESTPALIIPVMEY--VYRNQFKLPDLDILILGSDMVKAQDFKTLTD 1781
Cdd:COG0365 249 LLNGATVVLYEGrPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1782 RFGqsMRIINSYGVTEATidSSFyetsMGGEGTGDNVP--IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGA--GVAKG 1857
Cdd:COG0365 329 AVG--VPIVDGWGQTETG--GIF----ISNLPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1858 YHQKPDLTQMKFtknpFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQH 1936
Cdd:COG0365 401 YWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVvGVPD 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 1937 DKNGQAgLAAYIV------PSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:COG0365 477 EIRGQV-VKAFVVlkpgvePSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
454-947 |
4.44e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 158.37 E-value: 4.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 454 SPKAFTLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGG 533
Cdd:PRK06164 6 APRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 534 AYLPLDPAYPKERLSYMLKDSGASLLLTQPGCSAPNFSGETLEVDMTSL------------------------------- 582
Cdd:PRK06164 86 TVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDFAAILAAVPPDALpplraiavvddaadatpapapgarvqlfalp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 583 --ASEKAENHEFTPADGGSLAYViyTSGSTGQPKGVA------VEHRQAVSFLTGMqhqfplsEDDIVMVKTS-----FS 649
Cdd:PRK06164 166 dpAPPAAAGERAADPDAGALLFT--TSGTTSGPKLVLhrqatlLRHARAIARAYGY-------DPGAVLLAALpfcgvFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 650 FDASVWqlfwwSLSGASAYLLPPGWekDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERlsDRTSLKRV-FAGgepL 728
Cdd:PRK06164 237 FSTLLG-----ALAGGAPLVCEPVF--DAARTARALRRHRVTHTFGNDEMLRRILDTAGERA--DFPSARLFgFAS---F 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 729 APRTAARFASVLPQVSLIHG-YGPTE--ATVdAAFYVLDPERDRdrlRIPIGKPV-PGARLYVLDPHL-AVQPSGVAGEL 803
Cdd:PRK06164 305 APALGELAALARARGVPLTGlYGSSEvqALV-ALQPATDPVSVR---IEGGGRPAsPEARVRARDPQDgALLPDGESGEI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 804 YIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGV 883
Cdd:PRK06164 381 EIRAPSLMRGYLDNPDATARALTDDGYF------RTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGV 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 884 REAAVTVRTDSGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSG---KLDRNAL 947
Cdd:PRK06164 455 AAAQVVGATRDGKTVPVAFViptdgASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
6-425 |
9.26e-40 |
|
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: 154.49 E-value: 9.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 6 YSLTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEGEE-----LEPRLHLTEYKY 80
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGryeqvVLDKTVRFRIEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 81 YPLRIIDFSNVEMIEIEQWIQDQasiPFKLINSPLYQFYLLRI-DSHEVWLFAkFHHIIMDGISLNVMGNQIIDLYQKMK 159
Cdd:cd19066 82 IDLRNLADPEARLLELIDQIQQT---IYDLERGPLVRVALFRLaDERDVLVVA-IHHIIVDGGSFQILFEDISSVYDAAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 160 KKDPLPDQPEPSYLSYIEKESQYLQSPRFAKDRLFWTQTFEHPLEYHSLAdQTSLQKQSTSASRDTIILSPDLEQTIRI- 238
Cdd:cd19066 158 RQKPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLP-KAKRPSQVASYEVLTLEFFLRSEETKRLr 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 239 -FCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQL 317
Cdd:cd19066 237 eVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 318 SVMRHQRFPYNLLVNEL-RNEQKDLHNLIGISMQY--QPLQWHNADDFDYETALY-FSGYTANELSVQIQERIDnGTIQL 393
Cdd:cd19066 317 EAIEHQRVPFIELVRHLgVVPEAPKHPLFEPVFTFknNQQQLGKTGGFIFTTPVYtSSEGTVFDLDLEASEDPD-GDLLL 395
|
410 420 430
....*....|....*....|....*....|..
gi 363747658 394 NFDYQNTLFSLEDIKRIQSHLLTILENALHHP 425
Cdd:cd19066 396 RLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1519-1989 |
1.53e-39 |
|
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: 155.45 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1519 DNEIEISYRFLNERANRLARTLQNRKGPKP-TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADI 1597
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGdVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1598 LLLQQELKHLISNLPESEMSH---ICLDDESSYEENSCNLNLSPAPEE--------------PVYIIYTSGTTGAPKGVI 1660
Cdd:cd05911 86 IFTDPDGLEKVKEAAKELGPKdkiIVLDDKPDGVLSIEDLLSPTLGEEdedlppplkdgkddTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1661 VTYRNFT-HAALAWRQIYELDRKPVRLLqiaSFS-FDVFSGDLA--RTLTNGGTLIVCPdetRLEPAEIYKIMNSQRITV 1736
Cdd:cd05911 166 LSHRNLIaNLSQVQTFLYGNDGSNDVIL---GFLpLYHIYGLFTtlASLLNGATVIIMP---KFDSELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1737 MESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEatidssfyetsMGGEGT-- 1814
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNA-TIKQGYGMTE-----------TGGILTvn 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1815 --GDNVP--IGSPLPNVHM-YVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACW 1889
Cdd:cd05911 308 pdGDDKPgsVGRLLPNVEAkIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1890 LPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA-VQHDKNGQAGlAAYIVPSDvntNALRAAltKELPA 1968
Cdd:cd05911 382 DEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIgIPDEVSGELP-RAYVVRKP---GEKLTE--KEVKD 455
|
490 500 510
....*....|....*....|....*....|
gi 363747658 1969 YM---IPAH------LIPLENMPLTLNGKL 1989
Cdd:cd05911 456 YVakkVASYkqlrggVVFVDEIPKSASGKI 485
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1523-1995 |
1.94e-39 |
|
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: 153.60 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1523 EISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLq 1601
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGiRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1602 qelkhlisnlpesemshiclddessyeenscnlnlspapeEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDR 1681
Cdd:cd05934 82 ----------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1682 KPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPdetRLEPAEIYKIMNSQRITVMESTPAliipVMEYVYRnQFKLPDl 1761
Cdd:cd05934 122 DDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP---RFSASRFWSDVRRYGATVTNYLGA----MLSYLLA-QPPSPD- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1762 D----ILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTeatidssfyETSMG--GEGTGDNVP--IGSPLPNVHMYVLS 1833
Cdd:cd05934 193 DrahrLRAAYGAPNPPELHEEFEERFG--VRLLEGYGMT---------ETIVGviGPRDEPRRPgsIGRPAPGYEVRIVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1834 QTDQIQPIGVAGELCI---GGAGVAKGYHQKPDLTQMKFtKNPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGY 1910
Cdd:cd05934 262 DDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RNGW------FHTGDLGYRDADGFFYFVDRKKDMIRRRGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1911 RIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIV---PSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLN 1986
Cdd:cd05934 335 NISSAEVERAILRHPAVREAAVvAVPDEVGEDE-VKAVVVlrpGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPT 413
|
....*....
gi 363747658 1987 GKLDRNALP 1995
Cdd:cd05934 414 EKVAKAQLR 422
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
483-947 |
1.95e-39 |
|
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: 153.27 E-value: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 483 SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLlltq 562
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 563 pgcsapnfsgetlevdmtslasekaenheftpadgGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIV 642
Cdd:cd05912 77 -----------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNW 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 643 MVktsfsfdasVWQLFWWS-LS--------GASAYLLppgwEK-DSALIVQAIHQENVTTAHFIPAMLNSFLdqaEIERL 712
Cdd:cd05912 122 LC---------ALPLFHISgLSilmrsviyGMTVYLV----DKfDAEQVLHLINSGKVTIISVVPTMLQRLL---EILGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 713 SDRTSLKRVFAGGEPLAPrtaarfaSVLPQ-----VSLIHGYGPTEATvdAAFYVLDPERDRDRLRiPIGKPVPGARLYV 787
Cdd:cd05912 186 GYPNNLRCILLGGGPAPK-------PLLEQckekgIPVYQSYGMTETC--SQIVTLSPEDALNKIG-SAGKPLFPVELKI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 788 LDPHlavQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYR 867
Cdd:cd05912 256 EDDG---QPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGEN 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 868 IEPGEIEAALRSIEGVREAAVTVRTDS--GE-PelCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGK 941
Cdd:cd05912 326 IYPAEIEEVLLSHPAIKEAGVVGIPDDkwGQvP--VAFVvseRPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGK 403
|
....*.
gi 363747658 942 LDRNAL 947
Cdd:cd05912 404 LLRHEL 409
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
484-947 |
2.77e-39 |
|
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: 155.90 E-value: 2.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPA--YP-----KERLSYMLKDSGA 556
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPptYDepnarLRKLRHIWQLLGS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 557 SLLLTQPGcSAPNFSG-------ETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTG 629
Cdd:cd05906 120 PVVLTDAE-LVAEFAGletlsglPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 630 -MQHQfPLSEDDIVMVKTSFSFDASVWQLFWWSL-SG------ASAYLL--PPGWEKdsaLIVQaiHQENVTTA-HFIPA 698
Cdd:cd05906 199 kIQHN-GLTPQDVFLNWVPLDHVGGLVELHLRAVyLGcqqvhvPTEEILadPLRWLD---LIDR--YRVTITWApNFAFA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 699 MLNSFLdqaeiERLSDRT----SLKRVFAGGEPLAPRTAARFASVL-----PQVSLIHGYGPTEATVDAAFYVLDPERDR 769
Cdd:cd05906 273 LLNDLL-----EEIEDGTwdlsSLRYLVNAGEAVVAKTIRRLLRLLepyglPPDAIRPAFGMTETCSGVIYSRSFPTYDH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 770 DRLR--IPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVArWLP 847
Cdd:cd05906 348 SQALefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 848 DGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVRE---AAVTVRTDSGEPELCA--YVEGLQRNEVRAQLER----- 917
Cdd:cd05906 421 NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAETEELAifFVPEYDLQDALSETLRairsv 500
|
490 500 510
....*....|....*....|....*....|....*.
gi 363747658 918 ------LLPGYMVPaymIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05906 501 vsrevgVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
484-949 |
3.87e-39 |
|
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: 153.04 E-value: 3.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQP 563
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 564 gcsapnfsgetlevdmtSLASEKaenhefTPADGgslAYVIYTSGSTGQPKGVAVEHRQAVS-FLTGMQHqFPLSEDDIv 642
Cdd:cd05969 81 -----------------ELYERT------DPEDP---TLLHYTSGTTGTPKGVLHVHDAMIFyYFTGKYV-LDLHPDDI- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 643 mvktsfsfdasvwqlFW------WsLSGASAYLLPPgWEKDSALIV-----------QAIHQENVTTAHFIPAMLNSFLD 705
Cdd:cd05969 133 ---------------YWctadpgW-VTGTVYGIWAP-WLNGVTNVVyegrfdaeswyGIIERVKVTVWYTAPTAIRMLMK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 706 Q-AEIERLSDRTSLKRVFAGGEPLAPRTAARFASVLpQVSLIHGYGPTE-ATVDAAFYVLDPERDRDrlripIGKPVPGA 783
Cdd:cd05969 196 EgDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTEtGSIMIANYPCMPIKPGS-----MGKPLPGV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 784 RLYVLDPHLAVQPSGVAGELYIAGA--GVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQV 861
Cdd:cd05969 270 KAAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDII 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 862 KIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELC-AYV---EGLQ-----RNEVRAQLERLLPGYMVPAYMIEME 932
Cdd:cd05969 343 KTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIkAFIslkEGFEpsdelKEEIINFVRQKLGAHVAPREIEFVD 422
|
490
....*....|....*..
gi 363747658 933 QWPVTPSGKLDRNALPA 949
Cdd:cd05969 423 NLPKTRSGKIMRRVLKA 439
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
8-425 |
7.07e-39 |
|
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: 152.15 E-value: 7.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 8 LTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTEYKYYPLRIID 87
Cdd:cd19539 4 LSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 88 FSNVEM---IEIEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMKKKdPL 164
Cdd:cd19539 84 LSDPDSdreRRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKG-PA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 165 PDQPEP--SYLSYIEKESQYLQSPRFAKDRLFWTQTFEHPLEYHSLADQTslqkQSTSASRDT----IILSPDLEQTIRI 238
Cdd:cd19539 163 APLPELrqQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPTALPTDRP----RPAGFPYPGadlrFELDAELVAALRE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 239 FCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQLS 318
Cdd:cd19539 239 LAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 319 VMRHQRFPYNLLVNELrNEQKDL--HNLIGISmqyqplqwhnaddFDYETALYFSGYTANELSVQIQERIDNGT------ 390
Cdd:cd19539 319 AQRHQELPFQQLVAEL-PVDRDAgrHPLVQIV-------------FQVTNAPAGELELAGGLSYTEGSDIPDGAkfdlnl 384
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 363747658 391 --------IQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHP 425
Cdd:cd19539 385 tvteegtgLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1515-1994 |
7.72e-39 |
|
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: 153.68 E-value: 7.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1515 IAVIDNEIEISYRFLNERANRLARTLQnRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRD 1592
Cdd:cd05959 21 TAFIDDAGSLTYAELEAEARRVAGALR-ALGVKREerVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1593 SGADILLLQQEL---------------KHLISNLPE-SEMSHICLDDESSYEENScnlnLSPA---PEEPVYIIYTSGTT 1653
Cdd:cd05959 100 SRARVVVVSGELapvlaaaltksehtlVVLIVSGGAgPEAGALLLAELVAAEAEQ----LKPAathADDPAFWLYSSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1654 GAPKGVIVTYRNFTHAA-LAWRQIYELdRKPVRLLQIASFSFDVFSGD-LARTLTNGGTLIVCPDetRLEPAEIYKIMNS 1731
Cdd:cd05959 176 GRPKGVVHLHADIYWTAeLYARNVLGI-REDDVCFSAAKLFFAYGLGNsLTFPLSVGATTVLMPE--RPTPAAVFKRIRR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1732 QRITVMESTPALiipvmeyvYRNQFKLPD--------LDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEA----- 1798
Cdd:cd05959 253 YRPTVFFGVPTL--------YAAMLAAPNlpsrdlssLRLCVSAGEALPAEVGERWKARFG--LDILDGIGSTEMlhifl 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1799 --TIDSSFYETSmggegtgdnvpiGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFtknpfvS 1876
Cdd:cd05959 323 snRPGRVRYGTT------------GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF------Q 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1877 GErLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVP------ 1950
Cdd:cd05959 385 GE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLrpgyed 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 363747658 1951 SDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05959 464 SEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
461-947 |
1.14e-38 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 153.11 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 461 HGLFER-QAAF-TPERLAIRFSGGS-LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLP 537
Cdd:PRK07514 3 NNLFDAlRAAFaDRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 538 LDPAYPKERLSYMLKDSGASLLLtqpgCSAPNFSG-------------ETLEVD----MTSLASEKAENHEFTPADGGSL 600
Cdd:PRK07514 83 LNTAYTLAELDYFIGDAEPALVV----CDPANFAWlskiaaaagaphvETLDADgtgsLLEAAAAAPDDFETVPRGADDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 601 AYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVM-----VKTSFSFDASVWQLfwwsLSGASAYLLPpgwe 675
Cdd:PRK07514 159 AAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIhalpiFHTHGLFVATNVAL----LAGASMIFLP---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 676 K-DSALIVQAIHQENVTTAhfIPAMLNSFLDQAEIERlsDRTSLKRVF-AGGEPLAPRTAARFASVLPQVSLiHGYGPTE 753
Cdd:PRK07514 231 KfDPDAVLALMPRATVMMG--VPTFYTRLLQEPRLTR--EAAAHMRLFiSGSAPLLAETHREFQERTGHAIL-ERYGMTE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 754 ATVDAAfyvlDPeRDRDRLRIPIGKPVPGARLYVLDPHL-AVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFyp 832
Cdd:PRK07514 306 TNMNTS----NP-YDGERRAGTVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF-- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 833 germYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV--TVRTDSGE-------PELCAYV 903
Cdd:PRK07514 379 ----FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVigVPHPDFGEgvtavvvPKPGAAL 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 363747658 904 EGlqrNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK07514 455 DE---AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
459-942 |
1.51e-38 |
|
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: 154.66 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGG------SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAG 532
Cdd:cd17634 54 LAANALDRHLRENGDRTAIIYEGDdtsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 533 GAYLPLDPAYPKERLSYMLKDSGASLLLT-----QPGCSAP--NFSGETLEVDMTS------------------------ 581
Cdd:cd17634 134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITadggvRAGRSVPlkKNVDDALNPNVTSvehvivlkrtgsdidwqegrdlww 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 582 --LASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHR-QAVSFLTGMQHQFPLSEDDIVMVKTSFSF-DASVWQL 657
Cdd:cd17634 214 rdLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGgYLVYAATTMKYVFDYGPGDIYWCTADVGWvTGHSYLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 658 FWWSLSGASAYLLP--PGWeKDSALIVQAIHQENVTTAHFIPAMLNSFL--DQAEIERlSDRTSLKRVFAGGEPLAPRTA 733
Cdd:cd17634 294 YGPLACGATTLLYEgvPNW-PTPARMWQVVDKHGVNILYTAPTAIRALMaaGDDAIEG-TDRSSLRILGSVGEPINPEAY 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 734 ARFASVL--PQVSLIHGYGPTEAtvdaAFYVLDPERDRDRLRIPIG-KPVPGARLYVLDPHLAVQPSGVAGELYIAGA-- 808
Cdd:cd17634 372 EWYWKKIgkEKCPVVDTWWQTET----GGFMITPLPGAIELKAGSAtRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwp 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 809 GVARGYLNRPalteERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 888
Cdd:cd17634 448 GQTRTLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 889 T-VRTDSGEPELCAYV---------EGLqRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKL 942
Cdd:cd17634 524 VgIPHAIKGQAPYAYVvlnhgvepsPEL-YAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1503-1990 |
1.68e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 153.50 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1503 IFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHY 1581
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGlGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1582 PKARIEYILRDSGADILLLQQELKHLISN-LPESEMSH--ICLDDES---------SYEE----NSCNLNLSPAPEEPVY 1645
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYEREFAPRVAEvLPRLPKLRtlVVVEDGSgndllpgavDYEDalaaGSPERDFGERSPDDLY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1646 IIYTSGTTGAPKGVIvtyrnfthaalaWRQ---------------------IYELDRK-----PVRLL----------QI 1689
Cdd:PRK07798 168 LLYTGGTTGMPKGVM------------WRQedifrvllggrdfatgepiedEEELAKRaaagpGMRRFpapplmhgagQW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1690 ASFSfdvfsgdlarTLTNGGTlIVCPDETRLEPAEIYKIMNSQRITVMEST-PALIIP-VMEYVYRNQFKLPDLDILILG 1767
Cdd:PRK07798 236 AAFA----------ALFSGQT-VVLLPDVRFDADEVWRTIEREKVNVITIVgDAMARPlLDALEARGPYDLSSLFAIASG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1768 ----SDMVKAQdfktLTDRFGQSMrIINSYGVTEATIDSSFYETSMGGEGTGDNVPIGSplpnvHMYVLS-QTDQIQP-I 1841
Cdd:PRK07798 305 galfSPSVKEA----LLELLPNVV-LTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGP-----RTVVLDeDGNPVEPgS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1842 GVAGELCIGGAgVAKGYHQKPDLTQMKFtknPFVSGERLYRTGDRACWLPNGTIRLLGRmDYQVkIN--GYRIETEEIES 1919
Cdd:PRK07798 375 GEIGWIARRGH-IPLGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR-GSVC-INtgGEKVFPEEVEE 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 1920 VLLQTGLVREAAVA-VQHDKNGQAgLAAYIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLD 1990
Cdd:PRK07798 449 ALKAHPDVADALVVgVPDERWGQE-VVAVVQLREgarPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1078-1363 |
2.78e-38 |
|
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: 150.33 E-value: 2.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1078 AVLELEGK-LNPERMERAFKELIKRHESLRTSFEQDAggdpVQRIHDEVP-FTLQTTVLGERTEQEAAAAFIK------- 1148
Cdd:cd19535 28 AYLEFDGEdLDPDRLERAWNKLIARHPMLRAVFLDDG----TQQILPEVPwYGITVHDLRGLSEEEAEAALEElrerlsh 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1149 -PFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR--NLPALRIQYKDYAVWREGFKtGDAY 1225
Cdd:cd19535 104 rVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPgePLPPLELSFRDYLLAEQALR-ETAY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1226 KTQEAYWLKQLEG-----ELPVLDLPADHARPPVRSFagdkvSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRL 1300
Cdd:cd19535 183 ERARAYWQERLPTlppapQLPLAKDPEEIKEPRFTRR-----EHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARW 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 1301 SGQEDIIVGSPIAGRP--HKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDY 1363
Cdd:cd19535 258 SGQPRFLLNLTLFNRLplHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSY 322
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
1525-1994 |
5.22e-38 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 149.52 E-value: 5.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1525 SYRFLNERANRLARTLQN---RKGPkpTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQ 1601
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAqgiRSGS--RVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1602 QELKhlisnlpESEMSHICLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDR 1681
Cdd:TIGR01923 79 SLLE-------EKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1682 KPVRLLQIASFSFDVFSGdLARTLTNGGTL-IVCPDetrlepAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQfklpD 1760
Cdd:TIGR01923 152 DDNWLLSLPLYHISGLSI-LFRWLIEGATLrIVDKF------NQLLEMIANERVTHISLVPTQLNRLLDEGGHNE----N 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1761 LDILILGSDMVKAQDFKTLTDrfgQSMRIINSYGVTEATidSSFyeTSMGGEGTGDNVPIGSPLPNVHMYvLSQTDQIQp 1840
Cdd:TIGR01923 221 LRKILLGGSAIPAPLIEEAQQ---YGLPIYLSYGMTETC--SQV--TTATPEMLHARPDVGRPLAGREIK-IKVDNKEG- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1841 igvAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESV 1920
Cdd:TIGR01923 292 ---HGEIMVKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETV 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 1921 LLQTGLVREAAV-AVQHDKNGQAGLAAYIVPSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:TIGR01923 362 LYQHPGIQEAVVvPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
455-888 |
1.01e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 151.27 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 455 PKAFTL--HGLF---ERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAAR-GITNESIVGVLSERSPEMLIAVLAV 528
Cdd:PRK08314 2 PKSLTLpeTSLFhnlEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 529 LKAGGAYLPLDPAYPKERLSYMLKDSGASLLLT-------------------------------QPGCSAPNFSGETLEV 577
Cdd:PRK08314 82 LRANAVVVPVNPMNREEELAHYVTDSGARVAIVgselapkvapavgnlrlrhvivaqysdylpaEPEIAVPAWLRAEPPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 578 DM------TSLASEKAENHEFTPADGGS--LAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSF- 648
Cdd:PRK08314 162 QAlapggvVAWKEALAAGLAPPPHTAGPddLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLf 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 649 -------SFDASVWqlfwwslSGASAYLLPPgWEKDSALivQAIHQENVTTAHFIPAMLNSFLDQAEIERlSDRTSLKRV 721
Cdd:PRK08314 242 hvtgmvhSMNAPIY-------AGATVVLMPR-WDREAAA--RLIERYRVTHWTNIPTMVVDFLASPGLAE-RDLSSLRYI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 722 FAGGEPLaPRTAARFASVLPQVSLIHGYGPTEAtvdAAFYVLDPeRDRDRLRIpIGKPVPG--ARlyVLDPH-LAVQPSG 798
Cdd:PRK08314 311 GGGGAAM-PEAVAERLKELTGLDYVEGYGLTET---MAQTHSNP-PDRPKLQC-LGIPTFGvdAR--VIDPEtLEELPPG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 799 VAGELYIAGAGVARGYLNRPALTEERFLEdpfYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALR 878
Cdd:PRK08314 383 EVGEIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLY 459
|
490
....*....|
gi 363747658 879 SIEGVREAAV 888
Cdd:PRK08314 460 KHPAIQEACV 469
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
468-947 |
2.64e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 150.58 E-value: 2.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 468 AAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERL 547
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 548 SYMLKDSGASLLLTQ-----------PGCS---------------------APNFSGETLEVD-----MTSLASEKAENH 590
Cdd:PRK06178 123 SYELNDAGAEVLLALdqlapvveqvrAETSlrhvivtsladvlpaeptlplPDSLRAPRLAAAgaidlLPALRACTAPVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 591 EfTPADGGSLAYVIYTSGSTGQPKGVAVEHRQ----AVSFLTGMQhqfPLSEDDIVMvktsfsfdaSVWQLFWWS----- 661
Cdd:PRK06178 203 L-PPPALDALAALNYTGGTTGMPKGCEHTQRDmvytAAAAYAVAV---VGGEDSVFL---------SFLPEFWIAgenfg 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 662 -----LSGASAYLLPPgWEKDSALivQAIHQENVTTAhfipAML-NSFLDQAEIERLSDR--TSLKRVFAGG--EPLAPR 731
Cdd:PRK06178 270 llfplFSGATLVLLAR-WDAVAFM--AAVERYRVTRT----VMLvDNAVELMDHPRFAEYdlSSLRQVRVVSfvKKLNPD 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 732 TAARFA----SVLPQVSlihgYGPTEATVDAAFYVLDPERDRDRLRIPI--GKPVPGARLYVLDPHL-AVQPSGVAGELY 804
Cdd:PRK06178 343 YRQRWRaltgSVLAEAA----WGMTETHTCDTFTAGFQDDDFDLLSQPVfvGLPVPGTEFKICDFETgELLPLGAEGEIV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 805 IAGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR 884
Cdd:PRK06178 419 VRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVL 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 885 EAAVTVRTDSGEPEL-CAYVE-----GLQRNEVRAQLERLLPGYMVPAYMIeMEQWPVTPSGKLDRNAL 947
Cdd:PRK06178 492 GSAVVGRPDPDKGQVpVAFVQlkpgaDLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
465-947 |
3.05e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 148.85 E-value: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 465 ERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAAR-GITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYP 543
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 544 KERLSYMLKDSGASLLLTQPGCSA-----PNFSGETLEVDMTSLA-SEKAENHEFTPAdGGSLAYVI-YTSGSTGQPKGV 616
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNmalsmQKVSYVQRVISITSLKeIEDRKIDNFVEK-NESASFIIcYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 617 AVEhrQAVSFLTGMQHQFP--LSEDDIVMVKTSFsFDASVWQLFWW-SLSGASAYLLPPGWEKDSAliVQAIHQENVTTA 693
Cdd:PRK06839 168 VLT--QENMFWNALNNTFAidLTMHDRSIVLLPL-FHIGGIGLFAFpTLFAGGVIIVPRKFEPTKA--LSMIEKHKVTVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 694 HFIPAMLNSFLDQAEIERlSDRTSLKRVFAGGEPLAPRTAARFASvlPQVSLIHGYGPTEaTVDAAFYVLdpERDRDRLR 773
Cdd:PRK06839 243 MGVPTIHQALINCSKFET-TNLQSVRWFYNGGAPCPEELMREFID--RGFLFGQGFGMTE-TSPTVFMLS--EEDARRKV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 774 IPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGDVARWLPDGNVEF 853
Cdd:PRK06839 317 GSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC-------TGDLARVDEDGFVYI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 854 LGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEPELCAYV----EGLQRNEVRAQLERLLPGYMVPAY 927
Cdd:PRK06839 390 VGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVkwGEIPIAFIVkkssSVLIEKDVIEHCRLFLAKYKIPKE 469
|
490 500
....*....|....*....|
gi 363747658 928 MIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK06839 470 IVFLKELPKNATGKIQKAQL 489
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
483-947 |
8.33e-37 |
|
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: 146.59 E-value: 8.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 483 SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQ 562
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 563 pgcsapnfsgetlevdmtslasekaenhefTPADggsLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIV 642
Cdd:cd05907 85 ------------------------------DPDD---LATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 643 MvktSF-----SFDASVWQLFWWSLSGASAYLLPPG--------------------WEKDSALIVQAIhqenvttahfIP 697
Cdd:cd05907 132 L---SFlplahVFERRAGLYVPLLAGARIYFASSAEtllddlsevrptvflavprvWEKVYAAIKVKA----------VP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 698 AMLNSFLDQAEIERlsdrtsLKRVFAGGEPLAPRTAARFASV-LPqvsLIHGYGPTEATvdAAFYVLDPERDRDRLripI 776
Cdd:cd05907 199 GLKRKLFDLAVGGR------LRFAASGGAPLPAELLHFFRALgIP---VYEGYGLTETS--AVVTLNPPGDNRIGT---V 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 777 GKPVPGarlyvldPHLAVQPSgvaGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGR 856
Cdd:cd05907 265 GKPLPG-------VEVRIADD---GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 857 TDD-QVKIRGYRIEPGEIEAALRSIEGVREAAV------------TVRTDSGE-------PELCAYVEGLQRNEVRAQLE 916
Cdd:cd05907 329 KKDlIITSGGKNISPEPIENALKASPLISQAVVigdgrpflvaliVPDPEALEawaeehgIAYTDVAELAANPAVRAEIE 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 363747658 917 R-------LLPGY-MVPAYMIEMEQWPV-----TPSGKLDRNAL 947
Cdd:cd05907 409 AaveaanaRLSRYeQIKKFLLLPEPFTIengelTPTLKLKRPVI 452
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
471-947 |
8.84e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 147.34 E-value: 8.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 471 TPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYM 550
Cdd:PRK06145 15 TPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 551 LKDSGASLLLTQ------PGCSAPN-FSGETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAveHRQA 623
Cdd:PRK06145 95 LGDAGAKLLLVDeefdaiVALETPKiVIDAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVM--HSYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 624 VSFLTGMQHQFPL---SEDDIVMVKTSF---SFD----ASVWQlfwwslsgasAYLLPPGWEKDSALIVQAIHQENVTTA 693
Cdd:PRK06145 173 NLHWKSIDHVIALgltASERLLVVGPLYhvgAFDlpgiAVLWV----------GGTLRIHREFDPEAVLAAIERHRLTCA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 694 HFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYvldpERDRDRLR 773
Cdd:PRK06145 243 WMAPVMLSRVLTVPDRDRF-DLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLM----EAGREIEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 774 I-PIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermyKTGDVARWLPDGNVE 852
Cdd:PRK06145 318 IgSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 853 FLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV---EG--LQRNEVRAQLERLLPGYMVPA 926
Cdd:PRK06145 391 LTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIgVHDDRWGERITAVVvlnPGatLTLEALDRHCRQRLASFKVPR 470
|
490 500
....*....|....*....|.
gi 363747658 927 YMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK06145 471 QLKVRDELPRNPSGKVLKRVL 491
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
449-888 |
6.11e-36 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 146.78 E-value: 6.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 449 KTEAVSPKAFTLHGLFERQAAFTPERLAIRF-SGG---SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIA 524
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkEDGiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 525 VLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQ-------------------------PGCSAPNFSGETLEvDM 579
Cdd:COG1022 82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdqeqldkllevrdelpslrhivvldPRGLRDDPRLLSLD-EL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 580 TSLASEKAENHEFTP----ADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMvktSF-----SF 650
Cdd:COG1022 161 LALGREVADPAELEArraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL---SFlplahVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 651 D--ASVWQLFWwslsGASAYLLPPG---------------------WEK----------DSALIVQAI----------HQ 687
Cdd:COG1022 238 ErtVSYYALAA----GATVAFAESPdtlaedlrevkptfmlavprvWEKvyagiqakaeEAGGLKRKLfrwalavgrrYA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 688 ENVTTAHFIPAMLNSFLDQAEI-------ERLSDRtsLKRVFAGGEPLAPRTAARFASVlpQVSLIHGYGPTEATVDAAF 760
Cdd:COG1022 314 RARLAGKSPSLLLRLKHALADKlvfsklrEALGGR--LRFAVSGGAALGPELARFFRAL--GIPVLEGYGLTETSPVITV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 761 YVLDperdrdRLRI-PIGKPVPGARLYVldphlavqpsGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKT 839
Cdd:COG1022 390 NRPG------DNRIgTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHT 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 363747658 840 GDVARWLPDGNVEFLGRTDDQVKIR-GYRIEPGEIEAALRSIEGVREAAV 888
Cdd:COG1022 448 GDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
462-949 |
6.70e-36 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 147.87 E-value: 6.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 462 GLFERQAAFTPErlairfsggSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPA 541
Cdd:PRK06060 18 GWYDRPAFYAAD---------VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 542 YPKERLSYMLKDSGASLLLTQpGCSAPNFSGETLeVDMTSLASE--KAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVE 619
Cdd:PRK06060 89 LHRDDHALAARNTEPALVVTS-DALRDRFQPSRV-AEAAELMSEaaRVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 620 HRQAVSFLTGM-QHQFPLSEDDIVMVKTSFSFDASVWQLFWWSL-SGASAYLLPPGWEKDSALIVQAIHQENVTtaHFIP 697
Cdd:PRK06060 167 HADPLTFVDAMcRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLaTGGSAVINSAPVTPEAAAILSARFGPSVL--YGVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 698 AMLNSFLDQAEIERLSdrtSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEatVDAAFYvldpERDRDRLRI-PI 776
Cdd:PRK06060 245 NFFARVIDSCSPDSFR---SLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTE--VGQTFV----SNRVDEWRLgTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 777 GKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPalteerfleDPFYPGERMYKTGDVARWLPDGNVEFLGR 856
Cdd:PRK06060 316 GRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDTRDRVCIDSDGWVTYRCR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 857 TDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV-----EGLQRNEVRAQLERL---LPGYMVPAY 927
Cdd:PRK06060 387 ADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVaVRESTGASTLQAFLvatsgATIDGSVMRDLHRGLlnrLSAFKVPHR 466
|
490 500
....*....|....*....|..
gi 363747658 928 MIEMEQWPVTPSGKLDRNALPA 949
Cdd:PRK06060 467 FAVVDRLPRTPNGKLVRGALRK 488
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
459-944 |
4.84e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 143.60 E-value: 4.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL 538
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAYPKERLSYMLKDSGA----------SLLLTQPGCSAPnfsgET-LEVDMT----------------SLASEKAENHe 591
Cdd:PRK05605 113 NPLYTAHELEHPFEDHGArvaivwdkvaPTVERLRRTTPL----ETiVSVNMIaampllqrlalrlpipALRKARAALT- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 592 fTPADG--------------------------GSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFP-LSEDDIVMV 644
Cdd:PRK05605 188 -GPAPGtvpwetlvdaaiggdgsdvshprptpDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPgLGDGPERVL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 645 ktsfsfdaSVWQLF----------WWSLSGASAYLLPpgwEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEiERLSD 714
Cdd:PRK05605 267 --------AALPMFhaygltlcltLAVSIGGELVLLP---APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAE-ERGVD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 715 RTSLKRVFAGGEPLAPRTAARFASvLPQVSLIHGYGPTEATVDAAFYVLDPERdrdrlRI-PIGKPVPGARLYVLDPH-L 792
Cdd:PRK05605 335 LSGVRNAFSGAMALPVSTVELWEK-LTGGLLVEGYGLTETSPIIVGNPMSDDR-----RPgYVGVPFPDTEVRIVDPEdP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 793 AV-QPSGVAGELYIAGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPG 871
Cdd:PRK05605 409 DEtMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPA 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 872 EIEAALRSIEGVREAAVT--VRTDSGEPELCAYV--EG--LQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 944
Cdd:PRK05605 482 EVEEVLREHPGVEDAAVVglPREDGSEEVVAAVVlePGaaLDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1516-1994 |
5.15e-35 |
|
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: 140.67 E-value: 5.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1516 AVIDNEIEISYRFLNERANRLARTLQNR-KGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSG 1594
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLgVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1595 ADILLLQQElkhlisnlpesemsHIClddessyeenscnlnlspapeepvYIIYTSGTTGAPKGVIVTYRNFTHAALAW- 1673
Cdd:cd05919 83 ARLVVTSAD--------------DIA------------------------YLLYSSGTTGPPKGVMHAHRDPLLFADAMa 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1674 RQIYELdRKPVRLLQIASFSFDVFSGD-LARTLTNGGTLIVCPdeTRLEPAEIYKIMNSQRITVMESTPALIIPVMEYVY 1752
Cdd:cd05919 125 REALGL-TPGDRVFSSAKMFFGYGLGNsLWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDSCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1753 RNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEatIDSSFYETSMGGEGTGDnvpIGSPLPNVHMYVL 1832
Cdd:cd05919 202 GSPDALRSLRLCVSAGEALPRGLGERWMEHFG--GPILDGIGATE--VGHIFLSNRPGAWRLGS---TGRPVPGYEIRLV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1833 SQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTknpfvsgERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRI 1912
Cdd:cd05919 275 DEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1913 ETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSDVNTN------ALRAALTKELPAYMIPAHLIPLENMPLTLN 1986
Cdd:cd05919 348 SPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPqeslarDIHRHLLERLSAHKVPRRIAFVDELPRTAT 427
|
....*...
gi 363747658 1987 GKLDRNAL 1994
Cdd:cd05919 428 GKLQRFKL 435
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
459-947 |
6.70e-35 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 142.88 E-value: 6.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLA---IRFSGGS---LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAG 532
Cdd:PRK13295 25 TINDDLDACVASCPDKTAvtaVRLGTGAprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 533 GAYLPLDPAYPKERLSYMLKDSGASLLLT----------------QPgcSAPNFS------GETlEVDMTSLASEKAenH 590
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLVVpktfrgfdhaamarrlRP--ELPALRhvvvvgGDG-ADSFEALLITPA--W 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 591 EFTPADGGSLA----------YVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMV------KTSFSFDASV 654
Cdd:PRK13295 180 EQEPDAPAILArlrpgpddvtQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMaspmahQTGFMYGLMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 655 WQLFwwslsGASAYLLPPgWEKDSALIVqaIHQENVTtahFIPAMLNSFLDQAEIERLSDRT--SLKRVFAGGEPLaPRT 732
Cdd:PRK13295 260 PVML-----GATAVLQDI-WDPARAAEL--IRTEGVT---FTMASTPFLTDLTRAVKESGRPvsSLRTFLCAGAPI-PGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 733 AARFASVLPQVSLIHGYGPTEatvDAAFYVLDPERDRDRLRIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVAR 812
Cdd:PRK13295 328 LVERARAALGAKIVSAWGMTE---NGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 813 GYLNRPALTEERFledpfypgERMYKTGDVARWLPDGNVEFLGRTDDqVKIRG-YRIEPGEIEAALRSIEGVREAAVTVR 891
Cdd:PRK13295 405 GYLKRPQLNGTDA--------DGWFDTGDLARIDADGYIRISGRSKD-VIIRGgENIPVVEIEALLYRHPAIAQVAIVAY 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 892 TDS--GEpELCAYV-----EGLQRNEVRAQLE--RLLPGYMvPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK13295 476 PDErlGE-RACAFVvprpgQSLDFEEMVEFLKaqKVAKQYI-PERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1505-1994 |
1.18e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 141.15 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1505 EAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYP 1582
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKgeRIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1583 KARIEYILRDSGADILLLQQELKHLISNLP-ESEMSH-ICLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVI 1660
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMALSMQkVSYVQRvISITSLKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1661 VTYRNfthaaLAWRQIYEL--------DRKPV--RLLQIASFSFDVFSgdlarTLTNGGTLIVcPDetRLEPAEIYKIMN 1730
Cdd:PRK06839 169 LTQEN-----MFWNALNNTfaidltmhDRSIVllPLFHIGGIGLFAFP-----TLFAGGVIIV-PR--KFEPTKALSMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1731 SQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGS---DMVKAQDFKTLTDRFGQsmriinSYGVTEaTIDSSFyet 1807
Cdd:PRK06839 236 KHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapcPEELMREFIDRGFLFGQ------GFGMTE-TSPTVF--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1808 sMGGEGTGDNVP--IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlyRTGD 1885
Cdd:PRK06839 306 -MLSEEDARRKVgsIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1886 RACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAYIV-PSDVNTNA-LRAAL 1962
Cdd:PRK06839 378 LARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVvGRQHVKWGEIPIAFIVKkSSSVLIEKdVIEHC 457
|
490 500 510
....*....|....*....|....*....|..
gi 363747658 1963 TKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK06839 458 RLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
5-425 |
2.22e-34 |
|
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: 138.74 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 5 TYSLTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIR---FQLLEGEEL------EPRLHL 75
Cdd:cd19532 1 TEPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRtcfFTDPEDGEPmqgvlaSSPLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 76 teykyyplRIIDFSNVEmiEIEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLY 155
Cdd:cd19532 81 --------EHVQISDEA--EVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 156 QkmkkkDPLPDQPEPSYLSYIEKESQYLQSPRFAKDRLFWTQTFEH---PLEYHSLADQTSLQKQSTSAS-RDTIILSPD 231
Cdd:cd19532 151 N-----GQPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTlpePLPLLPFAKVKSRPPLTRYDThTAERRLDAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 232 LEQTIRIFCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVRT 311
Cdd:cd19532 226 LAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 312 IGREQLSVMRHQRFPYNLLVNELRNEQKDLHN-LIGISMQYQPLQWHNAD--DFDYETALYFSGYTANELSVQIQErIDN 388
Cdd:cd19532 306 TRDKAYAALAHSRVPFDVLLDELGVPRSATHSpLFQVFINYRQGVAESRPfgDCELEGEEFEDARTPYDLSLDIID-NPD 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 363747658 389 GTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHP 425
Cdd:cd19532 385 GDCLLTLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
459-947 |
4.53e-34 |
|
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: 139.18 E-value: 4.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGS--LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYL 536
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 537 PLDPAYPKERLSYMLKDSGASLLLTQPGCS-APNFSGETLEVDMTSLASEKAENHEFTPA------DGGSLAYVIYTSGS 609
Cdd:cd05923 82 LINPRLKAAELAELIERGEMTAAVIAVDAQvMDAIFQSGVRVLALSDLVGLGEPESAGPLiedpprEPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 610 TGQPKGVAVEHRQAVSFLTGMQHQFPL--SEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPgwEKDSALIVQAIHQ 687
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVE--EFDPADALKLIEQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 688 ENVTTAHFIPAMLNSFLDQAEI--ERLSdrtSLKRV-FAGgeplaprtAARFASVLPQVS------LIHGYGPTEATvdA 758
Cdd:cd05923 240 ERVTSLFATPTHLDALAAAAEFagLKLS---SLRHVtFAG--------ATMPDAVLERVNqhlpgeKVNIYGTTEAM--N 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 759 AFYVLDPeRDRDRLRIPIGKPVPGARLYVLDPHLAvqPSGVAGELYIAGAGVA--RGYLNRPALTEERFLEdpfypgeRM 836
Cdd:cd05923 307 SLYMRDA-RTGTEMRPGFFSEVRIVRIGGSPDEAL--ANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GW 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 837 YKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEPELCAYVeglqRNEVRAQ 914
Cdd:cd05923 377 YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADErwGQSVTACVV----PREGTLS 452
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 363747658 915 LERL--------LPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05923 453 ADELdqfcraseLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
484-947 |
4.69e-34 |
|
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: 138.03 E-value: 4.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTqp 563
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 564 gcsapnfsgetlevdmtslasEKAENHEFtpaDGGSLAYvIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIvm 643
Cdd:cd05973 79 ---------------------DAANRHKL---DSDPFVM-MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 644 vktsfsfdasvwqlFW------WS-----------LSGASAYLLPPGWEKDSALIVqaIHQENVTTAHFIPAMLNSFLDQ 706
Cdd:cd05973 132 --------------FWnaadpgWAyglyyaitgplALGHPTILLEGGFSVESTWRV--IERLGVTNLAGSPTAYRLLMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 707 AEIERLSDRTSLKRVFAGGEPLAPRTAARFASVLPqvSLIHG-YGPTEAtvdaAFYVLDPERDRDRLRI-PIGKPVPGAR 784
Cdd:cd05973 196 GAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG--VPIHDhYGQTEL----GMVLANHHALEHPVHAgSAGRAMPGWR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 785 LYVLDPHLAVQPSGVAGELYIAGAGVA----RGYLNrpalteerfLEDPFYPGeRMYKTGDVARWLPDGNVEFLGRTDDQ 860
Cdd:cd05973 270 VAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQL---------PDTPAIDG-GYYLTGDTVEFDPDGSFSFIGRADDV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 861 VKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELC-AYV---EGLQRN-EVRAQLERL----LPGYMVPAYMIEM 931
Cdd:cd05973 340 ITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVkAFVvlrGGHEGTpALADELQLHvkkrLSAHAYPRTIHFV 419
|
490
....*....|....*.
gi 363747658 932 EQWPVTPSGKLDRNAL 947
Cdd:cd05973 420 DELPKTPSGKIQRFLL 435
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1525-1994 |
5.05e-34 |
|
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: 137.85 E-value: 5.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1525 SYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGAdilllq 1601
Cdd:cd05972 2 SFRELKRESAKAANVLAKlglRKGDR--VAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1602 qelKHLISNLpesemshiclddessyeenscnlnlspapEEPVYIIYTSGTTGAPKGVIVTYR-NFTHAALAwrqIYELD 1680
Cdd:cd05972 74 ---KAIVTDA-----------------------------EDPALIYFTSGTTGLPKGVLHTHSyPLGHIPTA---AYWLG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1681 RKPVRL-LQIASFSFDVF-SGDLARTLTNGGTLIVCpDETRLEPAEIYKIMNSQRITVMESTPAliipvmeyVYR----- 1753
Cdd:cd05972 119 LRPDDIhWNIADPGWAKGaWSSFFGPWLLGATVFVY-EGPRFDAERILELLERYGVTSFCGPPT--------AYRmlikq 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1754 --NQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATIDSSFYETSMGGEGTgdnvpIGSPLPNVHMYV 1831
Cdd:cd05972 190 dlSSYKFSHLRLVVSAGEPLNPEVIEWWRAATG--LPIRDGYGQTETGLTVGNFPDMPVKPGS-----MGRPTPGYDVAI 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1832 LSQTDQIQPIGVAGELCI--GGAGVAKGYHQKPDLTQMKFtknpfvsGERLYRTGDRACWLPNGTIRLLGRMDYQVKING 1909
Cdd:cd05972 263 IDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASI-------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1910 YRIETEEIESVLLQTGLVREAA-VAVQHDKNGQAgLAAYIV------PSDVNTNALRAALTKELPAYMIPAHLIPLENMP 1982
Cdd:cd05972 336 YRIGPFEVESALLEHPAVAEAAvVGSPDPVRGEV-VKAFVVltsgyePSEELAEELQGHVKKVLAPYKYPREIEFVEELP 414
|
490
....*....|..
gi 363747658 1983 LTLNGKLDRNAL 1994
Cdd:cd05972 415 KTISGKIRRVEL 426
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1508-1994 |
7.60e-34 |
|
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: 138.41 E-value: 7.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNE--IEISYRFLNERANRLARTLqNRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPK 1583
Cdd:cd05923 11 ASRAPDACAIADPArgLRLTYSELRARIEAVAARL-HARGLRPGqrVAVVLPNSVEAVIALLALHRLGAVPALINPRLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1584 ARIEYILRDSGADILLLQQELKhlisNLPESEMSHICLDDESSYEENSCNLNLSPA-------PEEPVYIIYTSGTTGAP 1656
Cdd:cd05923 90 AELAELIERGEMTAAVIAVDAQ----VMDAIFQSGVRVLALSDLVGLGEPESAGPLiedpprePEQPAFVFYTSGTTGLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1657 KGVIVTYRNFTHAALAW---------RQIYELDRKPvrLLQIASFsFDVFSGDLArtltnGGTLIVCPDETRlePAEIYK 1727
Cdd:cd05923 166 KGAVIPQRAAESRVLFMstqaglrhgRHNVVLGLMP--LYHVIGF-FAVLVAALA-----LDGTYVVVEEFD--PADALK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1728 IMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILIL-GSDMVKaqdfkTLTDRFGQSM--RIINSYGVTEA---TID 1801
Cdd:cd05923 236 LIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFaGATMPD-----AVLERVNQHLpgEKVNIYGTTEAmnsLYM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1802 SSFYETSMGGEGTGDNVPIGSplpnvhmyVLSQTDQIQPIGVAGELCIGGAGVA--KGYHQKPDLTQMKFTknpfvsgER 1879
Cdd:cd05923 311 RDARTGTEMRPGFFSEVRIVR--------IGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ-------DG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1880 LYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVPSDVNTNAL 1958
Cdd:cd05923 376 WYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVViGVADERWGQS-VTACVVPREGTLSAD 454
|
490 500 510
....*....|....*....|....*....|....*....
gi 363747658 1959 RA---ALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05923 455 ELdqfCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
473-897 |
1.23e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 137.43 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 473 ERLAIRFSGGSLTYAELdmyaSRLAAHLAARgITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDP-AYPKERlSYML 551
Cdd:PRK07787 15 IADAVRIGGRVLSRSDL----AGAATAVAER-VAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPdSGVAER-RHIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQPGCSAPNFsgETLEVDMTSLASekaenHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQ 631
Cdd:PRK07787 89 ADSGAQAWLGPAPDDPAGL--PHVPVRLHARSW-----HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 632 HQFPLSEDDIVmvktsfsfdasVWQLFWWSLSGASAYLLPP---GwekdSALI------VQAIHQENVT--TAHF-IPAM 699
Cdd:PRK07787 162 EAWQWTADDVL-----------VHGLPLFHVHGLVLGVLGPlriG----NRFVhtgrptPEAYAQALSEggTLYFgVPTV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 700 LNsfldqaeieRLSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHG------YGPTEA--TVDAAFyvldperDRDR 771
Cdd:PRK07787 227 WS---------RIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGhrpverYGMTETliTLSTRA-------DGER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 772 LRIPIGKPVPGARLYVLDPHLAVQPSGVA--GELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDG 849
Cdd:PRK07787 291 RPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWF------RTGDVAVVDPDG 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 363747658 850 NVEFLGR-TDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTvrtdsGEP 897
Cdd:PRK07787 365 MHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVV-----GVP 408
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
459-942 |
1.65e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 138.14 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL 538
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAYPKERLSYMLKDSGASLLLTQPG--------------------CSAPNFSGETLEVDMTSLASEKAENHEFTPADGG 598
Cdd:PRK08316 92 NFMLTGEELAYILDHSGARAFLVDPAlaptaeaalallpvdtlilsLVLGGREAPGGWLDFADWAEAGSVAEPDVELADD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 599 SLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIvMVKT-----SFSFDASVWQLFWwslSGASAYLLPpg 673
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDI-PLHAlplyhCAQLDVFLGPYLY---VGATNVILD-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 674 wEKDSALIVQAIHQENVtTAHFIP-----AMLNSfldqAEIERlSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHG 748
Cdd:PRK08316 246 -APDPELILRTIEAERI-TSFFAPptvwiSLLRH----PDFDT-RDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 749 YGPTE----ATvdaafyVLDPErdrDRLRIP--IGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTE 822
Cdd:PRK08316 319 YGQTEiaplAT------VLGPE---EHLRRPgsAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 823 ERFLEDPFYpgermykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV-------------- 888
Cdd:PRK08316 390 EAFRGGWFH-------SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAViglpdpkwieavta 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 889 TVRTDSG----EPELCAYveglqrneVRAQlerlLPGYMVPAYMIEMEQWPVTPSGKL 942
Cdd:PRK08316 463 VVVPKAGatvtEDELIAH--------CRAR----LAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
463-1039 |
1.68e-33 |
|
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: 141.38 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAY 542
Cdd:COG3319 6 AAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 543 PKERLSYMLKDSGASLLLTQPGCSAPnFSGETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQ 622
Cdd:COG3319 86 LALAAAAAALLLAALALLLALLAALA-LALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 623 AVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNS 702
Cdd:COG3319 165 VLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 703 FLDQAEIERLSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIGKPVPG 782
Cdd:COG3319 245 AALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 783 ARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPF--YPGERMYKTGDVARWLPDGNVEFLGRTDDQ 860
Cdd:COG3319 325 LVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAgaGARGRLRRGGDRGRRLGGGLLLGLGRLRLQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 861 VKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPV---- 936
Cdd:COG3319 405 RLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLllll 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 937 TPSGKLDRNALPAPGGAADAETYTAPRNVTEMKLSQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRIAKEFDVQVPL 1016
Cdd:COG3319 485 LLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLL 564
|
570 580
....*....|....*....|...
gi 363747658 1017 KDVFAHPTVEGLATVIREGTDSP 1039
Cdd:COG3319 565 LALLLAPTLAALAAALAAAAAAA 587
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
599-947 |
2.91e-33 |
|
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: 132.84 E-value: 2.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 599 SLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWekds 678
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQ---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 679 aLIVQAIHQENVTTAHFIPAMLNSFLDqaEIERLSDRTSLKRVFAGGEPLAPRTAARFAsvLPQVSLIHGYGPTEATVDA 758
Cdd:cd17630 77 -ALAEDLAPPGVTHVSLVPTQLQRLLD--SGQGPAALKSLRAVLLGGAPIPPELLERAA--DRGIPLYTTYGMTETASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 759 AFYVLDPERDRDrlripIGKPVPGARLYVLDPhlavqpsgvaGELYIAGAGVARGYLNRPalTEERFLEDPFYPgermyk 838
Cdd:cd17630 152 ATKRPDGFGRGG-----VGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ--LVPEFNEDGWFT------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 839 TGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYVEGLQRN---EVRA 913
Cdd:cd17630 209 TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEelGQ-RPVAVIVGRGPAdpaELRA 287
|
330 340 350
....*....|....*....|....*....|....
gi 363747658 914 QLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd17630 288 WLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1497-1994 |
3.07e-33 |
|
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: 136.69 E-value: 3.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1497 DVPFHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYI 1575
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGiRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1576 PIDSHYPKARIEYILRDSGADILLLQQELKHLISNLPESEMSHiclddessyeenSCNlnlspapeEPVYIIYTSGTTGA 1655
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAVAYIVPDRHAGFDHRALARELAE------------SIP--------EVALFLLSGGTTGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1656 PKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQI-ASFSFDVFSGDLARTLTNGGTLIVCPDEtrlEPAEIYKIMNSQRI 1734
Cdd:cd05920 154 PKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLpAAHNFPLACPGVLGTLLAGGRVVLAPDP---SPDAAFPLIEREGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1735 TVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATI------DSSfyETS 1808
Cdd:cd05920 231 TVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLG--CTLQQVFGMAEGLLnytrldDPD--EVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1809 MGGEGTgdnvPIgSPLPNVHmyVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRAC 1888
Cdd:cd05920 307 IHTQGR----PM-SPDDEIR--VVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1889 WLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAA-VAVQHDKNGQAgLAAYIVPSD--VNTNALRAALTK- 1964
Cdd:cd05920 374 RTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAvVAMPDELLGER-SCAFVVLRDppPSAAQLRRFLREr 452
|
490 500 510
....*....|....*....|....*....|
gi 363747658 1965 ELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05920 453 GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
465-962 |
3.11e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 137.60 E-value: 3.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 465 ERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPK 544
Cdd:PRK07786 24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 545 ERLSYMLKDSGASLLLTQPGC---------SAPNF--------SGETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTS 607
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALapvatavrdIVPLLstvvvaggSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 608 GSTGQPKGVAVEHR----QAVSFLTGMQHQfplSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGwEKDSALIVQ 683
Cdd:PRK07786 184 GTTGRPKGAVLTHAnltgQAMTCLRTNGAD---INSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLG-AFDPGQLLD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 684 AIHQENVTTAHFIPAMLNSFLDQAEIErlsDRTSLKRVFAGGEPLAPRTAAR-FASVLPQVSLIHGYGPTEATvdAAFYV 762
Cdd:PRK07786 260 VLEAEKVTGIFLVPAQWQAVCAEQQAR---PRDLALRVLSWGAAPASDTLLRqMAATFPEAQILAAFGQTEMS--PVTCM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 763 LDPErDRDRLRIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGDV 842
Cdd:PRK07786 335 LLGE-DAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH-------SGDL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 843 ARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYVEGLQRNEVRAQLERL---- 918
Cdd:PRK07786 407 VRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLaefl 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 363747658 919 ---LPGYMVPAYMIEMEQWPVTPSGKLD----RNALPAPGGAADAETYTAP 962
Cdd:PRK07786 487 tdrLARYKHPKALEIVDALPRNPAGKVLktelRERYGACVNVERRSASAGF 537
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
5-425 |
3.84e-33 |
|
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: 135.14 E-value: 3.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 5 TYSLTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGA----------LNHSISRNDAIRFQLLEGEEleprlh 74
Cdd:cd20484 1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQAcqfvleqhpiLKSVIEEEDGVPFQKIEPSK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 75 lteykyyPLRII--DFSNVEMIEIEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQII 152
Cdd:cd20484 75 -------PLSFQeeDISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 153 DLYQKMKK-KDPLPDQPEPSYLSYIEKESQYLQSPRFAKDRLFWTQTFEHPLEYHSL-ADQTSLQKQSTSASRDTIILSP 230
Cdd:cd20484 148 DAYQALLQgKQPTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELpADRPRSSAPSFEGQTYTRRLPS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 231 DLEQTIRIFCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDTDFLSFVR 310
Cdd:cd20484 228 ELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 311 TIgreQLSV---MRHQRFPYNLLVNELRNEQKDLH-----------NLIGiSMQYQPLQWHNADDFDYETALYFSGYTAN 376
Cdd:cd20484 308 KL---QLTVldgLDHAAYPFPAMVRDLNIPRSQANspvfqvaffyqNFLQ-STSLQQFLAEYQDVLSIEFVEGIHQEGEY 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 363747658 377 ELSVQIQERIDNgtIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHP 425
Cdd:cd20484 384 ELVLEVYEQEDR--FTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
459-944 |
4.81e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 137.21 E-value: 4.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAI--RFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYL 536
Cdd:PRK12583 19 TIGDAFDATVARFPDREALvvRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 537 PLDPAYPKERLSYMLKDSGASLLLTQPGCSAPNFSGETLEVdMTSLASEKAEnhEFTPAD---------------GGSLA 601
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQEL-LPGLAEGQPG--ALACERlpelrgvvslapappPGFLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 602 Y-----------------------------VIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFsfda 652
Cdd:PRK12583 176 WhelqargetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL---- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 653 svWQLFWWSLS-----GASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEP 727
Cdd:PRK12583 252 --YHCFGMVLAnlgcmTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNF-DLSSLRTGIMAGAP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 728 LAPRTAARFASVLPQVSLIHGYGPTEATvdAAFYVLDPERDRDRLRIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAG 807
Cdd:PRK12583 329 CPIEVMRRVMDEMHMAEVQIAYGMTETS--PVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 808 AGVARGYLNRPALTEERFLEDPFypgerMYkTGDVARWLPDGNVEFLGRTDDQVkIR-GYRIEPGEIEAALRSIEGVREA 886
Cdd:PRK12583 407 YSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMI-IRgGENIYPREIEEFLFTHPAVADV 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 887 AVTVRTDS--GEpELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 944
Cdd:PRK12583 480 QVFGVPDEkyGE-EIVAWVrlhpgHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
459-947 |
5.01e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 137.19 E-value: 5.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFS-GGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLP 537
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 538 LDPAYPKERLSYMLKDSGASLLLTQPGCSAPNFSGETLE-------------VD-----MTSLA-SEKAENHE----FTP 594
Cdd:PRK06087 104 LLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPlqnqlpqlqqivgVDklapaTSSLSlSQIIADYEplttAIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 595 ADGGSLAYVIYTSGSTGQPKGVAVEHRQAV----SFLTGMQhqfpLSEDDIVMVKTSFS----FDASVWQLFwwsLSGAS 666
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTHNNILaserAYCARLN----LTWQDVFMMPAPLGhatgFLHGVTAPF---LIGAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 667 AYLLPPgWEKDSALivQAIHQENVTTAH----FIPAMLNSfLDQAEierlSDRTSLKRVFAGGEPLaPRTAARFASVlPQ 742
Cdd:PRK06087 257 SVLLDI-FTPDACL--ALLEQQRCTCMLgatpFIYDLLNL-LEKQP----ADLSALRFFLCGGTTI-PKKVARECQQ-RG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 743 VSLIHGYGPTEATVDAafyVLDPERDRDRLRIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTe 822
Cdd:PRK06087 327 IKLLSVYGSTESSPHA---VVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELT- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 823 ERFLEDpfypgERMYKTGDVARWLPDGNVEFLGRTDDqVKIR-GYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpEL 899
Cdd:PRK06087 403 ARALDE-----EGWYYSGDLCRMDEAGYIKITGRKKD-IIVRgGENISSREVEDILLQHPKIHDACVVAMPDErlGE-RS 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 900 CAYVEgLQRNEVRAQLERLL--------PGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK06087 476 CAYVV-LKAPHHSLTLEEVVaffsrkrvAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1525-1989 |
7.06e-33 |
|
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: 134.43 E-value: 7.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1525 SYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQE 1603
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGvGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1604 LKhlisnlpesEMSHiclddessyeenscnlnlSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKP 1683
Cdd:cd05903 83 FR---------QFDP------------------AAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1684 VRLLQIASFSFDVFSGDLARTLTNGGTLIVCpdeTRLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDI 1763
Cdd:cd05903 136 VFLVASPMAHQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1764 LILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTE-ATIDSSFYETSMGGEGTGDnvpiGSPLPNVHMYVLSQTDQIQPIG 1842
Cdd:cd05903 213 FVCGGATVPRSLARRAAELLG--AKVCSAYGSTEcPGAVTSITPAPEDRRLYTD----GRPLPGVEIKVVDDTGATLAPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1843 VAGELCIGGAGVAKGYHQKPDLTQMKFTknpfvsgERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLL 1922
Cdd:cd05903 287 VEGELLSRGPSVFLGYLDRPDLTADAAP-------EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLL 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 363747658 1923 QTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VNTNALRAALTKE-LPAYMIPAHLIPLENMPLTLNGKL 1989
Cdd:cd05903 360 GHPGVIEAAVVALPDERLGERACAVVVTKSgalLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1523-1994 |
1.90e-32 |
|
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: 132.99 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1523 EISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILL 1599
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNkgvRKGDR--VGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1600 LQQELkhlisnlpesemshiclddessyeenscnlnlspapEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYEL 1679
Cdd:cd05935 79 VGSEL------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1680 DRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCP---DETRLEPAEIYkimnsqRITVMESTPALIIPVMEYVYRNQF 1756
Cdd:cd05935 123 TPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMArwdRETALELIEKY------KVTFWTNIPTMLVDLLATPEFKTR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1757 KLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEAtidssFYETSMGGEGTGDNVPIGSPLPNVHMYVLSQTD 1836
Cdd:cd05935 197 DLSSLKVLTGGGAPMPPAVAEKLLKLTG--LRFVEGYGLTET-----MSQTHTNPPLRPKLQCLGIP*FGVDARVIDIET 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1837 QIQ-PIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKnpfVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETE 1915
Cdd:cd05935 270 GRElPPNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1916 EIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSDvntnALRAALTKE---------LPAYMIPAHLIPLENMPLTLN 1986
Cdd:cd05935 347 EVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP----EYRGKVTEEdiiewareqMAAYKYPREVEFVDELPRSAS 422
|
....*...
gi 363747658 1987 GKLDRNAL 1994
Cdd:cd05935 423 GKILWRLL 430
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1525-1994 |
2.02e-32 |
|
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: 134.68 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1525 SYRFLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQ 1602
Cdd:cd12119 27 TYAEVAERARRLANALRRL-GVKPgdRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1603 ELKHLISNL---PESEMSHICLDDESSYEENSCNLNLS----PAPEEPVY------------IIYTSGTTGAPKGVIVTY 1663
Cdd:cd12119 106 DFLPLLEAIaprLPTVEHVVVMTDDAAMPEPAGVGVLAyeelLAAESPEYdwpdfdentaaaICYTSGTTGNPKGVVYSH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1664 R-NFTHA-ALAWRQIYELDRKPVRLLqIASFsFDVFSGDLARTLTNGGTLIVCPDEtRLEPAEIYKIMNSQRITVMESTP 1741
Cdd:cd12119 186 RsLVLHAmAALLTDGLGLSESDVVLP-VVPM-FHVNAWGLPYAAAMVGAKLVLPGP-YLDPASLAELIEREGVTFAAGVP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1742 ALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFgqsMRIINSYGVTE----ATIDSSFYETSMGGEGTGDN 1817
Cdd:cd12119 263 TVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERG---VRVIHAWGMTEtsplGTVARPPSEHSNLSEDEQLA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1818 VPI--GSPLPNVHMYVLSQTDQIQPI-GVA-GELCIGGAGVAKGYHQKPDLTQmKFTKNPFvsgerlYRTGDRACWLPNG 1893
Cdd:cd12119 340 LRAkqGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESE-ALTEDGW------LRTGDVATIDEDG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1894 TIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAaYIVP---SDVNTNALRAALTKELPAY 1969
Cdd:cd12119 413 YLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAViGVPHPKWGERPLA-VVVLkegATVTAEELLEFLADKVAKW 491
|
490 500
....*....|....*....|....*
gi 363747658 1970 MIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd12119 492 WLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
459-947 |
2.53e-32 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 136.24 E-value: 2.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRF--SGG------SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLK 530
Cdd:PRK07529 26 STYELLSRAAARHPDAPALSFllDADpldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 531 AGGAYlPLDPAYPKERLSYMLKDSGASLLLT---QPGC-----------SAPNFSGeTLEVDM----------------- 579
Cdd:PRK07529 106 AGIAN-PINPLLEPEQIAELLRAAGAKVLVTlgpFPGTdiwqkvaevlaALPELRT-VVEVDLarylpgpkrlavplirr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 580 ----------TSLASEKAENHEF-TPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTS- 647
Cdd:PRK07529 184 kaharildfdAELARQPGDRLFSgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPl 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 648 FSFDASVWQLFWWSLSGASAYLLPP-GWEKDSAL-----IVQAiHQenVTTAHFIPAMLNSFLdQAEIERlSDRTSLKRV 721
Cdd:PRK07529 264 FHVNALLVTGLAPLARGAHVVLATPqGYRGPGVIanfwkIVER-YR--INFLSGVPTVYAALL-QVPVDG-HDISSLRYA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 722 FAGGEPLAPRTAARFASVLpQVSLIHGYGPTEATVDAAfyvLDPeRDRDRlRI-PIGKPVPG--ARLYVLDPHLAVQ--- 795
Cdd:PRK07529 339 LCGAAPLPVEVFRRFEAAT-GVRIVEGYGLTEATCVSS---VNP-PDGER-RIgSVGLRLPYqrVRVVILDDAGRYLrdc 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 796 PSGVAGELYIAGAGVARGYL----NRPALTEERFLedpfypgermyKTGDVARWLPDGNVEFLGRTDDQVkIR-GYRIEP 870
Cdd:PRK07529 413 AVDEVGVLCIAGPNVFSGYLeaahNKGLWLEDGWL-----------NTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 871 GEIEAALRSIEGVREAAVTVRTDSGEPEL-CAYVE---GLQRNE------VRAQL-ERLlpgyMVPAYMIEMEQWPVTPS 939
Cdd:PRK07529 481 AAIEEALLRHPAVALAAAVGRPDAHAGELpVAYVQlkpGASATEaellafARDHIaERA----AVPKHVRILDALPKTAV 556
|
....*...
gi 363747658 940 GKLDRNAL 947
Cdd:PRK07529 557 GKIFKPAL 564
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1508-1994 |
3.40e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 133.86 E-value: 3.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARI 1586
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGiGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1587 EYILRDSGADILLLQQELkhliSNLPESEMSHICLDDESSYEEN-------SCNLNLSPAPEEPVYIIYTSGTTGAPKGV 1659
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEF----DAIVALETPKIVIDAAAQADSRrlaqgglEIPPQAAVAPTDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1660 IVTYRNFthaalAWR---QIYELD-RKPVRLLQIASFsFDVFSGDLA--RTLTNGGTLIVcpdETRLEPAEIYKIMNSQR 1733
Cdd:PRK06145 168 MHSYGNL-----HWKsidHVIALGlTASERLLVVGPL-YHVGAFDLPgiAVLWVGGTLRI---HREFDPEAVLAAIERHR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1734 ITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGEG 1813
Cdd:PRK06145 239 LTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRA-RYIDAYGLTETCSGDTLMEAGREIEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1814 TGDNvpiGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlyRTGDRACWLPNG 1893
Cdd:PRK06145 318 IGST---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1894 TIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSDVNT---NALRAALTKELPAYM 1970
Cdd:PRK06145 388 FLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATltlEALDRHCRQRLASFK 467
|
490 500
....*....|....*....|....
gi 363747658 1971 IPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK06145 468 VPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
482-944 |
4.46e-32 |
|
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: 133.43 E-value: 4.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 482 GSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLT 561
Cdd:TIGR02262 29 SSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 562 QpGCSAPNFS-----------------GETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHR--Q 622
Cdd:TIGR02262 109 S-GALLPVIKaalgksphlehrvvvgrPEAGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSnpY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 623 AVSFLTGMQhQFPLSEDDIVMVKTSFSFDASVWQLFWWSLS-GASAYLLPPGWEKDSALIVQAIHQENVTTAhfIPAMLN 701
Cdd:TIGR02262 188 WTAELYARN-TLGIREDDVCFSAAKLFFAYGLGNALTFPMSvGATTVLMGERPTPDAVFDRLRRHQPTIFYG--VPTLYA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 702 SFLdQAEIERLSDRTSLKRVFAGGEPLAP----RTAARFAsvlpqVSLIHGYGPTEAtvdaaFYVLDPERDRDRLRIPIG 777
Cdd:TIGR02262 265 AML-ADPNLPSEDQVRLRLCTSAGEALPAevgqRWQARFG-----VDIVDGIGSTEM-----LHIFLSNLPGDVRYGTSG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 778 KPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLedpfypGErMYKTGDVARWLPDGNVEFLGRT 857
Cdd:TIGR02262 334 KPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQ------GE-WTRSGDKYVRNDDGSYTYAGRT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 858 DDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS-GEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEM 931
Cdd:TIGR02262 407 DDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEdGLIKPKAFVvlrpgQTALETELKEHVKDRLAPYKYPRWIVFV 486
|
490
....*....|...
gi 363747658 932 EQWPVTPSGKLDR 944
Cdd:TIGR02262 487 DDLPKTATGKIQR 499
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1504-1994 |
5.37e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 133.01 E-value: 5.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1504 FEAKAEeiPEHIAVID--NEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSH 1580
Cdd:PRK09088 3 FHARLQ--PQRLAAVDlaLGRRWTYAELDALVGRLAAVLRRRGcVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1581 YPKARIEYILRDSGADILllqqelkhlisnLPESEMSHICLDDES----SYEENSCNLNLSPA--PEEPVYIIYTSGTTG 1654
Cdd:PRK09088 81 LSASELDALLQDAEPRLL------------LGDDAVAAGRTDVEDlaafIASADALEPADTPSipPERVSLILFTSGTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1655 APKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDetrLEPAEIYKIMNSQRI 1734
Cdd:PRK09088 149 QPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNG---FEPKRTLGRLGDPAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1735 TVmesTPALIIPVMEYVYRNQfklPDLD--------ILILGSDMVKAQDFKTLTDrfgQSMRIINSYGVTEA------TI 1800
Cdd:PRK09088 226 GI---THYFCVPQMAQAFRAQ---PGFDaaalrhltALFTGGAPHAAEDILGWLD---DGIPMVDGFGMSEAgtvfgmSV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1801 DSSFYETSMGGEGTgdnvpigsPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTknpfvsGERL 1880
Cdd:PRK09088 297 DCDVIRAKAGAAGI--------PTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFT------GDGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1881 YRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKN-GQAGLAAyIVPSD---VNTN 1956
Cdd:PRK09088 363 FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwGEVGYLA-IVPADgapLDLE 441
|
490 500 510
....*....|....*....|....*....|....*...
gi 363747658 1957 ALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK09088 442 RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1523-1994 |
6.56e-32 |
|
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: 130.93 E-value: 6.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1523 EISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADill 1599
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAAlgvRKGDR--VALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1600 lqqelkhlisnlpesemshicLDDESSyeenscnlnlspapeepvyIIYTSGTTGAPKGVIVTYRNFTHAALAWRQ---I 1676
Cdd:cd05912 76 ---------------------LDDIAT-------------------IMYTSGTTGKPKGVQQTFGNHWWSAIGSALnlgL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1677 YELDR--KPVRLLQIASFSFdvfsgdLARTLTNGGTLIVCPdetRLEPAEIYKIMNSQRITVMESTPALIIPVMEyVYRN 1754
Cdd:cd05912 116 TEDDNwlCALPLFHISGLSI------LMRSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTMLQRLLE-ILGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1755 QFKlPDLDILILGSDMVKAQDFKTLTDRfgqSMRIINSYGVTE-----ATIDSSFYETSMGGegtgdnvpIGSPLPNVHm 1829
Cdd:cd05912 186 GYP-NNLRCILLGGGPAPKPLLEQCKEK---GIPVYQSYGMTEtcsqiVTLSPEDALNKIGS--------AGKPLFPVE- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1830 yvLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlyRTGDRACWLPNGTIRLLGRMDYQVKING 1909
Cdd:cd05912 253 --LKIEDDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1910 YRIETEEIESVLLQTGLVREAAVAVQHDKN-GQAGLAAYIVPSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGK 1988
Cdd:cd05912 324 ENIYPAEIEEVLLSHPAIKEAGVVGIPDDKwGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGK 403
|
....*.
gi 363747658 1989 LDRNAL 1994
Cdd:cd05912 404 LLRHEL 409
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
466-920 |
8.78e-32 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 133.49 E-value: 8.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 466 RQAAFTPERLAIRFSGG----------SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAY 535
Cdd:PRK09274 14 RAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 536 LPLDPAYPKERLSYMLKDSGASLLLTQP-------------GCSAPNFS-GETLEVDMTSLAS--EKAENHEFTPADGGS 599
Cdd:PRK09274 94 VLVDPGMGIKNLKQCLAEAQPDAFIGIPkahlarrlfgwgkPSVRRLVTvGGRLLWGGTTLATllRDGAAAPFPMADLAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 600 --LAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVktsfSFdaSVWQLFWWSLSGASayLLP------ 671
Cdd:PRK09274 174 ddMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLP----TF--PLFALFGPALGMTS--VIPdmdptr 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 672 PGwEKDSALIVQAIHQENVTtahfipamlNSFLDQAEIERLSDR--------TSLKRVFAGGEPLAPRTAARFASVLPQV 743
Cdd:PRK09274 246 PA-TVDPAKLFAAIERYGVT---------NLFGSPALLERLGRYgeangiklPSLRRVISAGAPVPIAVIERFRAMLPPD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 744 SLIH-GYGPTEA---TVDAAFYVLDPERDR-DRLR-IPIGKPVPGARLYVLD------PHLA---VQPSGVAGELYIAGA 808
Cdd:PRK09274 316 AEILtPYGATEAlpiSSIESREILFATRAAtDNGAgICVGRPVDGVEVRIIAisdapiPEWDdalRLATGEIGEIVVAGP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 809 GVARGYLNRPALTEERFLEDPfyPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGV-REAA 887
Cdd:PRK09274 396 MVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVkRSAL 473
|
490 500 510
....*....|....*....|....*....|....*
gi 363747658 888 VTVRTD-SGEPELCayVEGLQRNEV-RAQLERLLP 920
Cdd:PRK09274 474 VGVGVPgAQRPVLC--VELEPGVACsKSALYQELR 506
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1525-1994 |
1.77e-31 |
|
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: 130.31 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1525 SYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQE 1603
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGvGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1604 LkhlisnlpesemshiclddessYEENScnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKP 1683
Cdd:cd05969 82 L----------------------YERTD--------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1684 VRLLQ-----IASFSFDVFSgdlarTLTNGGTLIVcpDETRLEPAEIYKIMNSQRITVMESTPALIIPVMEY--VYRNQF 1756
Cdd:cd05969 132 IYWCTadpgwVTGTVYGIWA-----PWLNGVTNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgdELARKY 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1757 KLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTE-ATIDSSFYETSMGGEGTgdnvpIGSPLPNVHMYVLSQT 1835
Cdd:cd05969 205 DLSSLRFIHSVGEPLNPEAIRWGMEVFG--VPIHDTWWQTEtGSIMIANYPCMPIKPGS-----MGKPLPGVKAAVVDEN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1836 DQIQPIGVAGELCI--GGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWlpngtirLLGRMDYQVKINGYRIE 1913
Cdd:cd05969 278 GNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFW-------FVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1914 TEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV------PSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNG 1987
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlkegfePSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSG 430
|
....*..
gi 363747658 1988 KLDRNAL 1994
Cdd:cd05969 431 KIMRRVL 437
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1521-1994 |
2.13e-31 |
|
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: 132.02 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1521 EIEISYRFLNERANRLARTLQNRKGPKPTVAVLA-KRSIDAIVGVLAVMKAGGVYIP--IDSHYP-----KARIEYILRD 1592
Cdd:cd05906 37 EEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQfDDNEDFIPAFWACVLAGFVPAPltVPPTYDepnarLRKLRHIWQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1593 SGADILLLQQELKHLIsnLPESEMSHICLDDESSYEENSCNLNLSPA----PEEPVYIIYTSGTTGAPKGVIVTYRNFTH 1668
Cdd:cd05906 117 LGSPVVLTDAELVAEF--AGLETLSGLPGIRVLSIEELLDTAADHDLpqsrPDDLALLMLTSGSTGFPKAVPLTHRNILA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1669 AALAWRQIYELDRKPVRLLQIAsfsFD-----VFSGDLARTLtnGGTLIVCPDETRL-EPAEIYKIMNSQRITVMEStP- 1741
Cdd:cd05906 195 RSAGKIQHNGLTPQDVFLNWVP---LDhvgglVELHLRAVYL--GCQQVHVPTEEILaDPLRWLDLIDRYRVTITWA-Pn 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1742 ---ALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQ---DFKTLTDRFG-QSMRIINSYGVTE----ATIDSSFYETSMG 1810
Cdd:cd05906 269 fafALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKtirRLLRLLEPYGlPPDAIRPAFGMTEtcsgVIYSRSFPTYDHS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1811 GEGTgdNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRAcWL 1890
Cdd:cd05906 349 QALE--FVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1891 PNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVRE---AAVAVQHDKNGQAGLAAYIVPSDVNTNAL-------RA 1960
Cdd:cd05906 420 DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAETEELAIFFVPEYDLQDALsetlraiRS 499
|
490 500 510
....*....|....*....|....*....|....*..
gi 363747658 1961 ALTKEL---PAYMIPahlIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05906 500 VVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
480-950 |
3.06e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 130.97 E-value: 3.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 480 SGG-SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASL 558
Cdd:PRK12406 7 SGDrRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 559 LLTQPGCSAPNFSGETLEVDMTSLAS--EKAENH---------------------EFTPADGGSL---AYVIYTSGSTGQ 612
Cdd:PRK12406 87 LIAHADLLHGLASALPAGVTVLSVPTppEIAAAYrispalltppagaidwegwlaQQEPYDGPPVpqpQSMIYTSGTTGH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 613 PKGV---AVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDA-SVWQLFWWSLSGAsaYLLPPGWEKDSALivQAIHQE 688
Cdd:PRK12406 167 PKGVrraAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSApNAYGLRAGRLGGV--LVLQPRFDPEELL--QLIERH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 689 NVTTAHFIPAMLNSFLD-QAEIERLSDRTSLKRVFAGGEPlAPRTAARfasvlpqvSLIHGYGP--------TEATVdAA 759
Cdd:PRK12406 243 RITHMHMVPTMFIRLLKlPEEVRAKYDVSSLRHVIHAAAP-CPADVKR--------AMIEWWGPviyeyygsTESGA-VT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 760 FYvlDPErdrDRLRIP--IGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVAR-GYLNRPaltEERFLEDPfypgERM 836
Cdd:PRK12406 313 FA--TSE---DALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKP---EKRAEIDR----GGF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 837 YKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYVE-----GLQRN 909
Cdd:PRK12406 381 ITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAefGE-ALMAVVEpqpgaTLDEA 459
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 363747658 910 EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAP 950
Cdd:PRK12406 460 DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
459-949 |
4.49e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 131.20 E-value: 4.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL 538
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAYPKERLSYMLKDSGASLLL-----------------------TQPGCSAPNFSG-ETLEVDMTSLASEKAEnhefTP 594
Cdd:PRK07788 130 NTGFSGPQLAEVAAREGVKALVyddeftdllsalppdlgrlrawgGNPDDDEPSGSTdETLDDLIAGSSTAPLP----KP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 595 ADGGSLayVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDiVMVKTSFSFDAsvWQLFWWSLSGA--SAYLLPp 672
Cdd:PRK07788 206 PKPGGI--VILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGE-TTLLPAPMFHA--TGWAHLTLAMAlgSTVVLR- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 673 gwEK-DSALIVQAIHQENVTTAHFIPAMLNSFLDQ-AEIERLSDRTSLKRVFAGGEPLAP----RTAARFASVLPQVsli 746
Cdd:PRK07788 280 --RRfDPEATLEDIAKHKATALVVVPVMLSRILDLgPEVLAKYDTSSLKIIFVSGSALSPelatRALEAFGPVLYNL--- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 747 hgYGPTEATVDAafyVLDPErdrDRLRIP--IGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLN-RPALTEE 823
Cdd:PRK07788 355 --YGSTEVAFAT---IATPE---DLAEAPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDgRDKQIID 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 824 RFLEdpfypgermykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAY 902
Cdd:PRK07788 427 GLLS-----------SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIgVDDEEFGQRLRAF 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 903 V---EGLQRNE------VRAQLERllpgYMVPAYMIEMEQWPVTPSGKLDRNALPA 949
Cdd:PRK07788 496 VvkaPGAALDEdaikdyVRDNLAR----YKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1506-1952 |
1.05e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 128.57 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1506 AKAEEIPEhiAVIDNEIEISYRFLNERANRLARtlqnRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKAR 1585
Cdd:PRK07787 10 AAAADIAD--AVRIGGRVLSRSDLAGAATAVAE----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1586 IEYILRDSGADILLlqqelkhliSNLPES--EMSHICLDDE----SSYEEnscnlnlsPAPEEPVYIIYTSGTTGAPKGV 1659
Cdd:PRK07787 84 RRHILADSGAQAWL---------GPAPDDpaGLPHVPVRLHarswHRYPE--------PDPDAPALIVYTSGTTGPPKGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1660 IVTYR----NFTHAALAWRQIYElD----------------------RKPVRLLQIASFSFDVFsgdlARTLTNGGTLI- 1712
Cdd:PRK07787 147 VLSRRaiaaDLDALAEAWQWTAD-DvlvhglplfhvhglvlgvlgplRIGNRFVHTGRPTPEAY----AQALSEGGTLYf 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1713 --------VCPDEtrlepaEIYKIMNSQRITVMESTPaliipvmeyvyrnqfkLPdldililgsdmvkAQDFKTLTDRFG 1784
Cdd:PRK07787 222 gvptvwsrIAADP------EAARALRGARLLVSGSAA----------------LP-------------VPVFDRLAALTG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1785 QsmRIINSYGVTEATIDSSfyeTSMGGE---GTgdnvpIGSPLPNVHMYVLSQTDQIQPIGVA--GELCIGGAGVAKGYH 1859
Cdd:PRK07787 267 H--RPVERYGMTETLITLS---TRADGErrpGW-----VGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1860 QKPDLTQMKFTKNPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQ-VKINGYRIETEEIESVLLQTGLVREAAV-AVQHD 1937
Cdd:PRK07787 337 NRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIETALLGHPGVREAAVvGVPDD 410
|
490
....*....|....*
gi 363747658 1938 KNGQAgLAAYIVPSD 1952
Cdd:PRK07787 411 DLGQR-IVAYVVGAD 424
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1492-1994 |
1.22e-30 |
|
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: 129.50 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1492 EFAQK--------DVPFHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAI 1561
Cdd:COG1021 11 EFAARyreagywrGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL-GLRPgdRVVVQLPNVAEFV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1562 VGVLAVMKAGGvyIPID---SHYpKARIEYILRDSGADILL----------------LQQELKHLisnlpesemSHICLD 1622
Cdd:COG1021 90 IVFFALFRAGA--IPVFalpAHR-RAEISHFAEQSEAVAYIipdrhrgfdyralareLQAEVPSL---------RHVLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1623 DESS--------YEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQI-ASFS 1693
Cdd:COG1021 158 GDAGeftsldalLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALpAAHN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1694 FDVFS-GDLArTLTNGGTLIVCPDetrLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVK 1772
Cdd:COG1021 238 FPLSSpGVLG-VLYAGGTVVLAPD---PSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1773 AQDFKTLTDRFGqsMRIINSYGVTEATI------DSSfyETSMGGEGTgdnvPIgSPLPNVHmyVLSQTDQIQPIGVAGE 1846
Cdd:COG1021 314 PELARRVRPALG--CTLQQVFGMAEGLVnytrldDPE--EVILTTQGR----PI-SPDDEVR--IVDEDGNPVPPGEVGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1847 LCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACWLPNGTIRLLGRmdyqVK--IN--GYRIETEEIESVLL 1922
Cdd:COG1021 383 LLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGR----AKdqINrgGEKIAAEEVENLLL 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 1923 QTGLVREAA-VAVQHDKNGQAgLAAYIVPSD--VNTNALRAAL-TKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:COG1021 453 AHPAVHDAAvVAMPDEYLGER-SCAFVVPRGepLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1640-1994 |
1.72e-30 |
|
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: 125.47 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 PEEPVYIIYTSGTTGAPKGVIVTYRN------FTHAALAWRqiyELDRK--PVRLLQIasfsFDVFSGDLArTLTNGGTl 1711
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNivnngyFIGERLGLT---EQDRLciPVPLFHC----FGSVLGVLA-CLTHGAT- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1712 IVCPDETrLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKtltdrfgqsmRIIN 1791
Cdd:cd05917 72 MVFPSPS-FDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMK----------RVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1792 SYGVTEATIDSSFYETSMGGEGTGDNVPI-------GSPLPNVHMYVLSQTDQIQP-IGVAGELCIGGAGVAKGYHQKPD 1863
Cdd:cd05917 141 VMNMKDVTIAYGMTETSPVSTQTRTDDSIekrvntvGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1864 LTqmkftkNPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA-VQHDKNGQA 1942
Cdd:cd05917 221 KT------AEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVgVPDERYGEE 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 1943 gLAAYIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05917 295 -VCAWIRLKEgaeLTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
451-947 |
2.25e-30 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 128.85 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 451 EAVSPKAFTLHGLF---ERQAAFTPERLAIRFSGG--SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAV 525
Cdd:PRK05852 6 GAAPMASDFGPRIAdlvEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 526 LAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLL---TQPGCSAP----------------NFSGETLEVDMTSlaseK 586
Cdd:PRK05852 86 LAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLidaDGPHDRAEpttrwwpltvnvggdsGPSGGTLSVHLDA----A 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 587 AENHEFTPADGG---SLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLS 663
Cdd:PRK05852 162 TEPTPATSTPEGlrpDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 664 GASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERL-SDRTSLKRVFAGGEPLAPRTAA----RFAS 738
Cdd:PRK05852 242 SGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSgRKPAALRFIRSCSAPLTAETAQalqtEFAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 739 vlpqvSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPIGkPVP---GARLYVLDPHLAVQPSGVAGELYIAGAGVARGYL 815
Cdd:PRK05852 322 -----PVVCAFGMTEATHQVTTTQIEGIGQTENPVVSTG-LVGrstGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 816 NRPALTEERFLEDPFypgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS- 894
Cdd:PRK05852 396 GDPTITAANFTDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQl 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 895 -GEPELCAYVE----GLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK05852 469 yGEAVAAVIVPresaPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
602-943 |
4.10e-30 |
|
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: 124.42 E-value: 4.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 602 YVIYTSGSTGQPKGVAVEHRQA-VSFLTGMQHQFP--LSEDDIVMVKTS-----------FSFDASVWQLFWWSLSGASA 667
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIfRMLMGGADFGTGefTPSEDAHKAAAAaagtvmfpappLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 668 YLlpPGWEKDSALIVQAIHQENVTTAHFI-PAMLNSFLDQAEIERLSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLI 746
Cdd:cd05924 87 VL--PDDRFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 747 HGYGPTEATVDAAFYVldperdrdRLRIPIGKP--VPGARLYVLDPHLAVQPSGVAGELYIAGAG-VARGYLNRPALTEE 823
Cdd:cd05924 165 DAFGSSETGFTGSGHS--------AGSGPETGPftRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 824 RFLEdpfYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCA 901
Cdd:cd05924 237 TFPE---VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDErwGQ-EVVA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 363747658 902 YVE-----GLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLD 943
Cdd:cd05924 313 VVQlregaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
461-949 |
5.27e-30 |
|
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: 128.76 E-value: 5.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 461 HGLFERQAAFTPERLAIRFSG-----GSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAY 535
Cdd:cd05968 64 EQLLDKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 536 LPLDPAYPKERLSYMLKDSGASLLLTQPGcsapnFSGETLEVDMTSLASEKAEN--------------HEFTPADGGSLA 601
Cdd:cd05968 144 VPIFSGFGKEAAATRLQDAEAKALITADG-----FTRRGREVNLKEEADKACAQcptvekvvvvrhlgNDFTPAKGRDLS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 602 Y---------------------VIYTSGSTGQPKGVAveHRQAVSFLTG---MQHQFPLSEDDIVMVKTSFSFDASVWQL 657
Cdd:cd05968 219 YdeeketagdgaertesedplmIIYTSGTTGKPKGTV--HVHAGFPLKAaqdMYFQFDLKPGDLLTWFTDLGWMMGPWLI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 658 FWWSLSGASAYLLP--PGWEKDSALiVQAIHQENVTTAHFIPAMLNSFLDQAEIE-RLSDRTSLkRVFAG-GEPLAPRTA 733
Cdd:cd05968 297 FGGLILGATMVLYDgaPDHPKADRL-WRMVEDHEITHLGLSPTLIRALKPRGDAPvNAHDLSSL-RVLGStGEPWNPEPW 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 734 ARFASVL--PQVSLIHGYGPTEATVDA-AFYVLDPERdrdrlriPIG--KPVPGARLYVLDPHlaVQP-SGVAGELYIAG 807
Cdd:cd05968 375 NWLFETVgkGRNPIINYSGGTEISGGIlGNVLIKPIK-------PSSfnGPVPGMKADVLDES--GKPaRPEVGELVLLA 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 808 A--GVARGYLNrpalTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVRE 885
Cdd:cd05968 446 PwpGMTRGFWR----DEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 886 -AAVTVRTD-SGEPELCAYV--------EGLqRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPA 949
Cdd:cd05968 522 sAAIGVPHPvKGEAIVCFVVlkpgvtptEAL-AEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
466-947 |
5.64e-30 |
|
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: 126.05 E-value: 5.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 466 RQAAFTPERlairfsggSLTYAELDMYASRLA-AHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPK 544
Cdd:cd05958 1 RTCLRSPER--------EWTYRDLLALANRIAnVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 545 ERLSYMLKDSGASLLLtqpgCSapnfsgetlevdmtslasekaenHEFTPADG-GSLAYviyTSGSTGQPKGVAVEHRQA 623
Cdd:cd05958 73 KELAYILDKARITVAL----CA-----------------------HALTASDDiCILAF---TSGTTGAPKATMHFHRDP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 624 V-SFLTGMQHQFPLSEDD--IVMVKTSFSFDASVWQLFWWSLsGASAYLLPpgwEKDSALIVQAIHQENVTTAHFIPAML 700
Cdd:cd05958 123 LaSADRYAVNVLRLREDDrfVGSPPLAFTFGLGGVLLFPFGV-GASGVLLE---EATPDLLLSAIARYKPTVLFTAPTAY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 701 NSFLDQAEiERLSDRTSLKRVFAGGEPLAPRTAARFASVLpQVSLIHGYGPTEAtvdaaFYVLDPERDRDRLRIPIGKPV 780
Cdd:cd05958 199 RAMLAHPD-AAGPDLSSLRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGSTEM-----FHIFISARPGDARPGATGKPV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 781 PGARLYVLDPHLAVQPSGVAGELYIAGAGVARGylnrpaLTEERflEDPFYPGERMYkTGDVARWLPDGNVEFLGRTDDQ 860
Cdd:cd05958 272 PGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRY------LADKR--QRTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 861 VKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV---------EGLQRnEVRAQLERLLPGYMVPAYMIE 930
Cdd:cd05958 343 IVSGGYNIAPPEVEDVLLQHPAVAECAVVgHPDESRGVVVKAFVvlrpgvipgPVLAR-ELQDHAKAHIAPYKYPRAIEF 421
|
490
....*....|....*..
gi 363747658 931 MEQWPVTPSGKLDRNAL 947
Cdd:cd05958 422 VTELPRTATGKLQRFAL 438
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1500-1994 |
6.09e-30 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 126.91 E-value: 6.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1500 FHRIFEAKAEeiPEHIAV-IDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPI 1577
Cdd:PRK07514 6 FDALRAAFAD--RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGvKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1578 DSHYPKARIEYILRDSGADILLLQQELKHLISNLPESE-MSHI-CLDDESSYEENSCNLNLSP-------APEEPVYIIY 1648
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAgAPHVeTLDADGTGSLLEAAAAAPDdfetvprGADDLAAILY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1649 TSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRL----------LQIASFSfdvfsgdlarTLTNGGTLIVCPdet 1718
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIhalpifhthgLFVATNV----------ALLAGASMIFLP--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1719 RLEPAEIYKIMnsQRITVMESTPALiipvmeyvYRNQFKLPDLD--------ILILGSDMVKAQDFKTLTDRFGQsmRII 1790
Cdd:PRK07514 231 KFDPDAVLALM--PRATVMMGVPTF--------YTRLLQEPRLTreaaahmrLFISGSAPLLAETHREFQERTGH--AIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1791 NSYGVTEATIDSSF-YEtsmggegtGDNVP--IGSPLPNVHMYVL-SQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQ 1866
Cdd:PRK07514 299 ERYGMTETNMNTSNpYD--------GERRAgtVGFPLPGVSLRVTdPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1867 MKFTKNPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLA 1945
Cdd:PRK07514 371 EEFRADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAViGVPHPDFGEGVTA 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 363747658 1946 AyIVPS---DVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK07514 445 V-VVPKpgaALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
8-425 |
6.54e-30 |
|
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: 125.45 E-value: 6.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 8 LTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIR----------FQL-LEGEELEPRLHLT 76
Cdd:cd19538 4 LSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRtvfpeedgvpYQLiLEEDEATPKLEIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 77 EykyyplriidfsnVEMIEIEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQ 156
Cdd:cd19538 84 E-------------VDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 157 KMKKKD-----PLPDQpepsYLSYIEKESQYLQS-----PRFAKDRLFWTQTFEHpleyhsLADQTSLQ-------KQST 219
Cdd:cd19538 151 ARCKGEapelaPLPVQ----YADYALWQQELLGDesdpdSLIARQLAYWKKQLAG------LPDEIELPtdyprpaESSY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 220 SASRDTIILSPDLEQTIRIFCEEHKiniISLFM---ASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIR 296
Cdd:cd19538 221 EGGTLTFEIDSELHQQLLQLAKDNN---VTLFMvlqAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 297 ITVDPDTDFLSFVRTIGREQLSVMRHQRFPYNLLVNEL---RNEQKdlHNL--IGISMQYQPLQWHNADDFDYETALYFS 371
Cdd:cd19538 298 TDTSGNPSFRELLERVKETNLEAYEHQDIPFERLVEALnptRSRSR--HPLfqIMLALQNTPQPSLDLPGLEAKLELRTV 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 372 GYTANELSVQIQERIDNGT---IQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHP 425
Cdd:cd19538 376 GSAKFDLTFELREQYNDGTpngIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1512-1994 |
6.75e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 127.02 E-value: 6.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIdshYPKARIE--- 1587
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGlGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL---HPLGSLDdha 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1588 YILRDSGADILLLQQ---------------ELKHLISNLPESEMSHIcLDDESSYEENScnlnLSPA--PEEPVYIIYTS 1650
Cdd:PRK06188 103 YVLEDAGISTLIVDPapfveralallarvpSLKHVLTLGPVPDGVDL-LAAAAKFGPAP----LVAAalPPDIAGLAYTG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1651 GTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPvRLLQIASFSFDvfSGDL-ARTLTNGGTLIVCPdetRLEPAEIYKIM 1729
Cdd:PRK06188 178 GTTGKPKGVMGTHRSIATMAQIQLAEWEWPADP-RFLMCTPLSHA--GGAFfLPTLLRGGTVIVLA---KFDPAEVLRAI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1730 NSQRITVmestpALIIPVMEYVYRNQFKLPD-----LDILILGSDMVKAQDFKTLTDRFGQSMriINSYGVTEATIDSSF 1804
Cdd:PRK06188 252 EEQRITA-----TFLVPTMIYALLDHPDLRTrdlssLETVYYGASPMSPVRLAEAIERFGPIF--AQYYGQTEAPMVITY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1805 YetsmggeGTGDNVPI--------GSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFtKNPFVs 1876
Cdd:PRK06188 325 L-------RKRDHDPDdpkrltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWL- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1877 gerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---SD 1952
Cdd:PRK06188 396 -----HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAViGVPDEKWGEA-VTAVVVLrpgAA 469
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 363747658 1953 VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK06188 470 VDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
480-947 |
8.60e-30 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 127.27 E-value: 8.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 480 SGGSLTYAELDMYASRLAAHLAAR-GITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASL 558
Cdd:PLN02574 63 TGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 559 LLTQPG--CSAPNFSGETLEV----DMTSLASEKAENHEFTPADGGSL----------AYVIYTSGSTGQPKGVAVEHRQ 622
Cdd:PLN02574 143 AFTSPEnvEKLSPLGVPVIGVpenyDFDSKRIEFPKFYELIKEDFDFVpkpvikqddvAAIMYSSGTTGASKGVVLTHRN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 623 AVSFLT------GMQHQFPLSEDDIVMVKTSFS-FDASVWQLFWWSLsGASAYLLPpgwEKDSALIVQAIHQENVTtaHF 695
Cdd:PLN02574 223 LIAMVElfvrfeASQYEYPGSDNVYLAALPMFHiYGLSLFVVGLLSL-GSTIVVMR---RFDASDMVKVIDRFKVT--HF 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 696 --IPAMLNSFLDQAEIERLSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATvdaAFYVLDPERDRDRLR 773
Cdd:PLN02574 297 pvVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTEST---AVGTRGFNTEKLSKY 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 774 IPIGKPVPGARLYVLD-PHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVE 852
Cdd:PLN02574 374 SSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW------LRTGDIAYFDEDGYLY 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 853 FLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPEL-CAYV-----EGLQRNEVRAQLERLLPGYMVPA 926
Cdd:PLN02574 448 IVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIpVAFVvrrqgSTLSQEAVINYVAKQVAPYKKVR 527
|
490 500
....*....|....*....|.
gi 363747658 927 YMIEMEQWPVTPSGKLDRNAL 947
Cdd:PLN02574 528 KVVFVQSIPKSPAGKILRREL 548
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1512-1994 |
9.58e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 125.85 E-value: 9.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNRKGPK-PTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYIL 1590
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKgDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1591 RDSGADILLLQQELKH--------LISNLPESEMSHICLDDESSYEENSCnlnlspapeepvyIIYTSGTTGAPKGVIVT 1662
Cdd:PRK03640 96 DDAEVKCLITDDDFEAklipgisvKFAELMNGPKEEAEIQEEFDLDEVAT-------------IMYTSGTTGKPKGVIQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1663 YRNFTHAALAWRQ---IYELDR--KPVRLLQIASFSFdvfsgdLARTLTNGGTLIVcpdETRLEPAEIYKIMNSQRITVM 1737
Cdd:PRK03640 163 YGNHWWSAVGSALnlgLTEDDCwlAAVPIFHISGLSI------LMRSVIYGMRVVL---VEKFDAEKINKLLQTGGVTII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1738 ESTPA----LIIPVMEYVYRNQFKLpdldILILGSDMVKAqdfkTLTDRFGQSMRIINSYGVTE-----ATIDSSFYETS 1808
Cdd:PRK03640 234 SVVSTmlqrLLERLGEGTYPSSFRC----MLLGGGPAPKP----LLEQCKEKGIPVYQSYGMTEtasqiVTLSPEDALTK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1809 MGGegtgdnvpIGSPLPNVHMYVLSQTDQIQPiGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlyRTGDRAC 1888
Cdd:PRK03640 306 LGS--------AGKPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1889 WLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA-VQHDKNGQAGLAAYIVPSDVNTNALRAALTKELP 1967
Cdd:PRK03640 370 LDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVgVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLA 449
|
490 500
....*....|....*....|....*..
gi 363747658 1968 AYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK03640 450 KYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
485-944 |
3.57e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 125.11 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 485 TYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDS-------GAS 557
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTlrvigmiGAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 558 L-LLTQP-GCSAPNFSGETLEVDMTS--LASEKAENHEFTPADggsLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQ 633
Cdd:PRK07768 111 AvVVGEPfLAAAPVLEEKGIRVLTVAdlLAADPIDPVETGEDD---LALMQLTSGSTGSPKAVQITHGNLYANAEAMFVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 634 FPLSEDDIVMVKtsfsfdasvwqlfWWSLS---GASAYLLPP---GWE----------KDSALIVQAI--HQENVTTA-H 694
Cdd:PRK07768 188 AEFDVETDVMVS-------------WLPLFhdmGMVGFLTVPmyfGAElvkvtpmdflRDPLLWAELIskYRGTMTAApN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 695 FIPAMLNSFLDQAEIERLSDRTSLKRVFAGGEPLAPRTAARFASV-----LPQVSLIHGYGPTEATVDAAF------YVL 763
Cdd:PRK07768 255 FAYALLARRLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAgarfgLRPEAILPAYGMAEATLAVSFspcgagLVV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 764 DpERDRDRL----------------RIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYlnrpaLTEERFLE 827
Cdd:PRK07768 335 D-EVDADLLaalrravpatkgntrrLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 828 --DPfypgERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREA-AVTVRTDSG--------- 895
Cdd:PRK07768 409 aqDA----DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGnAVAVRLDAGhsregfava 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 896 -------EPELCAYVEGLQRNEVRAQLE------RLLPGYMVPAymiemeqwpvTPSGKLDR 944
Cdd:PRK07768 485 vesnafeDPAEVRRIRHQVAHEVVAEVGvrprnvVVLGPGSIPK----------TPSGKLRR 536
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
599-944 |
9.58e-29 |
|
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: 119.43 E-value: 9.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 599 SLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLL----PPGW 674
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQrkfnPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 675 ekdsaliVQAIHQENVTTAHFIPAMLNSFLDQAEIErlsdrTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEA 754
Cdd:cd17633 81 -------IRKINQYNATVIYLVPTMLQALARTLEPE-----SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 755 T-VDAAFYvldperDRDRLRIPIGKPVPGARLYVLDphlavQPSGVAGELYIAGAGVARGYLNRPALTEERFledpfypg 833
Cdd:cd17633 149 SfITYNFN------QESRPPNSVGRPFPNVEIEIRN-----ADGGEIGKIFVKSEMVFSGYVRGGFSNPDGW-------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 834 ermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYV---EGLQRNE 910
Cdd:cd17633 210 ---MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALysgDKLTYKQ 286
|
330 340 350
....*....|....*....|....*....|....
gi 363747658 911 VRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 944
Cdd:cd17633 287 LKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
605-947 |
1.25e-28 |
|
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: 119.69 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 605 YTSGSTGQPKGVAVEHRQAV--SFLTGMQHQFplSEDDIVMVKTSF--SFDASVWQLFwwSLSGASAYLLP-PGWekDSA 679
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVnnGYFIGERLGL--TEQDRLCIPVPLfhCFGSVLGVLA--CLTHGATMVFPsPSF--DPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 680 LIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAA 759
Cdd:cd05917 83 AVLEAIEKEKCTALHGVPTMFIAELEHPDFDKF-DLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 760 FYVLDPERDRdRLRIpIGKPVPGARLYVLDPHLAVQPS-GVAGELYIAGAGVARGYLNRPALTEERFLEDpfypgeRMYK 838
Cdd:cd05917 162 QTRTDDSIEK-RVNT-VGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD------GWLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 839 TGDVARWLPDGNVEFLGRTDDQVkIRG-YRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EG--LQRNE 910
Cdd:cd05917 234 TGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDEryGE-EVCAWIrlkEGaeLTEED 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 363747658 911 VRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05917 312 IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
479-942 |
4.02e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 121.55 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 479 FSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASL 558
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 559 LLTQPGCSA-------------PNFSGETLEVD-MTSLASEKAENHEFTPAD---GGSLAyviYTSGSTGQPKGV--AVE 619
Cdd:PRK08276 87 LIVSAALADtaaelaaelpagvPLLLVVAGPVPgFRSYEEALAAQPDTPIADetaGADML---YSSGTTGRPKGIkrPLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 620 HRQ----AVSFLTGMQHQFPLSEDDIVMVkTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALivQAIHQENVTTAHF 695
Cdd:PRK08276 164 GLDpdeaPGMMLALLGFGMYGGPDSVYLS-PAPLYHTAPLRFGMSALALGGTVVVMEKFDAEEAL--ALIERYRVTHSQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 696 IPAMLNSFLDQAEIERLS-DRTSLKRVFAGGEPLAPRTAARfasvlpqvsLIHGYGP--------TEAtvdAAFYVLDPE 766
Cdd:PRK08276 241 VPTMFVRMLKLPEEVRARyDVSSLRVAIHAAAPCPVEVKRA---------MIDWWGPiiheyyasSEG---GGVTVITSE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 767 rdrDRLRIP--IGKPVPGaRLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERfledpfYPGERMYKTGDVAr 844
Cdd:PRK08276 309 ---DWLAHPgsVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAA------RNPHGWVTVGDVG- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 845 WL-PDGnveFLGRTD---DQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYVEGLQ--------RNE 910
Cdd:PRK08276 378 YLdEDG---YLYLTDrksDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEemGE-RVKAVVQPADgadagdalAAE 453
|
490 500 510
....*....|....*....|....*....|..
gi 363747658 911 VRAQLERLLPGYMVPAYMIEMEQWPVTPSGKL 942
Cdd:PRK08276 454 LIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1502-1950 |
6.67e-28 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 122.13 E-value: 6.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1502 RIFEAKAEEIPEHIAVIDNE----IEISYRFLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYI 1575
Cdd:COG1022 15 DLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLAL-GVKPgdRVAILSDNRPEWVIADLAILAAGAVTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1576 PIDSHYPKARIEYILRDSGADILLLQQE-----LKHLISNLPESEmsHICLDDESSYEENSCNLNL-------------- 1636
Cdd:COG1022 94 PIYPTSSAEEVAYILNDSGAKVLFVEDQeqldkLLEVRDELPSLR--HIVVLDPRGLRDDPRLLSLdellalgrevadpa 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1637 -------SPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLL-----QIASFSFDVFSgdlart 1704
Cdd:COG1022 172 elearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSflplaHVFERTVSYYA------ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1705 LTNGGTLIVCPDETRLEPA-------------EIY-KIMNSQRITVMESTP----------ALIIPVMEYVYRNQ----- 1755
Cdd:COG1022 246 LAAGATVAFAESPDTLAEDlrevkptfmlavpRVWeKVYAGIQAKAEEAGGlkrklfrwalAVGRRYARARLAGKspsll 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1756 --FKLPDLDILIlgsdmvkaqdFKTLTDRFGQSMRIINS-----------------------YGVTEATIDSSFYEtsmg 1810
Cdd:COG1022 326 lrLKHALADKLV----------FSKLREALGGRLRFAVSggaalgpelarffralgipvlegYGLTETSPVITVNR---- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1811 gegTGDNVP--IGSPLPNVhmyvlsqtdQIQpIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRAC 1888
Cdd:COG1022 392 ---PGDNRIgtVGPPLPGV---------EVK-IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGE 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 1889 WLPNGTIRLLGRMdyqvK--I---NGYRIETEEIESVLLQTGLVREAAVaVQHDKNgqaGLAAYIVP 1950
Cdd:COG1022 453 LDEDGFLRITGRK----KdlIvtsGGKNVAPQPIENALKASPLIEQAVV-VGDGRP---FLAALIVP 511
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
468-947 |
8.67e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 120.27 E-value: 8.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 468 AAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLsERSPEMLIAVLAVLKAGGAYLPLDPAYPKERL 547
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAILL-ENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 548 SYMLKDSGASLLLTQPGCSAPnFSGETLEVDMTSLASEKAENHEFTPADGGSLA----YVIYTSGSTGQPKGVAVEHRQA 623
Cdd:PRK07638 90 KERLAISNADMIVTERYKLND-LPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQnapfYMGFTSGSTGKPKAFLRAQQSW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 624 VSFLTGMQHQFPLSEDDIVMVKTS-----FSFDAsVWQLFWwslsGASAYLLP---PGWEKDsalivqAIHQENVTTAHF 695
Cdd:PRK07638 169 LHSFDCNVHDFHMKREDSVLIAGTlvhslFLYGA-ISTLYV----GQTVHLMRkfiPNQVLD------KLETENISVMYT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 696 IPAMLNSFLdqaEIERLSDrTSLKRVFAGGEPLAPrTAARFASVLPQVSLIHGYGPTEATVDAAfyvLDPErdrDRLRIP 775
Cdd:PRK07638 238 VPTMLESLY---KENRVIE-NKMKIISSGAKWEAE-AKEKIKNIFPYAKLYEFYGASELSFVTA---LVDE---ESERRP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 776 --IGKPVPGARLYVLD-PHLAVQPsGVAGELYIAGAGVARGYLNRPALTEErfledpfyPGERMYKT-GDVARWLPDGNV 851
Cdd:PRK07638 307 nsVGRPFHNVQVRICNeAGEEVQK-GEIGTVYVKSPQFFMGYIIGGVLARE--------LNADGWMTvRDVGYEDEEGFI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 852 EFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GE-PElcAYVEGLQ-RNEVRAQLERLLPGYMVPAY 927
Cdd:PRK07638 378 YIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSywGEkPV--AIIKGSAtKQQLKSFCLQRLSSFKIPKE 455
|
490 500
....*....|....*....|
gi 363747658 928 MIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK07638 456 WHFVDEIPYTNSGKIARMEA 475
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1642-1994 |
1.07e-27 |
|
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: 116.28 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1642 EPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLL-----QIASFSFdvfsgdLARTLTNGGTLIVC-- 1714
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLslplyHVGGLAI------LVRSLLAGAELVLLer 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1715 ------------PDETRLEPAEIYKIMNSQritvmESTPALiipvmeyvyrnqfklPDLDILILGSDMVKAQDFKTLTDR 1782
Cdd:cd17630 75 nqalaedlappgVTHVSLVPTQLQRLLDSG-----QGPAAL---------------KSLRAVLLGGAPIPPELLERAADR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1783 fgqSMRIINSYGVTEATidSSFYETSMGGEGTGDNvpiGSPLPNVhmyvlsqtdQIQpIGVAGELCIGGAGVAKGYhQKP 1862
Cdd:cd17630 135 ---GIPLYTTYGMTETA--SQVATKRPDGFGRGGV---GVLLPGR---------ELR-IVEDGEIWVGGASLAMGY-LRG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1863 DLTqmkftknPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQ 1941
Cdd:cd17630 196 QLV-------PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVvGVPDEELGQ 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 363747658 1942 AGLAAYIVPSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd17630 269 RPVAVIVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
460-947 |
1.70e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 120.14 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 460 LHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLD 539
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 540 PAYPKERLSYMLKDSGASLLLTQ----PGCSAPNFSGETLEVDMTSLAS----------------------EKAENHEF- 592
Cdd:PRK06710 106 PLYTERELEYQLHDSGAKVILCLdlvfPRVTNVQSATKIEHVIVTRIADflpfpknllypfvqkkqsnlvvKVSESETIh 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 593 --------------TPADG-GSLAYVIYTSGSTGQPKGVAVEHRQAVS-FLTGMQHQFPLSE-DDIVMVKTSFSFDASVW 655
Cdd:PRK06710 186 lwnsvekevntgveVPCDPeNDLALLQYTGGTTGFPKGVMLTHKNLVSnTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 656 QLFWWSLSGASAYLLPPGWekDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAAR 735
Cdd:PRK06710 266 AVMNLSIMQGYKMVLIPKF--DMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEY-DISSIRACISGSAPLPVEVQEK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 736 FASVLPQvSLIHGYGPTEAT-VDAAFYVLDPerdrdrlRIP--IGKPVPG--ARLYVLDPHLAVQPsGVAGELYIAGAGV 810
Cdd:PRK06710 343 FETVTGG-KLVEGYGLTESSpVTHSNFLWEK-------RVPgsIGVPWPDteAMIMSLETGEALPP-GEIGEIVVKGPQI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 811 ARGYLNRPALTEErFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTV 890
Cdd:PRK06710 414 MKGYWNKPEETAA-VLQDGW------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIG 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363747658 891 RTDSGEPELCAYVEGLQRNEVRAQLE------RLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK06710 487 VPDPYRGETVKAFVVLKEGTECSEEElnqfarKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
466-960 |
1.96e-27 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 119.73 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 466 RQAAFTPERLAIRFSGGS--LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYP 543
Cdd:PRK05857 22 EQARQQPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 544 KERLSYMLKDSGASLLLTQPGC-----SAPNF--SGETLEVDMTSLASEKAENHEF----TPADGGS---LAyVIYTSGS 609
Cdd:PRK05857 102 IAAIERFCQITDPAAALVAPGSkmassAVPEAlhSIPVIAVDIAAVTRESEHSLDAaslaGNADQGSedpLA-MIFTSGT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 610 TGQPKGVAVEHRQAVSFLTGMQHQfPLSEDDIVMVKTSFS-FDASVWQLFWWSLSG-ASAYLLPPGWEKDSALiVQAIHQ 687
Cdd:PRK05857 181 TGEPKAVLLANRTFFAVPDILQKE-GLNWVTWVVGETTYSpLPATHIGGLWWILTClMHGGLCVTGGENTTSL-LEILTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 688 ENVTTAHFIPAMLNSFLdqAEIERLSDRTSLKRVFAGGEPLAPRTAARFASVlPQVSLIHGYGPTEATVDAafyVLDPER 767
Cdd:PRK05857 259 NAVATTCLVPTLLSKLV--SELKSANATVPSLRLVGYGGSRAIAADVRFIEA-TGVRTAQVYGLSETGCTA---LCLPTD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 768 DRDRLRI---PIGKPVPGARLYVLDPHLA------VQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDpfypgerMYK 838
Cdd:PRK05857 333 DGSIVKIeagAVGRPYPGVDVYLAATDGIgptapgAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDG-------WVN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 839 TGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDsgePELCAYVeGLQ----------- 907
Cdd:PRK05857 406 TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD---EEFGALV-GLAvvasaeldesa 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 908 ----RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAADAETYT 960
Cdd:PRK05857 482 aralKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVVV 538
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1640-1990 |
2.02e-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: 118.97 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 PEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQIASF-SFDvFSGDLARTLTNGGTLIVCPDEt 1718
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFhSFG-LTGCLWLPLLSGIKVVFHPNP- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1719 rLEPAEIYKIMNSQRITVMESTPALiipVMEYV-YRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTE 1797
Cdd:cd05909 224 -LDYKKIPELIYDKKATILLGTPTF---LRGYArAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG--IRILEGYGTTE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1798 ATIDSSFYETSMGG-EGTgdnvpIGSPLPNVHMYVLS-QTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQmkftknpFV 1875
Cdd:cd05909 298 CSPVISVNTPQSPNkEGT-----VGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1876 SGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQ--TGLVREAAVAVQHDKNGQAgLAAYIVPSDV 1953
Cdd:cd05909 366 FGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEilPEDNEVAVVSVPDGRKGEK-IVLLTTTTDT 444
|
330 340 350
....*....|....*....|....*....|....*...
gi 363747658 1954 NTNALRAALTK-ELPAYMIPAHLIPLENMPLTLNGKLD 1990
Cdd:cd05909 445 DPSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
603-942 |
2.31e-27 |
|
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: 115.68 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 603 VIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFsFDASVWQLFWWS--LSGASAYllpPGWEKDSAL 680
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPF-FHTFGYKAGIVAclLTGATVV---PVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 681 IVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAaf 760
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKF-DLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVAT-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 761 yVLDPERDRDRLRIPIGKPVPGARLYVLDPhlavqpsgvaGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTG 840
Cdd:cd17638 158 -MCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWL------HTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 841 DVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPEL-CAYV-----EGLQRNEVRAQ 914
Cdd:cd17638 221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVgKAFVvarpgVTLTEEDVIAW 300
|
330 340
....*....|....*....|....*...
gi 363747658 915 LERLLPGYMVPAYMIEMEQWPVTPSGKL 942
Cdd:cd17638 301 CRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
465-889 |
2.75e-27 |
|
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: 119.52 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 465 ERQAAFTPERLAIRFSGGS-----LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLD 539
Cdd:cd05970 24 DAMAKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPAT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 540 PAYPKERLSYMLKDSGASLLL-------------TQPGCSAPN----FSGETLE--VDMTSLASEKAEN----HEFTPAD 596
Cdd:cd05970 104 HQLTAKDIVYRIESADIKMIVaiaednipeeiekAAPECPSKPklvwVGDPVPEgwIDFRKLIKNASPDferpTANSYPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 597 GGSLAYVIYTSGSTGQPKGVAVEHRQAVS-FLTGMQHQfPLSEDDIVMVKTSFSFDASVW-QLFWWSLSGASAYLLppGW 674
Cdd:cd05970 184 GEDILLVYFSSGTTGMPKMVEHDFTYPLGhIVTAKYWQ-NVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVY--DY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 675 EK-DSALIVQAIHQENVTTaHFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASvLPQVSLIHGYGPTE 753
Cdd:cd05970 261 DKfDPKALLEKLSKYGVTT-FCAPPTIYRFLIREDLSRY-DLSSLRYCTTAGEALNPEVFNTFKE-KTGIKLMEGFGQTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 754 ATVD-AAFYVLDPErdrdrlriP--IGKPVPGARLYVLDPHLAVQPSGVAGELYIAGA-----GVARGYLNRPALTEERF 825
Cdd:cd05970 338 TTLTiATFPWMEPK--------PgsMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 826 LEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT 889
Cdd:cd05970 410 HDG-------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVT 466
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
484-877 |
3.36e-27 |
|
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: 118.23 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTqp 563
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 564 gcsapnfsgetlevdmtslasekaENHEftpadgGSLAYVIYTSGSTGQPKGVAVEHRqavSFLTGMQH---QFPLSEDD 640
Cdd:cd17640 84 ------------------------ENDS------DDLATIIYTSGTTGNPKGVMLTHA---NLLHQIRSlsdIVPPQPGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 641 IVMvktSF-----SFDASVwQLFWWSLSGASAYLLPPGWEKDSA-----------LIVQAIH---QENVTTAHFIPAMLN 701
Cdd:cd17640 131 RFL---SIlpiwhSYERSA-EYFIFACGCSQAYTSIRTLKDDLKrvkphyivsvpRLWESLYsgiQKQVSKSSPIKQFLF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 702 SFLDQAEIerlsdrtsLKRVFAGGEPLAPRTAARFASVlpQVSLIHGYGPTEATVdaafyVLDPERDRDRLRIPIGKPVP 781
Cdd:cd17640 207 LFFLSGGI--------FKFGISGGGALPPHVDTFFEAI--GIEVLNGYGLTETSP-----VVSARRLKCNVRGSVGRPLP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 782 GARLYVLDPHL-AVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQ 860
Cdd:cd17640 272 GTEIKIVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWF------NTGDLGWLTCGGELVLTGRAKDT 345
|
410
....*....|....*...
gi 363747658 861 VKIR-GYRIEPGEIEAAL 877
Cdd:cd17640 346 IVLSnGENVEPQPIEEAL 363
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1508-1994 |
3.45e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 119.38 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARI 1586
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGvGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1587 EYILRDSGADILLLQQELKHLI-SNLPESEMSHI-------CLDDESSYE---------------------ENSCNLNL- 1636
Cdd:PRK06178 123 SYELNDAGAEVLLALDQLAPVVeQVRAETSLRHVivtsladVLPAEPTLPlpdslraprlaaagaidllpaLRACTAPVp 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1637 --SPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQI-YELDRKPVRLlqiaSFsFDVF--SGD---LARTLTNG 1708
Cdd:PRK06178 203 lpPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVaVVGGEDSVFL----SF-LPEFwiAGEnfgLLFPLFSG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1709 GTLIVCpdeTRLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDililgsdMVKAQDF-KTLTDRFGQSM 1787
Cdd:PRK06178 278 ATLVLL---ARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLR-------QVRVVSFvKKLNPDYRQRW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1788 RIIN-------SYGVTEATIDSSFYEtsmgGEGTGD----NVPI--GSPLPNVHMYVLS-QTDQIQPIGVAGELCIGGAG 1853
Cdd:PRK06178 348 RALTgsvlaeaAWGMTETHTCDTFTA----GFQDDDfdllSQPVfvGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1854 VAKGYHQKPDLTqmkftKNPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA 1933
Cdd:PRK06178 424 LLKGYWNKPEAT-----AEALRDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVV 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 1934 VQHDKN-GQAGLaAYIVP---SDVNTNALRAALTKELPAYMIPAHLIpLENMPLTLNGKLDRNAL 1994
Cdd:PRK06178 497 GRPDPDkGQVPV-AFVQLkpgADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
473-888 |
1.04e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 117.47 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 473 ERLAIRFSGGSLTYAELDMYASRLAAHLAAR-GITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYML 551
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 552 KDSGASLLLTQPGcSAPNFSG-----ETLEVDMTSLASEKAENH----EFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQ 622
Cdd:PRK07867 98 AHADCQLVLTESA-HAELLDGldpgvRVINVDSPAWADELAAHRdaepPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 623 AVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPgweKDSAL-IVQAIHQENVTTAHFIPAMLN 701
Cdd:PRK07867 177 VASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRR---KFSASgFLPDVRRYGATYANYVGKPLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 702 SFLdqAEIERLSDRTSLKRVFAGGEPlAPRTAARFASVLpQVSLIHGYGPTEATVdaAFY------------------VL 763
Cdd:PRK07867 254 YVL--ATPERPDDADNPLRIVYGNEG-APGDIARFARRF-GCVVVDGFGSTEGGV--AITrtpdtppgalgplppgvaIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 764 DPErdrdrlripIGKPVPGArlyVLDPHLAVQPSGVAGELY-IAGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDV 842
Cdd:PRK07867 328 DPD---------TGTECPPA---EDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDL 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 363747658 843 ARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 888
Cdd:PRK07867 389 AYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAV 434
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1052-1360 |
1.43e-26 |
|
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: 115.23 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1052 YPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEgklNPERMER---AFKELIKRHESLRTSF-----EQdaggdPVQRIHD 1123
Cdd:cd19544 2 YPLAPLQEGILFHHLLAEEGDPYLLRSLLAFD---SRARLDAflaALQQVIDRHDILRTAIlweglSE-----PVQVVWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1124 EVPFTLQTTVL-GERTEQEAAAAFIKP----FDLSQAPLFRAQIVKISD-ERHLLLVDMHHIISDGVSVNILIREFGELY 1197
Cdd:cd19544 74 QAELPVEELTLdPGDDALAQLRARFDPrryrLDLRQAPLLRAHVAEDPAnGRWLLLLLFHHLISDHTSLELLLEEIQAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1198 NNR--NLPALrIQYKDY-AVWREGFKTGDAyktqEAYWLKQL----EGELP--VLDLPADHARPpvrsfagDKVSFTLDQ 1268
Cdd:cd19544 154 AGRaaALPPP-VPYRNFvAQARLGASQAEH----EAFFREMLgdvdEPTAPfgLLDVQGDGSDI-------TEARLALDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1269 EVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPeGGKPFVQY 1346
Cdd:cd19544 222 ELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQggAGADRALGMFINTLPLRVRL-GGRSVREA 300
|
330
....*....|....*.
gi 363747658 1347 LQEVRE--TALEAFEH 1360
Cdd:cd19544 301 VRQTHArlAELLRHEH 316
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1508-1949 |
2.09e-26 |
|
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: 116.18 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVID--NEIEISYRFLNERANRLARTLQNRKG-PKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKA 1584
Cdd:cd05904 15 ASAHPSRPALIDaaTGRALTYAELERRVRRLAAGLAKRGGrKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1585 RIEYILRDSGADILLLQQELkhlISNLPESEMSHICLDDESSYE-ENSCNLNLSPAPEEPVYII---------YTSGTTG 1654
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAEL---AEKLASLALPVVLLDSAEFDSlSFSDLLFEADEAEPPVVVIkqddvaallYSSGTTG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1655 APKGVIVTYRNFThAALA---WRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPdetRLEPAEIYKIMNS 1731
Cdd:cd05904 172 RSKGVMLTHRNLI-AMVAqfvAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMP---RFDLEELLAAIER 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1732 QRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSdmvkAQDFKTLTDRFGQ---SMRIINSYGVTEAT-IdssfyeT 1807
Cdd:cd05904 248 YKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGA----APLGKELIEAFRAkfpNVDLGQGYGMTESTgV------V 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1808 SMGGEGTGDNVPIGSP---LPNVHMYVLS-QTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKnpfvsgERLYRT 1883
Cdd:cd05904 318 AMCFAPEKDRAKYGSVgrlVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK------EGWLHT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 1884 GDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA-VQHDKNGQAGlAAYIV 1949
Cdd:cd05904 392 GDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIpYPDEEAGEVP-MAFVV 457
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
455-896 |
2.66e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 116.23 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 455 PKAFTLHG-LFERQAAFtPER--LAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKA 531
Cdd:PLN02246 20 PNHLPLHDyCFERLSEF-SDRpcLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 532 GGAYLPLDPAYPKERLSYMLKDSGASLLLTQPgCSAPNFSGETLEVDMTSLASEKAEN-----HEFTPADGGSLAYVI-- 604
Cdd:PLN02246 99 GAVTTTANPFYTPAEIAKQAKASGAKLIITQS-CYVDKLKGLAEDDGVTVVTIDDPPEgclhfSELTQADENELPEVEis 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 605 --------YTSGSTGQPKGVAVEHRqavSFLTGMQHQ-------FPLSEDDIVM-VKTSFSFdASVWQLFWWSLSGASAY 668
Cdd:PLN02246 178 pddvvalpYSSGTTGLPKGVMLTHK---GLVTSVAQQvdgenpnLYFHSDDVILcVLPMFHI-YSLNSVLLCGLRVGAAI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 669 LLPPGWEkdSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERlSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHG 748
Cdd:PLN02246 254 LIMPKFE--IGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEK-YDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 749 YGPTEA-TVDA---AFyVLDPerdrdrlrIPI-----GKPVPGARLYVLDPHLAVQ-PSGVAGELYIAGAGVARGYLNRP 818
Cdd:PLN02246 331 YGMTEAgPVLAmclAF-AKEP--------FPVksgscGTVVRNAELKIVDPETGASlPRNQPGEICIRGPQIMKGYLNDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 819 ALTEErfledpfypgermykTGDVARWLPDGNVEFLGRTD-----DQV----KIRGYRIEPGEIEAALRSIEGVREAAVT 889
Cdd:PLN02246 402 EATAN---------------TIDKDGWLHTGDIGYIDDDDelfivDRLkeliKYKGFQVAPAELEALLISHPSIADAAVV 466
|
....*....
gi 363747658 890 VRTD--SGE 896
Cdd:PLN02246 467 PMKDevAGE 475
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
600-943 |
2.68e-26 |
|
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: 115.51 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 600 LAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVM----VKTSFSFDASVWQLFwwsLSGASAYLLP-Pgw 674
Cdd:cd05909 149 PAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFgalpFFHSFGLTGCLWLPL---LSGIKVVFHPnP-- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 675 eKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLSdrtSLKRVFAGGEPLAPRTAARFASVLpQVSLIHGYGPTEA 754
Cdd:cd05909 224 -LDYKKIPELIYDKKATILLGTPTFLRGYARAAHPEDFS---SLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTEC 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 755 TVDAAfyVLDPERDRdrlRI-PIGKPVPG--ARLYVLDPHLAVqPSGVAGELYIAGAGVARGYLNRPALTEerfledpFY 831
Cdd:cd05909 299 SPVIS--VNTPQSPN---KEgTVGRPLPGmeVKIVSVETHEEV-PIGEGGLLLVRGPNVMLGYLNEPELTS-------FA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 832 PGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGV-REAAVTVRTDS--GEPE-LCAYVEGLQ 907
Cdd:cd05909 366 FGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGrkGEKIvLLTTTTDTD 445
|
330 340 350
....*....|....*....|....*....|....*..
gi 363747658 908 RNEVRAQL-ERLLPGYMVPAYMIEMEQWPVTPSGKLD 943
Cdd:cd05909 446 PSSLNDILkNAGISNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
463-947 |
2.72e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 116.46 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARgiTNESIVGVLSERSPEML---IAVLAVLKAGGAYLPLD 539
Cdd:PRK12492 29 VFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQH--TDLVPGDRIAVQMPNVLqypIAVFGALRAGLIVVNTN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 540 PAYPKERLSYMLKDSGASLL--LTQPGCSAPNFSGET-----LEVDMTSLASE--------------------------- 585
Cdd:PRK12492 107 PLYTAREMRHQFKDSGARALvyLNMFGKLVQEVLPDTgieylIEAKMGDLLPAakgwlvntvvdkvkkmvpayhlpqavp 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 586 --------KAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVS----FLTGMQHQFP-----LSEDDIVMVKT-- 646
Cdd:PRK12492 187 fkqalrqgRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAnmlqVRACLSQLGPdgqplMKEGQEVMIAPlp 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 647 ---SFSFDASVWQLFwwsLSGASAYLLPPgwEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFA 723
Cdd:PRK12492 267 lyhIYAFTANCMCMM---VSGNHNVLITN--PRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDL-DFSALKLTNS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 724 GGEPLAPRTAARFASvLPQVSLIHGYGPTEATVDAAfyvLDPERDRDRLRIpIGKPVPGARLYVLDPHLAVQPSGVAGEL 803
Cdd:PRK12492 341 GGTALVKATAERWEQ-LTGCTIVEGYGLTETSPVAS---TNPYGELARLGT-VGIPVPGTALKVIDDDGNELPLGERGEL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 804 YIAGAGVARGYLNRPALTEERFledpfyPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGV 883
Cdd:PRK12492 416 CIKGPQVMKGYWQQPEATAEAL------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 884 REAAVTVRTD--SGEPE---LCAYVEGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK12492 490 ANCAAIGVPDerSGEAVklfVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1521-1991 |
2.90e-26 |
|
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: 115.23 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1521 EIEISYRFLNERANRLARTLQ-NRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILL 1599
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKiNGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1600 lqqelkhlISNlpesemshiclddessyeenscnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQiYEL 1679
Cdd:cd05914 85 --------VSD-----------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKE-VVL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1680 DRKPVRLLQIASFSfDVF--SGDLARTLTNGGTlIVCPDETrlePAEIYKIMNSQRITVMestpaLIIPV---MEYVYRN 1754
Cdd:cd05914 127 LGKGDKILSILPLH-HIYplTFTLLLPLLNGAH-VVFLDKI---PSAKIIALAFAQVTPT-----LGVPVplvIEKIFKM 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1755 QfKLPDLDI--------LILGSDMVKAQDFKTLTDRFGQSMRIINSYGVT-EATIDSSFYEtsMG-----GEGTGDNVPI 1820
Cdd:cd05914 197 D-IIPKLTLkkfkfklaKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAKiNPDVEEFLRT--IGfpytiGYGMTETAPI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1821 --------------GSPLPNVHMyvlsQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDR 1886
Cdd:cd05914 274 isysppnrirlgsaGKVIDGVEV----RIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1887 ACWLPNGTIRLLGRM-DYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKngqAGLAAYIVPSDVNTNAL------- 1958
Cdd:cd05914 344 GKIDAEGYLYIRGRKkEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKK---LVALAYIDPDFLDVKALkqrniid 420
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 363747658 1959 ------RAALTKELPAY-MIPAHLIPLENMPLTLNGKLDR 1991
Cdd:cd05914 421 aikwevRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1524-1976 |
2.98e-26 |
|
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: 115.00 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLq 1601
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIAL-GVEPgdRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1602 qelkhlisnlpesemshiclddessyeenscnlnlsPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDR 1681
Cdd:cd05907 84 ------------------------------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1682 KPVRLlqiasfSFDVFSGDLART------LTNGGTLIVCPDETRLEPaeiykimNSQRI--TVMESTPAliipVMEYVYr 1753
Cdd:cd05907 128 GDRHL------SFLPLAHVFERRaglyvpLLAGARIYFASSAETLLD-------DLSEVrpTVFLAVPR----VWEKVY- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1754 nqfklpdldiliLGSDMVKAQDFK-TLTDR-FGQSMR-----------------------IINSYGVTEATIDSSFyetS 1808
Cdd:cd05907 190 ------------AAIKVKAVPGLKrKLFDLaVGGRLRfaasggaplpaellhffralgipVYEGYGLTETSAVVTL---N 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1809 MGGEGTGDNVpiGSPLPNVHmyvlsqtdqIQpIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRAC 1888
Cdd:cd05907 255 PPGDNRIGTV--GKPLPGVE---------VR-IADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGE 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1889 WLPNGTIRLLGRM-DYQVKINGYRIETEEIESVLLQTGLVREAAVAvqhdKNGQAGLAAYIVPsdvNTNALRAALTKELP 1967
Cdd:cd05907 317 IDEDGFLHITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVI----GDGRPFLVALIVP---DPEALEAWAEEHGI 389
|
....*....
gi 363747658 1968 AYMIPAHLI 1976
Cdd:cd05907 390 AYTDVAELA 398
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1500-1994 |
3.60e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 116.00 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1500 FHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIP 1576
Cdd:PRK06164 12 LASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAqgvRRGDR--VAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1577 IDSHYPKARIEYILRDSGADILLLQQELKHL-----ISNLPESEMSH----ICLDDESS-----------------YEEN 1630
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWPGFKGIdfaaiLAAVPPDALPPlraiAVVDDAADatpapapgarvqlfalpDPAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1631 SCNLNLSPAPEEPVYIIYT-SGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVrLLQIASFS--FDvFSGDLArTLTN 1707
Cdd:PRK06164 170 PAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAV-LLAALPFCgvFG-FSTLLG-ALAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1708 GGTLIVCPdetRLEPAEIYKIMNSQRIT-VMESTPAliipvmeyvYRNQFKLPDldililgsdmvKAQDFKTLtDRFG-- 1784
Cdd:PRK06164 247 GAPLVCEP---VFDAARTARALRRHRVThTFGNDEM---------LRRILDTAG-----------ERADFPSA-RLFGfa 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1785 ---------------QSMRIINSYGVTEA-------TIDSSFYETSMGGegtgdNVPIgSPLPNVHMyVLSQTDQIQPIG 1842
Cdd:PRK06164 303 sfapalgelaalaraRGVPLTGLYGSSEVqalvalqPATDPVSVRIEGG-----GRPA-SPEARVRA-RDPQDGALLPDG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1843 VAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLL 1922
Cdd:PRK06164 376 ESGEIEIRAPSLMRGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALE 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 1923 QTGLVREA-AVAVQHDknGQAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNG---KLDRNAL 1994
Cdd:PRK06164 450 ALPGVAAAqVVGATRD--GKTVPVAFVIPTDgasPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
460-947 |
4.34e-26 |
|
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: 115.70 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 460 LHGLFERQAAFtPERLAI--RFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLP 537
Cdd:cd17642 20 LHKAMKRYASV-PGTIAFtdAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 538 LDPAYPKERLSYmlkdsgaSLLLTQPG---CSAPNFSG--------------------------ETLEVDMTSLASEKAE 588
Cdd:cd17642 99 TNDIYNERELDH-------SLNISKPTivfCSKKGLQKvlnvqkklkiiktiiildskedykgyQCLYTFITQNLPPGFN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 589 NHEFTPADGG---SLAYVIYTSGSTGQPKGVAVEHRQAVS-FLTGMQHQF--PLSEDDIVMVKTSFSFDASVWQLFWWSL 662
Cdd:cd17642 172 EYDFKPPSFDrdeQVALIMNSSGSTGLPKGVQLTHKNIVArFSHARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 663 SGASAYLLPPGWEKdsaLIVQAIHQENVTTAHFIPAMLnSFLDQAEIERLSDRTSLKRVFAGGEPLAPRT----AARFAs 738
Cdd:cd17642 252 CGFRVVLMYKFEEE---LFLRSLQDYKVQSALLVPTLF-AFFAKSTLVDKYDLSNLHEIASGGAPLSKEVgeavAKRFK- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 739 vLPQVSliHGYGPTEATVDAafyVLDPERDrDRlriP--IGKPVPGARLYVLDPHLAvQPSGV--AGELYIAGAGVARGY 814
Cdd:cd17642 327 -LPGIR--QGYGLTETTSAI---LITPEGD-DK---PgaVGKVVPFFYAKVVDLDTG-KTLGPneRGELCVKGPMIMKGY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 815 LNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS 894
Cdd:cd17642 396 VNNPEATKALIDKDGWL------HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDE 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 895 GEPELCAYV----EGLQRNE------VRAQL---ERLLPGymvpayMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd17642 470 DAGELPAAVvvleAGKTMTEkevmdyVASQVstaKRLRGG------VKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1499-1994 |
5.72e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 115.52 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1499 PFHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYI 1575
Cdd:PRK06710 25 PLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKlgvEKGDR--VAIMLPNCPQAVIGYYGTLLAGGIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1576 PIDSHYPKARIEYILRDSGADILL----------------------------------------LQQELKHLISNLPESE 1615
Cdd:PRK06710 103 QTNPLYTERELEYQLHDSGAKVILcldlvfprvtnvqsatkiehvivtriadflpfpknllypfVQKKQSNLVVKVSESE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1616 MSHIClddESSYEENSCNLNLSPAPEEPVYII-YTSGTTGAPKGVIVTYRNFTHAALAWRQ-IYELDRKPVRLLQIASFs 1693
Cdd:PRK06710 183 TIHLW---NSVEKEVNTGVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQwLYNCKEGEEVVLGVLPF- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1694 FDVF--SGDLARTLTNGGTLIVCPdetRLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSD-- 1769
Cdd:PRK06710 259 FHVYgmTAVMNLSIMQGYKMVLIP---KFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSApl 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1770 MVKAQD-FKTLTdrfgqSMRIINSYGVTEAT--IDSSF-YETSMGGEgtgdnvpIGSPLPNVHMYVLS-QTDQIQPIGVA 1844
Cdd:PRK06710 336 PVEVQEkFETVT-----GGKLVEGYGLTESSpvTHSNFlWEKRVPGS-------IGVPWPDTEAMIMSlETGEALPPGEI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1845 GELCIGGAGVAKGYHQKPDLTQMkftknpfVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQT 1924
Cdd:PRK06710 404 GEIVVKGPQIMKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363747658 1925 GLVREAAVAVQHDKNGQAGLAAYIV---PSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK06710 477 EKVQEVVTIGVPDPYRGETVKAFVVlkeGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1508-1989 |
8.88e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 114.64 E-value: 8.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEIEISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKA 1584
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDlglKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1585 RIEYILRDSGADILLLQQELKHLISN---------------LPESEMSHICLDDESSYE-ENSCNLNLSPAPEEPVYIIY 1648
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALAPTAEAalallpvdtlilslvLGGREAPGGWLDFADWAEaGSVAEPDVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1649 TSGTTGAPKGVIVtyrnfTHAALAWRQI-------YELDRKPVRLLQI-ASFSFDVFSG-DLARTLTNggTLIVCPDetr 1719
Cdd:PRK08316 179 TSGTESLPKGAML-----THRALIAEYVscivagdMSADDIPLHALPLyHCAQLDVFLGpYLYVGATN--VILDAPD--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1720 lePAEIYKIMNSQRITVMESTPALIIPVMEYvyrnqfklPDLDILILGSdMVKAQ---------DFKTLTDRFGQsMRII 1790
Cdd:PRK08316 249 --PELILRTIEAERITSFFAPPTVWISLLRH--------PDFDTRDLSS-LRKGYygasimpveVLKELRERLPG-LRFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1791 NSYGVTE----ATIDSSfyETSMGGEGTGdnvpiGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQ 1866
Cdd:PRK08316 317 NCYGQTEiaplATVLGP--EEHLRRPGSA-----GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1867 MKFTKNPFVSGERLYRTGDracwlpnGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLA 1945
Cdd:PRK08316 390 EAFRGGWFHSGDLGVMDEE-------GYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAViGLPDPKWIEA-VT 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 363747658 1946 AYIVP---SDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKL 1989
Cdd:PRK08316 462 AVVVPkagATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1523-1994 |
1.62e-25 |
|
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: 112.53 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1523 EISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILL 1599
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEiglEKGDR--VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1600 lqqelkhlisnlpesemshiclDDESSyeenscnlnlspapeEPVYIIYTSGTTGAPKGVIVTYRnfthaalawrqiyel 1679
Cdd:cd05971 84 ----------------------TDGSD---------------DPALIIYTSGTTGPPKGALHAHR--------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1680 drkpVRL--LQIASFSFDVF--SGDLARTLTN----GGTL------------IVCPDETRLEPAEIYKIMNSQRITvMES 1739
Cdd:cd05971 112 ----VLLghLPGVQFPFNLFprDGDLYWTPADwawiGGLLdvllpslyfgvpVLAHRMTKFDPKAALDLMSRYGVT-TAF 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1740 TPALIIPVMEYVYrNQFKLPDLDILILGS--DMVKAQDFKTLTDRFGQSmrIINSYGVTEAtidsSFYETSMGGEGTGDN 1817
Cdd:cd05971 187 LPPTALKMMRQQG-EQLKHAQVKLRAIATggESLGEELLGWAREQFGVE--VNEFYGQTEC----NLVIGNCSALFPIKP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1818 VPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIggagvakgyhQKPDLTQM-KFTKNPFVSGERL----YRTGDRACWLPN 1892
Cdd:cd05971 260 GSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAV----------ELPDPVAFlGYWNNPSATEKKMagdwLLTGDLGRKDSD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1893 GTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV------PSDVNTNALRAALTKEL 1966
Cdd:cd05971 330 GYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpgetPSDALAREIQELVKTRL 409
|
490 500
....*....|....*....|....*...
gi 363747658 1967 PAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05971 410 AAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
464-925 |
3.87e-25 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 113.43 E-value: 3.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 464 FERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYP 543
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 544 KERLSYMLKDSGASLLLTQPGCsAPNFS--GETLEVDMTS----------------LASEKAENHEFTPADGGSL----- 600
Cdd:PRK08279 123 GAVLAHSLNLVDAKHLIVGEEL-VEAFEeaRADLARPPRLwvaggdtlddpegyedLAAAAAGAPTTNPASRSGVtakdt 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 601 AYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIV------------MVKTSfsfdaSVwqlfwwsLSGASAY 668
Cdd:PRK08279 202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLycclplyhntggTVAWS-----SV-------LAAGATL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 669 LLPpgwEKDSA----LIVQAihqENVTTAHFIPAMLNSFLDQAEIErlSDRT-SLKRVFAGGepLAP----RTAARFAsv 739
Cdd:PRK08279 270 ALR---RKFSAsrfwDDVRR---YRATAFQYIGELCRYLLNQPPKP--TDRDhRLRLMIGNG--LRPdiwdEFQQRFG-- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 740 LPQVslIHGYGPTEATVdaAFYVLDpERDR------DRLRIPI---------GKPVPGArlyvlDPHLAVQPSGVAGELY 804
Cdd:PRK08279 338 IPRI--LEFYAASEGNV--GFINVF-NFDGtvgrvpLWLAHPYaivkydvdtGEPVRDA-----DGRCIKVKPGEVGLLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 805 --IAGAGVARGYlNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEG 882
Cdd:PRK08279 408 grITDRGPFDGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPG 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 883 VREAAV---------------TVRTDSGepelcayvEGLQRNEVRAQLERLLPGYMVP 925
Cdd:PRK08279 487 VEEAVVygvevpgtdgragmaAIVLADG--------AEFDLAALAAHLYERLPAYAVP 536
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1643-1991 |
5.64e-25 |
|
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: 108.26 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1643 PVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVcpdETRLEP 1722
Cdd:cd17633 2 PFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGED-AILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1723 AEIYKIMNSQRITVMESTPALIipvmEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEAT-ID 1801
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTML----QALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKA-NLIEFYGTSELSfIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1802 SSFYETSMGGEGtgdnvpIGSPLPNVHMYVLSQTDqiqpiGVAGELCIggagvakgyhqKPDLTQMKFTKNPFVSGERLY 1881
Cdd:cd17633 153 YNFNQESRPPNS------VGRPFPNVEIEIRNADG-----GEIGKIFV-----------KSEMVFSGYVRGGFSNPDGWM 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1882 RTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAYIVPSdVNTNALRA 1960
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVvGIPDARFGEIAVALYSGDK-LTYKQLKR 289
|
330 340 350
....*....|....*....|....*....|.
gi 363747658 1961 ALTKELPAYMIPAHLIPLENMPLTLNGKLDR 1991
Cdd:cd17633 290 FLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
603-944 |
1.16e-24 |
|
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: 107.73 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 603 VIYTSGSTGQPKGVAVEHRQAVSFLTGMQ-HQFPLSEDDIVMVKTSFSFDASVWqlfwWSLSG--ASAYLLPPGWEKDSA 679
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQkEGLNWVVGDVTYLPLPATHIGGLW----WILTCliHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 680 LIVQAIHQENVTTAHFIPAMLNSFLDQAEiERLSDRTSLKRVFAGGE-PLAPRTaaRFASVLPQVSLIHGYGPTEATVda 758
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELK-SANATVPSLRLIGYGGSrAIAADV--RFIEATGLTNTAQVYGLSETGT-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 759 afyVLDPERDRDRLRI-PIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermy 837
Cdd:cd17635 157 ---ALCLPTDDDSIEInAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVN------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 838 kTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELC-AYV---EGLQRNEVRA 913
Cdd:cd17635 228 -TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVgLAVvasAELDENAIRA 306
|
330 340 350
....*....|....*....|....*....|....
gi 363747658 914 QLERL---LPGYMVPAYMIEMEQWPVTPSGKLDR 944
Cdd:cd17635 307 LKHTIrreLEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1638-1991 |
1.21e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 111.63 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1638 PAPEEPVYIIYTSGTTGAPKGVIVTYRN-FTHAA--LAWrqIYELDRKPVRLLQIASFsFDVFSGDLARTLTN--GGTLI 1712
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKGAQLTHRNlFANAAqgKAW--VPGLGDGPERVLAALPM-FHAYGLTLCLTLAVsiGGELV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1713 VCPdetRLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQsmRIINS 1792
Cdd:PRK05605 293 LLP---APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGG--LLVEG 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1793 YGVTEatidssfyeTS---MGGEGTGDNVP--IGSPLPNVHMYVLSQTD--QIQPIGVAGELCIGGAGVAKGYHQKPDLT 1865
Cdd:PRK05605 368 YGLTE---------TSpiiVGNPMSDDRRPgyVGVPFPDTEVRIVDPEDpdETMPDGEEGELLVRGPQVFKGYWNRPEET 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1866 QMKFTknpfvsgERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLA 1945
Cdd:PRK05605 439 AKSFL-------DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVV 511
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 363747658 1946 AYIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDR 1991
Cdd:PRK05605 512 AAVVLEPgaaLDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
597-947 |
2.66e-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: 107.18 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 597 GGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTS-FSFDASVWQLFWWSLSGASAYLL-PPGW 674
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAgPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 675 EKDSAL--IVQAIHQENVTTAHFIPAMLNSFLdQAEIERlsDRTSLKRVFAGGEPLAPRTAARFASVLpQVSLIHGYGPT 752
Cdd:cd05944 81 RNPGLFdnFWKLVERYRITSLSTVPTVYAALL-QVPVNA--DISSLRFAMSGAAPLPVELRARFEDAT-GLPVVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 753 EATVDAAfyVLDPERDRdrlRI-PIGKPVPGA--RLYVLDPHLAVQ-PSGV--AGELYIAGAGVARGYL----NRPALTE 822
Cdd:cd05944 157 EATCLVA--VNPPDGPK---RPgSVGLRLPYArvRIKVLDGVGRLLrDCAPdeVGEICVAGPGVFGGYLytegNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 823 ERFLedpfypgermyKTGDVARWLPDGNVEFLGRTDDQVkIRG-YRIEPGEIEAALRSIEGVREAAVTVRTDSGEPEL-C 900
Cdd:cd05944 232 DGWL-----------NTGDLGRLDADGYLFITGRAKDLI-IRGgHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELpV 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 363747658 901 AYVEGLQRNEVR-AQL-----ERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05944 300 AYVQLKPGAVVEeEELlawarDHVPERAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1524-1989 |
3.72e-24 |
|
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: 109.97 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLL 1600
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDlgvKKGDR--VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1601 QQE---------LKHLISNLPESEMSH----ICLDDESS---------------YEENSCNLNLSP-APEEPVYIIYTSG 1651
Cdd:cd17634 163 ADGgvragrsvpLKKNVDDALNPNVTSvehvIVLKRTGSdidwqegrdlwwrdlIAKASPEHQPEAmNAEDPLFILYTSG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1652 TTGAPKGVIVTYRNFthaalawrqiyeldrkPVRLLQIASFSFDVFSGDLARTLTN-----GGTLIV-----CPDETRL- 1720
Cdd:cd17634 243 TTGKPKGVLHTTGGY----------------LVYAATTMKYVFDYGPGDIYWCTADvgwvtGHSYLLygplaCGATTLLy 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1721 -------EPAEIYKIMNSQRITVMESTPALIIPVM----EYVYRnqFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMR- 1788
Cdd:cd17634 307 egvpnwpTPARMWQVVDKHGVNILYTAPTAIRALMaagdDAIEG--TDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCp 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1789 IINSYGVTEAtidSSFYETSMGGEGTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGA--GVAKGYHQKPDltq 1866
Cdd:cd17634 385 VVDTWWQTET---GGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE--- 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1867 mKFTKNPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAA-VAVQHDKNGQAgLA 1945
Cdd:cd17634 459 -RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAvVGIPHAIKGQA-PY 536
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 363747658 1946 AYIV------PSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKL 1989
Cdd:cd17634 537 AYVVlnhgvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1508-1994 |
5.02e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 108.71 E-value: 5.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIE 1587
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1588 YILRDSGADILLLQQELKhliSNLPESEMSHICLDD--ESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRN 1665
Cdd:PRK07638 91 ERLAISNADMIVTERYKL---NDLPDEEGRVIEIDEwkRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1666 FTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPdetRLEPAEIYKIMNSQRITVMESTPALIi 1745
Cdd:PRK07638 168 WLHSFDCNVHDFHMKRED-SVLIAGTLVHSLFLYGAISTLYVGQTVHLMR---KFIPNQVLDKLETENISVMYTVPTML- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1746 pvmEYVYR-NQFKLPDLDILILGSDMVKAQDfKTLTDRFgQSMRIINSYGVTEAtidsSFYETSMGGEGTGDNVPIGSPL 1824
Cdd:PRK07638 243 ---ESLYKeNRVIENKMKIISSGAKWEAEAK-EKIKNIF-PYAKLYEFYGASEL----SFVTALVDEESERRPNSVGRPF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1825 PNVhmyvlsqtdQIQPIGVAGELCIGGAgVAKGYHQKPdltqMKFTKnpFVSGERLYRTGDRACWLP---------NGTI 1895
Cdd:PRK07638 314 HNV---------QVRICNEAGEEVQKGE-IGTVYVKSP----QFFMG--YIIGGVLARELNADGWMTvrdvgyedeEGFI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1896 RLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAayIVPSDVNTNALRAALTKELPAYMIPAH 1974
Cdd:PRK07638 378 YIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVViGVPDSYWGEKPVA--IIKGSATKQQLKSFCLQRLSSFKIPKE 455
|
490 500
....*....|....*....|
gi 363747658 1975 LIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK07638 456 WHFVDEIPYTNSGKIARMEA 475
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1503-1994 |
6.77e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 108.82 E-value: 6.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1503 IFEAKAEEIPEHIAVI--DNEIEISYRFLNERANRLARTLQnRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPID 1578
Cdd:PRK05852 21 LVEVAATRLPEAPALVvtADRIAISYRDLARLVDDLAGQLT-RSGLLPgdRVALRMGSNAEFVVALLAASRADLVVVPLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1579 SHYPKARIEYILRDSGADILLLQQELKHlisnlPESEMSHICL--------DDESSYEENSCNLNLSPAP---------- 1640
Cdd:PRK05852 100 PALPIAEQRVRSQAAGARVVLIDADGPH-----DRAEPTTRWWpltvnvggDSGPSGGTLSVHLDAATEPtpatstpegl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1641 -EEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVcPDETR 1719
Cdd:PRK05852 175 rPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLL-PARGR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1720 LEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQF--KLPDLDILILGSDMVKAQDFKTLTDRFGQSMriINSYGVTE 1797
Cdd:PRK05852 254 FSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSgrKPAALRFIRSCSAPLTAETAQALQTEFAAPV--VCAFGMTE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1798 ATIDSSfyETSMGGEGTGDNvPIGSPLP-----NVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKN 1872
Cdd:PRK05852 332 ATHQVT--TTQIEGIGQTEN-PVVSTGLvgrstGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1873 PFvsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVPS 1951
Cdd:PRK05852 409 WL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVfGVPDQLYGEA-VAAVIVPR 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 363747658 1952 D---VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK05852 481 EsapPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1079-1453 |
7.69e-24 |
|
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: 107.01 E-value: 7.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1079 VLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGDPVQRIHDEV--PFTL---------QTTVLGERTEQEAAAAFI 1147
Cdd:cd19547 29 VLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLapPWALldwsgedpdRRAELLERLLADDRAAGL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1148 kpfDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNIL----IREFGELYNNR--NLPALRiQYKDYAVW-REGFK 1220
Cdd:cd19547 109 ---SLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIwgdvFRVYEELAHGRepQLSPCR-PYRDYVRWiRARTA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1221 TGDaykTQEAYWLKQLEgEL---PVLDLPADharppvRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFL 1297
Cdd:cd19547 185 QSE---ESERFWREYLR-DLtpsPFSTAPAD------REGEFDTVVHEFPEQLTRLVNEAARGYGVTTNAISQAAWSMLL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1298 SRLSGQEDIIVGSPIAGRPHK--DLEPILGMFVNTLALRTRPEGGKPFVQYLQEV-RETALEAfEHQDYPFEELVDKLEL 1374
Cdd:cd19547 255 ALQTGARDVVHGLTIAGRPPEleGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIhRDLATTA-AHGHVPLAQIKSWASG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1375 TRdMSRNPVFDAMFILQNVEKQDIDLREIKVRPANF-AHHISLFDITLIATEINgSICCEMEFSTEVFLKATIERWADHF 1453
Cdd:cd19547 334 ER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQIIDLhAQEKTEYPIGLIVLPLQ-KLAFHFNYDTTHFTRAQVDRFIEVF 411
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
453-942 |
1.03e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 108.20 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 453 VSPKAFTLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAG 532
Cdd:PRK07470 2 MSRRVMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 533 GAYLPLDPAYPKERLSYMLKDSGASLLLTQPG---------CSAPNFS------GETLEVDMTSLASEKAeNHEFTPA-- 595
Cdd:PRK07470 82 AVWVPTNFRQTPDEVAYLAEASGARAMICHADfpehaaavrAASPDLThvvaigGARAGLDYEALVARHL-GARVANAav 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 596 DGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTgmQHQ---FP-LSEDDIVMVKTSFSFDASVWQLFwwSLSGASAYLLP 671
Cdd:PRK07470 161 DHDDPCWFFFTSGTTGRPKAAVLTHGQMAFVIT--NHLadlMPgTTEQDASLVVAPLSHGAGIHQLC--QVARGAATVLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 672 PGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVLPQVsLIHGYGP 751
Cdd:PRK07470 237 PSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRY-DHSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 752 TEATvdAAFYVLDP----ERDRDRLRI-PIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFL 826
Cdd:PRK07470 315 GEVT--GNITVLPPalhdAEDGPDARIgTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 827 EDPFypgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEP--ELCAY 902
Cdd:PRK07470 393 DGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPvwGEVgvAVCVA 465
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 363747658 903 VEGLQRN--EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKL 942
Cdd:PRK07470 466 RDGAPVDeaELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
6-425 |
1.25e-23 |
|
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: 106.52 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 6 YSLTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTEYKYYPLRI 85
Cdd:cd19543 2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 86 IDFSNVEMIEIEQWIQ-----DQASiPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMKK 160
Cdd:cd19543 82 LDLSHLSEAEQEAELEalaeeDRER-GFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 161 KDPLPDQPEPSYLSYIekesQYLQSPRFAKDRLFWTQTFEHpleyhsLADQTSL-----QKQSTSASRDTII--LSPDLE 233
Cdd:cd19543 161 GQPPSLPPVRPYRDYI----AWLQRQDKEAAEAYWREYLAG------FEEPTPLpkelpADADGSYEPGEVSfeLSAELT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 234 QTIRIFCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAE--KEMLGMFVSSLPIRITVDPDTDFLSFVRT 311
Cdd:cd19543 231 ARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPgiETMVGLFINTLPVRVRLDPDQTVLELLKD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 312 IGREQLSVMRHQRFPynllVNELRN--EQKdlHNLIGISMQYQ--PLQ-----WHNADDFDYeTALYFSGYTANELSVQI 382
Cdd:cd19543 311 LQAQQLELREHEYVP----LYEIQAwsEGK--QALFDHLLVFEnyPVDesleeEQDEDGLRI-TDVSAEEQTNYPLTVVA 383
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 363747658 383 QERidnGTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHP 425
Cdd:cd19543 384 IPG---EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
459-941 |
1.49e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 107.97 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAI--RFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYL 536
Cdd:PRK08315 17 TIGQLLDRTAARYPDREALvyRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 537 PLDPAYPKERLSYMLKDSGASLLltqpgCSAPNFSG------------ETLEVDMTSLASEK-----------AENHEFT 593
Cdd:PRK08315 97 TINPAYRLSELEYALNQSGCKAL-----IAADGFKDsdyvamlyelapELATCEPGQLQSARlpelrrviflgDEKHPGM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 594 P------ADGGSLAY--------------VI---YTSGSTGQPKGVAVEHRQAVS--FLTGMQHQFplSEDD-------- 640
Cdd:PRK08315 172 LnfdellALGRAVDDaelaarqatldpddPIniqYTSGTTGFPKGATLTHRNILNngYFIGEAMKL--TEEDrlcipvpl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 641 -----IVM-VKTSFSfdasvwqlfwwslSGASayLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsD 714
Cdd:PRK08315 250 yhcfgMVLgNLACVT-------------HGAT--MVYPGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARF-D 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 715 RTSLkrvfaggeplapRTAARFASVLPQ------VSLIH------GYGPTEAT-------VDaafyvlDPErdrdRLRI- 774
Cdd:PRK08315 314 LSSL------------RTGIMAGSPCPIevmkrvIDKMHmsevtiAYGMTETSpvstqtrTD------DPL----EKRVt 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 775 PIGKPVPGARLYVLDPHL-AVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgerMYkTGDVARWLPDGNVEF 853
Cdd:PRK08315 372 TVGRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW-----MH-TGDLAVMDEEGYVNI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 854 LGRTDDQVkIR-GYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EG--LQRNEVRA----QLERllpg 921
Cdd:PRK08315 446 VGRIKDMI-IRgGENIYPREIEEFLYTHPKIQDVQVVGVPDEkyGE-EVCAWIilrPGatLTEEDVRDfcrgKIAH---- 519
|
570 580
....*....|....*....|
gi 363747658 922 YMVPAYMIEMEQWPVTPSGK 941
Cdd:PRK08315 520 YKIPRYIRFVDEFPMTVTGK 539
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
463-947 |
2.05e-23 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 107.38 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAftPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAylPLDPAY 542
Cdd:PRK10946 30 ILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 543 PKERL---SY--------MLKDSGASLL-------LTQPGCSAPN---FSGETLEVDMTSLASEKAENHEFTPADGGSLA 601
Cdd:PRK10946 106 SHQRSelnAYasqiepalLIADRQHALFsdddflnTLVAEHSSLRvvlLLNDDGEHSLDDAINHPAEDFTATPSPADEVA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 602 YVIYTSGSTGQPKGVAVEH-------RQAVS---------FLTGM--QHQFPLSEDDIVMVktsfsFDAsvwqlfwwsls 663
Cdd:PRK10946 186 FFQLSGGSTGTPKLIPRTHndyyysvRRSVEicgftpqtrYLCALpaAHNYPMSSPGALGV-----FLA----------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 664 GASAYLLP-PGwekdSALIVQAIHQENVTTAHFIPAMLNSFLDQ-AEIERLSDRTSLKRVFAGGEPLAPRTAARFASV-- 739
Cdd:PRK10946 250 GGTVVLAPdPS----ATLCFPLIEKHQVNVTALVPPAVSLWLQAiAEGGSRAQLASLKLLQVGGARLSETLARRIPAElg 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 740 --LPQVslihgYGPTEATVDaaFYVLDPerDRDRLRIPIGKPV-PGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLN 816
Cdd:PRK10946 326 cqLQQV-----FGMAEGLVN--YTRLDD--SDERIFTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 817 RPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS-- 894
Cdd:PRK10946 397 SPQHNASAFDANGFY------CSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDElm 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 895 GEPElCAYVegLQRNEVRA-QLERLLPG-----YMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK10946 471 GEKS-CAFL--VVKEPLKAvQLRRFLREqgiaeFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
34-425 |
2.28e-23 |
|
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: 105.47 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 34 VKFKGNIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTeYKYYPLRIIDFSNVEMiEIEQWIQDQASIPFkLINS 113
Cdd:cd19542 28 FDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVV-LKSLDPPIEEVETDED-SLDALTRDLLDDPT-LFGQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 114 PLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMkkkdplPDQPEPSYLSYIekesQYLQSPRFAKDRL 193
Cdd:cd19542 105 PPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQ------LLPPAPPFSDYI----SYLQSQSQEESLQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 194 FWTQTFE--HPLEYHSLADQTSLQKQSTSASRDTiilspdleQTIRIFCEEHKINIISLFMASFYICISRITSKKDLAIG 271
Cdd:cd19542 175 YWRKYLQgaSPCAFPSLSPKRPAERSLSSTRRSL--------AKLEAFCASLGVTLASLFQAAWALVLARYTGSRDVVFG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 272 TYYGNRG---SKAEkEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQLSVMRHQRFPYNLLVNELRNEQKDlhNLIGIS 348
Cdd:cd19542 247 YVVSGRDlpvPGID-DIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWPSG--TLFNTL 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 349 MQYQPLQWHNADDFDYETALYFSGYT-ANELSVQIQERIDNGTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHP 425
Cdd:cd19542 324 VSYQNFEASPESELSGSSVFELSAAEdPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1498-1950 |
2.46e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 107.35 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1498 VPFHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYI 1575
Cdd:PRK08314 10 TSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKgdRVLLYMQNSPQFVIAYYAILRANAVVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1576 PIDSHYPKARIEYILRDSGADILLLQQEL-------------KHLISN-------------LP-----ESEMSHICLDDE 1624
Cdd:PRK08314 90 PVNPMNREEELAHYVTDSGARVAIVGSELapkvapavgnlrlRHVIVAqysdylpaepeiaVPawlraEPPLQALAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1625 SSYEEnSCNLNLSPAPEEPVY-----IIYTSGTTGAPKGVIVTYRNFTHAALA---WRQiyeLDRKPVRLLQIASFSFDV 1696
Cdd:PRK08314 170 VAWKE-ALAAGLAPPPHTAGPddlavLPYTSGTTGVPKGCMHTHRTVMANAVGsvlWSN---STPESVVLAVLPLFHVTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1697 FSGDLARTLTNGGTLIVCPDETRLEPAEiykIMNSQRITVMESTPALIIPVMEYVYRNQFklpDLDILIL----GSDMVK 1772
Cdd:PRK08314 246 MVHSMNAPIYAGATVVLMPRWDREAAAR---LIERYRVTHWTNIPTMVVDFLASPGLAER---DLSSLRYigggGAAMPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1773 AQDFKtLTDRFGqsMRIINSYGVTEaTIdsSFyetsmggegTGDNVP-------IGSPLPNVHMYVLS-QTDQIQPIGVA 1844
Cdd:PRK08314 320 AVAER-LKELTG--LDYVEGYGLTE-TM--AQ---------THSNPPdrpklqcLGIPTFGVDARVIDpETLEELPPGEV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1845 GELCIGGAGVAKGYHQKPDLTQMKFTKnpfVSGERLYRTGDracwlpngtirlLGRMD---Y-----QVK--IN--GYRI 1912
Cdd:PRK08314 385 GEIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGD------------LGRMDeegYffitdRLKrmINasGFKV 449
|
490 500 510
....*....|....*....|....*....|....*....
gi 363747658 1913 ETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP 1950
Cdd:PRK08314 450 WPAEVENLLYKHPAIQEACViATPDPRRGET-VKAVVVL 487
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1641-1991 |
3.00e-23 |
|
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: 103.88 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1641 EEPVYIIYTSGTTGAPKGVIVTYRNFThAALAWRQIYEL----DRKPVRLLQIAsfsfdvFSGDLARTLT---NGGTLIV 1713
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFF-AVPDILQKEGLnwvvGDVTYLPLPAT------HIGGLWWILTcliHGGLCVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1714 CPDETRLEpaEIYKIMNSQRITVMESTPALIIP-VMEYVYRNQFkLPDLDILILGSDMVKAQDfKTLTDRFGQSmRIINS 1792
Cdd:cd17635 74 GGENTTYK--SLFKILTTNAVTTTCLVPTLLSKlVSELKSANAT-VPSLRLIGYGGSRAIAAD-VRFIEATGLT-NTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1793 YGVTEATiDSSFYETsmgGEGTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKN 1872
Cdd:cd17635 149 YGLSETG-TALCLPT---DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1873 PFVSGERLYRTGDracwlpnGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD 1952
Cdd:cd17635 225 WVNTGDLGERRED-------GFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 363747658 1953 V-NTNALRA---ALTKELPAYMIPAHLIPLENMPLTLNGKLDR 1991
Cdd:cd17635 298 ElDENAIRAlkhTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1521-1993 |
3.19e-23 |
|
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: 106.94 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1521 EIEISYRFLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIdsHYPK-----ARIEYILRDSGA 1595
Cdd:cd05931 22 EETLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL--PPPTpgrhaERLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1596 DILL----LQQELKHLISNLPESEMSHICLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAAL 1671
Cdd:cd05931 100 RVVLttaaALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1672 AWRQIYELDRK---------------------PV----RLLQIASFSFdvfsgdLARTLT-------NGGTLIVCPD--- 1716
Cdd:cd05931 180 QIRRAYGLDPGdvvvswlplyhdmgligglltPLysggPSVLMSPAAF------LRRPLRwlrlisrYRATISAAPNfay 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1717 ---ETRLEPAEiykimnsqritvmestpaliipvmeyvyrnqfkLPDLD-----ILILGSDMVKAQDFKTLTDRFG---- 1784
Cdd:cd05931 254 dlcVRRVRDED---------------------------------LEGLDlsswrVALNGAEPVRPATLRRFAEAFApfgf 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1785 --QSMRiiNSYGVTEAT----------------IDSSFYETSMGGEGTGDN-----VPIGSPLPNVHMYVL-SQTDQIQP 1840
Cdd:cd05931 301 rpEAFR--PSYGLAEATlfvsggppgtgpvvlrVDRDALAGRAVAVAADDPaarelVSCGRPLPDQEVRIVdPETGRELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1841 IGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTGDRAcWLPNGTIRLLGRMDYQVKINGYRIETEEIE-S 1919
Cdd:cd05931 379 DGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEaT 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1920 VLLQTGLVRE---AAVAVQHDKNGQAGLAAYIVPSDVNT------NALRAALTKE--LPAYMIpaHLIPLENMPLTLNGK 1988
Cdd:cd05931 458 AEEAHPALRPgcvAAFSVPDDGEERLVVVAEVERGADPAdlaaiaAAIRAAVAREhgVAPADV--VLVRPGSIPRTSSGK 535
|
....*
gi 363747658 1989 LDRNA 1993
Cdd:cd05931 536 IQRRA 540
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
468-888 |
3.98e-23 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 105.34 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 468 AAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERL 547
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 548 SYMLKDSGASLLLTqpGCSAPNFSGetlevDMTSLASEKAENHEFTPaDGGSLAYVIYTSGSTGQPKGVAVEHRQ----A 623
Cdd:PRK09029 93 EELLPSLTLDFALV--LEGENTFSA-----LTSLHLQLVEGAHAVAW-QPQRLATMTLTSGSTGLPKAAVHTAQAhlasA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 624 VSFLTGMQHQ--------FPLseddivmvktsfsFDAS----VWQlfwWSLSGASAYLlppgweKDSALIVQAIHQenVT 691
Cdd:PRK09029 165 EGVLSLMPFTaqdswllsLPL-------------FHVSgqgiVWR---WLYAGATLVV------RDKQPLEQALAG--CT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 692 TAHFIPAMLNSFLDQaeierLSDRTSLKRVFAGGeplaprtaarfaSVLPqVSLIH-----------GYGPTEA--TVDA 758
Cdd:PRK09029 221 HASLVPTQLWRLLDN-----RSEPLSLKAVLLGG------------AAIP-VELTEqaeqqgircwcGYGLTEMasTVCA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 759 AFYvlDPERDrdrlripIGKPVPGaRLYVLdphlavqpsgVAGELYIAGAGVARGYLNRPALTeerfledPFYPGERMYK 838
Cdd:PRK09029 283 KRA--DGLAG-------VGSPLPG-REVKL----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFA 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 363747658 839 TGDVARWLpDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 888
Cdd:PRK09029 336 TRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
774-1034 |
4.23e-23 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 102.14 E-value: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 774 IPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVA-RGYLNRPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVE 852
Cdd:COG3433 18 PVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLlRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 853 FLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEP--ELCAYVEGLQRNEVRAQLERLLPGY--MVPAYM 928
Cdd:COG3433 98 GLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGllLIVGAVAALDGLAAAAALAALDKVPpdVVAASA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 929 IEMEQWPVTPSGKLDRNALPAPGGAADAETYTAPRNVTEM-----KLSQLWEDVLKNGP--VGIHDNFFDRGGHSLKATA 1001
Cdd:COG3433 178 VVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETalteeELRADVAELLGVDPeeIDPDDNLFDLGLDSIRLMQ 257
|
250 260 270
....*....|....*....|....*....|...
gi 363747658 1002 LVSRiAKEFDVQVPLKDVFAHPTVEGLATVIRE 1034
Cdd:COG3433 258 LVER-WRKAGLDVSFADLAEHPTLAAWWALLAA 289
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
465-949 |
5.76e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 106.13 E-value: 5.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 465 ERQAA-FTPERLAIRFSGG----SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLD 539
Cdd:PRK04319 50 DRHADgGRKDKVALRYLDAsrkeKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 540 PAYPKERLSYMLKDSGASLLLTQPG------------------CSAPNFSGETLeVDMTSLASEKAENHEFTPADGGSLA 601
Cdd:PRK04319 130 EAFMEEAVRDRLEDSEAKVLITTPAllerkpaddlpslkhvllVGEDVEEGPGT-LDFNALMEQASDEFDIEWTDREDGA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 602 YVIYTSGSTGQPKGVAVEHrQAV--SFLTGmQHQFPLSEDDIvmvktsfsfdasvwqlFW------WsLSGASAYLLPPg 673
Cdd:PRK04319 209 ILHYTSGSTGKPKGVLHVH-NAMlqHYQTG-KYVLDLHEDDV----------------YWctadpgW-VTGTSYGIFAP- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 674 WEKDSALIV-----------QAIHQENVT---TAHFIPAMLNSFLDqaEIERLSDRTSLKRVFAGGEPLAPRtAARFA-S 738
Cdd:PRK04319 269 WLNGATNVIdggrfsperwyRILEDYKVTvwyTAPTAIRMLMGAGD--DLVKKYDLSSLRHILSVGEPLNPE-VVRWGmK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 739 VLPQVslIH-GYGPTE--ATVDAAFYVLDperdrdrLRI-PIGKPVPGARLYVLDPHLAVQPSGVAGELYIAgAG---VA 811
Cdd:PRK04319 346 VFGLP--IHdNWWMTEtgGIMIANYPAMD-------IKPgSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMM 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 812 RGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVR 891
Cdd:PRK04319 416 RGIWNNPEKYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGK 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 892 TDSGEPELC-AYV---EGLQ-----RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPA 949
Cdd:PRK04319 489 PDPVRGEIIkAFValrPGYEpseelKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1516-1994 |
6.25e-23 |
|
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: 104.48 E-value: 6.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1516 AVIDNEIEISYRFLNERANRLARTLQNRKGPKPTVAVLAkRSIDAIVGV---LAVMKAGGVYIPIDSHYPKARIEYILRD 1592
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLL-RGSNSPELVacwFGIQKAGAIAVATMPLLRPKELAYILDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1593 SgadilllqqelkhlisnlpesEMSHICLDDESSYEENSCNLNlspapeepvyiiYTSGTTGAPKGVIVTYRNFTHAALA 1672
Cdd:cd05958 82 A---------------------RITVALCAHALTASDDICILA------------FTSGTTGAPKATMHFHRDPLASADR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1673 W-RQIYELdRKPVRLLQIASFSFDV-FSGDLARTLTNGGTLIVCPDETrlePAEIYKIMNSQRITVMESTPALIIPVMEY 1750
Cdd:cd05958 129 YaVNVLRL-REDDRFVGSPPLAFTFgLGGVLLFPFGVGASGVLLEEAT---PDLLLSAIARYKPTVLFTAPTAYRAMLAH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1751 VYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATidsSFYETSMGGE---GTgdnvpIGSPLPNV 1827
Cdd:cd05958 205 PDAAGPDLSSLRKCVSAGEALPAALHRAWKEATG--IPIIDGIGSTEMF---HIFISARPGDarpGA-----TGKPVPGY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1828 HMYVLSQTDQIQPIGVAGELCIGGAgvaKGYHQKPDLTQMKFtknpfVSGERLYrTGDRACWLPNGTIRLLGRMDYQVKI 1907
Cdd:cd05958 275 EAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTY-----VQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1908 NGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV------PSDVNTNALRAALTKELPAYMIPAHLIPLENM 1981
Cdd:cd05958 346 GGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVlrpgviPGPVLARELQDHAKAHIAPYKYPRAIEFVTEL 425
|
490
....*....|...
gi 363747658 1982 PLTLNGKLDRNAL 1994
Cdd:cd05958 426 PRTATGKLQRFAL 438
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
484-944 |
6.42e-23 |
|
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: 104.83 E-value: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTqp 563
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 564 gcsapnfsgetlevdmtslaSEKAEnheftpadggsLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIV- 642
Cdd:cd05914 86 --------------------SDEDD-----------VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKIl 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 643 -MVKTSFSFDAsVWQLFWWSLSGASAYLLppgwEKDSALIVQAIHQENVTTAHFIPAML-------NSFLDQAEIER--- 711
Cdd:cd05914 135 sILPLHHIYPL-TFTLLLPLLNGAHVVFL----DKIPSAKIIALAFAQVTPTLGVPVPLviekifkMDIIPKLTLKKfkf 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 712 -----LSDRTSLKRVF---------------AGGEPLAPRTAARFASVlpQVSLIHGYGPTEATVDAAFYVldPERDRdr 771
Cdd:cd05914 210 klakkINNRKIRKLAFkkvheafggnikefvIGGAKINPDVEEFLRTI--GFPYTIGYGMTETAPIISYSP--PNRIR-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 772 lRIPIGKPVPGARLYVLDPhlavQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNV 851
Cdd:cd05914 284 -LGSAGKVIDGVEVRIDSP----DPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKIDAEGYL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 852 EFLGRTDDQ-VKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSG------EPELCAYVEGLQRN-------EVRAQLER 917
Cdd:cd05914 353 YIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLvalayiDPDFLDVKALKQRNiidaikwEVRDKVNQ 432
|
490 500
....*....|....*....|....*...
gi 363747658 918 LLPGY-MVPAYMIEMEQWPVTPSGKLDR 944
Cdd:cd05914 433 KVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
585-947 |
7.74e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 107.32 E-value: 7.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 585 EKAENHEFTPADggsLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSF--SFDASVwQLFWWSL 662
Cdd:PRK08633 772 KRLYGPTFKPDD---TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTV-TLWLPLL 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 663 SGASAYLLP-PgweKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARFASVLp 741
Cdd:PRK08633 848 EGIKVVYHPdP---TDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPL-MFASLRLVVAGAEKLKPEVADAFEEKF- 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 742 QVSLIHGYGPTEATVDAAFYVLDPERDRDRLRI-----PIGKPVPGARLYVLDPH-LAVQPSGVAGELYIAGAGVARGYL 815
Cdd:PRK08633 923 GIRILEGYGATETSPVASVNLPDVLAADFKRQTgskegSVGMPLPGVAVRIVDPEtFEELPPGEDGLILIGGPQVMKGYL 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 816 NRPALTEERFLEdpfYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSI--EGVREAAVTVRTD 893
Cdd:PRK08633 1003 GDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlgGEEVVFAVTAVPD 1079
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 894 S--GEPELCAYVEGLQRNE--VRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK08633 1080 EkkGEKLVVLHTCGAEDVEelKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1503-1994 |
8.72e-23 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 105.61 E-value: 8.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1503 IFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNrKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSH 1580
Cdd:PRK06155 26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAA-AGVKRgdRVALMCGNRIEFLDVFLGCAWLGAIAVPINTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1581 YPKARIEYILRDSGADILLLQQELKHLISNLPESEMS--HICLDDESSYEENSCNLNLSP-------------APEEPVY 1645
Cdd:PRK06155 105 LRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPlpAVWLLDAPASVSVPAGWSTAPlppldapapaaavQPGDTAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1646 IIYTSGTTGAPKGVIVtyrnfTHAALAWRQIY-----ELDRKPVRLLQIASFSFDVFSGdLARTLTNGGTLIVcpdETRL 1720
Cdd:PRK06155 185 ILYTSGTTGPSKGVCC-----PHAQFYWWGRNsaedlEIGADDVLYTTLPLFHTNALNA-FFQALLAGATYVL---EPRF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1721 EPAEIYKIMNSQRITVmestpALIIPVMEYVYRNQFKLPD-----LDILILGSdmVKAQDFKTLTDRFGqsMRIINSYGV 1795
Cdd:PRK06155 256 SASGFWPAVRRHGATV-----TYLLGAMVSILLSQPARESdrahrVRVALGPG--VPAALHAAFRERFG--VDLLDGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1796 TEAtidssfyetsmggegtgdNVPIGSPL------------PNVHMYVLSQTDQIQPIGVAGELCIGGA---GVAKGYHQ 1860
Cdd:PRK06155 327 TET------------------NFVIAVTHgsqrpgsmgrlaPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1861 KPDLTqMKFTKNPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNG 1940
Cdd:PRK06155 389 MPEKT-VEAWRNLW------FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELG 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 1941 QAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK06155 462 EDEVMAAVVLRDgtaLEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
463-947 |
8.87e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 105.49 E-value: 8.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSersPEML---IAVLAVLKAGGAYLPLD 539
Cdd:PRK07059 28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMM---PNVLqypVAIAAVLRAGYVVVNVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 540 PAYPKERLSYMLKDSGASLLLTqpgcsAPNFSGeTLE--VDMTSL----------------------------------- 582
Cdd:PRK07059 105 PLYTPRELEHQLKDSGAEAIVV-----LENFAT-TVQqvLAKTAVkhvvvasmgdllgfkghivnfvvrrvkkmvpawsl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 583 --------ASEKAENHEFTPAD--GGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQ--HQFPLS---EDDIVMVKTS 647
Cdd:PRK07059 179 pghvrfndALAEGARQTFKPVKlgPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEawLQPAFEkkpRPDQLNFVCA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 648 FS----FDASVWQLFWWSLsGASAYLLP-PgweKDSALIVQAIHQENVttaHFIPA---MLNSFLDQAEIERLsDRTSLK 719
Cdd:PRK07059 259 LPlyhiFALTVCGLLGMRT-GGRNILIPnP---RDIPGFIKELKKYQV---HIFPAvntLYNALLNNPDFDKL-DFSKLI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 720 RVFAGG----EPLAPRTAARFASvlpqvSLIHGYGPTE----ATVDAAfyvldperDRDRLRIPIGKPVPGARLYVLDPH 791
Cdd:PRK07059 331 VANGGGmavqRPVAERWLEMTGC-----PITEGYGLSEtspvATCNPV--------DATEFSGTIGLPLPSTEVSIRDDD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 792 LAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPG 871
Cdd:PRK07059 398 GNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFF------RTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 872 EIEAALRSIEGVREAAVTVRTD--SGEpELCAYV----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRN 945
Cdd:PRK07059 472 EIEEVVASHPGVLEVAAVGVPDehSGE-AVKLFVvkkdPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRR 550
|
..
gi 363747658 946 AL 947
Cdd:PRK07059 551 EL 552
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
484-888 |
9.01e-23 |
|
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: 104.19 E-value: 9.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLP----LDPAYPKERLsymlkDSGASLL 559
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRV-----DRGGAVY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 560 ltqpgcsapnfsgetlevdmtslasekAENHEFTPADGGSLAYviYTSGSTGQPKGVAVEHRQ-AVSFLTGMqHQFPLSE 638
Cdd:cd05974 76 ---------------------------AAVDENTHADDPMLLY--FTSGTTSKPKLVEHTHRSyPVGHLSTM-YWIGLKP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 639 DDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAHFIPAMLNSFLdQAEIERLsdRTSL 718
Cdd:cd05974 126 GDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLI-QQDLASF--DVKL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 719 KRVFAGGEPLAPRTAARFASVLpQVSLIHGYGPTEATVDAAFYVLDPERDRDrlripIGKPVPGARLYVLDPhlaVQPSG 798
Cdd:cd05974 203 REVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTETTALVGNSPGQPVKAGS-----MGRPLPGYRVALLDP---DGAPA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 799 VAGELYIA-----GAGVARGYLNRPALTEERfLEDPFYPgermykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEI 873
Cdd:cd05974 274 TEGEVALDlgdtrPVGLMKGYAGDPDKTAHA-MRGGYYR------TGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFEL 346
|
410
....*....|....*
gi 363747658 874 EAALRSIEGVREAAV 888
Cdd:cd05974 347 ESVLIEHPAVAEAAV 361
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1055-1360 |
9.46e-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: 103.15 E-value: 9.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1055 SSAQKRIYVLQQledggtgynmpaVLELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGDPVQRIHDEVPFT-LQTTV 1133
Cdd:cd19545 15 TARQPGAYVGQR------------VFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISwTESTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1134 LGERTEQEAAAafikPFDLSQaPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRNLPAlRIQYKDY- 1212
Cdd:cd19545 83 LDEYLEEDRAA----PMGLGG-PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PPPFSRFv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1213 ----AVWREGFKTgdayktqeaYWLKQLEGELPVL--DLPADHARPPVRSfagdkvsfTLDQEVASGLHKLARENGSTly 1286
Cdd:cd19545 157 kylrQLDDEAAAE---------FWRSYLAGLDPAVfpPLPSSRYQPRPDA--------TLEHSISLPSSASSGVTLAT-- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 1287 mVLLAAYTAFLSRLSGQEDIIVGSPIAGR--PHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEA--FEH 1360
Cdd:cd19545 218 -VLRAAWALVLSRYTGSDDVVFGVTLSGRnaPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMipFEH 294
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1508-1994 |
9.59e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 105.21 E-value: 9.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNE-IEISYRFLNERANRLARTLQNrKGPKPTVAV---LAKRSIDAIVgVLAVMKAGGVYIPIDSHYPK 1583
Cdd:PRK06087 33 ARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLA-KGIEPGDRVafqLPGWCEFTII-YLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1584 ARIEYILRDSGAD----------------ILLLQQELKHL-----ISNL----PESEMSHICLDDESSyeENSCNLNlsp 1638
Cdd:PRK06087 111 AELVWVLNKCQAKmffaptlfkqtrpvdlILPLQNQLPQLqqivgVDKLapatSSLSLSQIIADYEPL--TTAITTH--- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1639 aPEEPVYIIYTSGTTGAPKGVIVTYRN--FTHAA------LAWRQIYELdrkPVRLLQIASFsfdvFSGDLARTLTNGGT 1710
Cdd:PRK06087 186 -GDELAAVLFTSGTEGLPKGVMLTHNNilASERAycarlnLTWQDVFMM---PAPLGHATGF----LHGVTAPFLIGARS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1711 LIvcpdETRLEPAEIYKIMNSQRIT-VMESTPaLIIPVMEYVYRNQFKLPDLDILILGSDMVKAqdfKTLTDRFGQSMRI 1789
Cdd:PRK06087 258 VL----LDIFTPDACLALLEQQRCTcMLGATP-FIYDLLNLLEKQPADLSALRFFLCGGTTIPK---KVARECQQRGIKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1790 INSYGVTEAT------IDSSFyETSMGGEGTgdnvpigsPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPD 1863
Cdd:PRK06087 330 LSVYGSTESSphavvnLDDPL-SRFMHTDGY--------AAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1864 LTqmkftkNPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAG 1943
Cdd:PRK06087 401 LT------ARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGER 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 1944 LAAYIVPSD-VNTNALRAAL----TKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK06087 475 SCAYVVLKApHHSLTLEEVVaffsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1648-1994 |
1.07e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 105.29 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1648 YTSGTTGAPKGVIVTYRNF------THAALA---------WRQIYELDRKPVRLLQIASFSFD----VFSGdlartltNG 1708
Cdd:PRK12492 214 YTGGTTGLAKGAMLTHGNLvanmlqVRACLSqlgpdgqplMKEGQEVMIAPLPLYHIYAFTANcmcmMVSG-------NH 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1709 GTLIVCPdetRLEPAEIyKIMNSQRITVMESTPALIIPVMEYvyrNQFKLPDLDILIL----GSDMVKA--QDFKTLTdr 1782
Cdd:PRK12492 287 NVLITNP---RDIPGFI-KELGKWRFSALLGLNTLFVALMDH---PGFKDLDFSALKLtnsgGTALVKAtaERWEQLT-- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1783 fgqSMRIINSYGVTEAtidSSFYETSMGGE----GTgdnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGY 1858
Cdd:PRK12492 358 ---GCTIVEGYGLTET---SPVASTNPYGElarlGT-----VGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGY 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1859 HQKPDLTQmkftknPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVRE-AAVAVQHD 1937
Cdd:PRK12492 427 WQQPEATA------EALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANcAAIGVPDE 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 1938 KNGQAgLAAYIVPSD--VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK12492 501 RSGEA-VKLFVVARDpgLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1512-1994 |
1.29e-22 |
|
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: 104.30 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRS---IDAIVGVLAvmkAGGVYIPIDSHYPKARIE 1587
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGiSRGDTVAVLAPNTpamYELHFGVPM---AGAVLNALNTRLDAEEIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1588 YILRDSGADILLLQQELKH---LISNLPESEMshICLDDESsyeenscnlnlspapeEPVYIIYTSGTTGAPKGVIVTYR 1664
Cdd:cd12118 95 FILRHSEAKVLFVDREFEYedlLAEGDPDFEW--IPPADEW----------------DPIALNYTSGTTGRPKGVVYHHR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1665 NFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTlTNGGTLIVCPdetRLEPAEIYKIMNSQRITVMESTPALI 1744
Cdd:cd12118 157 GAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVA-AVGGTNVCLR---KVDAKAIYDLIEKHKVTHFCGAPTVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1745 IPVMEYVYRNQFKLPD-LDILILGSdmvkAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGEGTgdnvpigsP 1823
Cdd:cd12118 233 NMLANAPPSDARPLPHrVHVMTAGA----PPPAAVLAKMEELGFDVTHVYGLTETYGPATVCAWKPEWDEL--------P 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1824 LPN---------VHMYVLSQTDQIQPIGV---------AGELCIGGAGVAKGYHQKPDLtqmkfTKNPFVSGerLYRTGD 1885
Cdd:cd12118 301 TEErarlkarqgVRYVGLEEVDVLDPETMkpvprdgktIGEIVFRGNIVMKGYLKNPEA-----TAEAFRGG--WFHSGD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1886 RACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIV---PSDVNTNALRAA 1961
Cdd:cd12118 374 LAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVvARPDEKWGEV-PCAFVElkeGAKVTEEEIIAF 452
|
490 500 510
....*....|....*....|....*....|...
gi 363747658 1962 LTKELPAYMIPAHLIPLEnMPLTLNGKLDRNAL 1994
Cdd:cd12118 453 CREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1524-1994 |
2.93e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 104.07 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQ 1601
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHTDLKPgdRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1602 QELKHLISN-LPESEMSHIC-------------------------------------LDDESSYEENSCNLNLSPAPEEP 1643
Cdd:PRK05677 130 ANMAHLAEKvLPKTGVKHVIvtevadmlpplkrllinavvkhvkkmvpayhlpqavkFNDALAKGAGQPVTEANPQADDV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1644 VYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIY--------ELDRKPVRLLQIASFSFDVfsgdLARTLT-NGGTLIVC 1714
Cdd:PRK05677 210 AVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMgsnlnegcEILIAPLPLYHIYAFTFHC----MAMMLIgNHNILISN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1715 PdetRLEPAEIyKIMNSQRITVMESTPALIIPVMeyvyrNQFKLPDLDI----LILGSDMV----KAQDFKTLTdrfgqS 1786
Cdd:PRK05677 286 P---RDLPAMV-KELGKWKFSGFVGLNTLFVALC-----NNEAFRKLDFsalkLTLSGGMAlqlaTAERWKEVT-----G 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1787 MRIINSYGVTEATIDSSFYETSMGGEGTgdnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQ 1866
Cdd:PRK05677 352 CAICEGYGMTETSPVVSVNPSQAIQVGT-----IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1867 MKFTKNPFVsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQ-TGLVREAAVAVQHDKNGQAgLA 1945
Cdd:PRK05677 427 EILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAlPGVLQCAAIGVPDEKSGEA-IK 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 363747658 1946 AYIVP---SDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK05677 500 VFVVVkpgETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1523-1994 |
3.47e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 103.22 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1523 EISYRFLNERANRLAR---TLQNRKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILL 1599
Cdd:PRK08008 37 RYSYLELNEEINRTANlfySLGIRKGDK--VALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1600 LQQELKHLISNLPESE---MSHICLDDESSYEEN------------SCNLNLSPA--PEEPVYIIYTSGTTGAPKGVIVT 1662
Cdd:PRK08008 115 TSAQFYPMYRQIQQEDatpLRHICLTRVALPADDgvssftqlkaqqPATLCYAPPlsTDDTAEILFTSGTTSRPKGVVIT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1663 YRNFTHAAL--AWRQiyELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVcpdetrLE---PAEIYKIMNSQRITVM 1737
Cdd:PRK08008 195 HYNLRFAGYysAWQC--ALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVL------LEkysARAFWGQVCKYRATIT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1738 ESTPALI-----IPVMEyvYRNQFKLPDLDILILGSDMVKaQDFKTltdRFGqsMRIINSYGVTEaTI-----DSSFYE- 1806
Cdd:PRK08008 267 ECIPMMIrtlmvQPPSA--NDRQHCLREVMFYLNLSDQEK-DAFEE---RFG--VRLLTSYGMTE-TIvgiigDRPGDKr 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1807 --TSMGGEGTGDNVPI----GSPLPNvhmyvlsqtdqiqpiGVAGELCIGG-AG--VAKGYHQKPDLTQMKFTKNPFVsg 1877
Cdd:PRK08008 338 rwPSIGRPGFCYEAEIrddhNRPLPA---------------GEIGEICIKGvPGktIFKEYYLDPKATAKVLEADGWL-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1878 erlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VN 1954
Cdd:PRK08008 401 ----HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEgetLS 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 363747658 1955 TNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK08008 477 EEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
458-950 |
3.73e-22 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 103.30 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 458 FTLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLP 537
Cdd:PRK13382 43 MGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 538 LDPAYPKERLSYMLKDSGASLLL-------TQP----GCSAPNFSGE-TLEVDMTSLASEKAENHEFTPADGGSLAYVI- 604
Cdd:PRK13382 123 LNTSFAGPALAEVVTREGVDTVIydeefsaTVDralaDCPQATRIVAwTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVIl 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 605 YTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPL-SEDDIVMVKTSFSfdasVWQLFWWSLSGASAYLLPPGWEKDSALIVQ 683
Cdd:PRK13382 203 LTSGTTGTPKGARRSGPGGIGTLKAILDRTPWrAEEPTVIVAPMFH----AWGFSQLVLAASLACTIVTRRRFDPEATLD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 684 AIHQENVTTAHFIPAMLNSFLD-QAEIERLSDRTSLKRVFAGGEPLAP----RTAARFASVLpqvslIHGYGPTEATVDA 758
Cdd:PRK13382 279 LIDRHRATGLAVVPVMFDRIMDlPAEVRNRYSGRSLRFAAASGSRMRPdvviAFMDQFGDVI-----YNNYNATEAGMIA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 759 afyVLDPErdrDRLRIP--IGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYlnRPALTEErfledpFYPGerM 836
Cdd:PRK13382 354 ---TATPA---DLRAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD------FHDG--F 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 837 YKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV---EGLQ----- 907
Cdd:PRK13382 418 MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIgVDDEQYGQRLAAFVvlkPGASatpet 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 363747658 908 -RNEVRAQLERllpgYMVPAYMIEMEQWPVTPSGKLDRNALPAP 950
Cdd:PRK13382 498 lKQHVRDNLAN----YKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1522-1931 |
5.12e-22 |
|
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: 102.15 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1522 IEISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVyipidshyPkarieyILRDSGADIL 1598
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAygiRRGMR--AVLMVPPGPDFFALTFALFKAGAV--------P------VLIDPGMGRK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1599 LLQQelkhlisnlpesemshiCLDDEssyeENSCNLNLsPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYE 1678
Cdd:cd05910 65 NLKQ-----------------CLQEA----EPDAFIGI-PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1679 LDRKPVRLlqiASFS-FDVFSGDLARTltnggTLIVCPDETR---LEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRN 1754
Cdd:cd05910 123 IRPGEVDL---ATFPlFALFGPALGLT-----SVIPDMDPTRparADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQH 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1755 QFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMRIINSYGVTEA----TIDSS--FYETSMGGEGtGDNVPIGSPLPNVH 1828
Cdd:cd05910 195 GITLPSLRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEAlpvsSIGSRelLATTTAATSG-GAGTCVGRPIPGVR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1829 MYVLSQTDQ---------IQPIGVAGELCIGGAGVAKGYHQKPDLTqmKFTKNPFVSGERLYRTGDRACWLPNGTIRLLG 1899
Cdd:cd05910 274 VRIIEIDDEpiaewddtlELPRGEIGEITVTGPTVTPTYVNRPVAT--ALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCG 351
|
410 420 430
....*....|....*....|....*....|..
gi 363747658 1900 RMDYQVKINGYRIETEEIESVLLQTGLVREAA 1931
Cdd:cd05910 352 RKAHRVITTGGTLYTEPVERVFNTHPGVRRSA 383
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
484-903 |
5.45e-22 |
|
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: 102.68 E-value: 5.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGgayLPLDPAYP---KERLSYMLKDSGASLLL 560
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSAIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 561 TQPGCSapnfsgetlevdmtslasekaenheftpadggSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFP--LSE 638
Cdd:cd17639 83 TDGKPD--------------------------------DLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 639 DDIVM----VKTSFSFDASVWQLFWWSLSG-ASAYLL-------PPG--WE-KDSALI-VQAIHqENVTTAhfIPAMLN- 701
Cdd:cd17639 131 DDRYLaylpLAHIFELAAENVCLYRGGTIGyGSPRTLtdkskrgCKGdlTEfKPTLMVgVPAIW-DTIRKG--VLAKLNp 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 702 -SFLDQ-----------AEIERLSDRTSL-KRVFA---------------GGEPLAPRTAaRFASVL--PqvsLIHGYGP 751
Cdd:cd17639 208 mGGLKRtlfwtayqsklKALKEGPGTPLLdELVFKkvraalggrlrymlsGGAPLSADTQ-EFLNIVlcP---VIQGYGL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 752 TEaTVDAAFyVLDPErdrDRLRIPIGKPVPGARLYVLD-PHL-----AVQPSGvagELYIAGAGVARGYLNRPALTEERF 825
Cdd:cd17639 284 TE-TCAGGT-VQDPG---DLETGRVGPPLPCCEIKLVDwEEGgystdKPPPRG---EILIRGPNVFKGYYKNPEKTKEAF 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 826 LEDpfypgeRMYKTGDVARWLPDGNVEFLGRTDDQVKIR-GYRIEPGEIEAALRSIEGVreAAVTVRTDSGEPELCAYV 903
Cdd:cd17639 356 DGD------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLV--NNICVYADPDKSYPVAIV 426
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
481-947 |
6.25e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 102.92 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 481 GGSLTYAELDMYASRLAAHLaaRGITNESIVGVLSERSPEML---IAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGAS 557
Cdd:PRK05677 47 GKTLTYGELYKLSGAFAAWL--QQHTDLKPGDRIAVQLPNVLqypVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 558 LLL-----------------------TQPGCSAPNFSGETLE---------VDMTSL--------ASEKAENHEFTPAD- 596
Cdd:PRK05677 125 ALVclanmahlaekvlpktgvkhvivTEVADMLPPLKRLLINavvkhvkkmVPAYHLpqavkfndALAKGAGQPVTEANp 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 597 -GGSLAYVIYTSGSTGQPKGVAVEHRQAVSfltGMQHQFPLSEDDI-----VMVKT-------SFSFDASVWQLfwwslS 663
Cdd:PRK05677 205 qADDVAVLQYTGGTTGVAKGAMLTHRNLVA---NMLQCRALMGSNLnegceILIAPlplyhiyAFTFHCMAMML-----I 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 664 GASAYLLP-PgweKDSALIVQAIHQENVTTahFIPamLNSF---LDQAEIERLSDRTSLKRVFAGGEPLAPRTAARFASV 739
Cdd:PRK05677 277 GNHNILISnP---RDLPAMVKELGKWKFSG--FVG--LNTLfvaLCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 740 lPQVSLIHGYGPTEATVDAAFyvlDPerdRDRLRI-PIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRP 818
Cdd:PRK05677 350 -TGCAICEGYGMTETSPVVSV---NP---SQAIQVgTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 819 ALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVRE-AAVTVRTD-SGE 896
Cdd:PRK05677 423 EATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcAAIGVPDEkSGE 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 897 pELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK05677 497 -AIKVFVvvkpgETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1524-1991 |
6.25e-22 |
|
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: 103.34 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLA---RTLQNRKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILL- 1599
Cdd:cd05968 92 LTYGELLYEVKRLAnglRALGVGKGDR--VGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIt 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1600 ------------LQQELKHLISNLPESE----MSHICLD------DESSYEENSCNLNLSPA---PEEPVYIIYTSGTTG 1654
Cdd:cd05968 170 adgftrrgrevnLKEEADKACAQCPTVEkvvvVRHLGNDftpakgRDLSYDEEKETAGDGAErteSEDPLMIIYTSGTTG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1655 APKGVIVTYRNFthaalawrqiyeldrkPVRLLQIASFSFDVFSGDLAR----------------TLTNGGTLIV---CP 1715
Cdd:cd05968 250 KPKGTVHVHAGF----------------PLKAAQDMYFQFDLKPGDLLTwftdlgwmmgpwlifgGLILGATMVLydgAP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1716 DETrlEPAEIYKIMNSQRITVMESTPALIIPVMEYvyrnqfklpdldililGSDMVKAQDFKtltdrfgqSMRIINSYGv 1795
Cdd:cd05968 314 DHP--KADRLWRMVEDHEITHLGLSPTLIRALKPR----------------GDAPVNAHDLS--------SLRVLGSTG- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1796 teATID----SSFYETSMGGE--------------GTGDNVPI--------GSPLPNVHMYVLSqtDQIQPI-GVAGELC 1848
Cdd:cd05968 367 --EPWNpepwNWLFETVGKGRnpiinysggteisgGILGNVLIkpikpssfNGPVPGMKADVLD--ESGKPArPEVGELV 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1849 IGGA--GVAKGYHQKPDltqmKFTKNPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGL 1926
Cdd:cd05968 443 LLAPwpGMTRGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPA 518
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 1927 VRE-AAVAVQHDKNGQAgLAAYIV------PSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDR 1991
Cdd:cd05968 519 VLEsAAIGVPHPVKGEA-IVCFVVlkpgvtPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
483-962 |
7.80e-22 |
|
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: 103.16 E-value: 7.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 483 SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAG-------GAYLP------LDPAYPK----- 544
Cdd:cd05967 82 TYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAAkelasrIDDAKPKlivta 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 545 -------------ERLSYMLKDSG----ASLLLTQPGCSAPNFSGETlEVDMTSLASeKAENHEFTPADGGSLAYVIYTS 607
Cdd:cd05967 162 scgiepgkvvpykPLLDKALELSGhkphHVLVLNRPQVPADLTKPGR-DLDWSELLA-KAEPVDCVPVAATDPLYILYTS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 608 GSTGQPKGVAvehR----QAVSFLTGMQHQFPLSEDDIvmvktsfsfdasvwqlfWWSLS------------------GA 665
Cdd:cd05967 240 GTTGKPKGVV---RdnggHAVALNWSMRNIYGIKPGDV-----------------WWAASdvgwvvghsyivygpllhGA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 666 SAYL---LPPGWeKDSALIVQAIHQENVTTAHFIPAMLNS---FLDQAEIERLSDRTSLKRVFAGGEPLAPRTAARFASV 739
Cdd:cd05967 300 TTVLyegKPVGT-PDPGAFWRVIEKYQVNALFTAPTAIRAirkEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 740 LPqVSLIHGYGPTE-----ATVDAAFYVLDPerdrdRLRIPiGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAgVARGY 814
Cdd:cd05967 379 LG-VPVIDHWWQTEtgwpiTANPVGLEPLPI-----KAGSP-GKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGC 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 815 LNRPALTEERFLEDPF--YPGerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRT 892
Cdd:cd05967 451 LLTLWKNDERFKKLYLskFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVR 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 893 DS--GEPELCAYV--------EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPApggAADAETYTAP 962
Cdd:cd05967 529 DElkGQVPLGLVVlkegvkitAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK---IADGEDYTIP 605
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
452-947 |
7.87e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 102.33 E-value: 7.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 452 AVSPKAFtlhglFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKA 531
Cdd:PRK08162 17 PLTPLSF-----LERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 532 GgAYLP-----LDPaypkERLSYMLKDSGASLLLTQPGCSA---------------------PNFSGETL--EVDMTSLA 583
Cdd:PRK08162 92 G-AVLNtlntrLDA----ASIAFMLRHGEAKVLIVDTEFAEvarealallpgpkplvidvddPEYPGGRFigALDYEAFL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 584 SEKAENHEFT-PADGGSLAYVIYTSGSTGQPKGVAVEHR----QAVSFLT--GM-QHQfplseddiVMVKTSFSFDASVW 655
Cdd:PRK08162 167 ASGDPDFAWTlPADEWDAIALNYTSGTTGNPKGVVYHHRgaylNALSNILawGMpKHP--------VYLWTLPMFHCNGW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 656 qLFWWSLS---GASAYLlppgwEK-DSALIVQAIHQENVTtaHFIPA-MLNSFLDQAEIERLSDRTSLKRVFAGGEPLAP 730
Cdd:PRK08162 239 -CFPWTVAaraGTNVCL-----RKvDPKLIFDLIREHGVT--HYCGApIVLSALINAPAEWRAGIDHPVHAMVAGAAPPA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 731 RTAARFASVlpQVSLIHGYGPTE----ATVDAAFYVLD--PERDRDRLRIPIGKPVP---GARlyVLDPHlAVQPsgVA- 800
Cdd:PRK08162 311 AVIAKMEEI--GFDLTHVYGLTEtygpATVCAWQPEWDalPLDERAQLKARQGVRYPlqeGVT--VLDPD-TMQP--VPa 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 801 -----GELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEA 875
Cdd:PRK08162 384 dgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFH-------TGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVED 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 876 ALRSIEGVREAAVTVRTDS--GE-PelCAYVE---GLQ--RNEVRAQLERLLPGYMVPAyMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK08162 457 VLYRHPAVLVAAVVAKPDPkwGEvP--CAFVElkdGASatEEEIIAHCREHLAGFKVPK-AVVFGELPKTSTGKIQKFVL 533
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1519-1950 |
8.02e-22 |
|
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: 101.67 E-value: 8.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1519 DNEIEISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGA 1595
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSlgvKAGEK--VALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1596 DILLLqqelkhlisnlpesemshiclddessyeENScnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAAlawRQ 1675
Cdd:cd17640 79 VALVV----------------------------END--------SDDLATIIYTSGTTGNPKGVMLTHANLLHQI---RS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1676 IYELDRKPV--RLLQI--------ASFSFDVFSGDLARTLTNGGTLIvcPDETRLEPaeiykimnsqriTVMESTPALII 1745
Cdd:cd17640 120 LSDIVPPQPgdRFLSIlpiwhsyeRSAEYFIFACGCSQAYTSIRTLK--DDLKRVKP------------HYIVSVPRLWE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1746 PVMEYVYRNQFKLPDLDILILGSdMVKAQDFKTL----------TDRFGQS--MRIINSYGVTEATIDSSFYETSMGGEG 1813
Cdd:cd17640 186 SLYSGIQKQVSKSSPIKQFLFLF-FLSGGIFKFGisgggalpphVDTFFEAigIEVLNGYGLTETSPVVSARRLKCNVRG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1814 TgdnvpIGSPLPNVHMYVLS-QTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACWLPN 1892
Cdd:cd17640 265 S-----VGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCG 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 1893 GTIRLLGRM-DYQVKINGYRIETEEIESVLLQTGLVrEAAVAVQHDkngQAGLAAYIVP 1950
Cdd:cd17640 334 GELVLTGRAkDTIVLSNGENVEPQPIEEALMRSPFI-EQIMVVGQD---QKRLGALIVP 388
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
6-419 |
1.19e-21 |
|
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: 100.22 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 6 YSLTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTEYKYYPLRI 85
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 86 IDFSNVEMIE--IEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFA-KFHHIIMDGISLNVMGNQIIDLYQKMKKKD 162
Cdd:cd19536 82 LDLTPLEEQLdpLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLViSDHHSILDGWSLYLLVKEILAVYNQLLEYK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 163 PLPDQPEPSYLSYIEKE-SQYLQSPRFAkdrlFWTqtfehpleyHSLADQTS------LQKQSTSASRDT-IILSPDLEQ 234
Cdd:cd19536 162 PLSLPPAQPYRDFVAHErASIQQAASER----YWR---------EYLAGATLatlpalSEAVGGGPEQDSeLLVSVPLPV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 235 TIRIFCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNR--GSKAEKEMLGMFVSSLPIRITVdPDTDFLSFVRTI 312
Cdd:cd19536 229 RSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRseETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 313 GREQLSVMRHQRFPynllvneLRNEQKD---------LHNLIGISmQYQPLQWhNADDFDYETALYFSGYTAN---ELSV 380
Cdd:cd19536 308 QEQELESLSHEQVP-------LADIQRCsegeplfdsIVNFRHFD-LDFGLPE-WGSDEGMRRGLLFSEFKSNydvNLSV 378
|
410 420 430
....*....|....*....|....*....|....*....
gi 363747658 381 QIQEriDNGTIQlnFDYQNTLFSLEDIKRIQSHLLTILE 419
Cdd:cd19536 379 LPKQ--DRLELK--LAYNSQVLDEEQAQRLAAYYKSAIA 413
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
459-947 |
1.39e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 101.88 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAAR-GITNESIVGVLSERSPEMLIAVLAVLKAGGAYLP 537
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 538 LDPAYPKERLSYMLKDSGASLL------------------------------LTQPGCSAPNF--------------SGE 573
Cdd:PRK08751 106 VNPLYTPRELKHQLIDSGASVLvvidnfgttvqqviadtpvkqvittglgdmLGFPKAALVNFvvkyvkklvpeyriNGA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 574 TLEVDMTSLASE-KAENHEFTPADggsLAYVIYTSGSTGQPKGVAVEHR-------QAVSFLTGMQHQFPLSEDDIVMVK 645
Cdd:PRK08751 186 IRFREALALGRKhSMPTLQIEPDD---IAFLQYTGGTTGVAKGAMLTHRnlvanmqQAHQWLAGTGKLEEGCEVVITALP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 646 TSFSFDASVWQLFWWSLSGASAYLLPPgweKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFAGG 725
Cdd:PRK08751 263 LYHIFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQI-DFSSLKMTLGGG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 726 EPLAPRTAARFASVlPQVSLIHGYGPTEATVDAAFYVLD-PERDRDrlripIGKPVPGARLYVLDPHLAVQPSGVAGELY 804
Cdd:PRK08751 339 MAVQRSVAERWKQV-TGLTLVEAYGLTETSPAACINPLTlKEYNGS-----IGLPIPSTDACIKDDAGTVLAIGEIGELC 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 805 IAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR 884
Cdd:PRK08751 413 IKGPQVMKGYWKRPEETAKVMDADGWL------HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 885 E-AAVTVRTD-SGEPELCAYVE---GLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK08751 487 EvAAVGVPDEkSGEIVKVVIVKkdpALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1529-1997 |
1.74e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 100.93 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1529 LNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQELKHL 1607
Cdd:PRK12406 17 LAQRAARAAGGLAALGvRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1608 ISNLPESEMSHICL----DDESSY--EENSCNLNLS----------------PAPEEPVYIIYTSGTTGAPKGviVTYRN 1665
Cdd:PRK12406 97 LASALPAGVTVLSVptppEIAAAYriSPALLTPPAGaidwegwlaqqepydgPPVPQPQSMIYTSGTTGHPKG--VRRAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1666 FT-HAALAWRQ----IYELDRKPVRLL-----QIASFSFDVFSGDLartltnGGTLIVCPdetRLEPAEIYKIMNSQRIT 1735
Cdd:PRK12406 175 PTpEQAAAAEQmralIYGLKPGIRALLtgplyHSAPNAYGLRAGRL------GGVLVLQP---RFDPEELLQLIERHRIT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1736 VMESTPALIIPVM---EYVyRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmrIINSYGVTE---ATIDSSfyETSM 1809
Cdd:PRK12406 246 HMHMVPTMFIRLLklpEEV-RAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPV--IYEYYGSTEsgaVTFATS--EDAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1810 GGEGTgdnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAK-GYHQKPDltqmkftKNPFVSGERLYRTGDRAC 1888
Cdd:PRK12406 321 SHPGT-----VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPE-------KRAEIDRGGFITSGDVGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1889 WLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVP---SDVNTNALRAALTKE 1965
Cdd:PRK12406 389 LDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPqpgATLDEADIRAQLKAR 468
|
490 500 510
....*....|....*....|....*....|..
gi 363747658 1966 LPAYMIPAHLIPLENMPLTLNGKLDRNALPVP 1997
Cdd:PRK12406 469 LAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1502-1968 |
3.19e-21 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 100.74 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1502 RIFEAKAEEIPEHIAVID----------NEIEISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVM 1568
Cdd:PRK09274 10 RHLPRAAQERPDQLAVAVpggrgadgklAYDELSFAELDARSDAIAHGLNAagiGRGMR--AVLMVTPSLEFFALTFALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1569 KAGGVYIPIDSHYPKARIEYILRDSGADILLlQQELKHLISNL----PESEMSHICLDDE--------SSYEENSCNLNL 1636
Cdd:PRK09274 88 KAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI-GIPKAHLARRLfgwgKPSVRRLVTVGGRllwggttlATLLRDGAAAPF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1637 SPA---PEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLlqiASFS-FDVFSGDLartltnGGTLI 1712
Cdd:PRK09274 167 PMAdlaPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDL---PTFPlFALFGPAL------GMTSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1713 VCP-DETR---LEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMR 1788
Cdd:PRK09274 238 IPDmDPTRpatVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPDAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1789 IINSYGVTEA----TIDSS--FYETSMGGEgTGDNVPIGSPLPNVHMYVLSQTD----QIQ-----PIGVAGELCIGGAG 1853
Cdd:PRK09274 318 ILTPYGATEAlpisSIESReiLFATRAATD-NGAGICVGRPVDGVEVRIIAISDapipEWDdalrlATGEIGEIVVAGPM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1854 VAKGYHQKPDLTQMkfTKNPFVSGERLYRTGDrACWL-PNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLV-REAA 1931
Cdd:PRK09274 397 VTRSYYNRPEATRL--AKIPDGQGDVWHRMGD-LGYLdAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVkRSAL 473
|
490 500 510
....*....|....*....|....*....|....*..
gi 363747658 1932 VAVqhdKNGQAGLAAYIVPSDVNTNALRAALTKELPA 1968
Cdd:PRK09274 474 VGV---GVPGAQRPVLCVELEPGVACSKSALYQELRA 507
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1503-1991 |
5.04e-21 |
|
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: 99.88 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1503 IFEAKAEEIPEHIAVI-----DNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIP 1576
Cdd:cd05970 22 VVDAMAKEYPDKLALVwcddaGEERIFTFAELADYSDKTANFFKAMGiGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1577 IDSHYPKARIEYILRDSGADILL------LQQELKHLISNLPESEMSHICLDDES----SYEENSCNL---------NLS 1637
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVaiaednIPEEIEKAAPECPSKPKLVWVGDPVPegwiDFRKLIKNAspdferptaNSY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1638 PAPEEPVYIIYTSGTTGAPKGVivtYRNFTHaalawrqiyeldrkPVRLLQIASFSFDVFSGDLARTLTN---------- 1707
Cdd:cd05970 182 PCGEDILLVYFSSGTTGMPKMV---EHDFTY--------------PLGHIVTAKYWQNVREGGLHLTVADtgwgkavwgk 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1708 ------GGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPAliipvmeyVYR-------NQFKLPDLDILILGSDMVKAQ 1774
Cdd:cd05970 245 iygqwiAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPT--------IYRfliredlSRYDLSSLRYCTTAGEALNPE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1775 DFKTLTDRFGqsMRIINSYGVTEATIDSSFYETSMGGEGTgdnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGA-- 1852
Cdd:cd05970 317 VFNTFKEKTG--IKLMEGFGQTETTLTIATFPWMEPKPGS-----MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkg 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1853 ---GVAKGYHQKPDLTQMKFTknpfvsgERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVRE 1929
Cdd:cd05970 390 kpvGLFGGYYKDAEKTAEVWH-------DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLE 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 1930 AAV-AVQHDKNGQAgLAAYIV------PSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDR 1991
Cdd:cd05970 463 CAVtGVPDPIRGQV-VKATIVlakgyePSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1524-1994 |
6.09e-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: 341277 [Multi-domain] Cd Length: 437 Bit Score: 98.36 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHY-PKArIEYILRDSGADILLlq 1601
Cdd:cd05973 1 LTFGELRALSARFANALQELGvGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFgPKA-IEHRLRTSGARLVV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1602 qelkhlisnlpesemshiclddessyeensCNL-NLSPAPEEPVYIIYTSGTTGAPKGVIVTYRnfthAALAWR--QIYE 1678
Cdd:cd05973 78 ------------------------------TDAaNRHKLDSDPFVMMFTSGTTGLPKGVPVPLR----ALAAFGayLRDA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1679 LDRKP-VRLLQIAS--FSFDVFSGDLARTLTNGGTLIVcpdETRLEPAEIYKIMNSQRITVMESTPAliipvmeyVYRnq 1755
Cdd:cd05973 124 VDLRPeDSFWNAADpgWAYGLYYAITGPLALGHPTILL---EGGFSVESTWRVIERLGVTNLAGSPT--------AYR-- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1756 fklpdldILILGSDMVKAqdfktltdRFGQSMRIINSYG------VTE-------ATIDSSFYETSMG-----GEGTGDN 1817
Cdd:cd05973 191 -------LLMAAGAEVPA--------RPKGRLRRVSSAGepltpeVIRwfdaalgVPIHDHYGQTELGmvlanHHALEHP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1818 VPIGS---PLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVA----KGYHQKPDltqmkftknPFVSGeRLYRTGDRACWL 1890
Cdd:cd05973 256 VHAGSagrAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDT---------PAIDG-GYYLTGDTVEFD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1891 PNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV--PSDVNTNALRAALT----K 1964
Cdd:cd05973 326 PDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrGGHEGTPALADELQlhvkK 405
|
490 500 510
....*....|....*....|....*....|
gi 363747658 1965 ELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05973 406 RLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
451-856 |
6.75e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 100.12 E-value: 6.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 451 EAVSPKAFTLHGLFERQAAFTPER--LAIRFSGG----SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIA 524
Cdd:PRK12582 42 HPLGPYPRSIPHLLAKWAAEAPDRpwLAQREPGHgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 525 VLAVLKAGGAYLPLDPAYP-----KERLSYM---------LKDSGAsllLTQPGCSAPNFSGETL--------------- 575
Cdd:PRK12582 122 TLAAMQAGVPAAPVSPAYSlmshdHAKLKHLfdlvkprvvFAQSGA---PFARALAALDLLDVTVvhvtgpgegiasiaf 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 576 -EVDMTSLASEKAENHE-FTPAdggSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVktsfsfdas 653
Cdd:PRK12582 199 aDLAATPPTAAVAAAIAaITPD---TVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPV--------- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 654 vwQLFW--WS-------------LSGASAYL-----LPPGWEKdsalIVQAIHQENVTTAHFIP---AMLNSFLDQAEIE 710
Cdd:PRK12582 267 --SLDWmpWNhtmggnanfngllWGGGTLYIddgkpLPGMFEE----TIRNLREISPTVYGNVPagyAMLAEAMEKDDAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 711 RLSDRTSLKRVFAGG-----------EPLAPRTAARfasvlpQVSLIHGYGPTEA---TVDAAFyvlDPERDRDrlripI 776
Cdd:PRK12582 341 RRSFFKNLRLMAYGGatlsddlyermQALAVRTTGH------RIPFYTGYGATETaptTTGTHW---DTERVGL-----I 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 777 GKPVPGARLYVLdphlavqPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWL-PDGNVE--- 852
Cdd:PRK12582 407 GLPLPGVELKLA-------PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdPDDPEKgli 473
|
....
gi 363747658 853 FLGR 856
Cdd:PRK12582 474 FDGR 477
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
468-949 |
9.16e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 98.92 E-value: 9.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 468 AAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERL 547
Cdd:PRK13383 45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 548 SYMLKDSGASLLLTQPGcSAPNFSGETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGV--AVEHRQAVS 625
Cdd:PRK13383 125 AAALRAHHISTVVADNE-FAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRIVLLTSGTTGKPKGVprAPQLRSAVG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 626 FLTGMQHQFPLSEDDIVMVKTSFsFDASVWQLFWWSLSGASAYLLPPGWEKDSALIVQAIHQENVTTAhfIPAMLNSFLD 705
Cdd:PRK13383 204 VWVTILDRTRLRTGSRISVAMPM-FHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTA--VPVVLARILE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 706 QAEIERLSDR-TSLKRVFAGGEPLAPRTAARFASVLPQVsLIHGYGPTEATVDAafyVLDPERDRDRLRIpIGKPVPGAR 784
Cdd:PRK13383 281 LPPRVRARNPlPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGIGA---LATPADLRDAPET-VGKPVAGCP 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 785 LYVLDPHlaVQPSG--VAGELYIAGAGVARGYLN--RPALTEErfledpfypgerMYKTGDVARWLPDGNVEFLGRTDDQ 860
Cdd:PRK13383 356 VRILDRN--NRPVGprVTGRIFVGGELAGTRYTDggGKAVVDG------------MTSTGDMGYLDNAGRLFIVGREDDM 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 861 VKIRGYRIEPGEIEAALRSIEGVREAAVT-VRTDSGEPELCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQW 934
Cdd:PRK13383 422 IISGGENVYPRAVENALAAHPAVADNAVIgVPDERFGHRLAAFVvlhpgSGVDAAQLRDYLKDRVSRFEQPRDINIVSSI 501
|
490
....*....|....*
gi 363747658 935 PVTPSGKLDRNALPA 949
Cdd:PRK13383 502 PRNPTGKVLRKELPG 516
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
465-947 |
9.58e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 98.61 E-value: 9.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 465 ERQAAFTPERLA-IRFSGG-SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAY 542
Cdd:PRK13391 4 GIHAQTTPDKPAvIMASTGeVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 543 PKERLSYMLKDSGASLLLT--QPGCSAPNFSGET------LEVDMTSlASEKAENHE-------FTPADGGSL-AYVIYT 606
Cdd:PRK13391 84 TPAEAAYIVDDSGARALITsaAKLDVARALLKQCpgvrhrLVLDGDG-ELEGFVGYAeavaglpATPIADESLgTDMLYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 607 SGSTGQPKGVAVehrqavsfltgmqhqfPLSEDDIVMVKTSFSFDASVWQ------------------LFWWSL---SGA 665
Cdd:PRK13391 163 SGTTGRPKGIKR----------------PLPEQPPDTPLPLTAFLQRLWGfrsdmvylspaplyhsapQRAVMLvirLGG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 666 SAYLLppgwEK-DSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLS-DRTSLKRVFAGGEPLAPRTAARFASVLPQV 743
Cdd:PRK13391 227 TVIVM----EHfDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKyDLSSLEVAIHAAAPCPPQVKEQMIDWWGPI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 744 slIHG-YGPTEAtvdAAFYVLDPERDRDRlRIPIGKPVPGaRLYVLDPHLAVQPSGVAGELYIAGaGVARGYLNRPALTE 822
Cdd:PRK13391 303 --IHEyYAATEG---LGFTACDSEEWLAH-PGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 823 ERFLEDPfypgeRMYKTGDVARWLPDGnveFLGRTDDQVKI---RGYRIEPGEIEAALRSIEGVREAAV--TVRTDSGEp 897
Cdd:PRK13391 375 EARHPDG-----TWSTVGDIGYVDEDG---YLYLTDRAAFMiisGGVNIYPQEAENLLITHPKVADAAVfgVPNEDLGE- 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 898 ELCAYV---EGLQRN-----EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK13391 446 EVKAVVqpvDGVDPGpalaaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
484-947 |
1.05e-20 |
|
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: 97.92 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSgasllltqp 563
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEA--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 564 gcsAPN-FSGETLEVDMtslasekaenheftpadggslAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIV 642
Cdd:cd05910 74 ---EPDaFIGIPKADEP---------------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 643 MvkTSFSFDAsvwqLFWWSLSGASAylLP------PGwEKDSALIVQAIHQENVTTAHFIPAMLnsfldqaeiERLS--- 713
Cdd:cd05910 130 L--ATFPLFA----LFGPALGLTSV--IPdmdptrPA-RADPQKLVGAIRQYGVSIVFGSPALL---------ERVAryc 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 714 ---DRT--SLKRVFAGGEPLAPRTAARFASVL-PQVSLIHGYGPTEATVDAAFYVLDPERDR----DRLR-IPIGKPVPG 782
Cdd:cd05910 192 aqhGITlpSLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEALPVSSIGSRELLATTtaatSGGAgTCVGRPIPG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 783 ARLYVL----------DPHLAVqPSGVAGELYIAGAGVARGYLNRPALTEERFLEDpfyPGERM-YKTGDVARWLPDGNV 851
Cdd:cd05910 272 VRVRIIeiddepiaewDDTLEL-PRGEIGEITVTGPTVTPTYVNRPVATALAKIDD---NSEGFwHRMGDLGYLDDEGRL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 852 EFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAA-VTVRTDSG-------EPELCAYVEGLQ-RNEVRAQLERLLPGY 922
Cdd:cd05910 348 WFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAlVGVGKPGCqlpvlcvEPLPGTITPRARlEQELRALAKDYPHTQ 427
|
490 500
....*....|....*....|....*..
gi 363747658 923 MVPAYMIEmEQWPVTP--SGKLDRNAL 947
Cdd:cd05910 428 RIGRFLIH-PSFPVDIrhNAKIFREKL 453
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
457-949 |
1.22e-20 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 98.76 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 457 AFTLHGLFERQAAFTPERLAIRFsgGSLTYAELDMY--ASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGA 534
Cdd:PLN02479 19 ALTPLWFLERAAVVHPTRKSVVH--GSVRYTWAQTYqrCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 535 YLPLDPAYPKERLSYMLKDSGASLLLTQPgcsapNFSgeTLEVDMTSLASEKAENhEFTPA----------DGGSLAYVI 604
Cdd:PLN02479 97 VNCVNIRLNAPTIAFLLEHSKSEVVMVDQ-----EFF--TLAEEALKILAEKKKS-SFKPPllivigdptcDPKSLQYAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 605 ---------------------------------YTSGSTGQPKGVAVEHRQA------VSFLTGMQhqfplseDDIVMVK 645
Cdd:PLN02479 169 gkgaieyekfletgdpefawkppadewqsialgYTSGTTASPKGVVLHHRGAylmalsNALIWGMN-------EGAVYLW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 646 TSFSFDASVWqLFWWSL---SGASAYLLppgwEKDSALIVQAIHQENVTtaHFI--PAMLNSFLDQAEIERLSDRTSLKR 720
Cdd:PLN02479 242 TLPMFHCNGW-CFTWTLaalCGTNICLR----QVTAKAIYSAIANYGVT--HFCaaPVVLNTIVNAPKSETILPLPRVVH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 721 VFAGGeplaprtAARFASVLPQVS-----LIHGYGPTEATVDAAFYVLDPERD------RDRLRIPIGKPVPG-ARLYVL 788
Cdd:PLN02479 315 VMTAG-------AAPPPSVLFAMSekgfrVTHTYGLSETYGPSTVCAWKPEWDslppeeQARLNARQGVRYIGlEGLDVV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 789 DPH-LAVQPS--GVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGDVARWLPDGNVEFLGRTDDQVKIRG 865
Cdd:PLN02479 388 DTKtMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFH-------SGDLGVKHPDGYIEIKDRSKDIIISGG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 866 YRIEPGEIEAALRSIEGVREAAVTVRTDS--GEPElCAYV---EGLQRNEVRAQLERL-------LPGYMVPAYMIeMEQ 933
Cdd:PLN02479 461 ENISSLEVENVVYTHPAVLEASVVARPDErwGESP-CAFVtlkPGVDKSDEAALAEDImkfcrerLPAYWVPKSVV-FGP 538
|
570
....*....|....*.
gi 363747658 934 WPVTPSGKLDRNALPA 949
Cdd:PLN02479 539 LPKTATGKIQKHVLRA 554
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1805-2085 |
1.31e-20 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 94.82 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1805 YETSMGGEGTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGElcIGGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYRTG 1884
Cdd:COG3433 5 TPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGE--GGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1885 DRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQH----DKNGQAGLAAYIVPSDVNTNALRA 1960
Cdd:COG3433 83 DDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAalrgAGVGLLLIVGAVAALDGLAAAAAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1961 ALTKELPAYMIPAHLIP-LENMPLTLNGKLDRNALPVPNNVLSRPYTAPVND-----IQKTMAYIWEDVLSMS--RVGIH 2032
Cdd:COG3433 163 AALDKVPPDVVAASAVVaLDALLLLALKVVARAAPALAAAEALLAAASPAPAletalTEEELRADVAELLGVDpeEIDPD 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 363747658 2033 DSFFELGGDSIKALQVAARLAAEGWSMTIRDLFRYSTIQELCGHITPLASQAD 2085
Cdd:COG3433 243 DNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1508-1989 |
2.57e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 97.42 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNR---KGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKA 1584
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARgvrKGDR--ILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1585 RIEYILRDSGADILLLQQEL-KHL-ISNLPESEMSHICLDDESSYEEN-----SCNLNLSPAP-----EEPVYIIYTSGT 1652
Cdd:PRK07470 95 EVAYLAEASGARAMICHADFpEHAaAVRAASPDLTHVVAIGGARAGLDyealvARHLGARVANaavdhDDPCWFFFTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1653 TGAPKGVIVTYRNFT-----HAALAWRQIYELDRKPV-----------RLLQIAsfsfdvfsgdlartltNGGTLIVCPD 1716
Cdd:PRK07470 175 TGRPKAAVLTHGQMAfvitnHLADLMPGTTEQDASLVvaplshgagihQLCQVA----------------RGAATVLLPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1717 EtRLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILIL-GSDMVKAqDFKTLTDRFGQSmrIINSYGV 1795
Cdd:PRK07470 239 E-RFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYaGAPMYRA-DQKRALAKLGKV--LVQYFGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1796 TEATIDSSFYETSMGGEGTGDNVPIGS-PLPNVHMYVLSQTDQIQPI--GVAGELCIGGAGVAKGYHQKPDLTQMKFTKN 1872
Cdd:PRK07470 315 GEVTGNITVLPPALHDAEDGPDARIGTcGFERTGMEVQIQDDEGRELppGETGEICVIGPAVFAGYYNNPEANAKAFRDG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1873 PFvsgerlyRTGDracwlpngtirlLGRMDYQ--VKING-----Y-----RIETEEIESVLLQTGLVREAAV-AVQHDKN 1939
Cdd:PRK07470 395 WF-------RTGD------------LGHLDARgfLYITGrasdmYisggsNVYPREIEEKLLTHPAVSEVAVlGVPDPVW 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 363747658 1940 GQAGLAAyIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKL 1989
Cdd:PRK07470 456 GEVGVAV-CVARDgapVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1504-1997 |
2.66e-20 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 97.52 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1504 FEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRKGPKP-TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYP 1582
Cdd:PRK13382 49 FAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPrVVGIMCRNHRGFVEALLAANRIGADILLLNTSFA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1583 KARIEYILRDSGADILLLQQELKHLI----SNLPESEMSHICLDDESSYE-----ENSCNLNLSPAPEEPVYIIYTSGTT 1653
Cdd:PRK13382 129 GPALAEVVTREGVDTVIYDEEFSATVdralADCPQATRIVAWTDEDHDLTvevliAAHAGQRPEPTGRKGRVILLTSGTT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1654 GAPKGvivTYRNFTHAALAWRQIyeLDRKPVRLLQ---IAS-------FSFDVFSGDLARTLTNggtlivcpdETRLEPA 1723
Cdd:PRK13382 209 GTPKG---ARRSGPGGIGTLKAI--LDRTPWRAEEptvIVApmfhawgFSQLVLAASLACTIVT---------RRRFDPE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1724 EIYKIMNSQRITVMESTPALIIPVMEYV--YRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmrIINSYGVTEAtid 1801
Cdd:PRK13382 275 ATLDLIDRHRATGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV--IYNNYNATEA--- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1802 ssfyetSMGGEGTGDNV-----PIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDltqmKFTKNPFVS 1876
Cdd:PRK13382 350 ------GMIATATPADLraapdTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGST----KDFHDGFMA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1877 gerlyrTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVPSD--- 1952
Cdd:PRK13382 420 ------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAViGVDDEQYGQR-LAAFVVLKPgas 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 363747658 1953 VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVP 1997
Cdd:PRK13382 493 ATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
484-925 |
2.97e-20 |
|
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: 96.65 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAylpldpaypkerlsymlkdsgasllltqP 563
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV----------------------------A 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 564 GCSAPNFSGETLEvdmtslasekaenHEFTPADGGSL----AYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSED 639
Cdd:cd05940 56 ALINYNLRGESLA-------------HCLNVSSAKHLvvdaALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 640 DIVMvkTSFSFDASVWQLFWWS---LSGASAYLLppgwEKDSAL-IVQAIHQENVTTAHFIPAMLNSFLDQAEIErLSDR 715
Cdd:cd05940 123 DVLY--TCLPLYHSTALIVGWSaclASGATLVIR----KKFSASnFWDDIRKYQATIFQYIGELCRYLLNQPPKP-TERK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 716 TSLKRVFAGGepLAP----RTAARFAsvLPQVSLIhgYGPTEATVdaAFYVLD---------PERDRDRLRIPI------ 776
Cdd:cd05940 196 HKVRMIFGNG--LRPdiweEFKERFG--VPRIAEF--YAATEGNS--GFINFFgkpgaigrnPSLLRKVAPLALvkydle 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 777 -GKPVPGARLYVLDphlavQPSGVAGEL--YIAGAGVARGYLNrPALTEERFLEDPFYPGERMYKTGDVARWLPDGNVEF 853
Cdd:cd05940 268 sGEPIRDAEGRCIK-----VPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYF 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 854 LGRTDDQVKIRGYRIEPGEIEAALRSIEGVREA---AVTVRTDSGEPELCAYV----EGLQRNEVRAQLERLLPGYMVP 925
Cdd:cd05940 342 VDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEAnvyGVQVPGTDGRAGMAAIVlqpnEEFDLSALAAHLEKNLPGYARP 420
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
496-945 |
3.76e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 97.18 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 496 LAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQPGCSA-------- 567
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSwyeelqnd 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 568 --PN------------------FSGETLEVDMTSLASEKAENHEFTPADggsLAYVIYTSGSTGQPKGVAVEHR----QA 623
Cdd:PLN02860 125 rlPSlmwqvflespsssvfiflNSFLTTEMLKQRALGTTELDYAWAPDD---AVLICFTSGTTGRPKGVTISHSalivQS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 624 VSFLTGMQHqfplSEDDiVMVKTS--------FSFDASVwqlfwwsLSGASAYLLPpgwEKDSALIVQAIHQENVTTAHF 695
Cdd:PLN02860 202 LAKIAIVGY----GEDD-VYLHTAplchigglSSALAML-------MVGACHVLLP---KFDAKAALQAIKQHNVTSMIT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 696 IPAMLNSFLDQAEIERLSD-RTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVL-DPERDRDRLR 773
Cdd:PLN02860 267 VPAMMADLISLTRKSMTWKvFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLhDPTLESPKQT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 774 IP-----------------IGKPVPGARLYVLDPHlavqpSGVAGELYIAGAGVARGYLNRPALTEERFledpfyPGERM 836
Cdd:PLN02860 347 LQtvnqtksssvhqpqgvcVGKPAPHVELKIGLDE-----SSRVGRILTRGPHVMLGYWGQNSETASVL------SNDGW 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 837 YKTGDVArWLPD-GNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEPELCAYV----EGLQRNEV 911
Cdd:PLN02860 416 LDTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACvrlrDGWIWSDN 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 363747658 912 RAQLERL-----------------LPGYMVP-AYMIEMEQWPVTPSGKLDRN 945
Cdd:PLN02860 495 EKENAKKnltlssetlrhhcreknLSRFKIPkLFVQWRKPFPLTTTGKIRRD 546
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
463-904 |
3.83e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 97.32 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERqAAFTPERLAIRF------SGG---SLTYAELDMYASRLAAHLAARGITNESIVgVLSERSPEMLIAVLAVLKAGG 533
Cdd:PRK05850 7 LRER-ASLQPDDAAFTFidyeqdPAGvaeTLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQAGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 534 AYLPLDPAYP---KERLSYMLKDSGASLLLT--------------QPGCSAPNFsgetLEVDMTSLASEKAENheFTPAD 596
Cdd:PRK05850 85 IAVPLSVPQGgahDERVSAVLRDTSPSVVLTtsavvddvteyvapQPGQSAPPV----IEVDLLDLDSPRGSD--ARPRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 597 GGSLAYVIYTSGSTGQPKGVAVEHRQA-VSFLTGMQHQFPLSEDDIVMVKTSFSfdasvWQLFWWS-----------LSG 664
Cdd:PRK05850 159 LPSTAYLQYTSGSTRTPAGVMVSHRNViANFEQLMSDYFGDTGGVPPPDTTVVS-----WLPFYHDmglvlgvcapiLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 665 ASAYLLPP-GWEKDSALIVQAIhqenVTTAHFIPAMLNSFLDQAeierlSDRTS--------LKRVFA---GGEPLAPRT 732
Cdd:PRK05850 234 CPAVLTSPvAFLQRPARWMQLL----ASNPHAFSAAPNFAFELA-----VRKTSdddmagldLGGVLGiisGSERVHPAT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 733 AARFASV-----LPQVSLIHGYGPTEATVdaafYVLDPERDR-------DRLRIPIGKPVP-----GARL--Y------- 786
Cdd:PRK05850 305 LKRFADRfapfnLRETAIRPSYGLAEATV----YVATREPGQppesvrfDYEKLSAGHAKRcetggGTPLvsYgsprspt 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 787 --VLDPHLAVQ-PSGVAGELYIAGAGVARGYLNRPALTEERF---LEDPF--YPGERMYKTGDVArWLPDGNVEFLGRTD 858
Cdd:PRK05850 381 vrIVDPDTCIEcPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSpgTPEGPWLRTGDLG-FISEGELFIVGRIK 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 363747658 859 DQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSGEpELCAYVE 904
Cdd:PRK05850 460 DLLIVDGRNHYPDDIEATIQEITGGRVAAISVPDDGTE-KLVAIIE 504
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
484-849 |
5.50e-20 |
|
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: 96.52 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGIT--NESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLT 561
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 562 QPGCSApnFSGETLEvDMTslaseKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQ----FPLS 637
Cdd:cd05927 86 DAGVKV--YSLEEFE-KLG-----KKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKIleilNKIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 638 EDDI-------------VMVKTSFSFDASVWqlFWwslSGASAYLLP----------PG----WEKdsalIVQAIHQENV 690
Cdd:cd05927 158 PTDVyisylplahiferVVEALFLYHGAKIG--FY---SGDIRLLLDdikalkptvfPGvprvLNR----IYDKIFNKVQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 691 TTAHFIPAMLNSFLD--QAEIERLSDRTSL---KRVF---------------AGGEPLAPRTaARFASVLPQVSLIHGYG 750
Cdd:cd05927 229 AKGPLKRKLFNFALNykLAELRSGVVRASPfwdKLVFnkikqalggnvrlmlTGSAPLSPEV-LEFLRVALGCPVLEGYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 751 PTEATvdAAFYVLDPerdRDRLRIPIGKPVPGA--RL--------YVLDPHLavqpsgvAGELYIAGAGVARGYLNRPAL 820
Cdd:cd05927 308 QTECT--AGATLTLP---GDTSVGHVGGPLPCAevKLvdvpemnyDAKDPNP-------RGEVCIRGPNVFSGYYKDPEK 375
|
410 420
....*....|....*....|....*....
gi 363747658 821 TEERFLEDPFypgermYKTGDVARWLPDG 849
Cdd:cd05927 376 TAEALDEDGW------LHTGDIGEWLPNG 398
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
444-947 |
6.93e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 96.63 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 444 LCEFNKTeAVSPKAFtlhglFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLI 523
Cdd:PLN03102 6 LCEANNV-PLTPITF-----LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 524 AVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLL---------------LTQPGCSAPNFSGETL-EVDMTSLASEKA 587
Cdd:PLN03102 80 MHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILfvdrsfeplarevlhLLSSEDSNLNLPVIFIhEIDFPKRPSSEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 588 ENHEF-------TPADGGSLAYVI---------YTSGSTGQPKGVAVEHRQA----VSFLTGMQH-QFPlseddiVMVKT 646
Cdd:PLN03102 160 LDYECliqrgepTPSLVARMFRIQdehdpislnYTSGTTADPKGVVISHRGAylstLSAIIGWEMgTCP------VYLWT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 647 SFSFDASVWQLFWWSLS--GASA---YLLPPGwekdsalIVQAIHQENVTTAHFIPAMLNSFLDQAEIErLSDRTSLKRV 721
Cdd:PLN03102 234 LPMFHCNGWTFTWGTAArgGTSVcmrHVTAPE-------IYKNIEMHNVTHMCCVPTVFNILLKGNSLD-LSPRSGPVHV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 722 FAGGEPLAPRTAARFASVLPQVslIHGYGPTEATVDAAF------YVLDPERDRDRLRIPIGKPVPG-ARLYVLDPHL-- 792
Cdd:PLN03102 306 LTGGSPPPAALVKKVQRLGFQV--MHAYGLTEATGPVLFcewqdeWNRLPENQQMELKARQGVSILGlADVDVKNKETqe 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 793 AVQPSG-VAGELYIAGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPG 871
Cdd:PLN03102 384 SVPRDGkTMGEIVIKGSSIMKGYLKNPKATSEAFKHG-------WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 872 EIEAALRSIEGVREAAVT--------------VRTDSGEPELCAYVEGLQRNEvRAQLERL---LPGYMVPAYMIEMEQW 934
Cdd:PLN03102 457 EVENVLYKYPKVLETAVVamphptwgetpcafVVLEKGETTKEDRVDKLVTRE-RDLIEYCrenLPHFMCPRKVVFLQEL 535
|
570
....*....|...
gi 363747658 935 PVTPSGKLDRNAL 947
Cdd:PLN03102 536 PKNGNGKILKPKL 548
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
474-960 |
7.06e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 96.25 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 474 RLAIRFSGGSLTYAE-LDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLK 552
Cdd:PRK13388 17 TIAVRYGDRTWTWREvLAEAAARAAALIALADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 553 DSGASLLLTQPG----CSAPNFSGET-LEVDMTSLASEKAENHEFTPA---DGGSLAYVIYTSGSTGQPKGVAVEHRQAV 624
Cdd:PRK13388 97 RADCQLLVTDAEhrplLDGLDLPGVRvLDVDTPAYAELVAAAGALTPHrevDAMDPFMLIFTSGTTGAPKAVRCSHGRLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 625 SFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPgweKDSAL-IVQAIHQENVTTAHFIPAMLNSF 703
Cdd:PRK13388 177 FAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPA---KFSASgFLDDVRRYGATYFNYVGKPLAYI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 704 LdqAEIERLSDR-TSLKRVFagGEPLAPRTAARFASVLpQVSLIHGYGPTEATVDAAfyvldpeRDRDRLRIPIGKPVPG 782
Cdd:PRK13388 254 L--ATPERPDDAdNPLRVAF--GNEASPRDIAEFSRRF-GCQVEDGYGSSEGAVIVV-------REPGTPPGSIGRGAPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 783 ARLY-----------VLDPHLAV-QPSGVAGELY-IAGAGVARGYLNRPALTEERFledpfypgeR--MYKTGDVARWLP 847
Cdd:PRK13388 322 VAIYnpetltecavaRFDAHGALlNADEAIGELVnTAGAGFFEGYYNNPEATAERM---------RhgMYWSGDLAYRDA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 848 DGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD--SGEPELCAYV----EGLQRNEVRAQL--ERLL 919
Cdd:PRK13388 393 DGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDerVGDQVMAALVlrdgATFDPDAFAAFLaaQPDL 472
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 363747658 920 PGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAADAETYT 960
Cdd:PRK13388 473 GTKAWPRYVRIAADLPSTATNKVLKRELIAQGWATGDPVTL 513
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
2095-2525 |
7.27e-20 |
|
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: 94.96 E-value: 7.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2095 LTPIQRRFFgqvhaFHNHYNQSV------MLFSEKG-FNANALHLALRKITEHHDAIRMIFQRDQNGHVIQfnrgINHKD 2167
Cdd:cd19543 4 LSPMQEGML-----FHSLLDPGSgayveqMVITLEGpLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQ----VVLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2168 HELfGLYISDWTKAS-LERTHLDEKLAAEEtviQSK-MNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLED 2244
Cdd:cd19543 75 RKL-PWRELDLSHLSeAEQEAELEALAEED---RERgFDLARAPLMRLTLIRLGDDRYrLVWSFHHILLDGWSLPILLKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2245 LAAAYQQALEKKEIQLPPkTDSYLSYADGLTQ--IAESKQllsektYWQTILDAHTAF--LPKDIENVPDRLQMNsDAAA 2320
Cdd:cd19543 151 LFAIYAALGEGQPPSLPP-VRPYRDYIAWLQRqdKEAAEA------YWREYLAGFEEPtpLPKELPADADGSYEP-GEVS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2321 FVLSGDWTEKLLfETQQAYGTDANELLLTALGMALSEWAGHDQIVISTEGHGREGHVPNIDisRTVGWFTSIYPILLDMG 2400
Cdd:cd19543 223 FELSAELTARLQ-ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIE--TMVGLFINTLPVRVRLD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2401 IPEPF--------EDQLA---------YRIKTTKDMlrrvpnkgtGYGLLTHIgelrhkepeVSF-NY--LGQFSEEKEA 2460
Cdd:cd19543 300 PDQTVlellkdlqAQQLElreheyvplYEIQAWSEG---------KQALFDHL---------LVFeNYpvDESLEEEQDE 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 2461 ETFQLSyyqpsyEIAGEREREYELDINAlITDGRLQVKAVY-TQVFSKHSIECFMDRFhRHLIETI 2525
Cdd:cd19543 362 DGLRIT------DVSAEEQTNYPLTVVA-IPGEELTIKLSYdAEVFDEATIERLLGHL-RRVLEQV 419
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1499-1994 |
7.36e-20 |
|
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: 96.06 E-value: 7.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1499 PFHRIFEAKAEE-----------IPEHIAVID--NEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGV 1564
Cdd:cd17642 7 PFYPLEDGTAGEqlhkamkryasVPGTIAFTDahTGVNYSYAEYLEMSVRLAEALKKYGlKQNDRIAVCSENSLQFFLPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1565 LAVMKAGGVYIPIDSHY-----------PKARIEYILRDSGADILLLQQELKH----LISNLPESEMSHICLD------- 1622
Cdd:cd17642 87 IAGLFIGVGVAPTNDIYnereldhslniSKPTIVFCSKKGLQKVLNVQKKLKIiktiIILDSKEDYKGYQCLYtfitqnl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1623 ----DESSYEENSCNLNlspapEEPVYIIYTSGTTGAPKGVIVTYRN----FTHAalawRQ-IYELDRKP-VRLLQIASF 1692
Cdd:cd17642 167 ppgfNEYDFKPPSFDRD-----EQVALIMNSSGSTGLPKGVQLTHKNivarFSHA----RDpIFGNQIIPdTAILTVIPF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1693 --SFDVFSgdLARTLTNGGTLIVCP---DETRLEPAEIYKIMNsqriTVMESTPALIIPVMEYVyrNQFKLPDLDILILG 1767
Cdd:cd17642 238 hhGFGMFT--TLGYLICGFRVVLMYkfeEELFLRSLQDYKVQS----ALLVPTLFAFFAKSTLV--DKYDLSNLHEIASG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1768 SDMVKAQDFKTLTDRFGQSMrIINSYGVTEATidSSFYETSMGGEGTGdnvPIGSPLPNVHMYVLS-QTDQIQPIGVAGE 1846
Cdd:cd17642 310 GAPLSKEVGEAVAKRFKLPG-IRQGYGLTETT--SAILITPEGDDKPG---AVGKVVPFFYAKVVDlDTGKTLGPNERGE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1847 LCIGGAGVAKGYHQKPDLTQMKFTKNPFVsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGL 1926
Cdd:cd17642 384 LCVKGPMIMKGYVNNPEATKALIDKDGWL------HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPK 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 1927 VREAAVA-VQHDKNGQAGLAAYIVPSDVNTN---ALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd17642 458 IFDAGVAgIPDEDAGELPAAVVVLEAGKTMTekeVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
677-888 |
1.86e-19 |
|
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: 92.36 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 677 DSALIVQAIHQENVTTAHFIPAMLNSFLdQAEIERLSDRTSLKRVFA--GGEPLAPRTAARFASVLPqvslihGYGPTEA 754
Cdd:cd17636 76 DAEEVLELIEAERCTHAFLLPPTIDQIV-ELNADGLYDLSSLRSSPAapEWNDMATVDTSPWGRKPG------GYGQTEV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 755 TVDAAFYVLDperdRDRLRIpIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFledpfypGE 834
Cdd:cd17636 149 MGLATFAALG----GGAIGG-AGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-------RG 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 363747658 835 RMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 888
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAV 270
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1504-1991 |
2.13e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 94.84 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1504 FEAKAEEIPEHIAVIDNEIEI--SYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSH 1580
Cdd:PRK12583 24 FDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGvQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1581 YPKARIEYILRDSGADILLLQQELK---------HLISNLPES---EMSH---------ICLDDE-----SSYEE----- 1629
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICADAFKtsdyhamlqELLPGLAEGqpgALACerlpelrgvVSLAPApppgfLAWHElqarg 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1630 ---NSCNLNLSPA---PEEPVYIIYTSGTTGAPKGVIVTYRN------FTHAALAwrqIYELDR--KPVRLLQiasfSFD 1695
Cdd:PRK12583 184 etvSREALAERQAsldRDDPINIQYTSGTTGFPKGATLSHHNilnngyFVAESLG---LTEHDRlcVPVPLYH----CFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1696 VFSGDLArTLTNGGTLIVCPDEtrLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQD 1775
Cdd:PRK12583 257 MVLANLG-CMTVGACLVYPNEA--FDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1776 FKTLTDRFGQSMRIInSYGVTEATIDSsfYETsmggeGTGDNVP-----IGSPLPNVHMYVLSQTDQIQPIGVAGELCIG 1850
Cdd:PRK12583 334 MRRVMDEMHMAEVQI-AYGMTETSPVS--LQT-----TAADDLErrvetVGRTQPHLEVKVVDPDGATVPRGEIGELCTR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1851 GAGVAKGYHQKPDLTQMKFTKNPFVsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREA 1930
Cdd:PRK12583 406 GYSVMKGYWNNPEATAESIDEDGWM------HTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADV 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 1931 AV-AVQHDKNGQAgLAAYIV--PSD-VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDR 1991
Cdd:PRK12583 480 QVfGVPDEKYGEE-IVAWVRlhPGHaASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1637-1994 |
4.77e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 94.99 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1637 SPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVrLLQIASF--SFDvFSGDLARTLTNGGTLIVC 1714
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDV-ILSSLPFfhSFG-LTVTLWLPLLEGIKVVYH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1715 PDETrlEPAEIYKIMNSQRITVMESTPALIipvMEYVyRNQFKLPD----LDILILGSDMVK---AQDFKtltDRFGqsM 1787
Cdd:PRK08633 856 PDPT--DALGIAKLVAKHRATILLGTPTFL---RLYL-RNKKLHPLmfasLRLVVAGAEKLKpevADAFE---EKFG--I 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1788 RIINSYGVTEAT----------IDSSFYETSMGGEGTgdnvpIGSPLPNVHMYVLS-QTDQIQPIGVAGELCIGGAGVAK 1856
Cdd:PRK08633 925 RILEGYGATETSpvasvnlpdvLAADFKRQTGSKEGS-----VGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMK 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1857 GYHQKPDLTQmKFTKNpfVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGY-----RIEtEEIeSVLLQTGLVREAA 1931
Cdd:PRK08633 1000 GYLGDPEKTA-EVIKD--IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEmvplgAVE-EEL-AKALGGEEVVFAV 1074
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 1932 VAVQHDKNGQAgLAAYIVPSDVNTNALRAALTK-ELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK08633 1075 TAVPDEKKGEK-LVVLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
2096-2525 |
8.20e-19 |
|
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: 91.60 E-value: 8.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2096 TPIQRRFFGQVHAFHNHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIF-QRDQNGHVIQfnrgINHKDHELfgly 2174
Cdd:cd19542 5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQ----VVLKSLDP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2175 isDWTkaslERTHLDEKLAAEETVIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQAL 2253
Cdd:cd19542 77 --PIE----EVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVyLVLRISHALYDGVSLPIILRDLAAAYNGQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2254 ekkeiqLPPKTD--SYLSYADGLTQiAESKQllsektYWQTILDAHTAFLPKDIenVPDRLQMNSDAAafvlsgdwTEKL 2331
Cdd:cd19542 151 ------LPPAPPfsDYISYLQSQSQ-EESLQ------YWRKYLQGASPCAFPSL--SPKRPAERSLSS--------TRRS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2332 LFETQQAYG----TDANeLLLTALGMALSEWAGHDQIVISTEGHGREGHVPNIDisRTVGWFTSIypilldmgipepfed 2407
Cdd:cd19542 208 LAKLEAFCAslgvTLAS-LFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGID--DIVGPCINT--------------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2408 qLAYRIK-----TTKDMLRRV--------PNKGTGYGLLTHIGELRHKEPEvsFNYLGQFSEEKEAETFQLSYYQPSYEI 2474
Cdd:cd19542 270 -LPVRVKldpdwTVLDLLRQLqqqylrslPHQHLSLREIQRALGLWPSGTL--FNTLVSYQNFEASPESELSGSSVFELS 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 363747658 2475 AGEREREYELDINALITDGRLQVKAVY-TQVFSKHSIECFMDRFhRHLIETI 2525
Cdd:cd19542 347 AAEDPTEYPVAVEVEPSGDSLKVSLAYsTSVLSEEQAEELLEQF-DDILEAL 397
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1508-1989 |
1.06e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 92.53 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARI 1586
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGvGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1587 EYILRDSGADILLLQQELKHLISNLPESEMSHICL--------DDESSYEENSCNLNLSPAP-----EEPVYIIYTSGTT 1653
Cdd:PRK07786 107 AFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVvvaggssdDSVLGYEDLLAEAGPAHAPvdipnDSPALIMYTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1654 GAPKGVIVTYRNFTHAALAWRQIYELDRK------PVRLLQIASFsfdvfsGDLARTLTNGGTLIVCPDETrLEPAEIYK 1727
Cdd:PRK07786 187 GRPKGAVLTHANLTGQAMTCLRTNGADINsdvgfvGVPLFHIAGI------GSMLPGLLLGAPTVIYPLGA-FDPGQLLD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1728 IMNSQRItvmesTPALIIPVM-EYVYRNQFKLP-DLDILILGSDMVKAQDfkTLTDRFGQSMriinsygvTEATIDSSFY 1805
Cdd:PRK07786 260 VLEAEKV-----TGIFLVPAQwQAVCAEQQARPrDLALRVLSWGAAPASD--TLLRQMAATF--------PEAQILAAFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1806 ETSM--------GGEGTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSG 1877
Cdd:PRK07786 325 QTEMspvtcmllGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1878 ErLYRTGDracwlpNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQ-HDKNGQAGLAAYIVPSD---V 1953
Cdd:PRK07786 405 D-LVRQDE------EGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRaDEKWGEVPVAVAAVRNDdaaL 477
|
490 500 510
....*....|....*....|....*....|....*.
gi 363747658 1954 NTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKL 1989
Cdd:PRK07786 478 TLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1640-1994 |
1.49e-18 |
|
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: 92.70 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 PEEPVYIIYTSGTTGAPKGVIVT---YrnFTHAALAWRqiYELDRKPvrllqiasfsFDVF--SGDLART---------- 1704
Cdd:TIGR02188 236 SEDPLFILYTSGSTGKPKGVLHTtggY--LLYAAMTMK--YVFDIKD----------GDIFwcTADVGWItghsyivygp 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1705 LTNGGTLIV------CPDETRlepaeIYKIMNSQRITVMESTPALIIPVMEYvyrnqfklpdldililGSDMVKAQDFKT 1778
Cdd:TIGR02188 302 LANGATTVMfegvptYPDPGR-----FWEIIEKHKVTIFYTAPTAIRALMRL----------------GDEWVKKHDLSS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1779 LtdrfgqsmRIINS------------Y----GVTEATIDSSFYETSMGG------EGTGDNVPiGS---PLPNVHMYVLS 1833
Cdd:TIGR02188 361 L--------RLLGSvgepinpeawmwYykvvGKERCPIVDTWWQTETGGimitplPGATPTKP-GSatlPFFGIEPAVVD 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1834 QTDQIQPI-GVAGELCIGGA--GVAKGYHQKPDltqmKFTKNPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGY 1910
Cdd:TIGR02188 432 EEGNPVEGpGEGGYLVIKQPwpGMLRTIYGDHE----RFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGH 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1911 RIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIV------PSDVNTNALRAALTKELPAYMIPAHLIPLENMPL 1983
Cdd:TIGR02188 508 RLGTAEIESALVSHPAVAEAAVvGIPDDIKGQA-IYAFVTlkdgyePDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPK 586
|
410
....*....|.
gi 363747658 1984 TLNGKLDRNAL 1994
Cdd:TIGR02188 587 TRSGKIMRRLL 597
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
484-947 |
1.82e-18 |
|
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: 91.76 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLL--- 560
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFvgk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 561 ------TQPG-------CSAPNFSGETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGV----------- 616
Cdd:cd05932 87 lddwkaMAPGvpeglisISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVmltfgsfawaa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 617 --AVEH--------------------RQAV---SFLTGMQHQFPLSED----DIVMVKTSFSFDA-SVWQLFwwslsgas 666
Cdd:cd05932 167 qaGIEHigteendrmlsylplahvteRVFVeggSLYGGVLVAFAESLDtfveDVQRARPTLFFSVpRLWTKF-------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 667 ayllppgwekdsalivqaihQENVTtaHFIPAM-LNSFLDQAEIERLSDRTSLK-------RVFAGGE-PLAPRTAARFA 737
Cdd:cd05932 239 --------------------QQGVQ--DKIPQQkLNLLLKIPVVNSLVKRKVLKglgldqcRLAGCGSaPVPPALLEWYR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 738 SVlpQVSLIHGYGPTEATvdAAFYVLDPERDRDRLripIGKPVPGARLYVLDphlavqpsgvAGELYIAGAGVARGYLNR 817
Cdd:cd05932 297 SL--GLNILEAYGMTENF--AYSHLNYPGRDKIGT---VGNAGPGVEVRISE----------DGEILVRSPALMMGYYKD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 818 PALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKI-RGYRIEPGEIEAALRSIEGVrEAAVTVRTDSGE 896
Cdd:cd05932 360 PEATAEAFTADGF------LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVIGSGLPA 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 897 P-ELCAYVEGLQ-------RNEVRAQLERLL--------PGYMVPAYMIEMEQWPV-----TPSGKLDRNAL 947
Cdd:cd05932 433 PlALVVLSEEARlradafaRAELEASLRAHLarvnstldSHEQLAGIVVVKDPWSIdngilTPTLKIKRNVL 504
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1646-1989 |
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 363747658 1646 IIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELdRKPVRLLQIASF--SFDVFSGDLArTLTNGGTLIvcPDETrLEPA 1723
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADL-TEDDRYLIINPFfhTFGYKAGIVA-CLLTGATVV--PVAV-FDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1724 EIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqSMRIINSYGVTEATIdss 1803
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELG-FETVLTAYGLTEAGV--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1804 fyeTSMGgeGTGDNV-----PIGSPLPNVHMyvlsqtdqiqPIGVAGELCIGGAGVAKGYHQKPDLTQMKftknpfVSGE 1878
Cdd:cd17638 156 ---ATMC--RPGDDAetvatTCGRACPGFEV----------RIADDGEVLVRGYNVMQGYLDDPEATAEA------IDAD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1879 RLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGlAAYIV---PSDVN 1954
Cdd:cd17638 215 GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAViGVPDERMGEVG-KAFVVarpGVTLT 293
|
330 340 350
....*....|....*....|....*....|....*
gi 363747658 1955 TNALRAALTKELPAYMIPAHLIPLENMPLTLNGKL 1989
Cdd:cd17638 294 EEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1641-1990 |
2.35e-18 |
|
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: 89.36 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1641 EEPVYIIYTSGTTGAPKGVIvtyrnfthaalaWRQiyelDRKPVRLLQIASFSFDVFSGD-------------------- 1700
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVM------------WRQ----EDIFRMLMGGADFGTGEFTPSedahkaaaaaagtvmfpapp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1701 --------LARTLTNGGTLIVCPDEtRLEPAEIYKIMNSQRITVMEST-PALIIPVMEYVYR-NQFKLPDLDILILG--- 1767
Cdd:cd05924 67 lmhgtgswTAFGGLLGGQTVVLPDD-RFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDaGPYDLSSLFAISSGgal 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1768 -SDMVKAQDFKTLTDrfgqsMRIINSYGVTEatidSSFYETSMGGEGTGDNVPIGSPLPNVhmYVLSQTDQIQPIGVAGE 1846
Cdd:cd05924 146 lSPEVKQGLLELVPN-----ITLVDAFGSSE----TGFTGSGHSAGSGPETGPFTRANPDT--VVLDDDGRVVPPGSGGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1847 LCIGGAG-VAKGYHQKPDLTQMKFtknPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTG 1925
Cdd:cd05924 215 GWIARRGhIPLGYYGDEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHP 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 1926 LVREAAVAVQHD-KNGQ--AGLAAYIVPSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLD 1990
Cdd:cd05924 292 AVYDVLVVGRPDeRWGQevVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
463-947 |
2.64e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 91.27 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 463 LFERQAAFTPERLAIRFSGGSLTYAELDMYASRLAAHLAAR-GITNESIVGVLSersPEML---IAVLAVLKAGGAYLPL 538
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMM---PNLLqypIALFGILRAGMIVVNV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAYPKERLSYMLKDSGASLLLTqpgcsAPNFSgETLE----------VDMTSL-------------------------- 582
Cdd:PRK08974 105 NPLYTPRELEHQLNDSGAKAIVI-----VSNFA-HTLEkvvfktpvkhVILTRMgdqlstakgtlvnfvvkyikrlvpky 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 583 ----------ASEKAENHEFTPAD--GGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLtgMQHQF---PLSEDDIVMVKTS 647
Cdd:PRK08974 179 hlpdaisfrsALHKGRRMQYVKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAaygPLLHPGKELVVTA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 648 FS----FDASVWQLFWWSLSGASAYLLPPgweKDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLsDRTSLKRVFA 723
Cdd:PRK08974 257 LPlyhiFALTVNCLLFIELGGQNLLITNP---RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQEL-DFSSLKLSVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 724 GGEPLAPRTAARFASvLPQVSLIHGYGPTEAT--VDAAFYvldperDRDRLRIPIGKPVPGARLYVLDPHLAVQPSGVAG 801
Cdd:PRK08974 333 GGMAVQQAVAERWVK-LTGQYLLEGYGLTECSplVSVNPY------DLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 802 ELYIAGAGVARGYLNRPALTEErFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIE 881
Cdd:PRK08974 406 ELWVKGPQVMLGYWQRPEATDE-VIKDGW------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHP 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 882 GVRE-AAVTVRTD-SGEpELCAYV----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK08974 479 KVLEvAAVGVPSEvSGE-AVKIFVvkkdPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1524-1950 |
3.09e-18 |
|
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: 91.12 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQNRKGPKPT---VAVLAKRSIDAIVGVLAVMKAGGVYIPI-DSHYPKArIEYILRDSGADILL 1599
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPAPasfVGIYSINRPEWIISELACYAYSLVTVPLyDTLGPEA-IEYILNHAEISIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1600 LQQELKhLISnlpesemshicLDD-ESSYEENSCNLNLsPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALA----WR 1674
Cdd:cd05927 85 CDAGVK-VYS-----------LEEfEKLGKKNKVPPPP-PKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGvfkiLE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1675 QIYELDRKPV------------RLLQIASFSFDV----FSGDLaRTLTNggtlivcpDETRLEPA----------EIY-K 1727
Cdd:cd05927 152 ILNKINPTDVyisylplahifeRVVEALFLYHGAkigfYSGDI-RLLLD--------DIKALKPTvfpgvprvlnRIYdK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1728 IMNSqritvMESTPALIIPVMEYVYRNQ---------FKLPDLDILIlgsdmvkaqdFKTLTDRFGQSMRIINS------ 1792
Cdd:cd05927 223 IFNK-----VQAKGPLKRKLFNFALNYKlaelrsgvvRASPFWDKLV----------FNKIKQALGGNVRLMLTgsapls 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1793 ------------------YGVTeatidssfyETSMGGEGT--GDNVP--IGSPLPNVHM---------YVLSQTDQiqpi 1841
Cdd:cd05927 288 pevleflrvalgcpvlegYGQT---------ECTAGATLTlpGDTSVghVGGPLPCAEVklvdvpemnYDAKDPNP---- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1842 gvAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACWLPNGTIRLLGRmdyqvKIN------GYRIETE 1915
Cdd:cd05927 355 --RGEVCIRGPNVFSGYYKDPEKTAEALDEDGW------LHTGDIGEWLPNGTLKIIDR-----KKNifklsqGEYVAPE 421
|
490 500 510
....*....|....*....|....*....|....*
gi 363747658 1916 EIESVLLQTGLVREAAVavqHDKNGQAGLAAYIVP 1950
Cdd:cd05927 422 KIENIYARSPFVAQIFV---YGDSLKSFLVAIVVP 453
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
455-946 |
3.38e-18 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 91.34 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 455 PKAFTLHGLFERQAAFTPERLAIR---FSGGS------LTYAELDMYASRLAAHL---AARGitneSIVGVLSERSPEML 522
Cdd:PRK12476 31 PPGTTLISLIERNIANVGDTVAYRyldHSHSAagcaveLTWTQLGVRLRAVGARLqqvAGPG----DRVAILAPQGIDYV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 523 IAVLAVLKAGGAYLPL-DPAYP--KERLSYMLKDSGASLLLTQ--------------PGCSAPNfsgeTLEVDmtSLASE 585
Cdd:PRK12476 107 AGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTtaaaeavegflrnlPRLRRPR----VIAID--AIPDS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 586 KAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTgmqhQFPLSEDDIVMVKTSFSF-----DASVWQLFWW 660
Cdd:PRK12476 181 AGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLV----QMILSIDLLDRNTHGVSWlplyhDMGLSMIGFP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 661 SLSGASAYLLPPG--------WEKdsALIVQAIHQENVTTAhfiPAMLNSFLDQAEIERLSDRTSLKRV--FAGGEPLAP 730
Cdd:PRK12476 257 AVYGGHSTLMSPTafvrrpqrWIK--ALSEGSRTGRVVTAA---PNFAYEWAAQRGLPAEGDDIDLSNVvlIIGSEPVSI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 731 RTAARFASV-----LPQVSLIHGYGPTEATV-------DAAFYV---------------LDPERDRDRLRIPIGKPVPGA 783
Cdd:PRK12476 332 DAVTTFNKAfapygLPRTAFKPSYGIAEATLfvatiapDAEPSVvyldreqlgagravrVAADAPNAVAHVSCGQVARSQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 784 RLYVLDPHL-AVQPSGVAGELYIAGAGVARGYLNRPALTEERF---LEDPFYPGERMYKTGDVARWLP--------DGNV 851
Cdd:PRK12476 412 WAVIVDPDTgAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgakLQSRLAEGSHADGAADDGTWLRtgdlgvylDGEL 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 852 EFLGRTDDQVKIRGYRIEPGEIEA-ALRSIEGVREAAVTVRTDSGE--PELCAYVE---GLQRNE-------VRAQLERL 918
Cdd:PRK12476 492 YITGRIADLIVIDGRNHYPQDIEAtVAEASPMVRRGYVTAFTVPAEdnERLVIVAEraaGTSRADpapaidaIRAAVSRR 571
|
570 580 590
....*....|....*....|....*....|...
gi 363747658 919 --LPGY---MVPAYMIemeqwPVTPSGKLDRNA 946
Cdd:PRK12476 572 hgLAVAdvrLVPAGAI-----PRTTSGKLARRA 599
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1499-1995 |
3.67e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 90.76 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1499 PFHRIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQnRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIP 1576
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLL-ALGVRAGdgVAVLARNHRGFVLALYAAGKVGARIIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1577 IDSHYPKARIEYILRDSGADILLLQQELKHLISNLPESemshicLDDESSYEENSCNLNLS------------------- 1637
Cdd:PRK07788 129 LNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPD------LGRLRAWGGNPDDDEPSgstdetlddliagsstapl 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1638 PAPEEPV-YIIYTSGTTGAPKGVIvtyRNFTHAALAWRQIyeLDRKPVRLLQIASFSFDVFSG------DLARTLtnGGT 1710
Cdd:PRK07788 203 PKPPKPGgIVILTSGTTGTPKGAP---RPEPSPLAPLAGL--LSRVPFRAGETTLLPAPMFHAtgwahlTLAMAL--GST 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1711 LIVcpdETRLEPAEIYKIMNSQRITVMestpaLIIPVMeyvYRNQFKLPD----------LDILI-----LGSDMVKAqd 1775
Cdd:PRK07788 276 VVL---RRRFDPEATLEDIAKHKATAL-----VVVPVM---LSRILDLGPevlakydtssLKIIFvsgsaLSPELATR-- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1776 fktLTDRFGQsmRIINSYGVTE---ATIDSSfyETSMGGEGTGDNVPIGsplpnVHMYVLSQTDQIQPIGVAGELCIGGA 1852
Cdd:PRK07788 343 ---ALEAFGP--VLYNLYGSTEvafATIATP--EDLAEAPGTVGRPPKG-----VTVKILDENGNEVPRGVVGRIFVGNG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1853 GVAKGYHQKPDltqmKFTKNPFVSgerlyrTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV 1932
Cdd:PRK07788 411 FPFEGYTDGRD----KQIIDGLLS------SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 1933 -AVQHDKNGQAgLAAYIVPSD---VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALP 1995
Cdd:PRK07788 481 iGVDDEEFGQR-LRAFVVKAPgaaLDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1494-1999 |
5.31e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 90.45 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1494 AQKDVP---FHRIFEaKAEEIPEHIAV--IDNEIEISYRFLNERANRLARTLQNRKGPKPT-VAVLAKRSIDAIVGVLAV 1567
Cdd:PRK05857 8 AMPQLPstvLDRVFE-QARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSrVLVISDNGPETYLSVLAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1568 MKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQELKHLISNLPE--SEMSHICLDDESSYEENSCNL-------NLSP 1638
Cdd:PRK05857 87 AKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEalHSIPVIAVDIAAVTRESEHSLdaaslagNADQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1639 APEEPVYIIYTSGTTGAPKGVIVTYRNF-------THAALAWRQ--IYELDRKPVRLLQIASFSFdvfsgdLARTLTNGG 1709
Cdd:PRK05857 167 GSEDPLAMIFTSGTTGEPKAVLLANRTFfavpdilQKEGLNWVTwvVGETTYSPLPATHIGGLWW------ILTCLMHGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1710 TLIVCPDETrlepAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTdrfGQSMRI 1789
Cdd:PRK05857 241 LCVTGGENT----TSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIE---ATGVRT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1790 INSYGVTEATIDSSFYETSMGGEGTGDNVPIGSPLPNVHMYVLSQ------TDQIQPIGVAGELCIGGAGVAKGYHQKPD 1863
Cdd:PRK05857 314 AQVYGLSETGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATdgigptAPGAGPSASFGTLWIKSPANMLGYWNNPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1864 LTQMKFTKNPFVSGERLYRTGDracwlpnGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAG 1943
Cdd:PRK05857 394 RTAEVLIDGWVNTGDLLERRED-------GFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAL 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 1944 LAAYIVPS-DVNTNALR-------AALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALPVPNN 1999
Cdd:PRK05857 467 VGLAVVASaELDESAARalkhtiaARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAAT 530
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
2092-2421 |
8.72e-18 |
|
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: 88.59 E-value: 8.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2092 EAELTPIQRR--FFGQVHAFHNHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQfnRGINHKDHE 2169
Cdd:cd19539 1 RIPLSFAQERlwFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQ--EILPPGPAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2170 LFGLYISDWTKaslERTHLDEKLAAEetVIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAA 2248
Cdd:cd19539 79 LEVRDLSDPDS---DRERRLEELLRE--RESRGFDLDEEPPIRAVLGRFDPDDHvLVLVAHHTAFDAWSLDVFARDLAAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2249 YQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTIL-DAHTAFLPKDIEnVPDRLQMNSDAAAFVLSGDW 2327
Cdd:cd19539 154 YAARRKGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLrGAEPTALPTDRP-RPAGFPYPGADLRFELDAEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2328 TEKLlfeTQQAYGTDAN--ELLLTALGMALSEWAGHDQIVISTEGHGReghvPNIDISRTVGWFTSIYPILLDMGIPEPF 2405
Cdd:cd19539 233 VAAL---RELAKRARSSlfMVLLAAYCVLLRRYTGQTDIVVGTPVAGR----NHPRFESTVGFFVNLLPLRVDVSDCATF 305
|
330
....*....|....*.
gi 363747658 2406 EDQLAYRIKTTKDMLR 2421
Cdd:cd19539 306 RDLIARVRKALVDAQR 321
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1074-1459 |
9.69e-18 |
|
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: 88.46 E-value: 9.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1074 YNMPAVLELEGKLNPERMERAFKELIKRHESLRTSFEQDaGGDPVQRIHDEV--PFTLQTTVLGERTEQEAAAAFI---- 1147
Cdd:cd19534 22 FNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRRE-DGGWQQRIRGDVeeLFRLEVVDLSSLAQAAAIEALAaeaq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1148 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNN---RNLPAL--RIQYKDYAVWREGFKTG 1222
Cdd:cd19534 101 SSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQalaGEPIPLpsKTSFQTWAELLAEYAQS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1223 DAYKTQEAYWLKQLEGELPvlDLPADHarpPVRSFAGDKVSFTLDQE-VASGLHKLARENGSTLYMVLLAAYTAFLSRLS 1301
Cdd:cd19534 181 PALLEELAYWRELPAADYW--GLPKDP---EQTYGDARTVSFTLDEEeTEALLQEANAAYRTEINDLLLAALALAFQDWT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1302 GQEDIIVGSPIAGR----PHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETA---------------LEAFEHQD 1362
Cdd:cd19534 256 GRAPPAIFLEGHGReeidPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKEQLrripnkgigygilryLTPEGTKR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1363 YPF----EELVDKLELTRDMSRNPVFDAMFILQNVEKQDIDLReikvRPAnfahhisLFDITLIAteINGSICCEMEFST 1438
Cdd:cd19534 336 LAFhpqpEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDTP----RFA-------LLDINAVV--EGGQLVITVSYSR 402
|
410 420
....*....|....*....|.
gi 363747658 1439 EVFLKATIERWADHFIEFLHA 1459
Cdd:cd19534 403 NMYHEETIQQLADSYKEALEA 423
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
486-944 |
9.74e-18 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 89.44 E-value: 9.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 486 YAELDMYASRLAAHLAARGitNESIVGVLSERSPEMLIAVLAVLKAGGAYL----PLDPAYPKERLSYMLK---DSGASL 558
Cdd:PRK05851 34 WPEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAAVSilpgPVRGADDGRWADATLTrfaGIGVRT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 559 LLTQPG---CSAPNFSGETLEvDMTSLASeKAENHEFTPADGGSLAYVIYTSGSTGQPKgVAVEHRQAV-SFLTGMQHQF 634
Cdd:PRK05851 112 VLSHGShleRLRAVDSSVTVH-DLATAAH-TNRSASLTPPDSGGPAVLQGTAGSTGTPR-TAILSPGAVlSNLRGLNARV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 635 PLSED-DIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPG-----------WEKDSalivqaihQENVTTAhfiPAMLNS 702
Cdd:PRK05851 189 GLDAAtDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTafsaspfrwlsWLSDS--------RATLTAA---PNFAYN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 703 FldqaeIERLSDRTS------LKRVFAGGEPLAPRTAARFASVLPQVSLIHG-----YGPTEAT-------------VDA 758
Cdd:PRK05851 258 L-----IGKYARRVSdvdlgaLRVALNGGEPVDCDGFERFATAMAPFGFDAGaaapsYGLAESTcavtvpvpgiglrVDE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 759 afyVLDPERDRDRLRIPIGKPVPGARLYVLDPHlavQPSGVA----GELYIAGAGVARGYLNrpalteerflEDPFYPGE 834
Cdd:PRK05851 333 ---VTTDDGSGARRHAVLGNPIPGMEVRISPGD---GAAGVAgreiGEIEIRGASMMSGYLG----------QAPIDPDD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 835 rMYKTGDVArWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV-TVRTDSG--EPELCAYVE--GLQRN 909
Cdd:PRK05851 397 -WFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVvAVGTGEGsaRPGLVIAAEfrGPDEA 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 363747658 910 EVRAQL-ERLLP--GyMVPAYMIEME--QWPVTPSGKLDR 944
Cdd:PRK05851 475 GARSEVvQRVASecG-VVPSDVVFVApgSLPRTSSGKLRR 513
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1638-2087 |
1.28e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 89.71 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1638 PAPEEPV------YIIYTSGTTGAPKGVIVTYRN-FTHAALAWRQIYELDRKPVRLLQIASFsfdvFSGDLART----LT 1706
Cdd:PRK06060 136 PGGYEPMggdalaYATYTSGTTGPPKAAIHRHADpLTFVDAMCRKALRLTPEDTGLCSARMY----FAYGLGNSvwfpLA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1707 NGGTLIVCPDETRLEPAEiykiMNSQRI--TVMESTPALIIPVMEYVYRNQFKlpDLDILILGSDMVKAQDFKTLTDRFG 1784
Cdd:PRK06060 212 TGGSAVINSAPVTPEAAA----ILSARFgpSVLYGVPNFFARVIDSCSPDSFR--SLRCVVSAGEALELGLAERLMEFFG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1785 qSMRIINSYGVTEatIDSSFYETSMGGEGTGDnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDl 1864
Cdd:PRK06060 286 -GIPILDGIGSTE--VGQTFVSNRVDEWRLGT---LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1865 tqmkftknPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGL 1944
Cdd:PRK06060 359 --------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1945 AAYIVPS-------DVNTNALRAALTKeLPAYMIPAHLIPLENMPLTLNGKLDRNALPVpnnvlsrpytapvndiQKTMA 2017
Cdd:PRK06060 431 QAFLVATsgatidgSVMRDLHRGLLNR-LSAFKVPHRFAVVDRLPRTPNGKLVRGALRK----------------QSPTK 493
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 2018 YIWEDVLSMSRvgiHDSFFELGGDSIKALQVAARLAAEgwsMTIRDlfRYSTIQE---------LCGHITPLASQADQG 2087
Cdd:PRK06060 494 PIWELSLTEPG---SGVRAQRDDLSASNMTIAGGNDGG---ATLRE--RLVALRQerqrlvvdaVCAEAAKMLGEPDPW 564
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
602-947 |
1.32e-17 |
|
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: 88.59 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 602 YVIYTSGSTGQPKGVavehRQAvsfltgmqHQFPLSEDDIVMvktSFSFdasvwqLFWWSlsGASAYLLP-P-------G 673
Cdd:cd05929 129 KMLYSGGTTGRPKGI----KRG--------LPGGPPDNDTLM---AAAL------GFGPG--ADSVYLSPaPlyhaapfR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 674 W--------------EK-DSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLS-DRTSLKRVFAGGEPLAPRTAARFA 737
Cdd:cd05929 186 WsmtalfmggtlvlmEKfDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAyDLSSLKRVIHAAAPCPPWVKEQWI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 738 SVLPQVsLIHGYGPTEATvdaAFYVLDPErdrDRLRIP--IGKPVpGARLYVLDPHLAVQPSGVAGELYIAGAGvARGYL 815
Cdd:cd05929 266 DWGGPI-IWEYYGGTEGQ---GLTIINGE---EWLTHPgsVGRAV-LGKVHILDEDGNEVPPGEIGEVYFANGP-GFEYT 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 816 NRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV--TVRTD 893
Cdd:cd05929 337 NDPEKTAAARNEGGWS------TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVvgVPDEE 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 363747658 894 SGE-------PELCAYVEGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05929 411 LGQrvhavvqPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
480-900 |
1.79e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 88.88 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 480 SGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLL 559
Cdd:PLN02330 52 TGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 560 LTQ-------PGCSAPNFS-GETL---EVDMTSL------ASEKAENHEFTPADggsLAYVIYTSGSTGQPKGVAVEHRQ 622
Cdd:PLN02330 132 VTNdtnygkvKGLGLPVIVlGEEKiegAVNWKELleaadrAGDTSDNEEILQTD---LCALPFSSGTTGISKGVMLTHRN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 623 AVSFLTgmQHQFPLSEDDIVMVKT----SFSFDASVWQLFWWSLSGASAYLLPPGWEKDSALivQAIHQENVTTAHFIPA 698
Cdd:PLN02330 209 LVANLC--SSLFSVGPEMIGQVVTlgliPFFHIYGITGICCATLRNKGKVVVMSRFELRTFL--NALITQEVSFAPIVPP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 699 ML-----NSFLDQAEIERLSdrtsLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYVlDPERDRD-RL 772
Cdd:PLN02330 285 IIlnlvkNPIVEEFDLSKLK----LQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHG-DPEKGHGiAK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 773 RIPIGKPVPGARLYVLDPHLAVQ-PSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNV 851
Cdd:PLN02330 360 KNSVGFILPNLEVKFIDPDTGRSlPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWL------HTGDIGYIDDDGDI 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 363747658 852 EFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD--SGE-PELC 900
Cdd:PLN02330 434 FIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDeeAGEiPAAC 485
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1497-1994 |
3.23e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 88.15 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1497 DVPFHRI-FEAKAEEI-PEHIAVIDNEIEISYRFLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGV-LAVMKAGGV 1573
Cdd:PLN03102 11 NVPLTPItFLKRASECyPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMhFAVPMAGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1574 YIPIDSHYPKARIEYILRDSGADILL-------LQQELKHLIS------NLP-----ESEMSHICLDDESSYEensCNLN 1635
Cdd:PLN03102 91 LNPINTRLDATSIAAILRHAKPKILFvdrsfepLAREVLHLLSsedsnlNLPvifihEIDFPKRPSSEELDYE---CLIQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1636 L-SPAP------------EEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFS---G 1699
Cdd:PLN03102 168 RgEPTPslvarmfriqdeHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTftwG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1700 DLARTLTNggtliVCpdETRLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQ-FKLPDLDILILGSDMVKAQDFKt 1778
Cdd:PLN03102 248 TAARGGTS-----VC--MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLsPRSGPVHVLTGGSPPPAALVKK- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1779 lTDRFGqsMRIINSYGVTEATIDSSFYETSmggegtgDNvpiGSPLPNVHMYVLSQTDQIQPIGVA-------------- 1844
Cdd:PLN03102 320 -VQRLG--FQVMHAYGLTEATGPVLFCEWQ-------DE---WNRLPENQQMELKARQGVSILGLAdvdvknketqesvp 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1845 ------GELCIGGAGVAKGYHQKPdltqmKFTKNPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIE 1918
Cdd:PLN03102 387 rdgktmGEIVIKGSSIMKGYLKNP-----KATSEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1919 SVLLQTGLVREAA-VAVQHDKNGQAGLAAYIVPSDVNTNALRAA--LTKE----------LPAYMIPAHLIPLENMPLTL 1985
Cdd:PLN03102 460 NVLYKYPKVLETAvVAMPHPTWGETPCAFVVLEKGETTKEDRVDklVTRErdlieycrenLPHFMCPRKVVFLQELPKNG 539
|
....*....
gi 363747658 1986 NGKLDRNAL 1994
Cdd:PLN03102 540 NGKILKPKL 548
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2079-2525 |
3.67e-17 |
|
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: 88.76 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2079 PLASQADQGPAEGEAELTPIQRRFFGQVHAFHNHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQ 2158
Cdd:COG1020 6 AAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2159 FnrginhkDHELFGLYISDWTKASLERTHLDEKLAAEETVIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVS 2237
Cdd:COG1020 86 I-------QPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLlLLLALHHIISDGLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2238 WRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTIL--DAHTAFLPKDIENvPDRLQMN 2315
Cdd:COG1020 159 DGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLagLPPLLELPTDRPR-PAVQSYR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2316 SDAAAFVLSGDWTEKLLfETQQAYGTDANELLLTALGMALSEWAGHDQIVISTEGHGREGHvpniDISRTVGWFTSIYPI 2395
Cdd:COG1020 238 GARVSFRLPAELTAALR-ALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP----ELEGLVGFFVNTLPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2396 LLDMGIPEPFEDQLAyRIKTTK-----------DMLRRV--PNKGTGYGLLThigelrhkepEVSFNYLGQFSEEKEAET 2462
Cdd:COG1020 313 RVDLSGDPSFAELLA-RVRETLlaayahqdlpfERLVEElqPERDLSRNPLF----------QVMFVLQNAPADELELPG 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 2463 FQLSYYQPSYEIAgererEYELDINALITDGRLQVKAVY-TQVFSKHSIECFMDRFhRHLIETI 2525
Cdd:COG1020 382 LTLEPLELDSGTA-----KFDLTLTVVETGDGLRLTLEYnTDLFDAATIERMAGHL-VTLLEAL 439
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
511-947 |
4.91e-17 |
|
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: 87.14 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 511 VGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQPGCSA---------PNFSGETLE----- 576
Cdd:cd05928 70 VAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPevdsvasecPSLKTKLLVseksr 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 577 ---VDMTSLASEKAENHefTPADGGSL-AYVIY-TSGSTGQPKgvAVEHRQAvSFLTGM----QHQFPLSEDDIV--MVK 645
Cdd:cd05928 150 dgwLNFKELLNEASTEH--HCVETGSQePMAIYfTSGTTGSPK--MAEHSHS-SLGLGLkvngRYWLDLTASDIMwnTSD 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 646 TSFSfDASVWQLFWWSLSGAS--AYLLPpgwEKDSALIVQAIHQENVTTAHFIPAMLNSFLdQAEIERLSDRtSLKRVFA 723
Cdd:cd05928 225 TGWI-KSAWSSLFEPWIQGACvfVHHLP---RFDPLVILKTLSSYPITTFCGAPTVYRMLV-QQDLSSYKFP-SLQHCVT 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 724 GGEPLAPRTAARFaSVLPQVSLIHGYGPTEATVDAAfyvldperDRDRLRIP---IGKPVPGARLYVLDPHLAVQPSGVA 800
Cdd:cd05928 299 GGEPLNPEVLEKW-KAQTGLDIYEGYGQTETGLICA--------NFKGMKIKpgsMGKASPPYDVQIIDDNGNVLPPGTE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 801 GELYI-----AGAGVARGYLNRPALTEERFLEDpfypgerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEA 875
Cdd:cd05928 370 GDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVES 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 876 ALRSIEGVREAAVTVRTDSGEPELC-AYV-----------EGLQRnEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLD 943
Cdd:cd05928 443 ALIEHPAVVESAVVSSPDPIRGEVVkAFVvlapqflshdpEQLTK-ELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQ 521
|
....
gi 363747658 944 RNAL 947
Cdd:cd05928 522 RNEL 525
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1524-1966 |
7.13e-17 |
|
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: 86.50 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLqnRK---GPKPTVAVLAKRSIDAIVGVLAVMKAGgvyIPIDSHYPKarieyiLRDSGadilll 1600
Cdd:cd17639 6 MSYAEVWERVLNFGRGL--VElglKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAT------LGEDA------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1601 qqelkhLISNLPESEMSHICLDdessyeenscnlnlsPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQ-IYEL 1679
Cdd:cd17639 69 ------LIHSLNETECSAIFTD---------------GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrVPEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1680 DRKPVRLL------QIASFSFD---VFSGDL-----ARTLTNGGTLIVCPDETRLEP---AEIYKIMNSQRITVME---S 1739
Cdd:cd17639 128 LGPDDRYLaylplaHIFELAAEnvcLYRGGTigygsPRTLTDKSKRGCKGDLTEFKPtlmVGVPAIWDTIRKGVLAklnP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1740 TPALIIPVMEYVYrnQFKLPDLDILI---LGSDMVkaqdFKTL---------------------TDRFGQSM--RIINSY 1793
Cdd:cd17639 208 MGGLKRTLFWTAY--QSKLKALKEGPgtpLLDELV----FKKVraalggrlrymlsggaplsadTQEFLNIVlcPVIQGY 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1794 GVTE----ATIDSSF-YETSMggegtgdnvpIGSPLPNVHMYVLS------QTDQIQPigvAGELCIGGAGVAKGYHQKP 1862
Cdd:cd17639 282 GLTEtcagGTVQDPGdLETGR----------VGPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNP 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1863 DLTQMKFTknpfvsGERLYRTGDRACWLPNGTIRLLGRMDYQVKI-NGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQ 1941
Cdd:cd17639 349 EKTKEAFD------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLqNGEYIALEKLESIYRSNPLVNNICVYADPDKSYP 422
|
490 500
....*....|....*....|....*
gi 363747658 1942 AGLaayIVPsdvNTNALRAALTKEL 1966
Cdd:cd17639 423 VAI---VVP---NEKHLTKLAEKHG 441
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
465-944 |
7.60e-17 |
|
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: 86.85 E-value: 7.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 465 ERQAAFTPERLAIRFSGG------SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL 538
Cdd:cd05966 60 DRHLKERGDKVAIIWEGDepdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAYPKERLSYMLKDSGASLLLTqpgCSAPNFSGETL---------------------------EVDMT--------SLA 583
Cdd:cd05966 140 FAGFSAESLADRINDAQCKLVIT---ADGGYRGGKVIplkeivdealekcpsvekvlvvkrtggEVPMTegrdlwwhDLM 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 584 SEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVavEHRQAvSFLTG----MQHQFPLSEDDIvmvktsfsfdasvwqlFW 659
Cdd:cd05966 217 AKQSPECEPEWMDSEDPLFILYTSGSTGKPKGV--VHTTG-GYLLYaattFKYVFDYHPDDI----------------YW 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 660 ------W----S-------LSGASAYLL------P-PG--WEkdsalIVQAiHQenVTTAHFIPAMLNSFLDQA-EIERL 712
Cdd:cd05966 278 ctadigWitghSyivygplANGATTVMFegtptyPdPGryWD-----IVEK-HK--VTIFYTAPTAIRALMKFGdEWVKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 713 SDRTSLKRVFAGGEPLAPRTAARFASVL--PQVSLIHGYGPTE------ATVDAAfyvldperdrdrlrIPI-----GKP 779
Cdd:cd05966 350 HDLSSLRVLGSVGEPINPEAWMWYYEVIgkERCPIVDTWWQTEtggimiTPLPGA--------------TPLkpgsaTRP 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 780 VPGARLYVLDPHLAVQPSGVAGELYIAGA--GVARGYLNRPalteERFLEDPF--YPGerMYKTGDVARWLPDGNVEFLG 855
Cdd:cd05966 416 FFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDTYFskFPG--YYFTGDGARRDEDGYYWITG 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 856 RTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTD--SGEpELCAYV---EGLQ-----RNEVRAQLERLLPGYMVP 925
Cdd:cd05966 490 RVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHdiKGE-AIYAFVtlkDGEEpsdelRKELRKHVRKEIGPIATP 568
|
570
....*....|....*....
gi 363747658 926 AYMIEMEQWPVTPSGKLDR 944
Cdd:cd05966 569 DKIQFVPGLPKTRSGKIMR 587
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1635-1995 |
8.29e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 85.82 E-value: 8.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1635 NLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDrkpvrllQIASFS----FDVfSGDLA--RTLTNG 1708
Cdd:PRK07445 114 GILPNLETGWIMIPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQ-------QVNSFCvlplYHV-SGLMQfmRSFLTG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1709 GTLIVCPdETRLEPAEIYKIMNS-----------QRitVMESTPALIipvmeyvyrNQFKLpdldILILGsdmvkAQDFK 1777
Cdd:PRK07445 186 GKLVILP-YKRLKSGQELPPNPSdfflslvptqlQR--LLQLRPQWL---------AQFRT----ILLGG-----APAWP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1778 TLTD--RFgQSMRIINSYGVTEAtidSSFYETSMGGEGTGDNVPIGSPLPNVHMYVLSQTdqiqpigvAGELCIGGAGVA 1855
Cdd:PRK07445 245 SLLEqaRQ-LQLRLAPTYGMTET---ASQIATLKPDDFLAGNNSSGQVLPHAQITIPANQ--------TGNITIQAQSLA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1856 KGYHQkpdltqmkftknPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQ 1935
Cdd:PRK07445 313 LGYYP------------QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGL 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 1936 HDKN-GQAGLAAYI-VPSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNALP 1995
Cdd:PRK07445 381 PDPHwGEVVTAIYVpKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1502-1988 |
1.18e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 86.02 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1502 RIFEAKAEEIPEHIAVIDNE--IEISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIP 1576
Cdd:PRK08315 20 QLLDRTAARYPDREALVYRDqgLRWTYREFNEEVDALAKGLLAlgiEKGDR--VGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1577 IDSHYPKARIEYILRDSGADIL---------------------LLQQELKHLISN-LPESEMShICLDDESS-------- 1626
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALiaadgfkdsdyvamlyelapeLATCEPGQLQSArLPELRRV-IFLGDEKHpgmlnfde 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1627 ------------YEENSCNLNlspaPEEPVYIIYTSGTTGAPKGVIVTYRN-------------FTHAalawrqiyelDR 1681
Cdd:PRK08315 177 llalgravddaeLAARQATLD----PDDPINIQYTSGTTGFPKGATLTHRNilnngyfigeamkLTEE----------DR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1682 K--PVRLlqiasfsFDVFS---GDLArTLTNGGTlIVCPDEtRLEPAEIYKIMNSQRITVMESTPALIIPVMEyvyrnqf 1756
Cdd:PRK08315 243 LciPVPL-------YHCFGmvlGNLA-CVTHGAT-MVYPGE-GFDPLATLAAVEEERCTALYGVPTMFIAELD------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1757 kLPDLDILilgsdmvkaqDFKTLtdRFG---------QSM-RIINSYGVTEATIDSSFYETSMGGEGTGDNVPI------ 1820
Cdd:PRK08315 306 -HPDFARF----------DLSSL--RTGimagspcpiEVMkRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPLekrvtt 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1821 -GSPLPNVHMYVLS-QTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQmkftknpfvsgerlyRTGDRACWLPNGTirlL 1898
Cdd:PRK08315 373 vGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTA---------------EAIDADGWMHTGD---L 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1899 GRMD---YqVKINGyRIET-----------EEIESVLLQTGLVREAAVA-VQHDKNGQAgLAAYIVP---SDVNTNALRA 1960
Cdd:PRK08315 435 AVMDeegY-VNIVG-RIKDmiirggeniypREIEEFLYTHPKIQDVQVVgVPDEKYGEE-VCAWIILrpgATLTEEDVRD 511
|
570 580
....*....|....*....|....*...
gi 363747658 1961 ALTKELPAYMIPAHLIPLENMPLTLNGK 1988
Cdd:PRK08315 512 FCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
603-944 |
1.28e-16 |
|
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: 83.86 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 603 VIYTSGSTGQPKGVAVEHRQAVSflTGMQ--HQFPLSEDDIVMVK------TSFSFDASVWQLfwwslsGASAYLLppgw 674
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIA--ANLQliHAMGLTEADVYLNMlplfhiAGLNLALATFHA------GGANVVM---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 675 EK-DSALIVQAIHQENVTTAHFIPAMLNSFLDQAEiERLSDRTSLKRVfAGGEplAPRTAARFASVLPQVSLIhGYGPTE 753
Cdd:cd17637 73 EKfDPAEALELIEEEKVTLMGSFPPILSNLLDAAE-KSGVDLSSLRHV-LGLD--APETIQRFEETTGATFWS-LYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 754 AtvdAAFYVLDPERDRDRlriPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDpfypg 833
Cdd:cd17637 148 T---SGLVTLSPYRERPG---SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 834 erMYKTGDVARWLPDGNVEFLGRT--DDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GE--PELCAYVEG-- 905
Cdd:cd17637 217 --WHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPkwGEgiKAVCVLKPGat 294
|
330 340 350
....*....|....*....|....*....|....*....
gi 363747658 906 LQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDR 944
Cdd:cd17637 295 LTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
563-947 |
1.38e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 85.91 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 563 PGCSAPNFSGETLevdmtsLASEKAeNHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAV--SFLTGMQHQFPLSEDD 640
Cdd:PRK07008 148 PAGSTPLLCYETL------VGAQDG-DYDWPRFDENQASSLCYTSGTTGNPKGALYSHRSTVlhAYGAALPDAMGLSARD 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 641 IVM-VKTSFSFDAsvWQL-FWWSLSGASayLLPPGWEKDSALIVQAIHQENVTTAHFIPA---MLNSFLDQAEIeRLSdr 715
Cdd:PRK07008 221 AVLpVVPMFHVNA--WGLpYSAPLTGAK--LVLPGPDLDGKSLYELIEAERVTFSAGVPTvwlGLLNHMREAGL-RFS-- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 716 tSLKRVFAGGEPLAPRTAARFASVLpQVSLIHGYGPTE-------ATVDAAFYVLdPERDRDRLRIPIGKPVPGARLYVL 788
Cdd:PRK07008 294 -TLRRTVIGGSACPPAMIRTFEDEY-GVEVIHAWGMTEmsplgtlCKLKWKHSQL-PLDEQRKLLEKQGRVIYGVDMKIV 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 789 DPHLAVQP-SGVA-GELYIAGAGVARGYLNRpaltEERFLEDPFYPgermykTGDVARWLPDGNVEFLGRTDDQVKIRGY 866
Cdd:PRK07008 371 GDDGRELPwDGKAfGDLQVRGPWVIDRYFRG----DASPLVDGWFP------TGDVATIDADGFMQITDRSKDVIKSGGE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 867 RIEPGEIEAALRSIEGVREAA---------------VTVRTDSGEpelcayvegLQRNEVRAQLERLLPGYMVPAYMIEM 931
Cdd:PRK07008 441 WISSIDIENVAVAHPAVAEAAciacahpkwderpllVVVKRPGAE---------VTREELLAFYEGKVAKWWIPDDVVFV 511
|
410
....*....|....*.
gi 363747658 932 EQWPVTPSGKLDRNAL 947
Cdd:PRK07008 512 DAIPHTATGKLQKLKL 527
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1646-1994 |
1.99e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 83.56 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1646 IIYTSGTTGAPKGVIVTYRNF------THAAL---------------AWRQIyeLDR------KPVRLLQIASFSFDVFS 1698
Cdd:PRK07824 40 VVATSGTTGTPKGAMLTAAALtasadaTHDRLggpgqwllalpahhiAGLQV--LVRsviagsEPVELDVSAGFDPTALP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1699 GDLARtLTNGGTLivcpdeTRLEPAEIYKIMNSqritvMESTPALiipvmeyvyrnqfklPDLDILILGSDMVKAQDFKT 1778
Cdd:PRK07824 118 RAVAE-LGGGRRY------TSLVPMQLAKALDD-----PAATAAL---------------AELDAVLVGGGPAPAPVLDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1779 LTDrfgQSMRIINSYGVTEatidssfyeTSmggegtGDNVPIGSPLPNVHMYVlsqtdqiqpigVAGELCIGGAGVAKGY 1858
Cdd:PRK07824 171 AAA---AGINVVRTYGMSE---------TS------GGCVYDGVPLDGVRVRV-----------EDGRIALGGPTLAKGY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1859 HQKPDltqmkftkNPFVSGERLYRTGDrACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHD 1937
Cdd:PRK07824 222 RNPVD--------PDPFAEPGWFRTDD-LGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVfGLPDD 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1938 KNGQAGLAAYIV---PSDVnTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK07824 293 RLGQRVVAAVVGdggPAPT-LEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1524-1994 |
2.07e-16 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 85.46 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQNR---KGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGAD--IL 1598
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRglaKGAR--VAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEaiVV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1599 L------LQQ-----ELKH--------------LISNL---------PESEM-SHICLDDESSyeeNSCNLNLSP---AP 1640
Cdd:PRK07059 127 LenfattVQQvlaktAVKHvvvasmgdllgfkgHIVNFvvrrvkkmvPAWSLpGHVRFNDALA---EGARQTFKPvklGP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1641 EEPVYIIYTSGTTGAPKGVIVTYRNFTHAAL---AWRQ-IYELDRKPVRLLQIAS------FSFDVFSgdlARTLTNGGT 1710
Cdd:PRK07059 204 DDVAFLQYTGGTTGVSKGATLLHRNIVANVLqmeAWLQpAFEKKPRPDQLNFVCAlplyhiFALTVCG---LLGMRTGGR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1711 LIVCPDetrlePAEIykimnSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILilgsdmvkaqDFKTLTDRFGQSMR-- 1788
Cdd:PRK07059 281 NILIPN-----PRDI-----PGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKL----------DFSKLIVANGGGMAvq 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1789 --------------IINSYGVTE----AT---IDSSFYEtsmggeGTgdnvpIGSPLPNVHMYVLSQTDQIQPIGVAGEL 1847
Cdd:PRK07059 341 rpvaerwlemtgcpITEGYGLSEtspvATcnpVDATEFS------GT-----IGLPLPSTEVSIRDDDGNDLPLGEPGEI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1848 CIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVL-LQTGL 1926
Cdd:PRK07059 410 CIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVaSHPGV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1927 VREAAVAVQHDKNGQAgLAAYIVPSDVNTNA--LRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK07059 484 LEVAAVGVPDEHSGEA-VKLFVVKKDPALTEedVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1524-1932 |
2.71e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 84.95 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHY-PKA---RIEyilrDSGAD 1596
Cdd:PRK04319 74 YTYKELKELSNKFANVLKElgvEKGDR--VFIFMPRIPELYFALLGALKNGAIVGPLFEAFmEEAvrdRLE----DSEAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1597 ILLLQQEL-KHLISN-LPESEmsHICL-DDESSYEENSCNLN-----LSP-------APEEPVYIIYTSGTTGAPKGVI- 1660
Cdd:PRK04319 148 VLITTPALlERKPADdLPSLK--HVLLvGEDVEEGPGTLDFNalmeqASDefdiewtDREDGAILHYTSGSTGKPKGVLh 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1661 VTYRNFTHAALAWrqiYELDRKPVrllqiasfsfDVF-----SGDLART-------LTNGGTLIVcpDETRLEPAEIYKI 1728
Cdd:PRK04319 226 VHNAMLQHYQTGK---YVLDLHED----------DVYwctadPGWVTGTsygifapWLNGATNVI--DGGRFSPERWYRI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1729 MNSQRITVMESTPALIIPVMEyvyrnqfklpdldiliLGSDMVKAQDFKTLtdRFGQS------------------MRII 1790
Cdd:PRK04319 291 LEDYKVTVWYTAPTAIRMLMG----------------AGDDLVKKYDLSSL--RHILSvgeplnpevvrwgmkvfgLPIH 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1791 NSYGVTEatidssfyetsmggegTGD----NVP--------IGSPLPNVHMYVLSQTDQIQPIGVAGELCI--GGAGVAK 1856
Cdd:PRK04319 353 DNWWMTE----------------TGGimiaNYPamdikpgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMR 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 1857 GYHQKPDltqmKFTKNpFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV 1932
Cdd:PRK04319 417 GIWNNPE----KYESY-FAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1512-2008 |
6.46e-16 |
|
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: 83.90 E-value: 6.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVI------DNEIEISYRFLNERANRLARTLQN---RKG----------PKPTVAVLAKRSIDAIVGVLAvmkaGG 1572
Cdd:cd05967 65 GDQIALIydspvtGTERTYTYAELLDEVSRLAGVLRKlgvVKGdrviiympmiPEAAIAMLACARIGAIHSVVF----GG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1573 VYIP-----IDSHYPK------------ARIEYI-LRDSGadILLLQQELKH-LISNLPESEMShiCLDDESSYEENSCN 1633
Cdd:cd05967 141 FAAKelasrIDDAKPKlivtascgiepgKVVPYKpLLDKA--LELSGHKPHHvLVLNRPQVPAD--LTKPGRDLDWSELL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1634 LNLSPAP------EEPVYIIYTSGTTGAPKGVIVTyrNFTHA-ALAW--RQIYELdrKPVRLLQIAS-------FSFDVF 1697
Cdd:cd05967 217 AKAEPVDcvpvaaTDPLYILYTSGTTGKPKGVVRD--NGGHAvALNWsmRNIYGI--KPGDVWWAASdvgwvvgHSYIVY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1698 SgdlarTLTNGGTLIVC---PDETRlEPAEIYKIMNSQRITVMESTPALI--I----PVMEYVyrNQFKLPDLDILILGS 1768
Cdd:cd05967 293 G-----PLLHGATTVLYegkPVGTP-DPGAFWRVIEKYQVNALFTAPTAIraIrkedPDGKYI--KKYDLSSLRTLFLAG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1769 DMVKAQDFKTLTDRFGQSmrIINSYGVTEAtiDSSFYETSMGGEGTgdNVPIGS---PLPNVHMYVLSQTDQIQPIGVAG 1845
Cdd:cd05967 365 ERLDPPTLEWAENTLGVP--VIDHWWQTET--GWPITANPVGLEPL--PIKAGSpgkPVPGYQVQVLDEDGEPVGPNELG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1846 ELCIGGA---GVAKGYHQKPDLTQMK-FTKNPFVsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVL 1921
Cdd:cd05967 439 NIVIKLPlppGCLLTLWKNDERFKKLyLSKFPGY-----YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1922 LQTGLVREAAVAVQHDK-NGQAGLAAYIVPSDVN------TNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05967 514 LSHPAVAECAVVGVRDElKGQVPLGLVVLKEGVKitaeelEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
570
....*....|....*
gi 363747658 1995 -PVPNNvlsRPYTAP 2008
Cdd:cd05967 594 rKIADG---EDYTIP 605
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
2126-2272 |
7.18e-16 |
|
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: 82.79 E-value: 7.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2126 NANALHLALRKITEHHDAIRMIFqRDQNGHVIQFnrgINhkDHELFGLYISDWTKASLERTHLD-EKLAAEEtvIQSKMN 2204
Cdd:cd19531 37 DVAALERALNELVARHEALRTTF-VEVDGEPVQV---IL--PPLPLPLPVVDLSGLPEAEREAEaQRLAREE--ARRPFD 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 363747658 2205 VEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPktdsyLS--YAD 2272
Cdd:cd19531 109 LARGPLLRATLLRLGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPP-----LPiqYAD 174
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
465-844 |
7.22e-16 |
|
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: 83.64 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 465 ERQAAFTPER--LAIRFSGG---SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLD 539
Cdd:cd05921 2 AHWARQAPDRtwLAEREGNGgwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 540 PAYP-----KERLSYMLKdsgasllLTQPGC----SAPNFSG--ETLEVDMTSLA--------------------SEKAE 588
Cdd:cd05921 82 PAYSlmsqdLAKLKHLFE-------LLKPGLvfaqDAAPFARalAAIFPLGTPLVvsrnavagrgaisfaelaatPPTAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 589 NHEFTPADG-GSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFP-LSEDDIVMVKT---SFSFDAS-VWQLFWWSl 662
Cdd:cd05921 155 VDAAFAAVGpDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPfFGEEPPVLVDWlpwNHTFGGNhNFNLVLYN- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 663 sGASAYL-----LPPGWEKDSALIvqaihQENVTTAHF-IPA---MLNSFLDQAEIERLSDRTSLKRVFAGGEPLAPRTA 733
Cdd:cd05921 234 -GGTLYIddgkpMPGGFEETLRNL-----REISPTVYFnVPAgweMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 734 ARFASVLPQ-----VSLIHGYGPTEATVDAAFYVLDPERDRDrlripIGKPVPGARLYVLdphlavqPSGVAGELYIAGA 808
Cdd:cd05921 308 DRLQALAVAtvgerIPMMAGLGATETAPTATFTHWPTERSGL-----IGLPAPGTELKLV-------PSGGKYEVRVKGP 375
|
410 420 430
....*....|....*....|....*....|....*.
gi 363747658 809 GVARGYLNRPALTEERFLEDPFypgermYKTGDVAR 844
Cdd:cd05921 376 NVTPGYWRQPELTAQAFDEEGF------YCLGDAAK 405
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1640-1991 |
1.09e-15 |
|
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: 83.38 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 PEEPVYIIYTSGTTGAPKGVIVT---YrnFTHAALAWRqiYELDRKPVrllqiasfsfDVF--SGDLART---------- 1704
Cdd:cd05966 230 SEDPLFILYTSGSTGKPKGVVHTtggY--LLYAATTFK--YVFDYHPD----------DIYwcTADIGWItghsyivygp 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1705 LTNGGTLIVC------PDETRLepaeiYKIMNSQRITVMESTPALIIPVMEYvyrnqfklpdldililGSDMVKAQDFKT 1778
Cdd:cd05966 296 LANGATTVMFegtptyPDPGRY-----WDIVEKHKVTIFYTAPTAIRALMKF----------------GDEWVKKHDLSS 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1779 LtdrfgqsmRIINS------------Y----GVTEATIDSSFYETSMGG------EGTGDNVPiGS---PLPNVHMYVLS 1833
Cdd:cd05966 355 L--------RVLGSvgepinpeawmwYyeviGKERCPIVDTWWQTETGGimitplPGATPLKP-GSatrPFFGIEPAILD 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1834 QTDQIQPIGVAGELCIGGA--GVAK---GYHQKPDLTQMKFTKNpfvsgerLYRTGDRACWLPNGTIRLLGRMDYQVKIN 1908
Cdd:cd05966 426 EEGNEVEGEVEGYLVIKRPwpGMARtiyGDHERYEDTYFSKFPG-------YYFTGDGARRDEDGYYWITGRVDDVINVS 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1909 GYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIV------PSDVNTNALRAALTKELPAYMIPAHLIPLENM 1981
Cdd:cd05966 499 GHRLGTAEVESALVAHPAVAEAAVvGRPHDIKGEA-IYAFVTlkdgeePSDELRKELRKHVRKEIGPIATPDKIQFVPGL 577
|
410
....*....|
gi 363747658 1982 PLTLNGKLDR 1991
Cdd:cd05966 578 PKTRSGKIMR 587
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1648-1994 |
1.51e-15 |
|
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: 80.99 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1648 YTSGTTGAPKgvIVTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSG--DLARTLTNGGTLIVCPDETRLEPA-- 1723
Cdd:cd05944 9 HTGGTTGTPK--LAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSvvTLLTPLASGAHVVLAGPAGYRNPGlf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1724 -EIYKIMNSQRITVMESTPALIIPVMEyVYRNQfKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATIDS 1802
Cdd:cd05944 87 dNFWKLVERYRITSLSTVPTVYAALLQ-VPVNA-DISSLRFAMSGAAPLPVELRARFEDATG--LPVVEGYGLTEATCLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1803 SFYETSmGGEGTGDnvpIGSPLPNVHMYVL---SQTDQIQPIGV--AGELCIGGAGVAKGYhqkpdlTQMKFTKNPFVsG 1877
Cdd:cd05944 163 AVNPPD-GPKRPGS---VGLRLPYARVRIKvldGVGRLLRDCAPdeVGEICVAGPGVFGGY------LYTEGNKNAFV-A 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1878 ERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYI--VP-SDVN 1954
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqlKPgAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 363747658 1955 TNALRAALTKELPAYM-IPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05944 312 EEELLAWARDHVPERAaVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1508-1995 |
1.62e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 82.35 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEIEISYRFLNERANRLARTL-QNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARI 1586
Cdd:PRK13383 45 AARWPGRTAIIDDDGALSYRELQRATESLARRLtRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1587 EYILRDSGADILLLQQELKHLISNLPESemshICLDDESSYEENSCNLNLSPAPEEPVyIIYTSGTTGAPKGVIVTYRnF 1666
Cdd:PRK13383 125 AAALRAHHISTVVADNEFAERIAGADDA----VAVIDPATAGAEESGGRPAVAAPGRI-VLLTSGTTGKPKGVPRAPQ-L 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1667 THAALAWRQIyeLDRKPVRLLQIASFSFDVFS----GDLARTLTNGGTLIV---CPDETRLEPAEIYKimnSQRITVMES 1739
Cdd:PRK13383 199 RSAVGVWVTI--LDRTRLRTGSRISVAMPMFHglglGMLMLTIALGGTVLThrhFDAEAALAQASLHR---ADAFTAVPV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1740 TPALIIPVMEYVyRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMriINSYGVTEATIDssfyetSMGGEGTGDNVP 1819
Cdd:PRK13383 274 VLARILELPPRV-RARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDIL--YNGYGSTEVGIG------ALATPADLRDAP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1820 --IGSPLPNVHMYVLSQTDqiQPIG--VAGELCIGGAGVAKGYHQKpdltqmkfTKNPFVSGerLYRTGDRACWLPNGTI 1895
Cdd:PRK13383 345 etVGKPVAGCPVRILDRNN--RPVGprVTGRIFVGGELAGTRYTDG--------GGKAVVDG--MTSTGDMGYLDNAGRL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1896 RLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---SDVNTNALRAALTKELPAYMI 1971
Cdd:PRK13383 413 FIVGREDDMIISGGENVYPRAVENALAAHPAVADNAViGVPDERFGHR-LAAFVVLhpgSGVDAAQLRDYLKDRVSRFEQ 491
|
490 500
....*....|....*....|....
gi 363747658 1972 PAHLIPLENMPLTLNGKLDRNALP 1995
Cdd:PRK13383 492 PRDINIVSSIPRNPTGKVLRKELP 515
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1503-1900 |
1.75e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 82.79 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1503 IFEAKAEEIPEHIAVIDNE------IEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYI 1575
Cdd:PRK12582 54 LLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGlDPGRPVMILSGNSIEHALMTLAAMQAGVPAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1576 PIDSHYP-----KARIEY---------ILRDSGAdilLLQQELKHL---------ISNLPESEMShICLDD--------- 1623
Cdd:PRK12582 134 PVSPAYSlmshdHAKLKHlfdlvkprvVFAQSGA---PFARALAALdlldvtvvhVTGPGEGIAS-IAFADlaatpptaa 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1624 -ESSYEENScnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQI--YELDRKPVRLLQIASFSfDVFSGD 1700
Cdd:PRK12582 210 vAAAIAAIT--------PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLrpREPDPPPPVSLDWMPWN-HTMGGN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1701 LA--RTLTNGGTLIVcpDETRLEPAEIYK-IMNSQRI--TVMESTP---ALIIPVMEY---VYRNQFKlpDLDILILG-- 1767
Cdd:PRK12582 281 ANfnGLLWGGGTLYI--DDGKPLPGMFEEtIRNLREIspTVYGNVPagyAMLAEAMEKddaLRRSFFK--NLRLMAYGga 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1768 --SDMV--KAQDFKTLTDrfGQSMRIINSYGVTEA--TIDSSFYETSMGGEgtgdnvpIGSPLPNVHMYVLsqtdqiqPI 1841
Cdd:PRK12582 357 tlSDDLyeRMQALAVRTT--GHRIPFYTGYGATETapTTTGTHWDTERVGL-------IGLPLPGVELKLA-------PV 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363747658 1842 GVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACWL----PNGTIRLLGR 1900
Cdd:PRK12582 421 GDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdpddPEKGLIFDGR 477
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1523-1989 |
1.78e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 82.26 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1523 EISYRFLNERANRLARTLQN---RKGPkpTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADIL- 1598
Cdd:PRK08276 11 VVTYGELEARSNRLAHGLRAlglREGD--VVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1599 -------LLQQELKHLISNLPESEMSHICLDDESSYEEnscnlNLSPAPEEPV-------YIIYTSGTTGAPKGVIvtyR 1664
Cdd:PRK08276 89 vsaaladTAAELAAELPAGVPLLLVVAGPVPGFRSYEE-----ALAAQPDTPIadetagaDMLYSSGTTGRPKGIK---R 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1665 NFTHAalawrqiyELDRKPVRLLQIASFSFDVFSGDLA----------------RTLTNGGTLIVCPD---ETRLEPAEI 1725
Cdd:PRK08276 161 PLPGL--------DPDEAPGMMLALLGFGMYGGPDSVYlspaplyhtaplrfgmSALALGGTVVVMEKfdaEEALALIER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1726 YKIMNSQritvmestpalIIPVMeyvYRNQFKLPdldililgsDMVKAqdfktltdRFG-QSMRIINSYG------VTEA 1798
Cdd:PRK08276 233 YRVTHSQ-----------LVPTM---FVRMLKLP---------EEVRA--------RYDvSSLRVAIHAAapcpveVKRA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1799 TID---SSFYETSMGGEGTGDNV---------P--IGSPLPNVhMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDL 1864
Cdd:PRK08276 282 MIDwwgPIIHEYYASSEGGGVTVitsedwlahPgsVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1865 TQMKFTKNPFVSgerlyrTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAG 1943
Cdd:PRK08276 361 TAAARNPHGWVT------VGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVfGVPDEEMGERV 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 363747658 1944 LA-----AYIVPSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKL 1989
Cdd:PRK08276 435 KAvvqpaDGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1639-1994 |
1.80e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 82.23 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1639 APEEPVYIIYTSGTTGAPKGVIVTYRNFT---HAALAWRQIYE--LDRKPVRLLQIASFSFDVFSGDLARTLTNGGT--L 1711
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLVanmQQAHQWLAGTGklEEGCEVVITALPLYHIFALTANGLVFMKIGGCnhL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1712 IVCPDETRLEPAEIYKImnsqRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVK---AQDFKTLTdrfgqSMR 1788
Cdd:PRK08751 286 ISNPRDMPGFVKELKKT----RFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQrsvAERWKQVT-----GLT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1789 IINSYGVTEATIDSSFYETSMggegTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQmk 1868
Cdd:PRK08751 357 LVEAYGLTETSPAACINPLTL----KEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETA-- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1869 ftknPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVL-LQTGLVREAAVAVQHDKNGQAgLAAY 1947
Cdd:PRK08751 431 ----KVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIaMMPGVLEVAAVGVPDEKSGEI-VKVV 505
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 363747658 1948 IVPSDVNTNA--LRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK08751 506 IVKKDPALTAedVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
459-947 |
2.09e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 82.04 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 459 TLHGLFERQAAFTPERLAIRF--SGGS---LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGG 533
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALIFesSGGVvrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 534 AYLPLDPAYPKERLSYMLKDSGASLLLTQP-----------------------GCSAPNFSGEtleVDMTSLASEK-AEN 589
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTSAqfypmyrqiqqedatplrhicltRVALPADDGV---SSFTQLKAQQpATL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 590 HEFTPADGGSLAYVIYTSGSTGQPKGVAVEHR--QAVSFLTGMQHQfpLSEDDIVM-VKTSFSFDASVWQLFWWSLSGAS 666
Cdd:PRK08008 165 CYAPPLSTDDTAEILFTSGTTSRPKGVVITHYnlRFAGYYSAWQCA--LRDDDVYLtVMPAFHIDCQCTAAMAAFSAGAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 667 AYLLppgwEKDSA-LIVQAIHQENVTTAHFIPAMLNSFLDQ--AEIER------------LSDRTslKRVFAggeplapr 731
Cdd:PRK08008 243 FVLL----EKYSArAFWGQVCKYRATITECIPMMIRTLMVQppSANDRqhclrevmfylnLSDQE--KDAFE-------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 732 taARFAsvlpqVSLIHGYGPTEATVDaafyvLDPERDRDRLRIP-IGKPVPGARLYVLDPHLAVQPSGVAGELYI---AG 807
Cdd:PRK08008 309 --ERFG-----VRLLTSYGMTETIVG-----IIGDRPGDKRRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 808 AGVARGYLNRPALTEERFLEDPFYpgermyKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAA 887
Cdd:PRK08008 377 KTIFKEYYLDPKATAKVLEADGWL------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIV 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 888 VTVRTDSGEPE-LCAYV-----EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK08008 451 VVGIKDSIRDEaIKAFVvlnegETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1508-1994 |
4.15e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEI--EISYRFLNERANRLARTLQNrKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPK 1583
Cdd:PRK13390 7 AQIAPDRPAVIVAETgeQVSYRQLDDDSAALARVLYD-AGLRTgdVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1584 ARIEYILRDSGADILLLQQELKHLISNLPESEMSHIC----LDDESSYEENSCNLNlSPAPEEP--VYIIYTSGTTGAPK 1657
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSfggeIDGFGSFEAALAGAG-PRLTEQPcgAVMLYSSGTTGFPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1658 GVivtyrnftHAALAWRQIyelDRKPVRLLQIASFSFDVFSGDL---------ARTL-------TNGGTLIVCpdeTRLE 1721
Cdd:PRK13390 165 GI--------QPDLPGRDV---DAPGDPIVAIARAFYDISESDIyyssapiyhAAPLrwcsmvhALGGTVVLA---KRFD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1722 PAEIYKIMNSQRITVMESTPALIIPVMEY--VYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmrIINSYGVTEA- 1798
Cdd:PRK13390 231 AQATLGHVERYRITVTQMVPTMFVRLLKLdaDVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPI--VYEYYSSTEAh 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1799 ---TIDSSFYETSMGGEGTgdnvpigSPLPNVHmyVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLT-QMKFTKNPF 1874
Cdd:PRK13390 309 gmtFIDSPDWLAHPGSVGR-------SVLGDLH--ICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTaAAQHPAHPF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1875 VSgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQ-----AGLAAYI 1948
Cdd:PRK13390 380 WT-----TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAViGVPDPEMGEqvkavIQLVEGI 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 363747658 1949 VPSDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK13390 455 RGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1508-1994 |
5.31e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 80.30 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEIEISYRFLNERANRLARTLQnRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKAR 1585
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFA-QQGVVEgsGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1586 IEYILRDSGADILLLQQELKHLIsnlpesemshicLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRN 1665
Cdd:PRK09029 92 LEELLPSLTLDFALVLEGENTFS------------ALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1666 ftHAALAwrqiyeldrkpVRLLQIASFS-----------FDVfSGD--LARTLTNGGTLIVcPDETRLEPAeiykimnsq 1732
Cdd:PRK09029 160 --HLASA-----------EGVLSLMPFTaqdswllslplFHV-SGQgiVWRWLYAGATLVV-RDKQPLEQA--------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1733 ritVMESTPALIIP--VMEYVYRNQFKLPDLDILiLGSDMVKAqdfkTLTDRFGQsmRIINS---YGVTEA--TI----- 1800
Cdd:PRK09029 216 ---LAGCTHASLVPtqLWRLLDNRSEPLSLKAVL-LGGAAIPV----ELTEQAEQ--QGIRCwcgYGLTEMasTVcakra 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1801 DSSfyetsmggegtgDNVpiGSPLPNvHMYVLsqtdqiqpigVAGELCIGGAGVAKGYHQKPDLTqmkftknPFVSGERL 1880
Cdd:PRK09029 286 DGL------------AGV--GSPLPG-REVKL----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGW 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1881 YRTGDRACWLpNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKN-GQAGLAAYIVPSDVNTNALR 1959
Cdd:PRK09029 334 FATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEfGQRPVAVVESDSEAAVVNLA 412
|
490 500 510
....*....|....*....|....*....|....*...
gi 363747658 1960 AALTKELPAYMIPAHLIPlenMPLTL-NG--KLDRNAL 1994
Cdd:PRK09029 413 EWLQDKLARFQQPVAYYL---LPPELkNGgiKISRQAL 447
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
2095-2474 |
6.33e-15 |
|
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: 79.80 E-value: 6.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2095 LTPIQRRFFgqvhaFHNHYN--QSVMLFS----EKG-FNANALHLALRKITEHHDAIRMIFQRDQNGHVIQfnrgINHKD 2167
Cdd:cd19536 4 LSSLQEGML-----FHSLLNpgGSVYLHNytytVGRrLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQ----VVHRQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2168 HELFGLYISDWtkaslertHLDEKLAA-----EETVIQsKMNVEKGPLLQAGLFKTAEGDH--LLIALHHLVIDGVSWRI 2240
Cdd:cd19536 75 AQVPVTELDLT--------PLEEQLDPlraykEETKIR-RFDLGRAPLVRAALVRKDERERflLVISDHHSILDGWSLYL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2241 LLEDLAAAYQQALEKKEIQLPPKtdsyLSYADGLTQIAESKQLLSEKTYWQTIL---DAHTAFLPKDIENVPDRLqmnsD 2317
Cdd:cd19536 146 LVKEILAVYNQLLEYKPLSLPPA----QPYRDFVAHERASIQQAASERYWREYLagaTLATLPALSEAVGGGPEQ----D 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2318 AAAFVLSGDWTEKLLFETQQayGTDANELLLTALGMALSEWAGHDQIVISTEGHGREGHVPNIDisRTVGWFTSIYPILL 2397
Cdd:cd19536 218 SELLVSVPLPVRSRSLAKRS--GIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAE--RLLGLFLNTLPLRV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2398 D------MGIPEPFEDQLAYRIKTTKDMLRRVPNKGTGYGLLTHIGELRHKepEVSFNYLGQFSEEKEAETFQLSYYQPS 2471
Cdd:cd19536 294 TlseetvEDLLKRAQEQELESLSHEQVPLADIQRCSEGEPLFDSIVNFRHF--DLDFGLPEWGSDEGMRRGLLFSEFKSN 371
|
...
gi 363747658 2472 YEI 2474
Cdd:cd19536 372 YDV 374
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1485-1994 |
7.08e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 80.42 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1485 EFNKTQVEFAQK--------DVPFHRIFEAKAEeiPEHIAVIDNEIEISYRFLNERANRLARTLQnRKGPKP--TVAVLA 1554
Cdd:PRK10946 4 PFTRWPEEFARRyrekgywqDLPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLR-RQGIKPgdTALVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1555 KRSIDAIVGVLAVMKAGGVyiPIDSHYPKARIEyiLRDSGADI---LLL---QQELKH-------LISNLPEseMSHICL 1621
Cdd:PRK10946 81 GNVAEFYITFFALLKLGVA--PVNALFSHQRSE--LNAYASQIepaLLIadrQHALFSdddflntLVAEHSS--LRVVLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1622 DDESS-------YEENSCNLNLSPAPEEPVYIIYTSG-TTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQI-ASF 1692
Cdd:PRK10946 155 LNDDGehslddaINHPAEDFTATPSPADEVAFFQLSGgSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALpAAH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1693 SFDVFS-GDLArTLTNGGTLIVCPDEtrlEPAEIYKIMNSQRITVMESTPALIIPVMEYV----YRNQfkLPDLDILILG 1767
Cdd:PRK10946 235 NYPMSSpGALG-VFLAGGTVVLAPDP---SATLCFPLIEKHQVNVTALVPPAVSLWLQAIaeggSRAQ--LASLKLLQVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1768 ----SDMVKAQDFKTLTDR----FGQSMRIINsYGVTEATIDSSFyeTSMGgegtgdnVPIGsplPNVHMYVLSQTDQIQ 1839
Cdd:PRK10946 309 garlSETLARRIPAELGCQlqqvFGMAEGLVN-YTRLDDSDERIF--TTQG-------RPMS---PDDEVWVADADGNPL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1840 PIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIES 1919
Cdd:PRK10946 376 PQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIEN 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 1920 VLLQTGLVREAA-VAVQHDKNGQAGLAAYIVPSDVNTNALRAALTKELPA-YMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK10946 450 LLLRHPAVIHAAlVSMEDELMGEKSCAFLVVKEPLKAVQLRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
464-856 |
7.09e-15 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 80.69 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 464 FERQAAFTPER--LAIRFSGG---SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL 538
Cdd:PRK08180 45 LVHWAQEAPDRvfLAERGADGgwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 539 DPAY-----PKERLSYMLKdsgasllLTQPGC----SAPNFS-----------------GETLEVDMTSLAS-----EKA 587
Cdd:PRK08180 125 SPAYslvsqDFGKLRHVLE-------LLTPGLvfadDGAAFAralaavvpadvevvavrGAVPGRAATPFAAllatpPTA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 588 ENHEFTPADGG-SLAYVIYTSGSTGQPKGVAVEHR-----QAvsfltgMQHQ-FP-LSEDDIVMVktsfsfDASVWQ--- 656
Cdd:PRK08180 198 AVDAAHAAVGPdTIAKFLFTSGSTGLPKAVINTHRmlcanQQ------MLAQtFPfLAEEPPVLV------DWLPWNhtf 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 657 ---------LFWwslsGASAYL-----LPPGWEKDSALIvqaihQENVTTAHF-IPA---MLNSFL--DQAEIERLSDRt 716
Cdd:PRK08180 266 ggnhnlgivLYN----GGTLYIddgkpTPGGFDETLRNL-----REISPTVYFnVPKgweMLVPALerDAALRRRFFSR- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 717 sLKRVFAGGEPLAPRTAARF-----ASVLPQVSLIHGYGPTEaTVDAAFYVLDPerdRDRLRIpIGKPVPGARLYVLdph 791
Cdd:PRK08180 336 -LKLLFYAGAALSQDVWDRLdrvaeATCGERIRMMTGLGMTE-TAPSATFTTGP---LSRAGN-IGLPAPGCEVKLV--- 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 792 lavqPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWL----PDGNVEFLGR 856
Cdd:PRK08180 407 ----PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRFVdpadPERGLMFDGR 465
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
455-892 |
8.35e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 80.54 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 455 PKAFTLHGLFERQAAFTPERLAIRFSGGS---------LTYAELdmyASRLAAhLAAR--GITN-ESIVGVLSERSPEML 522
Cdd:PRK07769 18 PPNTNLVRHVERWAKVRGDKLAYRFLDFSterdgvardLTWSQF---GARNRA-VGARlqQVTKpGDRVAILAPQNLDYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 523 IAVLAVLKAGGAYLPL-DPAYP--KERLSYMLKDSGASLLLTQPGCSA----------PNFSGETLEVDmtSLASEKAEN 589
Cdd:PRK07769 94 IAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEgvrkffrarpAKERPRVIAVD--AVPDEVGAT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 590 HEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLSGA---- 665
Cdd:PRK07769 172 WVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHyitf 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 666 ---SAYLLPPG-WEKDSAlivqaihQENVTTAHFIPAMLNSFLDQA-------EIERLSDRTSLKRVFAGGEPLAPRTAA 734
Cdd:PRK07769 252 mspAAFVRRPGrWIRELA-------RKPGGTGGTFSAAPNFAFEHAaarglpkDGEPPLDLSNVKGLLNGSEPVSPASMR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 735 RFASV-----LPQVSLIHGYGPTEATVDAAFYVLDPER-----DRDRL------RIPIGKP--VPGAR---------LYV 787
Cdd:PRK07769 325 KFNEAfapygLPPTAIKPSYGMAEATLFVSTTPMDEEPtviyvDRDELnagrfvEVPADAPnaVAQVSagkvgvsewAVI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 788 LDPHLAV-QPSGVAGELYIAGAGVARGYLNRPALTEERF---LEDPFYP--------GERMYKTGDVARWLpDGNVEFLG 855
Cdd:PRK07769 405 VDPETASeLPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLSEshaegapdDALWVRTGDYGVYF-DGELYITG 483
|
490 500 510
....*....|....*....|....*....|....*..
gi 363747658 856 RTDDQVKIRGYRIEPGEIEAAlrsiegVREAAVTVRT 892
Cdd:PRK07769 484 RVKDLVIIDGRNHYPQDLEYT------AQEATKALRT 514
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1502-1972 |
2.06e-14 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 79.15 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1502 RIFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQNR---KGpkPTVAVLAKRSIDAIVGVLAVMKAGGVYIPID 1578
Cdd:PRK08279 41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARgvgKG--DVVALLMENRPEYLAAWLGLAKLGAVVALLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1579 SHYPKARIEYILRDSGADILLLQQELKHLISNLPESEMSHICL----DDESSYEENSCNLN--LSPAP------------ 1640
Cdd:PRK08279 119 TQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLwvagGDTLDDPEGYEDLAaaAAGAPttnpasrsgvta 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1641 EEPVYIIYTSGTTGAPKGVIVTYRNFThAALAWrqiyeldrkpvrllqiasfsfdvFSGDLART---------------- 1704
Cdd:PRK08279 199 KDTAFYIYTSGTTGLPKAAVMSHMRWL-KAMGG-----------------------FGGLLRLTpddvlycclplyhntg 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1705 --------LTNGGTLIVCP--------DETRLEPA-------EI--YkIMNSqritvmestpaliiPVMEYVYRNQFKlp 1759
Cdd:PRK08279 255 gtvawssvLAAGATLALRRkfsasrfwDDVRRYRAtafqyigELcrY-LLNQ--------------PPKPTDRDHRLR-- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1760 dldiLILGSDMvKAQDFKTLTDRFGQsMRIINSYGVTEATIdsSFYETsmggegtgDNVP--IG-SPLPNVHMYVLSQTD 1836
Cdd:PRK08279 318 ----LMIGNGL-RPDIWDEFQQRFGI-PRILEFYAASEGNV--GFINV--------FNFDgtVGrVPLWLAHPYAIVKYD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1837 QI--QPI------------GVAGELC--IGGAGVAKGYHQkPDLTQMKFTKNPFVSGERLYRTGDRACWLPNGTIRLLGR 1900
Cdd:PRK08279 382 VDtgEPVrdadgrcikvkpGEVGLLIgrITDRGPFDGYTD-PEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDR 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 1901 M-D-YQVKinGYRIETEEIESVLLQTGLVREAAV-AVQ-HDKNGQAGLAAyIVPSDVNT---NALRAALTKELPAYMIP 1972
Cdd:PRK08279 461 LgDtFRWK--GENVATTEVENALSGFPGVEEAVVyGVEvPGTDGRAGMAA-IVLADGAEfdlAALAAHLYERLPAYAVP 536
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
7-419 |
3.00e-14 |
|
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: 77.23 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 7 SLTHAQRRVWFTELLEPNTSICNLT-ACvKFKGNIELDTLEGALN-----HSISRNdaiRFQLLEGeelepRLHLTEYKY 80
Cdd:cd19537 3 ALSPIEREWWHKYQLSTGTSSFNVSfAC-RLSGDVDRDRLASAWNtvlarHRILRS---RYVPRDG-----GLRRSYSSS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 81 YP----LRIIDfsnvemieieqwIQDQASIPFKLINSPLyqfylLRI---DSHevwLFAKFHHIIMDGISLNVMGNQIID 153
Cdd:cd19537 74 PPrvqrVDTLD------------VWKEINRPFDLEREDP-----IRVfisPDT---LLVVMSHIICDLTTLQLLLREVSA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 154 LYQKMKkkdPLPDQPEpsylsyiekesqYLQSPRFAK-----DRLFWTqtfehplEYHSLADQTSLQKQSTSAS-RDT-- 225
Cdd:cd19537 134 AYNGKL---LPPVRRE------------YLDSTAWSRpaspeDLDFWS-------EYLSGLPLLNLPRRTSSKSyRGTsr 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 226 -IILSPDLEQTIRIFCEEHKINIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAEKEMLGMFVSSLPIRITVDPDT- 303
Cdd:cd19537 192 vFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPSSSd 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 304 ----DFLSFVRTIGREQLS-VMrhqrfPYNLLVNELrneqkdlhnliGISMQY--QPL-----QWHnaDDFDYETALYFS 371
Cdd:cd19537 272 asaaDFLRAVRRSSQAALAhAI-----PWHQLLEHL-----------GLPPDSpnHPLfdvmvTFH--DDRGVSLALPIP 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 372 G----YTANE-----LSVQIQErIDNGTIQLNFDYQNTLFSLEDIKRIQSHLLTILE 419
Cdd:cd19537 334 GveplYTWAEgakfpLMFEFTA-LSDDSLLLRLEYDTDCFSEEEIDRIESLILAALE 389
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
961-1034 |
5.79e-14 |
|
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: 69.11 E-value: 5.79e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 961 APRNVTEMKLSQLWEDVLKNGP--VGIHDNFF-DRGGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLATVIRE 1034
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDPeeITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
467-947 |
6.41e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 467 QAAFTPERLAIRF--SGGSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPK 544
Cdd:PRK13390 6 HAQIAPDRPAVIVaeTGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 545 ERLSYMLKDSGASLLLTQP---GCSAPnfSGETLEVDMTSLAS-EKAENHEFTPADGGSL-------AYVIYTSGSTGQP 613
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAaldGLAAK--VGADLPLRLSFGGEiDGFGSFEAALAGAGPRlteqpcgAVMLYSSGTTGFP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 614 KGVA--VEHRQA-------VSFLTGMqhqFPLSEDDIVMVKTSFSFDASvwqLFWWSLSGASAYLLPPGWEKDSALIVQA 684
Cdd:PRK13390 164 KGIQpdLPGRDVdapgdpiVAIARAF---YDISESDIYYSSAPIYHAAP---LRWCSMVHALGGTVVLAKRFDAQATLGH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 685 IHQENVTTAHFIPAMLNSFLD-QAEIERLSDRTSLKRVFAGGEPLAPRTAARFASVLPQVsLIHGYGPTEA----TVDAA 759
Cdd:PRK13390 238 VERYRITVTQMVPTMFVRLLKlDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYYSSTEAhgmtFIDSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 760 FYVLDPERdrdrlripIGKPVPGArLYVLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERflEDPFYPgerMYKT 839
Cdd:PRK13390 317 DWLAHPGS--------VGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAA--QHPAHP---FWTT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 840 -GDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDsgePEL-------CAYVEGLQRNEv 911
Cdd:PRK13390 383 vGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPD---PEMgeqvkavIQLVEGIRGSD- 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 363747658 912 raQLERLL--------PGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK13390 459 --ELARELidytrsriAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1642-1932 |
6.97e-14 |
|
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: 75.42 E-value: 6.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1642 EPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLArTLTNGGTLIVCPdetRLE 1721
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLA-TFHAGGTNVFVR---RVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1722 PAEIYKIMNSQRITvmestPALIIP--VMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTD-RFGQSMRiinSYGVTEA 1798
Cdd:cd17636 77 AEEVLELIEAERCT-----HAFLLPptIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVDTsPWGRKPG---GYGQTEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1799 TIDSSFYetSMGGEGTGDNvpiGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTknpfvSGe 1878
Cdd:cd17636 149 MGLATFA--ALGGGAIGGA---GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-----GG- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 1879 rLYRTGDRACWLPNGTIRLLG---RMdyqVKINGYRIETEEIESVLLQTGLVREAAV 1932
Cdd:cd17636 218 -WHHTNDLGRREPDGSLSFVGpktRM---IKSGAENIYPAEVERCLRQHPAVADAAV 270
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
8-419 |
7.35e-14 |
|
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: 76.52 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 8 LTHAQRrvWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIR--FQLLEGEeLEPRLHLTEYKYYPLRI 85
Cdd:cd19534 4 LTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRmrFRREDGG-WQQRIRGDVEELFRLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 86 IDFSNVEMIE-IEQWIQD-QASIpfKLINSPLYQ---FYLLRiDSHEVWLFAkfHHIIMDGISLnvmgnQII--DL---Y 155
Cdd:cd19534 81 VDLSSLAQAAaIEALAAEaQSSL--DLEEGPLLAaalFDGTD-GGDRLLLVI--HHLVVDGVSW-----RILleDLeaaY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 156 QKMKKKDPLPDQPEPSYLSYIEKESQYLQSPRFAKDRLFWTQTFehPLEYHSL-ADQTSLQKQSTSASrdtIILSPdlEQ 234
Cdd:cd19534 151 EQALAGEPIPLPSKTSFQTWAELLAEYAQSPALLEELAYWRELP--AADYWGLpKDPEQTYGDARTVS---FTLDE--EE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 235 TIRIFCEEHK---INIISLFMASFYICISRITSKKDLAI-----GtyygnRGSKAEK----EMLGMFVSSLPIRITVDPD 302
Cdd:cd19534 224 TEALLQEANAayrTEINDLLLAALALAFQDWTGRAPPAIfleghG-----REEIDPGldlsRTVGWFTSMYPVVLDLEAS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 303 TDFLSFVRTIgREQLSVMRHQRFPYNLL--VNELRNEQKDLHNLIGISMQY--------------QPLQWHNADDFDYET 366
Cdd:cd19534 299 EDLGDTLKRV-KEQLRRIPNKGIGYGILryLTPEGTKRLAFHPQPEISFNYlgqfdqgerddalfVSAVGGGGSDIGPDT 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 367 ALYFsgytanelSVQIQERIDNGTIQLNFDYQNTLFSLEDIKR----IQSHLLTILE 419
Cdd:cd19534 378 PRFA--------LLDINAVVEGGQLVITVSYSRNMYHEETIQQladsYKEALEALIE 426
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
484-958 |
1.32e-13 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 76.36 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAAR-GITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYM------------ 550
Cdd:PRK05620 39 TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIinhaedevivad 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 551 --LKDSGASLLLTQPGCSAPNFSGETlevDMTSLASEKAENHEFTP----ADGGSLAY------------VIYTSGSTGQ 612
Cdd:PRK05620 119 prLAEQLGEILKECPCVRAVVFIGPS---DADSAAAHMPEGIKVYSyealLDGRSTVYdwpeldettaaaICYSTGTTGA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 613 PKGVAVEHRQAvsFLTGMQhqfpLSEDDIVMVK--TSFSFDASVWQLFWWS------LSGASayLLPPGWEKDSALIVQA 684
Cdd:PRK05620 196 PKGVVYSHRSL--YLQSLS----LRTTDSLAVThgESFLCCVPIYHVLSWGvplaafMSGTP--LVFPGPDLSAPTLAKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 685 IHQENVTTAHFIPAMLNSFLDQAEiERLSDRTSLKRVFAGGEPLAPRT----AARFAsvlpqVSLIHGYGPTEATvdAAF 760
Cdd:PRK05620 268 IATAMPRVAHGVPTLWIQLMVHYL-KNPPERMSLQEIYVGGSAVPPILikawEERYG-----VDVVHVWGMTETS--PVG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 761 YVLDPE-----RDRDRLRIPIGKpVPGARLY--VLDPHLAVQPSGVAGELYIAGAGVARGYLNRPALTE----------- 822
Cdd:PRK05620 340 TVARPPsgvsgEARWAYRVSQGR-FPASLEYriVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEGggaastfrged 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 823 -----ERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--G 895
Cdd:PRK05620 419 vedanDRFTADGW------LRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDkwG 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 896 EPELCAYV--EGLQRN-----EVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRN--------------ALPAPGGAA 954
Cdd:PRK05620 493 ERPLAVTVlaPGIEPTretaeRLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKdlrqhladgdfeiiKLKGPGESG 572
|
....
gi 363747658 955 DAET 958
Cdd:PRK05620 573 ESDS 576
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1522-1901 |
1.38e-13 |
|
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: 75.97 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1522 IEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIdshYPKA---RIEYILRDSGADI 1597
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGlEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTLnpdTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1598 LLLQQ--ELKHLISNLPESEMSHIC--LDDESSYEENSCNLN--------LSPAPEEPVYIIYTSGTTGAPKGVIVTYRN 1665
Cdd:cd05932 82 LFVGKldDWKAMAPGVPEGLISISLppPSAANCQYQWDDLIAqhppleerPTRFPEQLATLIYTSGTTGQPKGVMLTFGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1666 FTHAALAwrQIYELDRKPV-RLL------QIASFSFdVFSGDLArtltnGGTLIVCPDETRLEPAEiykiMNSQRITVME 1738
Cdd:cd05932 162 FAWAAQA--GIEHIGTEENdRMLsylplaHVTERVF-VEGGSLY-----GGVLVAFAESLDTFVED----VQRARPTLFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1739 STPALIIPVMEYVYRnqfKLP--DLDILI----------------LGSDMVK---------AQDFKTLTDRFGqsMRIIN 1791
Cdd:cd05932 230 SVPRLWTKFQQGVQD---KIPqqKLNLLLkipvvnslvkrkvlkgLGLDQCRlagcgsapvPPALLEWYRSLG--LNILE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1792 SYGVTEatidsSFYETSMGGEGTGDNVPIGSPLPNVHMyvlsqtdqiqPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTK 1871
Cdd:cd05932 305 AYGMTE-----NFAYSHLNYPGRDKIGTVGNAGPGVEV----------RISEDGEILVRSPALMMGYYKDPEATAEAFTA 369
|
410 420 430
....*....|....*....|....*....|
gi 363747658 1872 NPFVsgerlyRTGDRACWLPNGTIRLLGRM 1901
Cdd:cd05932 370 DGFL------RTGDKGELDADGNLTITGRV 393
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
696-947 |
2.73e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 73.93 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 696 IPAMLNSFLDQAE-IERLSdrtSLKRVFAGGEPLaPRTAARFASVLpQVSLIHGYGPTEAtvdAAFYVLDperdrdrlri 774
Cdd:PRK07824 133 VPMQLAKALDDPAaTAALA---ELDAVLVGGGPA-PAPVLDAAAAA-GINVVRTYGMSET---SGGCVYD---------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 775 piGKPVPGARLYVLDphlavqpsgvaGELYIAGAGVARGYLNRPalteerflEDPFYPGERMYKTGDVARwLPDGNVEFL 854
Cdd:PRK07824 195 --GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV--------DPDPFAEPGWFRTDDLGA-LDDGVLTVL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 855 GRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEPELCAYVEGLQRNEV----RAQLERLLPGYMVPAYM 928
Cdd:PRK07824 253 GRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDrlGQRVVAAVVGDGGPAPTlealRAHVARTLDRTAAPREL 332
|
250
....*....|....*....
gi 363747658 929 IEMEQWPVTPSGKLDRNAL 947
Cdd:PRK07824 333 HVVDELPRRGIGKVDRRAL 351
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1498-1994 |
3.25e-13 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 75.26 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1498 VPFhrIFEAKAEeiPEHIAVIDNE--IEISYRFLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGV 1573
Cdd:PLN02574 43 VSF--IFSHHNH--NGDTALIDSStgFSISYSELQPLVKSMAAGLYHVMGVRQgdVVLLLLPNSVYFPVIFLAVLSLGGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1574 YIPIDSHYPKARIEYILRDSGADILLLQQELKHLISNL-------PES-EMSHICLDDESSYEENSCNLNLSPAP----E 1641
Cdd:PLN02574 119 VTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLgvpvigvPENyDFDSKRIEFPKFYELIKEDFDFVPKPvikqD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1642 EPVYIIYTSGTTGAPKGVIVTYRNFTH-----------------------AALAWRQIYELDRKPVRLLQIasfsfdvfs 1698
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIAmvelfvrfeasqyeypgsdnvylAALPMFHIYGLSLFVVGLLSL--------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1699 gdlartltnGGTLIVCpdeTRLEPAEIYKIMNSQRITVMESTPaliiPVMEYVYR-------NQFKlpDLDILILGSdmv 1771
Cdd:PLN02574 270 ---------GSTIVVM---RRFDASDMVKVIDRFKVTHFPVVP----PILMALTKkakgvcgEVLK--SLKQVSCGA--- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1772 kAQDFKTLTDRFGQSM---RIINSYGVTEAT-IDSSFYETsmggEGTGDNVPIGSPLPNVHMYVLS-QTDQIQPIGVAGE 1846
Cdd:PLN02574 329 -APLSGKFIQDFVQTLphvDFIQGYGMTESTaVGTRGFNT----EKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1847 LCIGGAGVAKGYHQKPDLTQMKFTKNPFVsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGL 1926
Cdd:PLN02574 404 LWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPE 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 363747658 1927 VREAAVAVQHDKNGQAGLAAYIVP---SDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PLN02574 478 IIDAAVTAVPDKECGEIPVAFVVRrqgSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1512-1994 |
3.30e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 75.27 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1512 PEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKrSIDAIV-GVLAVMKAGGVYIPIDSHYPKARIEYI 1589
Cdd:PLN02479 34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSiGPGSTVAVIAP-NIPAMYeAHFGVPMAGAVVNCVNIRLNAPTIAFL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1590 LRDSGADILLLQQELKHLISN----LPESEMSH------ICLDDES---------------SYEE----NSCNLNLSPAP 1640
Cdd:PLN02479 113 LEHSKSEVVMVDQEFFTLAEEalkiLAEKKKSSfkppllIVIGDPTcdpkslqyalgkgaiEYEKfletGDPEFAWKPPA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1641 EE--PVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFD--VFSGDLArtlTNGGTLIVCpd 1716
Cdd:PLN02479 193 DEwqSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNgwCFTWTLA---ALCGTNICL-- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1717 eTRLEPAEIYKIMNSQRITVMESTPALI-----IPVMEYVyrnqFKLPDL-DILILGSdmvkAQDFKTLTDRFGQSMRII 1790
Cdd:PLN02479 268 -RQVTAKAIYSAIANYGVTHFCAAPVVLntivnAPKSETI----LPLPRVvHVMTAGA----APPPSVLFAMSEKGFRVT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1791 NSYGVTEATIDSsfyeTSMGGEGTGDNVPIG-----SPLPNVHMYVLSQTDQIQPIGVA---------GELCIGGAGVAK 1856
Cdd:PLN02479 339 HTYGLSETYGPS----TVCAWKPEWDSLPPEeqarlNARQGVRYIGLEGLDVVDTKTMKpvpadgktmGEIVMRGNMVMK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1857 GYHQKPdltqmKFTKNPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQH 1936
Cdd:PLN02479 415 GYLKNP-----KANEEAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARP 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 1937 DKNGQAGLAAYIVPSDVNTNALRAALT--------KELPAYMIPAHLI--PLenmPLTLNGKLDRNAL 1994
Cdd:PLN02479 488 DERWGESPCAFVTLKPGVDKSDEAALAedimkfcrERLPAYWVPKSVVfgPL---PKTATGKIQKHVL 552
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
596-888 |
3.46e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 75.17 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 596 DGGSLAYVIYTSGSTGQPKGVAVEHRQAV--SFLTGMQHQFPLSEDDIVMVKTSFsFDASVWQLFwWSLSGASAYLLPPG 673
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSHRSNVlhALMANNGDALGTSAADTMLPVVPL-FHANSWGIA-FSAPSMGTKLVMPG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 674 WEKDSALIVQAIHQENVTTAHFIPA---MLNSFLdQAEIERLSDrtsLKRVFAGGEPlAPRTAARfASVLPQVSLIHGYG 750
Cdd:PRK06018 253 AKLDGASVYELLDTEKVTFTAGVPTvwlMLLQYM-EKEGLKLPH---LKMVVCGGSA-MPRSMIK-AFEDMGVEVRHAWG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 751 PTE-------ATVDAAFYVLDPERDRDRLRIPiGKPVPGARLYVLDPHLAVQPS-GVA-GELYIAGAGVARGYLNrpalT 821
Cdd:PRK06018 327 MTEmsplgtlAALKPPFSKLPGDARLDVLQKQ-GYPPFGVEMKITDDAGKELPWdGKTfGRLKVRGPAVAAAYYR----V 401
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 822 EERFLEDpfypgERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 888
Cdd:PRK06018 402 DGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAV 463
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
484-944 |
3.57e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 75.04 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGG--AYLPLdPAYPKERLSY------MLKDSG 555
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLvpVPLPL-PMGFGGRESYiaqlrgMLASAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 556 ASLLLTQPGC-----SAPNFSGETLEVDMTSLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGM 630
Cdd:PRK09192 129 PAAIITPDELlpwvnEATHGNPLLHVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 631 QHqfplsedDIVMVKTSfsfDASVWQLFWWSLSGASAYLLPP--------------------GWEKdsaLIvqaihQENV 690
Cdd:PRK09192 209 SH-------DGLKVRPG---DRCVSWLPFYHDMGLVGFLLTPvatqlsvdylptrdfarrplQWLD---LI-----SRNR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 691 TTAHFIPamlnSF--------LDQAEIERLsDRTSLKRVFAGGEPLAPRT----AARFASV-------LPQvslihgYGP 751
Cdd:PRK09192 271 GTISYSP----PFgyelcarrVNSKDLAEL-DLSCWRVAGIGADMIRPDVlhqfAEAFAPAgfddkafMPS------YGL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 752 TEATVDAAFYVLDP-----ERDRDRLR------------------IPIGKPVPGARLYVLDPHLAVQPSGVAGELYIAGA 808
Cdd:PRK09192 340 AEATLAVSFSPLGSgivveEVDRDRLEyqgkavapgaetrrvrtfVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGP 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 809 GVARGYLNRP----ALTEERFLEdpfypgermykTGDVArWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR 884
Cdd:PRK09192 420 SLMSGYFRDEesqdVLAADGWLD-----------TGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELR 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 885 --EAAVTVRTDSGEPELCAYVEG-LQRNEVRAQLERLLPGY------------MVPAYMIemeqwPVTPSGKLDR 944
Cdd:PRK09192 488 sgDAAAFSIAQENGEKIVLLVQCrISDEERRGQLIHALAALvrsefgveaaveLVPPHSL-----PRTSSGKLSR 557
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1503-1994 |
3.67e-13 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 75.09 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1503 IFEAKAEEIPEHIAVIDNEIEISYRFLNERANRLARTLQN----RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPID 1578
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNglglKKGDR--VALMMPNLLQYPIALFGILRAGMIVVNVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1579 SHYPKARIEYILRDSGADILLLQQELKHLISNLPE-SEMSHICL----DDESSYEENSCNL------NLSP--------- 1638
Cdd:PRK08974 106 PLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFkTPVKHVILtrmgDQLSTAKGTLVNFvvkyikRLVPkyhlpdais 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1639 ------------------APEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYE-LDRKPVRLLQIASFSFDVFsg 1699
Cdd:PRK08974 186 frsalhkgrrmqyvkpelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGpLLHPGKELVVTALPLYHIF-- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1700 dlART------LTNGGT--LIVCPdetRLEPAEIyKIMNSQRITVMESTPALIipvMEYVYRNQFKLPDLDILIL--GSD 1769
Cdd:PRK08974 264 --ALTvncllfIELGGQnlLITNP---RDIPGFV-KELKKYPFTAITGVNTLF---NALLNNEEFQELDFSSLKLsvGGG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1770 M----VKAQDFKTLTDRfgqsmRIINSYGVTEAT-------IDSSFYETSmggegtgdnvpIGSPLPNVHMYVLSQTDQI 1838
Cdd:PRK08974 335 MavqqAVAERWVKLTGQ-----YLLEGYGLTECSplvsvnpYDLDYYSGS-----------IGLPVPSTEIKLVDDDGNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1839 QPIGVAGELCIGGAGVAKGYHQKPDLTQmKFTKNPFVSgerlyrTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIE 1918
Cdd:PRK08974 399 VPPGEPGELWVKGPQVMLGYWQRPEATD-EVIKDGWLA------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIE 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 1919 SVLLQTGLVRE-AAVAVQHDKNGQAgLAAYIVPSD--VNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK08974 472 DVVMLHPKVLEvAAVGVPSEVSGEA-VKIFVVKKDpsLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2125-2302 |
4.03e-13 |
|
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: 74.03 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2125 FNANALHLALRKITEHHDAIRM-IFQRDQNGHVIQfnrGINHKdhelfglyisdwTKASLERTHLDEKLAAEETV--IQS 2201
Cdd:cd19532 36 LDVARLERAVRAVGQRHEALRTcFFTDPEDGEPMQ---GVLAS------------SPLRLEHVQISDEAEVEEEFerLKN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2202 -KMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQAlekkeiQLPPKTDSYLSYADGLTQIAE 2279
Cdd:cd19532 101 hVYDLESGETMRIVLLSLSPTEHyLIFGYHHIAMDGVSFQIFLRDLERAYNGQ------PLLPPPLQYLDFAARQRQDYE 174
|
170 180
....*....|....*....|...
gi 363747658 2280 SKQLLSEKTYWQTILDAHTAFLP 2302
Cdd:cd19532 175 SGALDEDLAYWKSEFSTLPEPLP 197
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1504-1994 |
4.26e-13 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 74.70 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1504 FEAKAEEIPEHIAVIDNEIE------ISYRFLNERANRLARTLqNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYI 1575
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGL-ARLGVGRgdVVSCQLPNWWEFTVLYLACSRIGAVLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1576 PIDSHYPKARIEYILRDSGADILLLQQE---------LKHLISNLPEseMSHICL---DDESSYEENSCN---------- 1633
Cdd:PRK13295 109 PLMPIFRERELSFMLKHAESKVLVVPKTfrgfdhaamARRLRPELPA--LRHVVVvggDGADSFEALLITpaweqepdap 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1634 ---LNLSPAPEEPVYIIYTSGTTGAPKGVIVTyrnfthAALAWRQIYELdrkPVRLlqiasfsfDVFSGD---LARTLTN 1707
Cdd:PRK13295 187 ailARLRPGPDDVTQLIYTSGTTGEPKGVMHT------ANTLMANIVPY---AERL--------GLGADDvilMASPMAH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1708 ------GGTLIVCPDETRL-----EPAEIYKIMNSQRIT-VMESTPALIiPVMEYVYRNQFKLPDLDILILGSDMVKAQD 1775
Cdd:PRK13295 250 qtgfmyGLMMPVMLGATAVlqdiwDPARAAELIRTEGVTfTMASTPFLT-DLTRAVKESGRPVSSLRTFLCAGAPIPGAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1776 FKTLTDRFGQSmrIINSYGVTEATIdssfyeTSMGGEGTGDNVPI---GSPLPNVHMYVLSQTDQIQPIGVAGELCIGGA 1852
Cdd:PRK13295 329 VERARAALGAK--IVSAWGMTENGA------VTLTKLDDPDERASttdGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1853 GVAKGYHQKPDLTQMkftknpfvSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV 1932
Cdd:PRK13295 401 SNFGGYLKRPQLNGT--------DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAI 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 1933 AVQHDKNGQAGLAAYIVP---SDVNTNALRAAL-TKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK13295 473 VAYPDERLGERACAFVVPrpgQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1521-1994 |
4.50e-13 |
|
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: 74.42 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1521 EIEISYRFLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADIL 1598
Cdd:cd05928 39 EVKWSFRELGSLSRKAANVLSGACGLQRgdRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1599 LLQQEL----------------KHLISN------------LPESEMSHICLDDESsyeenscnlnlspapEEPVYIIYTS 1650
Cdd:cd05928 119 VTSDELapevdsvasecpslktKLLVSEksrdgwlnfkelLNEASTEHHCVETGS---------------QEPMAIYFTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1651 GTTGAPKGVIVTYRNFTHAALAWRQiYELDRKPVRLLQIASFSFDVFS--GDLARTLTNGGTLIV--CPdetRLEPAEIY 1726
Cdd:cd05928 184 GTTGSPKMAEHSHSSLGLGLKVNGR-YWLDLTASDIMWNTSDTGWIKSawSSLFEPWIQGACVFVhhLP---RFDPLVIL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1727 KIMNSQRITVMESTPAliipvmeyVYR-------NQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEAT 1799
Cdd:cd05928 260 KTLSSYPITTFCGAPT--------VYRmlvqqdlSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTG--LDIYEGYGQTETG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1800 IDSSFYETSMGGEGTgdnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIggagvaKGYHQKPDLTQMKFTKNP--FVSG 1877
Cdd:cd05928 330 LICANFKGMKIKPGS-----MGKASPPYDVQIIDDNGNVLPPGTEGDIGI------RVKPIRPFGLFSGYVDNPekTAAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1878 ER--LYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSDVNT 1955
Cdd:cd05928 399 IRgdFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFL 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 363747658 1956 NALRAALTKEL--------PAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:cd05928 479 SHDPEQLTKELqqhvksvtAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1524-1949 |
4.69e-13 |
|
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: 74.14 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPidshypkarieyilrdsgADILLLQQ 1602
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGvGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1603 ELKHLIsnlpESEMSHICLDDESSyeenscnlnlspAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAwrQIYELDRK 1682
Cdd:cd05974 63 DLRDRV----DRGGAVYAAVDENT------------HADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLS--TMYWIGLK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1683 PVRL-LQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMESTPAliipvmeyVYR-------N 1754
Cdd:cd05974 125 PGDVhWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPT--------VWRmliqqdlA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1755 QFKLPDLDILILGS-------DMVKAQDFKTLTDRFGQsmriinsygvTEATIdssfyetsMGGEGTGDNVPIGS---PL 1824
Cdd:cd05974 197 SFDVKLREVVGAGEplnpeviEQVRRAWGLTIRDGYGQ----------TETTA--------LVGNSPGQPVKAGSmgrPL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1825 PNVHMYVLsqtDQIQPIGVAGELCIG-----GAGVAKGYHQKPDLTQMkftknpfVSGERLYRTGDRACWLPNGTIRLLG 1899
Cdd:cd05974 259 PGYRVALL---DPDGAPATEGEVALDlgdtrPVGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVG 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 363747658 1900 RMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV 1949
Cdd:cd05974 329 RADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIV 378
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1508-1949 |
5.27e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 74.25 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVIDNEI--EISYRFLNERANRLARTLQN---RKGpKPTVAVLAKRSIDAIVgVLAVMKAGGVYIPIDSHYP 1582
Cdd:PLN02330 38 AELYADKVAFVEAVTgkAVTYGEVVRDTRRFAKALRSlglRKG-QVVVVVLPNVAEYGIV-ALGIMAAGGVFSGANPTAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1583 KARIEYILRDSGADILLLQ----QELKHLisNLPESEMSHICLDDESSYEE--NSCNLNLSPAPEEPVY------IIYTS 1650
Cdd:PLN02330 116 ESEIKKQAEAAGAKLIVTNdtnyGKVKGL--GLPVIVLGEEKIEGAVNWKEllEAADRAGDTSDNEEILqtdlcaLPFSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1651 GTTGAPKGVIVTYRNFThaALAWRQIYELdrKPVRLLQIASFSFDVF------SGDLARTLTNGGTLIVCpdeTRLEPAE 1724
Cdd:PLN02330 194 GTTGISKGVMLTHRNLV--ANLCSSLFSV--GPEMIGQVVTLGLIPFfhiygiTGICCATLRNKGKVVVM---SRFELRT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1725 IYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDI-LILGSDMVKAQDFKTLTDRFGQSMRIINSYGVTEATIDSS 1803
Cdd:PLN02330 267 FLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1804 FYETSMGGEGTGDNVPIGSPLPNVHM-YVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVsgerlyR 1882
Cdd:PLN02330 347 THGDPEKGHGIAKKNSVGFILPNLEVkFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWL------H 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 1883 TGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV 1949
Cdd:PLN02330 421 TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVV 487
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
471-941 |
6.31e-13 |
|
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: 74.23 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 471 TPERLAI-RFSGGS---LTYAELDMYASRLAAHLAARGI-TNESIVGVLSErSPEMLIAVLAVLKAGGAYLPLDPAY--- 542
Cdd:cd05943 82 ADDPAAIyAAEDGErteVTWAELRRRVARLAAALRALGVkPGDRVAGYLPN-IPEAVVAMLATASIGAIWSSCSPDFgvp 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 543 ----------PK-----ERLSYMLK--DSGASLLLTQPGcsAPNFSgETLEVDMTS-------------------LASEK 586
Cdd:cd05943 161 gvldrfgqiePKvlfavDAYTYNGKrhDVREKVAELVKG--LPSLL-AVVVVPYTVaagqpdlskiakaltledfLATGA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 587 AENHEFTPADGGSLAYVIYTSGSTGQPK-------GVAVEHRQAVSFLTGMQHQfplsedDIVMVKTSFSfdasvWQLFW 659
Cdd:cd05943 238 AGELEFEPLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEHILHCDLRPG------DRLFYYTTCG-----WMMWN 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 660 WSLS----GASAYLL--PPGWEKDSALIvQAIHQENVTT----AHFIPAMLNSFLDQAEIERLSdrtSLKRVFAGGEPLA 729
Cdd:cd05943 307 WLVSglavGATIVLYdgSPFYPDTNALW-DLADEEGITVfgtsAKYLDALEKAGLKPAETHDLS---SLRTILSTGSPLK 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 730 PRTAARFAS-VLPQVSLIHGYGPTEatVDAAFYVLDPErdrdrlrIPIGK-----PVPGARLYVLDPHlAVQPSGVAGEL 803
Cdd:cd05943 383 PESFDYVYDhIKPDVLLASISGGTD--IISCFVGGNPL-------LPVYRgeiqcRGLGMAVEAFDEE-GKPVWGEKGEL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 804 YIagagvARGYLNRPAlteeRFLEDP---------F--YPGerMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGE 872
Cdd:cd05943 453 VC-----TKPFPSMPV----GFWNDPdgsryraayFakYPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAE 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 873 IEAALRSIEGVREA-AVTVRTDSGEPELCAYV---EGLQ-----RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGK 941
Cdd:cd05943 522 IYRVVEKIPEVEDSlVVGQEWKDGDERVILFVklrEGVElddelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1641-1994 |
8.77e-13 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 74.16 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1641 EEPVYIIYTSGTTGAPKGVIVTYRNF-THAALAWRqiYELDRKPVRLLQ-------IASFSFDVFSgdlarTLTNGGTLI 1712
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGGYmVYTATTFK--YAFDYKPTDVYWctadcgwITGHSYVTYG-----PMLNGATVL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1713 VC------PDetrlePAEIYKIMNSQRITVMESTPALIIPVM----EYVYRNQFKlpdlDILILGS--DMVKAQDFKTLT 1780
Cdd:PLN02654 348 VFegapnyPD-----SGRCWDIVDKYKVTIFYTAPTLVRSLMrdgdEYVTRHSRK----SLRVLGSvgEPINPSAWRWFF 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1781 DRFGQSmriinsygvtEATIDSSFYETSMGG------EGTGDNVPIGSPLP--NVHMYVLSQTDQIQPIGVAGELCIGGA 1852
Cdd:PLN02654 419 NVVGDS----------RCPISDTWWQTETGGfmitplPGAWPQKPGSATFPffGVQPVIVDEKGKEIEGECSGYLCVKKS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1853 --GVAK---GYHQKPDLTQMKFTKNPFVSGERLYRTGDRACWLPngtirllGRMDYQVKINGYRIETEEIESVLLQTGLV 1927
Cdd:PLN02654 489 wpGAFRtlyGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLT-------GRVDDVINVSGHRIGTAEVESALVSHPQC 561
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 1928 REAA-VAVQHDKNGQaGLAAYI-----VP-SDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PLN02654 562 AEAAvVGIEHEVKGQ-GIYAFVtlvegVPySEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
602-949 |
1.03e-12 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 73.83 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 602 YVIYTSGSTGQPKGVaveHRQ----AVSFLTGMQHQFPLSEDDiVMVKTS-------FSF-------------------- 650
Cdd:PRK10524 237 YILYTSGTTGKPKGV---QRDtggyAVALATSMDTIFGGKAGE-TFFCASdigwvvgHSYivyapllagmatimyeglpt 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 651 --DASVWqlfwWSLsgasayllppgwekdsalivqaIHQENVTTAHFIPA---MLNSFlDQAEIERlSDRTSLKRVFAGG 725
Cdd:PRK10524 313 rpDAGIW----WRI----------------------VEKYKVNRMFSAPTairVLKKQ-DPALLRK-HDLSSLRALFLAG 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 726 EPLAPRTAARFASVLpQVSLIHGYGPTEATVDAAFYVLDPERDRDRLRIPiGKPVPGARLYVLDpHLAVQPSGvAGElyi 805
Cdd:PRK10524 365 EPLDEPTASWISEAL-GVPVIDNYWQTETGWPILAIARGVEDRPTRLGSP-GVPMYGYNVKLLN-EVTGEPCG-PNE--- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 806 AGAGVARGYLNRPALT-----EERFLEDPFYP-GERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRS 879
Cdd:PRK10524 438 KGVLVIEGPLPPGCMQtvwgdDDRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISS 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 880 IEGVREAAV----------------TVRTDSG--EPELCAYVEGlqrnEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGK 941
Cdd:PRK10524 518 HPAVAEVAVvgvkdalkgqvavafvVPKDSDSlaDREARLALEK----EIMALVDSQLGAVARPARVWFVSALPKTRSGK 593
|
....*...
gi 363747658 942 LDRNALPA 949
Cdd:PRK10524 594 LLRRAIQA 601
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
592-943 |
1.08e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 74.23 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 592 FTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVM----VKTSFSFDASvwqLFWWSLSGASA 667
Cdd:PRK06814 787 FCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFnalpVFHSFGLTGG---LVLPLLSGVKV 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 668 YLLPpgwekdSAL----IVQAIHQENVT----TAHFipamLNSFldqAEIERLSDRTSLKRVFAGGEPLAPRT----AAR 735
Cdd:PRK06814 864 FLYP------SPLhyriIPELIYDTNATilfgTDTF----LNGY---ARYAHPYDFRSLRYVFAGAEKVKEETrqtwMEK 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 736 FAsvlpqVSLIHGYGPTEATVDAAFYVldPERDRDRlriPIGKPVPGARlYVLDPHLAVqPSGvaGELYIAGAGVARGYL 815
Cdd:PRK06814 931 FG-----IRILEGYGVTETAPVIALNT--PMHNKAG---TVGRLLPGIE-YRLEPVPGI-DEG--GRLFVRGPNVMLGYL 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 816 --NRPALTEErfledpfyPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEA-----------ALRSIE- 881
Cdd:PRK06814 997 raENPGVLEP--------PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEElaaelwpdalhAAVSIPd 1068
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 882 ---GVREAAVTVRTDSGEPELCAYVEGLQRNEVraqlerllpgyMVPAYMIEMEQWPVTPSGKLD 943
Cdd:PRK06814 1069 arkGERIILLTTASDATRAAFLAHAKAAGASEL-----------MVPAEIITIDEIPLLGTGKID 1122
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
473-947 |
1.16e-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. 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: 73.23 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 473 ERLAIRFsgGSLTYAELDMY-------ASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKE 545
Cdd:cd05915 9 GRKEVVS--RLHTGEVHRTTyaevyqrARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 546 RLSYMLKDSGASLLLTQPGCSAPNFSGETLEVDMTSLASEKAENHEFT--------------PADGGSLAYVIYTSGSTG 611
Cdd:cd05915 87 EIAYILNHAEDKVLLFDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYlayeealgeeadpvRVPERAACGMAYTTGTTG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 612 QPKGVAVEHRQAVSFLT--GMQHQFPLSEDDIVMVKTSFsFDASVWqLFWWSLSGASAYLLPPGWEKDSALIVQAIHQEN 689
Cdd:cd05915 167 LPKGVVYSHRALVLHSLaaSLVDGTALSEKDVVLPVVPM-FHVNAW-CLPYAATLVGAKQVLPGPRLDPASLVELFDGEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 690 VTTAHFIPAMLNSFLDQAEIERLSDRTSLKRVFAGGEPlaPRTAARFASVLP-QVSLIHG----YGPTEATVDAAFYVLD 764
Cdd:cd05915 245 VTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAA--PRSLIARFERMGvEVRQGYGltetSPVVVQNFVKSHLESL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 765 PERDRDRLRIPIGKPVPGARLYVLDPHLAVQPSGVAGELYIA--GAGVARGYLNRPALTEERFLEDPFYpgermyKTGDV 842
Cdd:cd05915 323 SEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQlkGPWITGGYYGNEEATRSALTPDGFF------RTGDI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 843 ARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYVEgLQRNEVRAQ------ 914
Cdd:cd05915 397 AVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPkwQE-RPLAVVV-PRGEKPTPEelnehl 474
|
490 500 510
....*....|....*....|....*....|...
gi 363747658 915 LERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05915 475 LKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
484-947 |
1.33e-12 |
|
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: 72.84 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQp 563
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 564 gcsapnfsgetLEVDMTSLASE---KAENHEFTpadggSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDD 640
Cdd:cd05939 83 -----------LLDPLLTQSSTeppSQDDVNFR-----DKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPED 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 641 IVMVKTSFSFDAS----VWQLFWWSLS-------GASAYllppgWeKDSAlivqaihQENVTTAHFIPAMLNSFLDQAEI 709
Cdd:cd05939 147 VVYDCLPLYHSAGgimgVGQALLHGSTvvirkkfSASNF-----W-DDCV-------KYNCTIVQYIGEICRYLLAQPPS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 710 ERlSDRTSLKRVFAGGepLAPRTAARFASV--LPQVSLIhgYGPTEAT----------------------------VDAA 759
Cdd:cd05939 214 EE-EQKHNVRLAVGNG--LRPQIWEQFVRRfgIPQIGEF--YGATEGNsslvnidnhvgacgfnsrilpsvypirlIKVD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 760 FYVLDPERDRDRLRIPIGKPVPGA---RLYVLDPHLAVQpsgvagelyiagagvarGYLNRPAlTEERFLEDPFYPGERM 836
Cdd:cd05939 289 EDTGELIRDSDGLCIPCQPGEPGLlvgKIIQNDPLRRFD-----------------GYVNEGA-TNKKIARDVFKKGDSA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 837 YKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAA---VTVRTDSGEPELCAYV---EGLQRNE 910
Cdd:cd05939 351 FLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVvygVEVPGVEGRAGMAAIVdpeRKVDLDR 430
|
490 500 510
....*....|....*....|....*....|....*..
gi 363747658 911 VRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:cd05939 431 FSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1642-1991 |
1.37e-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: 71.53 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1642 EPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLArTLTNGGTLIVCPdetRLE 1721
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALA-TFHAGGANVVME---KFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1722 PAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDIlILGSDMVK-AQDFKTLTDrfgqsMRIINSYGVTEAti 1800
Cdd:cd17637 77 PAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRH-VLGLDAPEtIQRFEETTG-----ATFWSLYGQTET-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1801 dSSFYETSMGGEGTGDnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHQKPDLTQMKFtKNPFvsgerl 1880
Cdd:cd17637 149 -SGLVTLSPYRERPGS---AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGW------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1881 YRTGDracwlpngtirlLGRMDYQ--------------VKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAA 1946
Cdd:cd17637 218 HHTGD------------LGRFDEDgylwyagrkpekelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKA 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 363747658 1947 YIVpsdvnTNALRAALTKELPA--------YMIPAHLIPLENMPLTLNGKLDR 1991
Cdd:cd17637 286 VCV-----LKPGATLTADELIEfvgsriarYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1508-1994 |
1.50e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 72.80 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVI---DNEIeISYRFLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYP 1582
Cdd:PRK13391 7 AQTTPDKPAVImasTGEV-VTYRELDERSNRLAHLFRSL-GLKRgdHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1583 KARIEYILRDSGADILLLQQELKHLISNLPEsEMSHI--CL----DDES----SYEENSCNLNLSPAPEEP--VYIIYTS 1650
Cdd:PRK13391 85 PAEAAYIVDDSGARALITSAAKLDVARALLK-QCPGVrhRLvldgDGELegfvGYAEAVAGLPATPIADESlgTDMLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1651 GTTGAPKGV--------IVTYRNFTH-AALAWR----QIYeldRKPVRLLQIASFSFdvfsgdLARTLTNGGTLIVCPD- 1716
Cdd:PRK13391 164 GTTGRPKGIkrplpeqpPDTPLPLTAfLQRLWGfrsdMVY---LSPAPLYHSAPQRA------VMLVIRLGGTVIVMEHf 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1717 --ETRLEPAEIYKIMNSQRITVMESTpALIIPvmEYVyRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQsmrIINS-Y 1793
Cdd:PRK13391 235 daEQYLALIEEYGVTHTQLVPTMFSR-MLKLP--EEV-RDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGP---IIHEyY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1794 GVTEAT----IDSsfyETSMGGEGTGDNVPIGSPlpnvhmYVLSQTDQIQPIGVAGELCIGGaGVAKGYHQKPDLTQMKF 1869
Cdd:PRK13391 308 AATEGLgftaCDS---EEWLAHPGTVGRAMFGDL------HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEAR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1870 TKNPFVSgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYI 1948
Cdd:PRK13391 378 HPDGTWS-----TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVfGVPNEDLGEE-VKAVV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 363747658 1949 VPSD-VNTNA-----LRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK13391 452 QPVDgVDPGPalaaeLIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2094-2409 |
1.79e-12 |
|
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: 72.14 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2094 ELTPIQRRFF---------GQV--HAfhnhYNQsvmlFSEKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQfnrg 2162
Cdd:cd19535 3 PLTDVQYAYWigrqddqelGGVgcHA----YLE----FDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2163 inhkDHELFGLYISDWTKASLErtHLDEKLAAE-ETVIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRI 2240
Cdd:cd19535 71 ----EVPWYGITVHDLRGLSEE--EAEAALEELrERLSHRVLDVERGPLFDIRLSLLPEGRTrLHLSIDLLVADALSLQI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2241 LLEDLAAAYQQAlekkEIQLPPKTDSYLSYadgLTQIAESKQLLSE--KTYWQTILDAhtafLP--------KDIENVPD 2310
Cdd:cd19535 145 LLRELAALYEDP----GEPLPPLELSFRDY---LLAEQALRETAYEraRAYWQERLPT----LPpapqlplaKDPEEIKE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2311 ----RLQMNSDAAafvlsgDWteKLLFETQQAYGTDANELLLTALGMALSEWAGHDQIVIsteghgreghvpNI------ 2380
Cdd:cd19535 214 prftRREHRLSAE------QW--QRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLL------------NLtlfnrl 273
|
330 340 350
....*....|....*....|....*....|....*
gi 363747658 2381 ----DISRTVGWFTSIypILL--DMGIPEPFEDQL 2409
Cdd:cd19535 274 plhpDVNDVVGDFTSL--LLLevDGSEGQSFLERA 306
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
600-944 |
2.71e-12 |
|
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: 72.14 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 600 LAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSL-SGASAYLLPpgwekDS 678
Cdd:cd05908 108 LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLiAGMNQYLMP-----TR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 679 ALIVQAI--------HQENVTTA-HFIPAMLNSFLDQAEIERLsDRTSLKRVFAGGEPLAPRTAARF-----ASVLPQVS 744
Cdd:cd05908 183 LFIRRPIlwlkkaseHKATIVSSpNFGYKYFLKTLKPEKANDW-DLSSIRMILNGAEPIDYELCHEFldhmsKYGLKRNA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 745 LIHGYGPTEATVDAAFYVLD-------------------PERDRDRLR----IPIGKPVPGARLYVLDPHLAVQPSGVAG 801
Cdd:cd05908 262 ILPVYGLAEASVGASLPKAQspfktitlgrrhvthgepePEVDKKDSEcltfVEVGKPIDETDIRICDEDNKILPDGYIG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 802 ELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVArWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIE 881
Cdd:cd05908 342 HIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELE 414
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 882 GV---REAAVTV-RTDSGEPELCAYVEGlqrnevRAQLERLLP-GYMVPAYMIEMEQW-----------PVTPSGKLDR 944
Cdd:cd05908 415 GVelgRVVACGVnNSNTRNEEIFCFIEH------RKSEDDFYPlGKKIKKHLNKRGGWqinevlpirriPKTTSGKVKR 487
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
1565-1994 |
3.17e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 72.12 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1565 LAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQEL-KHLISNLPE----------------SEMSHI-----CLD 1622
Cdd:PRK05620 82 FAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLaEQLGEILKEcpcvravvfigpsdadSAAAHMpegikVYS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1623 DESSYEENSCNLNLSPAPEE-PVYIIYTSGTTGAPKGVIvtyrnFTHAALaWRQiyeldrkPVRLLQIASFS-------- 1693
Cdd:PRK05620 162 YEALLDGRSTVYDWPELDETtAAAICYSTGTTGAPKGVV-----YSHRSL-YLQ-------SLSLRTTDSLAvthgesfl 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1694 -----FDVFSGDLARTLTNGGTLIVCPDETrLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGS 1768
Cdd:PRK05620 229 ccvpiYHVLSWGVPLAAFMSGTPLVFPGPD-LSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1769 DMVKAQDFKTLTDRFGqsMRIINSYGVTEATIDSSFYETSMGGEG-TGDNVPIGSPLPNVHM--------YVLSQTDQIQ 1839
Cdd:PRK05620 308 SAVPPILIKAWEERYG--VDVVHVWGMTETSPVGTVARPPSGVSGeARWAYRVSQGRFPASLeyrivndgQVMESTDRNE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1840 pigvaGELCIGGAGVAKGYHQKP----DLTQMKFTKNPFVSGERLY------RTGDRACWLPNGTIRLLGRMDYQVKING 1909
Cdd:PRK05620 386 -----GEIQVRGNWVTASYYHSPteegGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1910 YRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAYIVPSDVNTNA-----LRAALTKELPAYMIPAHLIPLENMPL 1983
Cdd:PRK05620 461 EWIYSAQLENYIMAAPEVVECAViGYPDDKWGERPLAVTVLAPGIEPTRetaerLRDQLRDRLPNWMLPEYWTFVDEIDK 540
|
490
....*....|.
gi 363747658 1984 TLNGKLDRNAL 1994
Cdd:PRK05620 541 TSVGKFDKKDL 551
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1640-1990 |
5.94e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 71.92 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 PEEPVYIIYTSGTTGAPKGVIVTYRNF-THAAlawrqiyeldrkpvrllQIAS---FS-----FDV--------FSGDLA 1702
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLlANRA-----------------QVAAridFSpedkvFNAlpvfhsfgLTGGLV 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1703 RTLTNGGTLIVCPD--ETRLEPAEIYKImNSqriTVMESTPALIipvMEYV-YRNQFKLPDLDILILGSDMVKAQDFKTL 1779
Cdd:PRK06814 855 LPLLSGVKVFLYPSplHYRIIPELIYDT-NA---TILFGTDTFL---NGYArYAHPYDFRSLRYVFAGAEKVKEETRQTW 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1780 TDRFGqsMRIINSYGVTEATIDSSFyETSMGGE-GTgdnvpIGSPLPNVHmyvlSQTDQIQPIGVAGELCIGGAGVAKGY 1858
Cdd:PRK06814 928 MEKFG--IRILEGYGVTETAPVIAL-NTPMHNKaGT-----VGRLLPGIE----YRLEPVPGIDEGGRLFVRGPNVMLGY 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1859 --HQKPDLTQmkftknPFVSGErlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIE---TEEIESVLLQTGLvrEAAVA 1933
Cdd:PRK06814 996 lrAENPGVLE------PPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISlaaVEELAAELWPDAL--HAAVS 1065
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 1934 VQHDKNGQAgLAAYIVPSDVN-TNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLD 1990
Cdd:PRK06814 1066 IPDARKGER-IILLTTASDATrAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
606-919 |
6.80e-12 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 70.18 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 606 TSGSTGQPKGVA--------VEHRQAVSFltgmqHQFPLSEDDIVMVktSFSFDasvwqLFWWSL---SGA---SAYLLP 671
Cdd:COG1541 91 SSGTTGKPTVVGytrkdldrWAELFARSL-----RAAGVRPGDRVQN--AFGYG-----LFTGGLglhYGAerlGATVIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 672 --PGwekDSALIVQAIHQENVTTAHFIPAMLNSFLDQAEIERLS-DRTSLKRVFAGGEPLAPRTAARFASVLPqVSLIHG 748
Cdd:COG1541 159 agGG---NTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDpRDLSLKKGIFGGEPWSEEMRKEIEERWG-IKAYDI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 749 YGPTEATVDAAFyvldpE-RDRDRLRIPigkpvPGARLY-VLDP-HLAVQPSGVAGELYIAgagvargylnrpALTEE-- 823
Cdd:COG1541 235 YGLTEVGPGVAY-----EcEAQDGLHIW-----EDHFLVeIIDPeTGEPVPEGEEGELVVT------------TLTKEam 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 824 ---RfledpfypgermYKTGDVARWLPD-----------GNVefLGRTDDQVKIRGYRIEPGEIEAALRSIEGVR-EAAV 888
Cdd:COG1541 293 pliR------------YRTGDLTRLLPEpcpcgrthpriGRI--LGRADDMLIIRGVNVFPSQIEEVLLRIPEVGpEYQI 358
|
330 340 350
....*....|....*....|....*....|....
gi 363747658 889 TVRTDSGEPELCAYVE---GLQRNEVRAQLERLL 919
Cdd:COG1541 359 VVDREGGLDELTVRVElapGASLEALAEAIAAAL 392
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
6-326 |
1.01e-11 |
|
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: 69.65 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 6 YSLTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIRFQLLEGEELEPRLHLTEYKYYPLRI 85
Cdd:cd19547 2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 86 IDFS------NVEMIEieQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQKMK 159
Cdd:cd19547 82 LDWSgedpdrRAELLE--RLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 160 K-KDPL--PDQPEPSYLSYIE-KESQYLQSPRFAKDRL-------FWTQTFEHPLEYHSLADQ--TSLQKQSTSASRDTI 226
Cdd:cd19547 160 HgREPQlsPCRPYRDYVRWIRaRTAQSEESERFWREYLrdltpspFSTAPADREGEFDTVVHEfpEQLTRLVNEAARGYG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 227 ILSPDLEQtirifceehkiniislfmASFYICISRITSKKDLAIGTYYGNRGSKAE--KEMLGMFVSSLPIRITVDPDTD 304
Cdd:cd19547 240 VTTNAISQ------------------AAWSMLLALQTGARDVVHGLTIAGRPPELEgsEHMVGIFINTIPLRIRLDPDQT 301
|
330 340
....*....|....*....|..
gi 363747658 305 FLSFVRTIGREQLSVMRHQRFP 326
Cdd:cd19547 302 VTGLLETIHRDLATTAAHGHVP 323
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1524-1972 |
1.24e-11 |
|
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: 69.69 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGAdilllqq 1602
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGlKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSA------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1603 elKHLISnlpesemshiclddessyeenscnlnlspapeEPVYIIYTSGTTGAPKGVIVTYRN-------FTHAALAWRQ 1675
Cdd:cd05940 77 --KHLVV--------------------------------DAALYIYTSGTTGLPKAAIISHRRawrggafFAGSGGALPS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1676 --IYelDRKPvrlLQIASFSFDVFSGDLArtltNGGTLIVCP--------DETRLEPAEIYK--------IMNSqritvm 1737
Cdd:cd05940 123 dvLY--TCLP---LYHSTALIVGWSACLA----SGATLVIRKkfsasnfwDDIRKYQATIFQyigelcryLLNQ------ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1738 estpaliiPVMEYVYRNQFKLpdldilILGSDMvKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGEGTgdn 1817
Cdd:cd05940 188 --------PPKPTERKHKVRM------IFGNGL-RPDIWEEFKERFGVP-RIAEFYAATEGNSGFINFFGKPGAIGR--- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1818 vpIGSPLPNVHMYVLSQTD--QIQPI------------GVAGELC--IGGAGVAKGYhQKPDLTQMKFTKNPFVSGERLY 1881
Cdd:cd05940 249 --NPSLLRKVAPLALVKYDleSGEPIrdaegrcikvprGEPGLLIsrINPLEPFDGY-TDPAATEKKILRDVFKKGDAWF 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1882 RTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQ---HDknGQAGLAAYIVPSDVNTN- 1956
Cdd:cd05940 326 NTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVyGVQvpgTD--GRAGMAAIVLQPNEEFDl 403
|
490
....*....|....*..
gi 363747658 1957 -ALRAALTKELPAYMIP 1972
Cdd:cd05940 404 sALAAHLEKNLPGYARP 420
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1550-2010 |
2.60e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 69.06 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1550 VAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYP----KARIEYIlrdsGADILLLQQE-----LKHLISNLPeSEMSHIC 1620
Cdd:PLN02860 60 VAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSfeeaKSAMLLV----RPVMLVTDETcsswyEELQNDRLP-SLMWQVF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1621 LDDESSYEEN-----------------SCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKP 1683
Cdd:PLN02860 135 LESPSSSVFIflnsflttemlkqralgTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1684 VrLLQIASFsfdVFSGDLARTLTN---GGTLIVCPdetRLEPAEIYKIMNSQRITVMESTPALIIPVMEYVYR--NQFKL 1758
Cdd:PLN02860 215 V-YLHTAPL---CHIGGLSSALAMlmvGACHVLLP---KFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKsmTWKVF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1759 PDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEA-------TIDSSFYETSMGGEGTGDN-----------VPI 1820
Cdd:PLN02860 288 PSVRKILNGGGSLSSRLLPDAKKLFPNA-KLFSAYGMTEAcssltfmTLHDPTLESPKQTLQTVNQtksssvhqpqgVCV 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1821 GSPLPNVHMYVlsQTDQIQPIgvaGELCIGGAGVAKGYHQKPDLTQMKFTKNPFVSgerlyrTGDRACWLPNGTIRLLGR 1900
Cdd:PLN02860 367 GKPAPHVELKI--GLDESSRV---GRILTRGPHVMLGYWGQNSETASVLSNDGWLD------TGDIGWIDKAGNLWLIGR 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1901 MDYQVKINGYRIETEEIESVLLQ-TGLVREAAVAVQHDKNGQAgLAAYI------VPSDVNTNALRAALT---------- 1963
Cdd:PLN02860 436 SNDRIKTGGENVYPEEVEAVLSQhPGVASVVVVGVPDSRLTEM-VVACVrlrdgwIWSDNEKENAKKNLTlssetlrhhc 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 363747658 1964 --KELPAYMIPAHLIPLEN-MPLTLNGKLDRNAlpVPNNVLSRPYTAPVN 2010
Cdd:PLN02860 515 reKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDE--VRREVLSHLQSLPSN 562
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
519-954 |
3.32e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 68.14 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 519 PEMLIA-VLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQpgcsapnfsgetlEVDMTSLASEKAENHEftpadg 597
Cdd:PRK08308 42 PFDIITlVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLLYG-------------ESDFTKLEAVNYLAEE------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 598 GSLayVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDD--IVMVKTSFSFDasvwqLFWWSLS----GASAYLLP 671
Cdd:PRK08308 103 PSL--LQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDEtpIVACPVTHSYG-----LICGVLAaltrGSKPVIIT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 672 PGWEKDSALIVQAIHQENVTTAhfiPAMLNSfldqaeIERLSDRT-SLKRVFAGGEPLAprtAARFASVLPQVS-LIHGY 749
Cdd:PRK08308 176 NKNPKFALNILRNTPQHILYAV---PLMLHI------LGRLLPGTfQFHAVMTSGTPLP---EAWFYKLRERTTyMMQQY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 750 GPTEA-TVDAAFYVLDPERdrdrlripIGKPVPgarlyvldpHLAVQpsgvagelyiagAGVARgylNRPaltEERFLED 828
Cdd:PRK08308 244 GCSEAgCVSICPDMKSHLD--------LGNPLP---------HVSVS------------AGSDE---NAP---EEIVVKM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 829 pfypGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV--- 903
Cdd:PRK08308 289 ----GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvaGE-RVKAKVish 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 363747658 904 EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNALPAPGGAA 954
Cdd:PRK08308 364 EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
471-934 |
3.48e-11 |
|
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: 68.64 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 471 TPERLAIRFSGgsLTYAELDMYASRLAA-HLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSY 549
Cdd:cd17632 57 TTLRLLPRFET--ITYAELWERVGAVAAaHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 550 MLKDSGASLL------------LTQPGCSAPN---FSGETlEVDMTSLASEKA-------------------ENHEFTPA 595
Cdd:cd17632 135 ILAETEPRLLavsaehldlaveAVLEGGTPPRlvvFDHRP-EVDAHRAALESArerlaavgipvttltliavRGRDLPPA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 596 -------DGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMqhqFPLSEDD----IVMVKTSFSFDASVWQLFWWSLSG 664
Cdd:cd17632 214 plfrpepDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKV---SSIQDIRppasITLNFMPMSHIAGRISLYGTLARG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 665 ASAYLLPpgwEKDSALIVQAIHQENVTTAHFIPAMLNSFLD--QAEIERLSD------------RTSLKRVFAGGE---- 726
Cdd:cd17632 291 GTAYFAA---ASDMSTLFDDLALVRPTELFLVPRVCDMLFQryQAELDRRSVagadaetlaervKAELRERVLGGRllaa 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 727 -----PLAPRTAARFASVLpQVSLIHGYGPTEATVdaafyVLdpeRDRDRLRIPIGK----PVPGARLYVLD-PHlavqP 796
Cdd:cd17632 368 vcgsaPLSAEMKAFMESLL-DLDLHDGYGSTEAGA-----VI---LDGVIVRPPVLDyklvDVPELGYFRTDrPH----P 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 797 SgvaGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDV-ARWLPDgNVEFLGRTDDQVKI-RGYRIEPGEIE 874
Cdd:cd17632 435 R---GELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVmAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLE 504
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 875 AALRSIEGVREA------------AVTVRTDSGepeLCAYVEGLQRNEVRAQLERL-----LPGYMVPA-YMIEMEQW 934
Cdd:cd17632 505 AVFAASPLVRQIfvygnserayllAVVVPTQDA---LAGEDTARLRAALAESLQRIareagLQSYEIPRdFLIETEPF 579
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
479-928 |
3.63e-11 |
|
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: 68.23 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 479 FSGGSLTYAELDMYASRLAAHL-AARGITNESIVGVLSERSPEMLIAVLAVLKAGGAylpldPAYpkerLSYmlkdsgas 557
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA-----PAF----INY-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 558 llltqpgcsapNFSGETLevdmtsLASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLS 637
Cdd:cd05937 64 -----------NLSGDPL------IHCLKLSGSRFVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 638 EDDIVMVKTSFSFDASVWQLFWWSLSGASAYLLPPG------WEK--DS-ALIVQAIHQenvtTAHFIPAMLNSFLDQAE 708
Cdd:cd05937 127 NGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKfsasqfWKDvrDSgATIIQYVGE----LCRYLLSTPPSPYDRDH 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 709 IERLsdrtslkrvfAGGEPLAP----RTAARFAsvlpqVSLIHG-YGPTEATV--------------------------- 756
Cdd:cd05937 203 KVRV----------AWGNGLRPdiweRFRERFN-----VPEIGEfYAATEGVFaltnhnvgdfgagaighhglirrwkfe 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 757 -DAAFYVLDPERD----RDR----LRIPIGKPvpGARLYvldphlAVQPSGVAGelyiagagvARGYLNRPALTEERFLE 827
Cdd:cd05937 268 nQVVLVKMDPETDdpirDPKtgfcVRAPVGEP--GEMLG------RVPFKNREA---------FQGYLHNEDATESKLVR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 828 DPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREA---AVTVRTDSGEPElCAYVE 904
Cdd:cd05937 331 DVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAnvyGVKVPGHDGRAG-CAAIT 409
|
490 500 510
....*....|....*....|....*....|...
gi 363747658 905 GLQRNEVR--------AQLERL-LPGYMVPAYM 928
Cdd:cd05937 410 LEESSAVPteftksllASLARKnLPSYAVPLFL 442
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
485-904 |
3.88e-11 |
|
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: 68.60 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 485 TYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQ-- 562
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEde 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 563 -------------PGC--------------------SAPNFSGETLEVDMtslASEKAENHEFTPADGGSLAYVIYTSGS 609
Cdd:cd17641 93 eqvdklleiadriPSVryviycdprgmrkyddprliSFEDVVALGRALDR---RDPGLYEREVAAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 610 TGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVmvktsFSFDASVW---QLF-----WWSLS------------------ 663
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEY-----VSVLPLPWigeQMYsvgqaLVCGFivnfpeepetmmedlrei 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 664 GASAYLLPPG-WE----------KDSALIVQAIHQENVTTA----------HFIPAMLNS---FLDQAEIERLSDR---T 716
Cdd:cd17641 245 GPTFVLLPPRvWEgiaadvrarmMDATPFKRFMFELGMKLGlraldrgkrgRPVSLWLRLaswLADALLFRPLRDRlgfS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 717 SLKRVFAGGEPLAPRTAARFASV---LPQVslihgYGPTEAtvdAAFYVLDPERDRDRlrIPIGKPVPGARLYVLDphla 793
Cdd:cd17641 325 RLRSAATGGAALGPDTFRFFHAIgvpLKQL-----YGQTEL---AGAYTVHRDGDVDP--DTVGVPFPGTEVRIDE---- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 794 vqpsgvAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDDQVKI-RGYRIEPGE 872
Cdd:cd17641 391 ------VGEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQF 458
|
490 500 510
....*....|....*....|....*....|..
gi 363747658 873 IEAALRSIEGVREAAVTVRtdsGEPELCAYVE 904
Cdd:cd17641 459 IENKLKFSPYIAEAVVLGA---GRPYLTAFIC 487
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
969-1026 |
4.35e-11 |
|
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: 60.27 E-value: 4.35e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 969 KLSQLWEDVLK--NGPVGIHDNFFDRGGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVE 1026
Cdd:pfam00550 2 RLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
718-948 |
4.36e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 67.71 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 718 LKRVFAGGEPLAP--RTAARFAsvlpQVSLIHGYGPTEAtvdAAFYV-LDPErdrDRLR--IPIGKPVPGARLYVLDPHl 792
Cdd:PRK07445 232 FRTILLGGAPAWPslLEQARQL----QLRLAPTYGMTET---ASQIAtLKPD---DFLAgnNSSGQVLPHAQITIPANQ- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 793 avqpsgvAGELYIAGAGVARGYLnrPALTEERfledpfypgeRMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGE 872
Cdd:PRK07445 301 -------TGNITIQAQSLALGYY--PQILDSQ----------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 873 IEAALRSIEGVREAAVTVRTDS--GEPELCAYV---EGLQRNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGKLDRNAL 947
Cdd:PRK07445 362 VEAAILATGLVQDVCVLGLPDPhwGEVVTAIYVpkdPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
.
gi 363747658 948 P 948
Cdd:PRK07445 442 Q 442
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1916-1988 |
4.61e-11 |
|
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: 60.64 E-value: 4.61e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 1916 EIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---SDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGK 1988
Cdd:pfam13193 1 EVESALVSHPAVAEAAVvGVPDELKGEA-PVAFVVLkpgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
593-877 |
4.73e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 68.60 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 593 TPADggsLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFP-LSEDDIVMVKTSFsfdASVWQLFWWSL---SGAS-A 667
Cdd:PLN02387 248 SPND---IAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPkLGKNDVYLAYLPL---AHILELAAESVmaaVGAAiG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 668 YLLP-----------PGWEKD-SALivqaihQENVTTAhfIPAMLN------------------SFLDQAEIERLS---- 713
Cdd:PLN02387 322 YGSPltltdtsnkikKGTKGDaSAL------KPTLMTA--VPAILDrvrdgvrkkvdakgglakKLFDIAYKRRLAaieg 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 714 -------------DRTSLKRVFA-----------GGEPLAPRTAaRFASVLPQVSLIHGYGPTEATVDAAFYVL-DPERD 768
Cdd:PLN02387 394 swfgawglekllwDALVFKKIRAvlggrirfmlsGGAPLSGDTQ-RFINICLGAPIGQGYGLTETCAGATFSEWdDTSVG 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 769 RdrlripIGKPVPGARLYVLD----PHLAVQPSGVAGELYIAGAGVARGYLNRPALTEERFLEDPfyPGERMYKTGDVAR 844
Cdd:PLN02387 473 R------VGPPLPCCYVKLVSweegGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDE--RGMRWFYTGDIGQ 544
|
330 340 350
....*....|....*....|....*....|....
gi 363747658 845 WLPDGNVEFLGRTDDQVKIR-GYRIEPGEIEAAL 877
Cdd:PLN02387 545 FHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1522-1993 |
4.90e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 68.23 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1522 IEISYRFLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDShyPK-----ARIEYILRDSGAD 1596
Cdd:PRK12476 67 VELTWTQLGVRLRAVGARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFA--PElpghaERLDTALRDAEPT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1597 ILL----LQQELKHLISNLPESEMSHICLDDESSyeeNSCNLNLSPAP---EEPVYIIYTSGTTGAPKGVIVTYR----N 1665
Cdd:PRK12476 145 VVLtttaAAEAVEGFLRNLPRLRRPRVIAIDAIP---DSAGESFVPVEldtDDVSHLQYTSGSTRPPVGVEITHRavgtN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1666 FTHAALAwrqIYELDRkpvrllQIASFSFDVFSGDLA------RTLTNGGTLIVCPDETRLEPAEIYKIMNSQRITVMES 1739
Cdd:PRK12476 222 LVQMILS---IDLLDR------NTHGVSWLPLYHDMGlsmigfPAVYGGHSTLMSPTAFVRRPQRWIKALSEGSRTGRVV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1740 TPAliiPVMEYVYRNQFKLP----DLD----ILILGSDMVKAQDFKTLTDRFGQ----SMRIINSYGVTEATI------- 1800
Cdd:PRK12476 293 TAA---PNFAYEWAAQRGLPaegdDIDlsnvVLIIGSEPVSIDAVTTFNKAFAPyglpRTAFKPSYGIAEATLfvatiap 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1801 DSSFYETSMGGE--GTGDNVPIGSPLPNVHMYV------LSQ--------TDQIQPIGVAGELCIGGAGVAKGYHQKPDL 1864
Cdd:PRK12476 370 DAEPSVVYLDREqlGAGRAVRVAADAPNAVAHVscgqvaRSQwavivdpdTGAELPDGEVGEIWLHGDNIGRGYWGRPEE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1865 TQMKF-----TKNPFVS-------GERLYRTGDRACWLpNGTIRLLGRMDYQVKINGYRIETEEIE-SVLLQTGLVRE-- 1929
Cdd:PRK12476 450 TERTFgaklqSRLAEGShadgaadDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEaTVAEASPMVRRgy 528
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363747658 1930 -AAVAVQHDKNGQAGLAAYIVPSDVNTN------ALRAALTKElpaYMIPAH---LIPLENMPLTLNGKLDRNA 1993
Cdd:PRK12476 529 vTAFTVPAEDNERLVIVAERAAGTSRADpapaidAIRAAVSRR---HGLAVAdvrLVPAGAIPRTTSGKLARRA 599
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1525-1988 |
5.23e-11 |
|
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: 67.84 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1525 SYRFLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVyipidshypKARIEYILRDSGadilllqq 1602
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDLGVQAgdFVAIDLTNSPEFVFLWLGLWSIGAA---------PAFINYNLSGDP-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1603 elkhLISNLPESEMSHICLDDESsyeenscnlnlspapeePVYIIYTSGTTGAPKGVIVTY-RNFTHAAL--AWRQIYEL 1679
Cdd:cd05937 70 ----LIHCLKLSGSRFVIVDPDD-----------------PAILIYTSGTTGLPKAAAISWrRTLVTSNLlsHDLNLKNG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1680 DR--KPVRLLQIASFSFDvfsgdLARTLTNGGTLIVCP--------DETRLEPAEIYKIMnSQRITVMESTPALIIPVME 1749
Cdd:cd05937 129 DRtyTCMPLYHGTAAFLG-----ACNCLMSGGTLALSRkfsasqfwKDVRDSGATIIQYV-GELCRYLLSTPPSPYDRDH 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1750 YV---YRNQFKlPDLdililgsdmvkAQDFKtltDRFGQSMrIINSYGVTEATidSSFYETSMGGEGTGdnvPIGSPLPN 1826
Cdd:cd05937 203 KVrvaWGNGLR-PDI-----------WERFR---ERFNVPE-IGEFYAATEGV--FALTNHNVGDFGAG---AIGHHGLI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1827 VHM-----YVLSQ----TDQI-----------QPIGVAGELCI----GGAGVAKGYHQKPDLTQMKFTKNPFVSGERLYR 1882
Cdd:cd05937 262 RRWkfenqVVLVKmdpeTDDPirdpktgfcvrAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1883 TGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREA---AVAVQHdKNGQAGLAAYI------VPSDV 1953
Cdd:cd05937 342 TGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAnvyGVKVPG-HDGRAGCAAITleessaVPTEF 420
|
490 500 510
....*....|....*....|....*....|....*
gi 363747658 1954 NTNALRAALTKELPAYMIPAHLIPLENMPLTLNGK 1988
Cdd:cd05937 421 TKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHK 455
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1501-2004 |
5.38e-11 |
|
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: 68.07 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1501 HRIFEAKAEEIPEHIAVIDNEI-EISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVY---- 1574
Cdd:cd05943 75 NLLRHADADDPAAIYAAEDGERtEVTWAELRRRVARLAAALRALGvKPGDRVAGYLPNIPEAVVAMLATASIGAIWsscs 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1575 --------------------IPIDSH-YPKARIeyilrDSGADILLLQQEL---KHLI---SNLPESEMSHICLDDESSY 1627
Cdd:cd05943 155 pdfgvpgvldrfgqiepkvlFAVDAYtYNGKRH-----DVREKVAELVKGLpslLAVVvvpYTVAAGQPDLSKIAKALTL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1628 EE-----NSCNLNLSPAP-EEPVYIIYTSGTTGAPKGvIVtyrnFTHAALAWRQIYELdrkpvrLLQiasfsFDVFSGD- 1700
Cdd:cd05943 230 EDflatgAAGELEFEPLPfDHPLYILYSSGTTGLPKC-IV----HGAGGTLLQHLKEH------ILH-----CDLRPGDr 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1701 --------------LARTLTNGGTlIVCPDETRLEPAE--IYKIMNSQRITVMESTPALIIPVME--YVYRNQFKLPDLD 1762
Cdd:cd05943 294 lfyyttcgwmmwnwLVSGLAVGAT-IVLYDGSPFYPDTnaLWDLADEEGITVFGTSAKYLDALEKagLKPAETHDLSSLR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1763 -ILILGSDmVKAQDFKTLTDRFGQSMRIINSYGVTEatIDSSFyetsMGGegtGDNVPIG-SPL--PNVHMYVLSQTDQI 1838
Cdd:cd05943 373 tILSTGSP-LKPESFDYVYDHIKPDVLLASISGGTD--IISCF----VGG---NPLLPVYrGEIqcRGLGMAVEAFDEEG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1839 QP-IGVAGELCIGGA--GVAKGYHQKPDLTQMK---FTKNPFVsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRI 1912
Cdd:cd05943 443 KPvWGEKGELVCTKPfpSMPVGFWNDPDGSRYRaayFAKYPGV-----WAHGDWIEITPRGGVVILGRSDGTLNPGGVRI 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1913 ETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV--PSDVNTNALRAALTKELPAYMIPAHL----IPLENMPLTLN 1986
Cdd:cd05943 518 GTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKlrEGVELDDELRKRIRSTIRSALSPRHVpakiIAVPDIPRTLS 597
|
570
....*....|....*...
gi 363747658 1987 GKldRNALPVPNNVLSRP 2004
Cdd:cd05943 598 GK--KVEVAVKKIIAGRP 613
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1641-1991 |
7.52e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 67.86 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1641 EEPVYIIYTSGTTGAPKGVIVT---YrnFTHAALAWRqiYELDRKPVrllqiasfsfDVF------------S----GDL 1701
Cdd:PRK00174 245 EDPLFILYTSGSTGKPKGVLHTtggY--LVYAAMTMK--YVFDYKDG----------DVYwctadvgwvtghSyivyGPL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1702 ArtltNGGTLIV------CPDETRlepaeIYKIMNSQRITVMESTPALIIPVMEYvyrnqfklpdldililGSDMVKAQD 1775
Cdd:PRK00174 311 A----NGATTLMfegvpnYPDPGR-----FWEVIDKHKVTIFYTAPTAIRALMKE----------------GDEHPKKYD 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1776 FKTLtdrfgqsmRIINSYGVT---EA-------------TIDSSFYETSMGG------EGTGDNVPiGS---PLPNVHMY 1830
Cdd:PRK00174 366 LSSL--------RLLGSVGEPinpEAwewyykvvggercPIVDTWWQTETGGimitplPGATPLKP-GSatrPLPGIQPA 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1831 VLSQTDQIQPIGVAGELCIggagvakgyhQKPDLTQM--------KFTKNPFVSGERLYRTGDRACWLPNGTIRLLGRMD 1902
Cdd:PRK00174 437 VVDEEGNPLEGGEGGNLVI----------KDPWPGMMrtiygdheRFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVD 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1903 YQVKINGYRIETEEIESVLLQTGLVREAA-VAVQHDKNGQaGLAAYIV------PSDVNTNALRAALTKELPAYMIPAHL 1975
Cdd:PRK00174 507 DVLNVSGHRLGTAEIESALVAHPKVAEAAvVGRPDDIKGQ-GIYAFVTlkggeePSDELRKELRNWVRKEIGPIAKPDVI 585
|
410
....*....|....*.
gi 363747658 1976 IPLENMPLTLNGKLDR 1991
Cdd:PRK00174 586 QFAPGLPKTRSGKIMR 601
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1640-1991 |
8.14e-11 |
|
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: 67.13 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 PEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPvRLLQIASFSFD--VFSGDLARTLTNGGTLIVCPDE 1717
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKD-RILSWMPLTHDmgLIAFHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1718 TRLEPAEIYKIMNSQRITVMeSTP----ALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQ-SMR---I 1789
Cdd:cd05908 184 FIRRPILWLKKASEHKATIV-SSPnfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKyGLKrnaI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1790 INSYGVTEAT-------IDSSFYETSMGGEGTGDNVPI----------------GSPLPNVHMYVLSQTDQIQPIGVAGE 1846
Cdd:cd05908 263 LPVYGLAEASvgaslpkAQSPFKTITLGRRHVTHGEPEpevdkkdsecltfvevGKPIDETDIRICDEDNKILPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1847 LCIGGAGVAKGYHQKPDLTQMKFTKNPFVsgerlyRTGDRAcWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQ--- 1923
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEEleg 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 1924 TGLVREAAVAVQHDKNGQAGLAAYIVPSDvNTNALrAALTKElpaymIPAHL-----------IPLENMPLTLNGKLDR 1991
Cdd:cd05908 416 VELGRVVACGVNNSNTRNEEIFCFIEHRK-SEDDF-YPLGKK-----IKKHLnkrggwqinevLPIRRIPKTTSGKVKR 487
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1649-1994 |
9.31e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 67.29 E-value: 9.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1649 TSGTTGAPKGVIVTYRNftHAALAWRQIYELDRKPVRLLQIASFSFDVFS--GDLARTLTNGGTLIVCP-----DETRLe 1721
Cdd:PRK07529 221 TGGTTGMPKLAQHTHGN--EVANAWLGALLLGLGPGDTVFCGLPLFHVNAllVTGLAPLARGAHVVLATpqgyrGPGVI- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1722 pAEIYKIMNSQRITVMESTPALI-----IPVmeyvyrNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQsmRIINSYGVT 1796
Cdd:PRK07529 298 -ANFWKIVERYRINFLSGVPTVYaallqVPV------DGHDISSLRYALCGAAPLPVEVFRRFEAATGV--RIVEGYGLT 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1797 EATIDSSFyeTSMGGE-GTGDnvpIGSPLPNVHMYVLSQTDQ---IQPIGVA--GELCIGGAGVAKGYhqkpdlTQMKFT 1870
Cdd:PRK07529 369 EATCVSSV--NPPDGErRIGS---VGLRLPYQRVRVVILDDAgryLRDCAVDevGVLCIAGPNVFSGY------LEAAHN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1871 KNPFVsGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDknGQAG--LAAYI 1948
Cdd:PRK07529 438 KGLWL-EDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPD--AHAGelPVAYV 514
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 363747658 1949 --VP-SDVNTNALRAALTKELP---AymIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK07529 515 qlKPgASATEAELLAFARDHIAeraA--VPKHVRILDALPKTAVGKIFKPAL 564
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
485-883 |
9.73e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 67.35 E-value: 9.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 485 TYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLTQPG 564
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 565 C------SAPN----------FSG---------ETLEVDMTS----LASEKAENHEFTPADGGSLAYVIYTSGSTGQPKG 615
Cdd:PLN02614 161 KiselfkTCPNsteymktvvsFGGvsreqkeeaETFGLVIYAwdefLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 616 VAVEHRQAVSFLTGMQHQF-----PLSEDDIVM--VKTSFSFDASVWQLFWwSLSGASAYllppgWEKDSALIVQAIHQE 688
Cdd:PLN02614 241 VMISNESIVTLIAGVIRLLksanaALTVKDVYLsyLPLAHIFDRVIEECFI-QHGAAIGF-----WRGDVKLLIEDLGEL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 689 NVTTAHFIPAMLNSFLDQAEiERLSDRTSLKR---------------------------------------------VFA 723
Cdd:PLN02614 315 KPTIFCAVPRVLDRVYSGLQ-KKLSDGGFLKKfvfdsafsykfgnmkkgqshveasplcdklvfnkvkqglggnvriILS 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 724 GGEPLAPRTAArFASVLPQVSLIHGYGPTEATVdAAFYVLDPERDrdrLRIPIGKPVPGarlyvLDPHLAVQP------- 796
Cdd:PLN02614 394 GAAPLASHVES-FLRVVACCHVLQGYGLTESCA-GTFVSLPDELD---MLGTVGPPVPN-----VDIRLESVPemeydal 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 797 -SGVAGELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGDVARWLPDGNVEFLGRtddqvKIRGYRIEPGEIeA 875
Cdd:PLN02614 464 aSTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLH-------TGDVGEWQPNGSMKIIDR-----KKNIFKLSQGEY-V 530
|
....*...
gi 363747658 876 ALRSIEGV 883
Cdd:PLN02614 531 AVENIENI 538
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
2095-2421 |
1.88e-10 |
|
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: 65.85 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2095 LTPIQRR--FFGQVHAFHNHYNqsvmLFSEKGFNAN----ALHLALRKITEHHDAIRMIFQRDqNGHVIQfnrginhkdh 2168
Cdd:cd19533 4 LTSAQRGvwFAEQLDPEGSIYN----LAEYLEITGPvdlaVLERALRQVIAEAETLRLRFTEE-EGEPYQ---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2169 elfglYISDWTKASLE----RTHLDEKLAAE---ETVIQSKMNVEKGPLLQAGLFKTAEGDHLLIA-LHHLVIDGVSWRI 2240
Cdd:cd19533 69 -----WIDPYTPVPIRhidlSGDPDPEGAAQqwmQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQrVHHIVMDGFSFAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2241 LLEDLAAAYQQALEKKEIQLPPKTdSYLSYADGLTQIAESKQLLSEKTYWQtildahtaflpKDIENVPDRLQMNSDAAA 2320
Cdd:cd19533 144 FGQRVAEIYTALLKGRPAPPAPFG-SFLDLVEEEQAYRQSERFERDRAFWT-----------EQFEDLPEPVSLARRAPG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2321 FVLSG--------DWTEKLLFETQQAYGTDANELLLTALGMALSEWAGHDQIVISTEGHGREGHVPNIdisrTVGWFTSI 2392
Cdd:cd19533 212 RSLAFlrrtaelpPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQ----TPGMVANT 287
|
330 340
....*....|....*....|....*....
gi 363747658 2393 YPILLDMGIPEPFEDQLAYRIKTTKDMLR 2421
Cdd:cd19533 288 LPLRLTVDPQQTFAELVAQVSRELRSLLR 316
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1520-1995 |
2.29e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 65.44 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1520 NEIEISYRFLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGAdILL 1599
Cdd:PRK08308 5 NDEEYSKSDFDLRLQRYEEMEQFQEAAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGC-HGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1600 LQQELKHLISNLPESemshiclddessyeenscnlnlspAPEEPVYIIYTSGTTGAPKGVivtyrnfthaALAWRQI--- 1676
Cdd:PRK08308 84 LYGESDFTKLEAVNY------------------------LAEEPSLLQYSSGTTGEPKLI----------RRSWTEIdre 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1677 ---Y------ELDRKPVRLLQIaSFSFDVFSGDLArTLTNGGTLIVCpdeTRLEPAEIYKIMNSQRITVMESTPALI--- 1744
Cdd:PRK08308 130 ieaYnealncEQDETPIVACPV-THSYGLICGVLA-ALTRGSKPVII---TNKNPKFALNILRNTPQHILYAVPLMLhil 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1745 ---IPVMEYVYRnqfklpdldILILGSDMvKAQDFKTLTDRfgqSMRIINSYGVTEATIDSSFYETSMGGEgtgdnvpIG 1821
Cdd:PRK08308 205 grlLPGTFQFHA---------VMTSGTPL-PEAWFYKLRER---TTYMMQQYGCSEAGCVSICPDMKSHLD-------LG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1822 SPLPnvHMYVLSQTDQIQPigvaGELCIggagvakgyhqkpdltqmkftknpfVSGERLYRTGDRACWLPNGTIRLLGRM 1901
Cdd:PRK08308 265 NPLP--HVSVSAGSDENAP----EEIVV-------------------------KMGDKEIFTKDLGYKSERGTLHFMGRM 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1902 DYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDK-NGQAGLAAYIVPSDVNTNALRAALTKELPAYMIPAHLIPLEN 1980
Cdd:PRK08308 314 DDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvAGERVKAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTE 393
|
490
....*....|....*
gi 363747658 1981 MPLTLNGKLDRNALP 1995
Cdd:PRK08308 394 IPKNANGKVSRKLLE 408
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
479-888 |
2.53e-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: 65.78 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 479 FSGGSLTYAELDMYASRLA-AHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGAS 557
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAArALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 558 LLLTQPGCSA------PNFSGETLEVDMTS-----------LASEKAENHEFTPAD------GGSLAYVIYTSGSTGQPK 614
Cdd:cd05938 81 VLVVAPELQEaveevlPALRADGVSVWYLShtsntegvislLDKVDAASDEPVPASlrahvtIKSPALYIYTSGTTGLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 615 GVAVEHRQAVSfLTGMQHQFPLSEDDIVMVKTSFSFDASVWQLFWWSLS-GASAYLLPpgweKDSA-LIVQAIHQENVTT 692
Cdd:cd05938 161 AARISHLRVLQ-CSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIElGATCVLKP----KFSAsQFWDDCRKHNVTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 693 AHFIPAMLNSFLDQAeiERLSDRTSLKRVfAGGEPLAPRTAARFASVLPQVSLIHGYGPTEATVDAAFYV---------- 762
Cdd:cd05938 236 IQYIGELLRYLCNQP--QSPNDRDHKVRL-AIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTgkigavgrvs 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 763 -------------LDPE-----RDRDRLRIPIGKPVPG---ARLYVLDPHLavqpsgvagelyiagagvarGYLNRPALT 821
Cdd:cd05938 313 ylykllfpfelikFDVEkeepvRDAQGFCIPVAKGEPGllvAKITQQSPFL--------------------GYAGDKEQT 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 822 EERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 888
Cdd:cd05938 373 EKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNV 439
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1620-1994 |
3.13e-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: 65.09 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1620 CLDDESSYEENSCNLNLSPAPEE--PVYIIYTSGTTGAPKGVI-----VTYRNFTHAALA------WRQIYELdrkPVRL 1686
Cdd:cd05929 102 ALDGLEDYEAAEGGSPETPIEDEaaGWKMLYSGGTTGRPKGIKrglpgGPPDNDTLMAAAlgfgpgADSVYLS---PAPL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1687 LQIASFSFdvfsgdLARTLTNGGTLIVCPdetRLEPAEIYKIMNSQRITVMESTPAL---IIPVMEYVyRNQFKLPDLDI 1763
Cdd:cd05929 179 YHAAPFRW------SMTALFMGGTLVLME---KFDPEEFLRLIERYRVTFAQFVPTMfvrLLKLPEAV-RNAYDLSSLKR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1764 LI-LGSDM---VKAQdfktLTDRFGQsmRIINSYGVTEAT----IDSSFYETSMGGEGtgdnVPIGSplpnvHMYVLSQT 1835
Cdd:cd05929 249 VIhAAAPCppwVKEQ----WIDWGGP--IIWEYYGGTEGQgltiINGEEWLTHPGSVG----RAVLG-----KVHILDED 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1836 DQIQPIGVAGELCIGGAGvAKGYHQKPDLTQMKFTKNPFVS-GERLYRTGDracwlpnGTIRLLGRMDYQVKINGYRIET 1914
Cdd:cd05929 314 GNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTlGDVGYLDED-------GYLYLTDRRSDMIISGGVNIYP 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1915 EEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAY-----IVPSDVNTNALRAALTKELPAYMIPaHLIPLE-NMPLTLNG 1987
Cdd:cd05929 386 QEIENALIAHPKVLDAAVvGVPDEELGQRVHAVVqpapgADAGTALAEELIAFLRDRLSRYKCP-RSIEFVaELPRDDTG 464
|
....*..
gi 363747658 1988 KLDRNAL 1994
Cdd:cd05929 465 KLYRRLL 471
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
484-863 |
3.64e-10 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 65.63 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 484 LTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPL-DPAYPKE----------RLSYMLK 552
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLyDTLGANAvefiinhaevSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 553 DSGASLLLTQPGCSApNFSGETLEVDMTSLASEKAE------------------NHEFTPADGGSLAYVIYTSGSTGQPK 614
Cdd:PLN02861 158 SKISSILSCLPKCSS-NLKTIVSFGDVSSEQKEEAEelgvscfsweefslmgslDCELPPKQKTDICTIMYTSGTTGEPK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 615 GVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSF------------------DASVWqlFWwslSGASAYLL------ 670
Cdd:PLN02861 237 GVILTNRAIIAEVLSTDHLLKVTDRVATEEDSYFSYlplahvydqvietyciskGASIG--FW---QGDIRYLMedvqal 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 671 --------PPGWEKDSALIVQAIHQENVTTAHFIPAMLN-------SFLDQAEIERLSDRTSLKRV-----------FAG 724
Cdd:PLN02861 312 kptifcgvPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNyklgnlrKGLKQEEASPRLDRLVFDKIkeglggrvrllLSG 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 725 GEPLaPRTAARFASVLPQVSLIHGYGPTEA------TVDAAFYVLDperdrdrlriPIGKPVPG--ARLYVLdPHLAVQP 796
Cdd:PLN02861 392 AAPL-PRHVEEFLRVTSCSVLSQGYGLTEScggcftSIANVFSMVG----------TVGVPMTTieARLESV-PEMGYDA 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363747658 797 -SGVA-GELYIAGAGVARGYLNRPALTEERFLEDPFYpgermykTGDVARWLPDGNVEFLGRTDDQVKI 863
Cdd:PLN02861 460 lSDVPrGEICLRGNTLFSGYHKRQDLTEEVLIDGWFH-------TGDIGEWQPNGAMKIIDRKKNIFKL 521
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
777-903 |
4.67e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 65.16 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 777 GKPVPGARLYVLDPHLAVQPSGVAGELYIAGA--GVARGYLNRPalteERFLEDPF--YPGerMYKTGDVARWLPDGNVE 852
Cdd:PRK00174 427 TRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFstFKG--MYFTGDGARRDEDGYYW 500
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 363747658 853 FLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDS--GEpELCAYV 903
Cdd:PRK00174 501 ITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDikGQ-GIYAFV 552
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1638-1950 |
4.95e-10 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 65.12 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1638 PAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAA------------------LAWRQIYEldrkpvRLLQIASFSFDV--- 1696
Cdd:PLN02736 218 PKPEDVATICYTSGTTGTPKGVVLTHGNLIANVagsslstkfypsdvhisyLPLAHIYE------RVNQIVMLHYGVavg 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1697 -FSGDLARTLTNGGTL---IVC--PdetRLEpAEIY-KIMNsqriTVMESTPaliipVMEYVYRNQFKLPDlDILILGSD 1769
Cdd:PLN02736 292 fYQGDNLKLMDDLAALrptIFCsvP---RLY-NRIYdGITN----AVKESGG-----LKERLFNAAYNAKK-QALENGKN 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1770 MVKAQD---FKTLTDRFGQSMRIINS------------------------YGVTEAT-IDSSFYEtsmggegtGDNVP-- 1819
Cdd:PLN02736 358 PSPMWDrlvFNKIKAKLGGRVRFMSSgasplspdvmeflricfggrvlegYGMTETScVISGMDE--------GDNLSgh 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1820 IGSPLPNVHMYV-----LSQTDQIQPIGvAGELCIGGAGVAKGYHQKPDLTQmkftknPFVSGERLYRTGDRACWLPNGT 1894
Cdd:PLN02736 430 VGSPNPACEVKLvdvpeMNYTSEDQPYP-RGEICVRGPIIFKGYYKDEVQTR------EVIDEDGWLHTGDIGLWLPGGR 502
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 1895 IRLLGRMDYQVKI-NGYRIETEEIESVLLQTGLVREAAVavqHDKNGQAGLAAYIVP 1950
Cdd:PLN02736 503 LKIIDRKKNIFKLaQGEYIAPEKIENVYAKCKFVAQCFV---YGDSLNSSLVAVVVV 556
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
2007-2077 |
5.41e-10 |
|
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: 57.94 E-value: 5.41e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 2007 APVNDIQKTMAYIWEDVLSM--SRVGIHDSFF-ELGGDSIKALQVAARLAAE-GWSMTIRDLFRYSTIQELCGHI 2077
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYL 75
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
2126-2317 |
7.06e-10 |
|
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: 63.82 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2126 NANALHLALRKITEHHDAIRMIFQrDQNGHVIQFnrgINHKDHELFGLYISDwtkasLERTHLDEKLAAEetvIQSKMNV 2205
Cdd:cd19538 37 DVQALQQALYDVVERHESLRTVFP-EEDGVPYQL---ILEEDEATPKLEIKE-----VDEEELESEINEA---VRYPFDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2206 EKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYAdgLTQiaesKQLL 2284
Cdd:cd19538 105 SEEPPFRATLFELGENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLPVQYADYA--LWQ----QELL 178
|
170 180 190
....*....|....*....|....*....|...
gi 363747658 2285 SEKTYWQTILDAHTAFLPKDIENVPDRLQMNSD 2317
Cdd:cd19538 179 GDESDPDSLIARQLAYWKKQLAGLPDEIELPTD 211
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1525-1989 |
1.69e-09 |
|
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: 63.24 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1525 SYRFLNERANRLARTLQNRKG-------------PKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILR 1591
Cdd:cd17632 58 TLRLLPRFETITYAELWERVGavaaahdpeqpvrPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1592 DSGADILLLQQE-LKHLISNLPESEMSH-------------------------------ICLDDESSYEENSCNLNLSPA 1639
Cdd:cd17632 138 ETEPRLLAVSAEhLDLAVEAVLEGGTPPrlvvfdhrpevdahraalesarerlaavgipVTTLTLIAVRGRDLPPAPLFR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 PEE----PVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGT--LIV 1713
Cdd:cd17632 218 PEPdddpLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTayFAA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1714 CPDETRL-------EPAEI-------------YKIMNSQRITVMESTPALIIPVMEYVyRNQFKLPDLDILILGSDMVKA 1773
Cdd:cd17632 298 ASDMSTLfddlalvRPTELflvprvcdmlfqrYQAELDRRSVAGADAETLAERVKAEL-RERVLGGRLLAAVCGSAPLSA 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1774 QdFKTLTDRFGQsMRIINSYGVTEAtidssfyetsmgGEGTGDNVPIGSPlpnVHMYVLS--------QTDQIQPigvAG 1845
Cdd:cd17632 377 E-MKAFMESLLD-LDLHDGYGSTEA------------GAVILDGVIVRPP---VLDYKLVdvpelgyfRTDRPHP---RG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1846 ELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKIN-GYRIETEEIESVLLQT 1924
Cdd:cd17632 437 ELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDRRNNVLKLSqGEFVTVARLEAVFAAS 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1925 GLVREAAVavqHDKNGQAGLAAYIVPSD-----VNTNALRAALTK---------ELPAYMIPAHLIpLENMPLTL-NGKL 1989
Cdd:cd17632 511 PLVRQIFV---YGNSERAYLLAVVVPTQdalagEDTARLRAALAEslqriareaGLQSYEIPRDFL-IETEPFTIaNGLL 586
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
2019-2072 |
2.18e-09 |
|
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: 55.65 E-value: 2.18e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 2019 IWEDVLSMS--RVGIHDSFFELGGDSIKALQVAARLAAE-GWSMTIRDLFRYSTIQE 2072
Cdd:pfam00550 6 LLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2206-2407 |
2.57e-09 |
|
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: 61.95 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2206 EKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLL 2284
Cdd:cd20484 106 ENGPLMRVHLFSRSEQEHfVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPASYYDFVAWEQDMLAGAEGE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2285 SEKTYWQTILdahTAFLPkDIENVPDR-----LQMNSDAAAFVLSGDWTEKL-LFETQQAYGTDAneLLLTALGMALSEW 2358
Cdd:cd20484 186 EHRAYWKQQL---SGTLP-ILELPADRprssaPSFEGQTYTRRLPSELSNQIkSFARSQSINLST--VFLGIFKLLLHRY 259
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 363747658 2359 AGHDQIVISTEGHGReghvPNIDISRTVGWFTSIYPILLDMGIPEPFED 2407
Cdd:cd20484 260 TGQEDIIVGMPTMGR----PEERFDSLIGYFINMLPIRSRILGEETFSD 304
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1646-1934 |
4.08e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 62.30 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1646 IIYTSGTTGAPKGVIVTYRNFTHAALAWRQ-IYELDRKP------VRLLQIAS-FSFDVFSGDLAR----------TLTN 1707
Cdd:PTZ00216 269 IMYTSGTTGDPKGVMHTHGSLTAGILALEDrLNDLIGPPeedetyCSYLPLAHiMEFGVTNIFLARgaligfgsprTLTD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1708 GgTLIVCPDETRLEP---AEIYKIMNSQRITVMESTPaliiPV----------------------MEYVYRNQ--FKLPD 1760
Cdd:PTZ00216 349 T-FARPHGDLTEFRPvflIGVPRIFDTIKKAVEAKLP----PVgslkrrvfdhayqsrlralkegKDTPYWNEkvFSAPR 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1761 LdilILGSDM-----------VKAQDFKTLTdrFGqsmRIINSYGVTEaTIdssfyetSMGG-EGTGDNVP--IGSPLPN 1826
Cdd:PTZ00216 424 A---VLGGRVramlsgggplsAATQEFVNVV--FG---MVIQGWGLTE-TV-------CCGGiQRTGDLEPnaVGQLLKG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1827 VHMYVL-----SQTDQIQPigvAGELCIGGAGVAKGYHQKPDLTQMKFTKNPFvsgerlYRTGDRACWLPNGTIRLLGRM 1901
Cdd:PTZ00216 488 VEMKLLdteeyKHTDTPEP---RGEILLRGPFLFKGYYKQEELTREVLDEDGW------FHTGDVGSIAANGTLRIIGRV 558
|
330 340 350
....*....|....*....|....*....|....
gi 363747658 1902 DYQVK-INGYRIETEEIESVLLQTGLVREAAVAV 1934
Cdd:PTZ00216 559 KALAKnCLGEYIALEALEALYGQNELVVPNGVCV 592
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1640-1923 |
5.66e-09 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 61.37 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 PEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGgtLIVCPDETR 1719
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSG--VPVVFAYNP 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1720 LEPAEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKaQDFKTLTDRFGQSMRIINSYGVTEA- 1798
Cdd:PRK06334 260 LYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFK-DSLYQEALKTFPHIQLRQGYGTTECs 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1799 ------TIDSSFYETSmggegtgdnvpIGSPLPNVHMYVLSQTDQIQ-PIGVAGELCIGGAGVAKGYHQKpDLTQmkftk 1871
Cdd:PRK06334 339 pvitinTVNSPKHESC-----------VGMPIRGMDVLIVSEETKVPvSSGETGLVLTRGTSLFSGYLGE-DFGQ----- 401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 363747658 1872 nPFVS--GERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQ 1923
Cdd:PRK06334 402 -GFVElgGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILME 454
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
96-425 |
6.83e-09 |
|
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: 60.77 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 96 IEQWIQDQASIPFKLiNSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVMGNQIIDLYQkmkkkDPLPDQPePSYLSY 175
Cdd:cd19545 83 LDEYLEEDRAAPMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQ-----GEPVPQP-PPFSRF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 176 IekesQYLQSPRFAKDRLFWTQTFE---------HP-LEYHSLADQTslqkqstsasrdtiilspdLEQTIRI-FCEEHK 244
Cdd:cd19545 156 V----KYLRQLDDEAAAEFWRSYLAgldpavfppLPsSRYQPRPDAT-------------------LEHSISLpSSASSG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 245 INIISLFMASFYICISRITSKKDLAIGTYYGNRGSKAE--KEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQLSVMRH 322
Cdd:cd19545 213 VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPgiEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPF 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 323 Q------------------RFPyNLLVNELRNEQKDLHNLI-GISMQYQPLQWhnaddfdyetalyFSGYTaneLSVQIQ 383
Cdd:cd19545 293 EhtglqnirrlgpdaraacNFQ-TLLVVQPALPSSTSESLElGIEEESEDLED-------------FSSYG---LTLECQ 355
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 363747658 384 erIDNGTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALHHP 425
Cdd:cd19545 356 --LSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1645-1994 |
1.38e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 60.11 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1645 YIIYTSGTTGAPKGVIVTYRNFT-HA-ALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTngGTLIVCPDEtRLEP 1722
Cdd:PRK07008 180 SLCYTSGTTGNPKGALYSHRSTVlHAyGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLT--GAKLVLPGP-DLDG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1723 AEIYKIMNSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEatids 1802
Cdd:PRK07008 257 KSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYG--VEVIHAWGMTE----- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1803 sfyetsMGGEGT-------GDNVPI----------GSPLPNVHMYVLSQTDQIQPI-GVA-GELCIGGAGVAKGYHQKPD 1863
Cdd:PRK07008 330 ------MSPLGTlcklkwkHSQLPLdeqrkllekqGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1864 ltqmkftkNPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAA-VAVQHDKNGQA 1942
Cdd:PRK07008 404 --------SPLVDG--WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAAcIACAHPKWDER 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 1943 GLAAyIVP---SDVNTNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK07008 474 PLLV-VVKrpgAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1524-1984 |
1.73e-08 |
|
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: 60.00 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQ 1601
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHAGLRPgdTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1602 QELKHLISN-LPE--SEMSHICLDDESSYEENSCNL--NLSPAPEEPVYI--------------IYTSGTTGAPKGVIVT 1662
Cdd:cd05938 86 PELQEAVEEvLPAlrADGVSVWYLSHTSNTEGVISLldKVDAASDEPVPAslrahvtikspalyIYTSGTTGLPKAARIS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1663 YR------NFTHA--ALAWRQIYEldrkPVRLLQIASFSFDvFSGDLARtltnGGTLIVCPdetrlepaeiyKIMNSQ-- 1732
Cdd:cd05938 166 HLrvlqcsGFLSLcgVTADDVIYI----TLPLYHSSGFLLG-IGGCIEL----GATCVLKP-----------KFSASQfw 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1733 ------RITVMEstpaLIIPVMEYVYrNQFKLPDLDI----LILGSDmVKAQDFKTLTDRFGQsMRIINSYGVTEATIDS 1802
Cdd:cd05938 226 ddcrkhNVTVIQ----YIGELLRYLC-NQPQSPNDRDhkvrLAIGNG-LRADVWREFLRRFGP-IRIREFYGSTEGNIGF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1803 SFYETSMGGEGTgdnvpIGSPLPNVHMYVLSQTD--QIQPIGVAGELCI----GGAG--VAK--------GYHQKPDLTQ 1866
Cdd:cd05938 299 FNYTGKIGAVGR-----VSYLYKLLFPFELIKFDveKEEPVRDAQGFCIpvakGEPGllVAKitqqspflGYAGDKEQTE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1867 MKFTKNPFVSGERLYRTGDracwlpngtirlLGRMDYQ------------VKINGYRIETEEIESVLLQTGLVREA---A 1931
Cdd:cd05938 374 KKLLRDVFKKGDVYFNTGD------------LLVQDQQnflyfhdrvgdtFRWKGENVATTEVADVLGLLDFLQEVnvyG 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 1932 VAVQ-HDknGQAGLAAYIV--PSDVNTNALRAALTKELPAYMIPAHLIPLENMPLT 1984
Cdd:cd05938 442 VTVPgHE--GRIGMAAVKLkpGHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEIT 495
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1504-1741 |
2.36e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 59.58 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1504 FEAKAEEI-PEHIAVIDNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKrSIDAIVGV-LAVMKAGGVYIPIDSH 1580
Cdd:PRK08162 23 FLERAAEVyPDRPAVIHGDRRRTWAETYARCRRLASALARRGiGRGDTVAVLLP-NIPAMVEAhFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1581 YPKARIEYILRDSGADILLLQQELKHLISN-LPESEMSHICL--DDESSYEENSCNLNLS----------------PAPE 1641
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDTEFAEVAREaLALLPGPKPLVidVDDPEYPGGRFIGALDyeaflasgdpdfawtlPADE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1642 -EPVYIIYTSGTTGAPKGVIVTYR----NFTHAALAWrqiyELDRKPVRLLQIASF-----SFdvfsgdlARTLT-NGGT 1710
Cdd:PRK08162 182 wDAIALNYTSGTTGNPKGVVYHHRgaylNALSNILAW----GMPKHPVYLWTLPMFhcngwCF-------PWTVAaRAGT 250
|
250 260 270
....*....|....*....|....*....|.
gi 363747658 1711 lIVCpdETRLEPAEIYKIMNSQRITVMESTP 1741
Cdd:PRK08162 251 -NVC--LRKVDPKLIFDLIREHGVTHYCGAP 278
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1508-1885 |
3.41e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 59.12 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1508 AEEIPEHIAVI-----DNEIEISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDSHY 1581
Cdd:PRK08180 49 AQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGlSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1582 -----PKARIEYILR---------DSGAD-------ILLLQQELkhLISNLPESEMSHICLDDEssyEENSCNLNLSPA- 1639
Cdd:PRK08180 129 slvsqDFGKLRHVLElltpglvfaDDGAAfaralaaVVPADVEV--VAVRGAVPGRAATPFAAL---LATPPTAAVDAAh 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 ----PEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIY-ELDRKPVRLLQIASFSfDVFSG--DLARTLTNGGTLI 1712
Cdd:PRK08180 204 aavgPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFpFLAEEPPVLVDWLPWN-HTFGGnhNLGIVLYNGGTLY 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1713 VcpDETRLEPAEIYK-IMNSQRI--TVMESTPA---LIIPVMEY--VYRNQFkLPDLDILIL-GSDMvkAQDfktLTDRF 1783
Cdd:PRK08180 283 I--DDGKPTPGGFDEtLRNLREIspTVYFNVPKgweMLVPALERdaALRRRF-FSRLKLLFYaGAAL--SQD---VWDRL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1784 --------GQSMRIINSYGVTEATIDSSF--YETSMGGEgtgdnvpIGSPLPNVHMyvlsqtdQIQPIGVAGELCIGGAG 1853
Cdd:PRK08180 355 drvaeatcGERIRMMTGLGMTETAPSATFttGPLSRAGN-------IGLPAPGCEV-------KLVPVGGKLEVRVKGPN 420
|
410 420 430
....*....|....*....|....*....|..
gi 363747658 1854 VAKGYHQKPDLTQMKFTKNPFvsgerlYRTGD 1885
Cdd:PRK08180 421 VTPGYWRAPELTAEAFDEEGY------YRSGD 446
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
2112-2395 |
1.30e-07 |
|
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: 56.55 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2112 HYNQSVMLFSeKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQFNRGINHKDHELFglyisDWTKASLER-THLDE 2190
Cdd:cd19547 24 YFNQNVLELV-GGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWALL-----DWSGEDPDRrAELLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2191 KLAAEETViqSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPkTDSYLS 2269
Cdd:cd19547 98 RLLADDRA--AGLSLADCPLYRLTLVRLGGGRHyLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGREPQLSP-CRPYRD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2270 YADGLTqiAESKQLLSEKTYWQTILDAHTaflPKDIENVPDRLQMNSDAAAFVLSGDWTEkLLFETQQAYGTDANELLLT 2349
Cdd:cd19547 175 YVRWIR--ARTAQSEESERFWREYLRDLT---PSPFSTAPADREGEFDTVVHEFPEQLTR-LVNEAARGYGVTTNAISQA 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 363747658 2350 ALGMALSEWAGHDQIVistegHGR--EGHVPNIDISR-TVGWFTSIYPI 2395
Cdd:cd19547 249 AWSMLLALQTGARDVV-----HGLtiAGRPPELEGSEhMVGIFINTIPL 292
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1643-1991 |
2.16e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 56.29 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1643 PVYIIYTSGTTGAPKGVIVTyrNFTHA---ALAWRQIYELDrKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCP-DET 1718
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRS--NGPHLvglKYYWRSIIEKD-IPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEgGII 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1719 RLEPAE--IYKIMNSQRITVMESTPALIIPVMEY-----VYRNQFKLPDLDILILGSDMVKaqdfKTLTDRFGQSMRI-- 1789
Cdd:PTZ00237 333 KNKHIEddLWNTIEKHKVTHTLTLPKTIRYLIKTdpeatIIRSKYDLSNLKEIWCGGEVIE----ESIPEYIENKLKIks 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1790 INSYGVTEATIdSSFYETSMggegtgDNVPI---GSPLPNVHMYVLSQTDQIQPIGVAGELCIG---GAGVAKGYHQKPD 1863
Cdd:PTZ00237 409 SRGYGQTEIGI-TYLYCYGH------INIPYnatGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1864 LTQMKFTKNPfvsgeRLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAG 1943
Cdd:PTZ00237 482 KFKQLFSKFP-----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNV 556
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 1944 LAAYIV--------PSDVN--TNALRAALTKELPAYMIPAHLIPLENMPLTLNGKLDR 1991
Cdd:PTZ00237 557 PIGLLVlkqdqsnqSIDLNklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
578-869 |
2.91e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 56.27 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 578 DMTSlasEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLtgmqhqFPLSEDDIVM---VKTSFSFdASV 654
Cdd:PTZ00342 287 DMTK---NKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTV------VPLCKHSIFKkynPKTHLSY-LPI 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 655 WQLFWWSLSGASAYLlppG-----WEKDSALIVQAIHQENVTTAHFIPAMLNSFLDQ--AEIERLS--DRTSLKRVFA-- 723
Cdd:PTZ00342 357 SHIYERVIAYLSFML---GgtiniWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNimTEINNLPplKRFLVKKILSlr 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 724 -----------------------------------GGEPLAPRTAARFaSVLPQVSLIHGYGPTEATvdAAFYVLDpERD 768
Cdd:PTZ00342 434 ksnnnggfskflegithisskikdkvnpnlevilnGGGKLSPKIAEEL-SVLLNVNYYQGYGLTETT--GPIFVQH-ADD 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 769 RDRLRIpiGKPVPGARLYVLDPHLAVQPSGV--AGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWL 846
Cdd:PTZ00342 510 NNTESI--GGPISPNTKYKVRTWETYKATDTlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQIN 581
|
330 340
....*....|....*....|....
gi 363747658 847 PDGNVEFLGRTDDQVKI-RGYRIE 869
Cdd:PTZ00342 582 KNGSLTFLDRSKGLVKLsQGEYIE 605
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
872-941 |
3.20e-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: 49.85 E-value: 3.20e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363747658 872 EIEAALRSIEGVREAAVTVRTDS--GEpELCAYV---EGLQ--RNEVRAQLERLLPGYMVPAYMIEMEQWPVTPSGK 941
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDElkGE-APVAFVvlkPGVEllEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1526-1991 |
3.88e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 55.40 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1526 YRFLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDshYPKA---RIEYI------LRDSG 1594
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL-GLKPgdRVALIAETDGDFVEAFFACQYAGLVPVPLP--LPMGfggRESYIaqlrgmLASAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1595 ADILLLQQELKHLISNLPESE-----MSHICLDDEssyEENSCNLNlSPAPEEPVYIIYTSGTTGAPKGVIVTYR----N 1665
Cdd:PRK09192 129 PAAIITPDELLPWVNEATHGNpllhvLSHAWFKAL---PEADVALP-RPTPDDIAYLQYSSGSTRFPRGVIITHRalmaN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1666 FTHAALAWRQIYELDR------------------KPVrllqIASFSFDVF-SGDLA-RTLT-------NGGTLIVCPDET 1718
Cdd:PRK09192 205 LRAISHDGLKVRPGDRcvswlpfyhdmglvgfllTPV----ATQLSVDYLpTRDFArRPLQwldlisrNRGTISYSPPFG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1719 rlepaeiYKI----MNSQRitvmestpaliipvmeyvyrnqfkLPDLD-----ILILGSDMVKAQDFKTLTDRFGQS--- 1786
Cdd:PRK09192 281 -------YELcarrVNSKD------------------------LAELDlscwrVAGIGADMIRPDVLHQFAEAFAPAgfd 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1787 -MRIINSYGVTEATIDSSFYETSMGG----------EGTGDNVPI-------------GSPLPNVHMYVLSQTDQIQPIG 1842
Cdd:PRK09192 330 dKAFMPSYGLAEATLAVSFSPLGSGIvveevdrdrlEYQGKAVAPgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPER 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1843 VAGELCIGGAGVAKGYHQKPDLTQMkftknpfVSGERLYRTGDRAcWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLL 1922
Cdd:PRK09192 410 VVGHICVRGPSLMSGYFRDEESQDV-------LAADGWLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAE 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 1923 QTGLVR--EAAVAVQHDKNGQAglAAYIVPSDVNTNALRAALTKELPAYMIPAH-------LIPLENMPLTLNGKLDR 1991
Cdd:PRK09192 482 QEPELRsgDAAAFSIAQENGEK--IVLLVQCRISDEERRGQLIHALAALVRSEFgveaaveLVPPHSLPRTSSGKLSR 557
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
482-888 |
4.96e-07 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 55.29 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 482 GSLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVLAVLKAGGAYLPLDPAYPKERLSYMLKDSGASLLLT 561
Cdd:PLN02654 119 ASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 562 qpgCSAPNFSGETLE----VDMTSLASEK---------------AENHEFTP------------------------ADGG 598
Cdd:PLN02654 199 ---CNAVKRGPKTINlkdiVDAALDESAKngvsvgicltyenqlAMKREDTKwqegrdvwwqdvvpnyptkcevewVDAE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 599 SLAYVIYTSGSTGQPKGVAveHRQA---VSFLTGMQHQFPLSEDDIVMVKTSFSF-DASVWQLFWWSLSGASAYLLP--P 672
Cdd:PLN02654 276 DPLFLLYTSGSTGKPKGVL--HTTGgymVYTATTFKYAFDYKPTDVYWCTADCGWiTGHSYVTYGPMLNGATVLVFEgaP 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 673 GWeKDSALIVQAIHQENVTTAHFIPAMLNSFL-DQAEIERLSDRTSLKRVFAGGEPLAPRTAARFASVL--PQVSLIHGY 749
Cdd:PLN02654 354 NY-PDSGRCWDIVDKYKVTIFYTAPTLVRSLMrDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVgdSRCPISDTW 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 750 GPTEAtvdaAFYVLDPerdrdrlrIPIGKPV-PGARLYvldPHLAVQPSgVAGELYIAGAGVARGYL----NRPAL---- 820
Cdd:PLN02654 433 WQTET----GGFMITP--------LPGAWPQkPGSATF---PFFGVQPV-IVDEKGKEIEGECSGYLcvkkSWPGAfrtl 496
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 821 --TEERFLEDPFYPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAV 888
Cdd:PLN02654 497 ygDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAV 566
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
2096-2381 |
8.10e-07 |
|
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: 53.84 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2096 TPIQRRFFG----QVHAFHNHYNQSVmlfsEKGFNANALHLALRKITEHHDAIRM-IFQRDQNG--HVIqfnrginHKDH 2168
Cdd:cd19545 5 TPLQEGLMAltarQPGAYVGQRVFEL----PPDIDLARLQAAWEQVVQANPILRTrIVQSDSGGllQVV-------VKES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2169 ELfglyisDWTKASLERTHLDEKLAAEETViqskmnveKGPLLQAGLFK-TAEGDHLLIALHHLVIDGVSWRILLEDLAA 2247
Cdd:cd19545 74 PI------SWTESTSLDEYLEEDRAAPMGL--------GGPLVRLALVEdPDTERYFVWTIHHALYDGWSLPLILRQVLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2248 AYQQaleKKEIQLPPKTD--SYLSYADgltqIAESKQllsektYWQTILD-----AHTAFLPKDIENVPDRLQMNSDAAA 2320
Cdd:cd19545 140 AYQG---EPVPQPPPFSRfvKYLRQLD----DEAAAE------FWRSYLAgldpaVFPPLPSSRYQPRPDATLEHSISLP 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 363747658 2321 FVLSGDWTekllfetqqaygtdANELLLTALGMALSEWAGHDQIVISTEGHGREGHVPNID 2381
Cdd:cd19545 207 SSASSGVT--------------LATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIE 253
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1514-1994 |
1.22e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 53.88 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1514 HIAVIDNEIEISYR-FLNERANR--LARTLQNRKGPkPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDshyPKARIEYIL 1590
Cdd:PRK13388 17 TIAVRYGDRTWTWReVLAEAAARaaALIALADPDRP-LHVGVLLGNTPEMLFWLAAAALGGYVLVGLN---TTRRGAALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1591 RD-SGAD--ILLLQQELKHLISNLPESEMSHICLDDESSYEENSCNLNLSPA----PEEPVYIIYTSGTTGAPKGVIVTY 1663
Cdd:PRK13388 93 ADiRRADcqLLVTDAEHRPLLDGLDLPGVRVLDVDTPAYAELVAAAGALTPHrevdAMDPFMLIFTSGTTGAPKAVRCSH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1664 RNFTHAALAWRQIYELDRKPVRLLQIASF-SFDVFSGdLARTLTNGGTLIVCP--------DETRLEPAeiyKIMN--SQ 1732
Cdd:PRK13388 173 GRLAFAGRALTERFGLTRDDVCYVSMPLFhSNAVMAG-WAPAVASGAAVALPAkfsasgflDDVRRYGA---TYFNyvGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1733 RITVMESTPaliipvmeyvyrnqfKLPDlDI---LILG-----SDmvkaQDFKTLTDRFGqsMRIINSYGVTE----ATI 1800
Cdd:PRK13388 249 PLAYILATP---------------ERPD-DAdnpLRVAfgneaSP----RDIAEFSRRFG--CQVEDGYGSSEgaviVVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1801 DSSFYETSmggegtgdnvpIGSPLPNVHMYvlsQTDQIQPIGVA---------------GELC-IGGAGVAKGYHQKPDL 1864
Cdd:PRK13388 307 EPGTPPGS-----------IGRGAPGVAIY---NPETLTECAVArfdahgallnadeaiGELVnTAGAGFFEGYYNNPEA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1865 TQMKFTKNPFVSGERLYRTGDracwlpnGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAG 1943
Cdd:PRK13388 373 TAERMRHGMYWSGDLAYRDAD-------GWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVyAVPDERVGDQV 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 1944 LAAYIV--PSDVNTNALRAALT--KELPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK13388 446 MAALVLrdGATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
601-949 |
1.57e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 53.67 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 601 AYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMvktSF--SFDA---SVWQLFWWsLSGASA-YLLPPGW 674
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMM---SFlpPFHAygfNSCTLFPL-LSGVPVvFAYNPLY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 675 EKDsalIVQAIHQENVTTAHFIPAMLNSFLDQAEIERlSDRTSLKRVFAGGEPLAPRTAARFASVLPQVSLIHGYGPTEA 754
Cdd:PRK06334 262 PKK---IVEMIDEAKVTFLGSTPVFFDYILKTAKKQE-SCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTEC 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 755 T-VDAAFYVLDPERDRdrlriPIGKPVPGARLYVL--DPHLAVqPSGVAGELYIAGAGVARGYL-NRPAlteERFLEdpf 830
Cdd:PRK06334 338 SpVITINTVNSPKHES-----CVGMPIRGMDVLIVseETKVPV-SSGETGLVLTRGTSLFSGYLgEDFG---QGFVE--- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 831 YPGERMYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALrsIEGVREAA------VTVRTDSGEPE-LCAYV 903
Cdd:PRK06334 406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL--MEGFGQNAadhagpLVVCGLPGEKVrLCLFT 483
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 363747658 904 E-GLQRNEVRAQLERL-LPGYMVPAYMIEMEQWPVTPSGKLDRNALPA 949
Cdd:PRK06334 484 TfPTSISEVNDILKNSkTSSILKISYHHQVESIPMLGTGKPDYCSLNA 531
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
2211-2249 |
2.20e-06 |
|
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: 52.81 E-value: 2.20e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 363747658 2211 LQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAY 2249
Cdd:cd19540 110 LRARLFRLGPDEHvLVLVVHHIAADGWSMAPLARDLATAY 149
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
8-425 |
2.67e-06 |
|
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: 52.43 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 8 LTHAQRRVWFTELLEPNTSICNLTACVKFKGNIELDTLEGALNHSISRNDAIR----------FQL-LEGEELEPRLHLT 76
Cdd:cd19540 4 LSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRtvfpeddggpYQVvLPAAEARPDLTVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 77 EykyyplriidfsnVEMIEIEQWIQDQASIPFKLINSPLYQFYLLRIDSHEVWLFAKFHHIIMDGISLNVM--------- 147
Cdd:cd19540 84 D-------------VTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLardlataya 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 148 ----GN---------QIID--LYQKmkkkDPLPDQPEPSYLSyiekeSQYLQsprfakdrlFWTQTfehpleyhsLA--- 209
Cdd:cd19540 151 arraGRapdwaplpvQYADyaLWQR----ELLGDEDDPDSLA-----ARQLA---------YWRET---------LAglp 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 210 DQTSL-------QKQSTSASRDTIILSPDLEQTIRIFCEEHKIniiSLFM---ASFYICISRITSKKDLAIGTYYGNRGS 279
Cdd:cd19540 204 EELELptdrprpAVASYRGGTVEFTIDAELHARLAALAREHGA---TLFMvlhAALAVLLSRLGAGDDIPIGTPVAGRGD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 280 KAEKEMLGMFVSSLPIRITVDPDTDFLSFVRTIGREQLSVMRHQRFPYNLLVNELRNEQkdlhnligiSMQYQPL----- 354
Cdd:cd19540 281 EALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAHQDVPFERLVEALNPPR---------STARHPLfqvml 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 355 QWHNADDFDYE------TALYFSGYTAN-ELSVQIQERIDN----GTIQLNFDYQNTLFSLEDIKRIQSHLLTILENALH 423
Cdd:cd19540 352 AFQNTAAATLElpgltvEPVPVDTGVAKfDLSFTLTERRDAdgapAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVA 431
|
..
gi 363747658 424 HP 425
Cdd:cd19540 432 DP 433
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1640-1927 |
4.72e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 51.95 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 PEEPVYIIYTSGTTGAPKGVIVTYRNFT-------------HAALAWRQIY--------ELDR----------------- 1681
Cdd:PLN02614 222 KSDICTIMYTSGTTGDPKGVMISNESIVtliagvirllksaNAALTVKDVYlsylplahIFDRvieecfiqhgaaigfwr 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1682 -------------KPVRLLQIASFSFDVFSGdLARTLTNGGTLivcpDETRLEPAEIYKIMNSQR-ITVMESTPALIIPV 1747
Cdd:PLN02614 302 gdvklliedlgelKPTIFCAVPRVLDRVYSG-LQKKLSDGGFL----KKFVFDSAFSYKFGNMKKgQSHVEASPLCDKLV 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1748 MEYVyrNQFKLPDLDILILGSDMVKAQDFKTLtdRFGQSMRIINSYGVTEATIDS-SFYETSMGGEGTgdnvpIGSPLPN 1826
Cdd:PLN02614 377 FNKV--KQGLGGNVRIILSGAAPLASHVESFL--RVVACCHVLQGYGLTESCAGTfVSLPDELDMLGT-----VGPPVPN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1827 VHMYVLSQTD-QIQPIGVA--GELCIGGAGVAKGYHQKPDLtqmkfTKNPFVSGerLYRTGDRACWLPNGTIRLLGRMDY 1903
Cdd:PLN02614 448 VDIRLESVPEmEYDALASTprGEICIRGKTLFSGYYKREDL-----TKEVLIDG--WLHTGDVGEWQPNGSMKIIDRKKN 520
|
330 340
....*....|....*....|....*
gi 363747658 1904 QVKI-NGYRIETEEIESVLLQTGLV 1927
Cdd:PLN02614 521 IFKLsQGEYVAVENIENIYGEVQAV 545
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
983-1034 |
7.74e-06 |
|
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: 46.09 E-value: 7.74e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 363747658 983 VGIHDNFFDRGGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLATVIRE 1034
Cdd:smart00823 33 IDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
590-877 |
8.01e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 51.28 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 590 HEFTPADGGSLAYVIYTSGSTGQPKGVAvehRQAVSFLTGMQ-HQFPLSEDDIvmVKTSFSFDASVWQLF----WWSLSG 664
Cdd:PTZ00237 246 YEYVPVESSHPLYILYTSGTTGNSKAVV---RSNGPHLVGLKyYWRSIIEKDI--PTVVFSHSSIGWVSFhgflYGSLSL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 665 ASAYLL-------PPGWEKDsalIVQAIHQENVTTAHFIPAMLNSFL----DQAEIERLSDRTSLKRVFAGGEPLAPRTA 733
Cdd:PTZ00237 321 GNTFVMfeggiikNKHIEDD---LWNTIEKHKVTHTLTLPKTIRYLIktdpEATIIRSKYDLSNLKEIWCGGEVIEESIP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 734 ARFASVLpQVSLIHGYGPTEATVdAAFYvldperDRDRLRIPI---GKPVPGARLYVLDPHLAVQPSGVAGELYIA---G 807
Cdd:PTZ00237 398 EYIENKL-KIKSSRGYGQTEIGI-TYLY------CYGHINIPYnatGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmP 469
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 808 AGVARGYLNRPALTEERFLEDPFYpgermYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAAL 877
Cdd:PTZ00237 470 PSFATTFYKNDEKFKQLFSKFPGY-----YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSI 534
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1521-1665 |
9.96e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 50.88 E-value: 9.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1521 EIEISYRFLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPI-DSHYP--KARIEYILRDSGADI 1597
Cdd:PRK07769 53 ARDLTWSQFGARNRAVGARLQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSA 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 363747658 1598 LLLQQE----LKHLISNLPESEMSHICLDDESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRN 1665
Cdd:PRK07769 133 ILTTTDsaegVRKFFRARPAKERPRVIAVDAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLN 204
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
601-943 |
1.01e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 51.25 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 601 AYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSF--SFDASVwQLFWWSLSGASAYLLPpgwekdS 678
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYP------S 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 679 AL---IV-QAIHQENVTTAHFIPAMLNSFldqAEIERLSDRTSLKRVFAGGEPLAPRTAA----RFAsvlpqVSLIHGYG 750
Cdd:PRK08043 441 PLhyrIVpELVYDRNCTVLFGTSTFLGNY---ARFANPYDFARLRYVVAGAEKLQESTKQlwqdKFG-----LRILEGYG 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 751 PTE-ATVDAafyvldperdrdrLRIP-------IGKPVPG--ARLyvldphLAVQPSGVAGELYIAGAGVARGYL--NRP 818
Cdd:PRK08043 513 VTEcAPVVS-------------INVPmaakpgtVGRILPGmdARL------LSVPGIEQGGRLQLKGPNIMNGYLrvEKP 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 819 ALTEERFLEDPfyPGER---MYKTGDVARWLPDGNVEFLGRTDDQVKIRGYRIEPGEIEAALRSIEGVREAAVTVRTDSG 895
Cdd:PRK08043 574 GVLEVPTAENA--RGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDAS 651
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 363747658 896 EPElcAYV-----EGLQRNEVRAQLERL-LPGYMVPAYMIEMEQWPVTPSGKLD 943
Cdd:PRK08043 652 KGE--ALVlfttdSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1524-1950 |
1.57e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 50.23 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1524 ISYRFLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPI-DSHYPKArIEYILRDSGADILLLQ 1601
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGvNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLyDTLGANA-VEFIINHAEVSIAFVQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1602 Q-ELKHLISNLPESEmSHI-----------CLDDES--------SYEE----NSCNLNLSPAPEEPV-YIIYTSGTTGAP 1656
Cdd:PLN02861 157 EsKISSILSCLPKCS-SNLktivsfgdvssEQKEEAeelgvscfSWEEfslmGSLDCELPPKQKTDIcTIMYTSGTTGEP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1657 KGVIVTYRNFTHAALAWRQIYELDRKpVRLLQIASFSF----DVFSGDLARTLTNGGTLI---------VCPDETRLEPA 1723
Cdd:PLN02861 236 KGVILTNRAIIAEVLSTDHLLKVTDR-VATEEDSYFSYlplaHVYDQVIETYCISKGASIgfwqgdiryLMEDVQALKPT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1724 ------EIYKIMNSQRITVMESTPALIIPVMEYVYrnQFKL-------------PDLDILIlgsdmvkaqdFKTLTDRFG 1784
Cdd:PLN02861 315 ifcgvpRVYDRIYTGIMQKISSGGMLRKKLFDFAY--NYKLgnlrkglkqeeasPRLDRLV----------FDKIKEGLG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1785 QSMRIINS------------------------YGVTEATiDSSFyeTSMGGE----GTgdnvpIGSPLPNVHmyvlSQTD 1836
Cdd:PLN02861 383 GRVRLLLSgaaplprhveeflrvtscsvlsqgYGLTESC-GGCF--TSIANVfsmvGT-----VGVPMTTIE----ARLE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1837 QIQPIGV-------AGELCIGGAGVAKGYHQKPDLtqmkfTKNPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKIN- 1908
Cdd:PLN02861 451 SVPEMGYdalsdvpRGEICLRGNTLFSGYHKRQDL-----TEEVLIDG--WFHTGDIGEWQPNGAMKIIDRKKNIFKLSq 523
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 363747658 1909 GYRIETEEIESVLLQTGLVREAAVavqHDKNGQAGLAAYIVP 1950
Cdd:PLN02861 524 GEYVAVENLENTYSRCPLIASIWV---YGNSFESFLVAVVVP 562
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1601-1927 |
1.63e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 50.50 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1601 QQELKHL--ISNLPESEMSHICLDDESSYEENS----CNLNLS------------------PAPEEPVYIIYTSGTTGAP 1656
Cdd:PLN02387 186 SKQLKKLidISSQLETVKRVIYMDDEGVDSDSSlsgsSNWTVSsfseveklgkenpvdpdlPSPNDIAVIMYTSGSTGLP 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1657 KGVIVTYRNFTHAALAWRQIY-ELDRKPVRL--------LQIASFSFDVFSGDL-----ARTLTNGGTLI---VCPDETR 1719
Cdd:PLN02387 266 KGVMMTHGNIVATVAGVMTVVpKLGKNDVYLaylplahiLELAAESVMAAVGAAigygsPLTLTDTSNKIkkgTKGDASA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1720 LEPaeiykimnsqriTVMESTPALIIPVMEYVYRN-------QFKLPDLDI-----LILGS------------DMVKaqd 1775
Cdd:PLN02387 346 LKP------------TLMTAVPAILDRVRDGVRKKvdakgglAKKLFDIAYkrrlaAIEGSwfgawglekllwDALV--- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1776 FKTLTD------RF---------GQSMRIIN---------SYGVTEATIDSSFYE---TSMGgegtgdnvPIGSPLPnvH 1828
Cdd:PLN02387 411 FKKIRAvlggriRFmlsggaplsGDTQRFINiclgapigqGYGLTETCAGATFSEwddTSVG--------RVGPPLP--C 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1829 MYV---------LSQTDQIQPigvAGELCIGGAGVAKGYHQKPDLTQMKFTKNPfvSGERLYRTGDRACWLPNGTIRLLG 1899
Cdd:PLN02387 481 CYVklvsweeggYLISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVDE--RGMRWFYTGDIGQFHPDGCLEIID 555
|
410 420
....*....|....*....|....*....
gi 363747658 1900 RMDYQVKI-NGYRIETEEIESVLLQTGLV 1927
Cdd:PLN02387 556 RKKDIVKLqHGEYVSLGKVEAALSVSPYV 584
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
1640-1990 |
1.98e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 50.09 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1640 PEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYEL---DRKPVRLLQIASFSFDVfsGDLARTLTNGGT-LIVCP 1715
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFtpnDRFMSALPLFHSFGLTV--GLFTPLLTGAEVfLYPSP 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1716 DETRLEPAEIYkimnSQRITVMESTPALIipvMEYV-YRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYG 1794
Cdd:PRK08043 442 LHYRIVPELVY----DRNCTVLFGTSTFL---GNYArFANPYDFARLRYVVAGAEKLQESTKQLWQDKFG--LRILEGYG 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1795 VTEATIDSSFyetsmggegtgdNVP-------IGSPLPNVHMYVLSqtdqIQPIGVAGELCIGGAGVAKGYH--QKPDLT 1865
Cdd:PRK08043 513 VTECAPVVSI------------NVPmaakpgtVGRILPGMDARLLS----VPGIEQGGRLQLKGPNIMNGYLrvEKPGVL 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1866 QMKFTKNpfVSGER---LYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQA 1942
Cdd:PRK08043 577 EVPTAEN--ARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE 654
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 363747658 1943 GLAAYIVPSDVNTNAL-RAALTKELPAYMIPAHLIPLENMPLTLNGKLD 1990
Cdd:PRK08043 655 ALVLFTTDSELTREKLqQYAREHGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
2027-2077 |
2.38e-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: 44.93 E-value: 2.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 363747658 2027 SRVGIHDSFFELGGDSIKALQVAARLAAE-GWSMTIRDLFRYSTIQELCGHI 2077
Cdd:smart00823 31 EAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHL 82
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
2215-2424 |
2.41e-05 |
|
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: 49.40 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2215 LFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQaleKKEIQLPPKTDSYLSYADG-------LTQIAESKQLLSE 2286
Cdd:cd19546 117 LFALSDTEHvLLLVVHRIAADDESLDVLVRDLAAAYGA---RREGRAPERAPLPLQFADYalwerelLAGEDDRDSLIGD 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2287 K-TYWQTILDAH--TAFLPKDIENvPDRLQMNSDAAAFVLSGDWTEKLLfETQQAYGTDANELLLTALGMALSEWAGHDQ 2363
Cdd:cd19546 194 QiAYWRDALAGApdELELPTDRPR-PVLPSRRAGAVPLRLDAEVHARLM-EAAESAGATMFTVVQAALAMLLTRLGAGTD 271
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363747658 2364 IVISTEGHGREGHvpnIDISRTVGWFTSIYPILLDMGIPEPFEDQLAYRIKTTKDMLRR--VP 2424
Cdd:cd19546 272 VTVGTVLPRDDEE---GDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHqdVP 331
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
606-883 |
2.67e-05 |
|
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: 49.16 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 606 TSGSTGQPKGVAVEHRQAVSFLTGMQ---HQFPLSEDDIVMVKTSFSFDASVWQLFW--WSLsGASAYLLPPGWekdSAL 680
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLDVWAELVArclDAAGVTPGDRVQNAYGYGLFTGGLGFHYgaERL-GALVIPAGGGN---TER 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 681 IVQAIHQENVTTAHFIPAMLNSFLDQAEIERLSDRT-SLKRVFAGGEPLAPRTAARFASVLPqVSLIHGYGPTEAT---- 755
Cdd:cd05913 162 QLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRElSLKVGIFGAEPWTEEMRKRIERRLG-IKAYDIYGLTEIIgpgv 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 756 ------------VDAAFY--VLDPErdrdrlripIGKPVPGarlyvldphlavqpsGVAGELYIAGagvargyLNRPALt 821
Cdd:cd05913 241 afeceekdglhiWEDHFIpeIIDPE---------TGEPVPP---------------GEVGELVFTT-------LTKEAM- 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 363747658 822 eerfledpfyPGERmYKTGDVARWLPDGNVE---------FLGRTDDQVKIRGYRIEPGEIEAALRSIEGV 883
Cdd:cd05913 289 ----------PLIR-YRTRDITRLLPGPCPCgrthrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGL 348
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1840-1956 |
3.07e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 49.43 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1840 PIGV--AGELCIGGAGVAKGYHQKPDLTQ--MKftknpfvsgERLYRTGDRACWLPNGTIRLLGRMDYQVKIN-GYRIET 1914
Cdd:PLN02430 459 PLGEppRGEICVRGKCLFSGYYKNPELTEevMK---------DGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVAL 529
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 363747658 1915 EEIESVLLQTGLVREAAVavqHDKNGQAGLAAYIVPSDVNTN 1956
Cdd:PLN02430 530 EYLENVYGQNPIVEDIWV---YGDSFKSMLVAVVVPNEENTN 568
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1495-1937 |
4.21e-05 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 48.82 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1495 QKDVPFHR-IFEaKAEEIPEHIAVIDNEIEISYRF----LNERanRLARTLQN---RKGPkpTVAVLAKRSIDAIVGVLA 1566
Cdd:PLN02246 20 PNHLPLHDyCFE-RLSEFSDRPCLIDGATGRVYTYadveLLSR--RVAAGLHKlgiRQGD--VVMLLLPNCPEFVLAFLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1567 VMKAGGVYIPIDSHYPKARIEYILRDSGADILLLQQELKHLISNLP-ESEMSHICLDDE----------SSYEENSCnLN 1635
Cdd:PLN02246 95 ASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAeDDGVTVVTIDDPpegclhfselTQADENEL-PE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1636 LSPAPEEPVYIIYTSGTTGAPKGVIVTYRNF-THAAlawRQI------YELDRKPVRLLQIASFSFDVFSGDLARTLTNG 1708
Cdd:PLN02246 174 VEISPDDVVALPYSSGTTGLPKGVMLTHKGLvTSVA---QQVdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1709 GTLIVCPdetRLEPAEIYKIMNSQRITVMESTPALII-----PVMEyvyrnQFKLPDLDILI-----LGSDMVKAQDFKT 1778
Cdd:PLN02246 251 AAILIMP---KFEIGALLELIQRHKVTIAPFVPPIVLaiaksPVVE-----KYDLSSIRMVLsgaapLGKELEDAFRAKL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1779 LTDRFGQsmriinSYGVTEA----TIDSSF----YETSMGGEGTgdnvpigsPLPNVHMYVL-SQTDQIQPIGVAGELCI 1849
Cdd:PLN02246 323 PNAVLGQ------GYGMTEAgpvlAMCLAFakepFPVKSGSCGT--------VVRNAELKIVdPETGASLPRNQPGEICI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1850 GGAGVAKGYHQKPDLTQmkftknpfvsgerlyRTGDRACWLPNGTIRLL---------GRMDYQVKINGYRIETEEIESV 1920
Cdd:PLN02246 389 RGPQIMKGYLNDPEATA---------------NTIDKDGWLHTGDIGYIddddelfivDRLKELIKYKGFQVAPAELEAL 453
|
490
....*....|....*..
gi 363747658 1921 LLQTGLVREAAVAVQHD 1937
Cdd:PLN02246 454 LISHPSIADAAVVPMKD 470
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2079-2398 |
4.77e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.19 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2079 PLA--SQA--DQGP-AEGEAE----LTPIQrrffgQVHAFHNHYNQSV------MLFSEKGFNANALHLALRKITEHHDA 2143
Cdd:PRK12316 4080 PLAglDQArlDALPlPLGEIEdiypLSPMQ-----QGMLFHSLYEQEAgdyinqMRVDVQGLDVERFRAAWQAALDRHDV 4154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2144 IRMIF-QRDQNGHVIQfnrgINHKDHELfGLYISDWTKASLERTHLDEKLAAEEtviQSKMNVEKGPLLQAGLFKTAEGD 2222
Cdd:PRK12316 4155 LRSGFvWQGELGRPLQ----VVHKQVSL-PFAELDWRGRADLQAALDALAAAER---ERGFDLQRAPLLRLVLVRTAEGR 4226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2223 HLLIAL-HHLVIDGVSWRILLEDLAAAYQQalekkeiQLPPKTDsyLSYADGLTQIAESKQLLSEKtYWQT---ILDAHT 2298
Cdd:PRK12316 4227 HHLIYTnHHILMDGWSNSQLLGEVLERYSG-------RPPAQPG--GRYRDYIAWLQRQDAAASEA-FWREqlaALDEPT 4296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 2299 AfLPKDIENVPDRLQMNSDAAAFVLSGDWTEKLLfETQQAYGTDANELLLTALGMALSEWAGHDQIVISTEGHGREGHVP 2378
Cdd:PRK12316 4297 R-LAQAIARADLRSANGYGEHVRELDATATARLR-EFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELP 4374
|
330 340
....*....|....*....|
gi 363747658 2379 NIDisRTVGWFTSIYPILLD 2398
Cdd:PRK12316 4375 GIE--GQIGLFINTLPVIAT 4392
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1637-1932 |
5.03e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 48.52 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1637 SPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPd 1716
Cdd:PRK07867 148 VADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRR- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1717 etrlepaeiyKIMNSQritVMESTPALIIPVMEYVYRN-QFKL-----PD-----LDILiLGSDMVkAQDFKTLTDRFGq 1785
Cdd:PRK07867 227 ----------KFSASG---FLPDVRRYGATYANYVGKPlSYVLatperPDdadnpLRIV-YGNEGA-PGDIARFARRFG- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1786 sMRIINSYGVTEATIdsSFYETSMGGEGT----GDNVPI-----GSPLPNVHMYVLSQTDQIQPIgvaGELC-IGGAGVA 1855
Cdd:PRK07867 291 -CVVVDGFGSTEGGV--AITRTPDTPPGAlgplPPGVAIvdpdtGTECPPAEDADGRLLNADEAI---GELVnTAGPGGF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1856 KGYHqkpdltqmkftKNPFVSGERL----YRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAA 1931
Cdd:PRK07867 365 EGYY-----------NDPEADAERMrggvYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVA 433
|
.
gi 363747658 1932 V 1932
Cdd:PRK07867 434 V 434
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1874-1994 |
7.18e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 48.02 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1874 FVS------GERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAA 1946
Cdd:PRK10524 462 FVKtywslfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVvGVKDALKGQVAVAF 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 363747658 1947 YIV--PSDVNTNALRAALTKE--------LPAYMIPAHLIPLENMPLTLNGKLDRNAL 1994
Cdd:PRK10524 542 VVPkdSDSLADREARLALEKEimalvdsqLGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1550-1699 |
3.59e-04 |
|
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: 45.81 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1550 VAVLAKRSIDAIVGVLAVMKAGGVYIPI-DSHYPKArIEYILRDSGADILL------------LQQELKHLIS------N 1610
Cdd:cd05933 36 VGILGFNSPEWFIAAVGAIFAGGIAVGIyTTNSPEA-CQYVAETSEANILVvenqkqlqkilqIQDKLPHLKAiiqykeP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1611 LPESEMSHICLDD-----ESSYEENSCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYRNFTHAALAWRQIYELDRKPVR 1685
Cdd:cd05933 115 LKEKEPNLYSWDEfmelgRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVG 194
|
170 180
....*....|....*....|...
gi 363747658 1686 ---------LLQIASFSFDVFSG 1699
Cdd:cd05933 195 qesvvsylpLSHIAAQILDIWLP 217
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
718-856 |
6.51e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 44.97 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 718 LKRVFAGGEPLAPRTAARFASVLPQVslIHGYGPTEATVDAAFYV---LDPErdrdrlriPIGKPVPGARLYVLD----- 789
Cdd:PTZ00216 430 VRAMLSGGGPLSAATQEFVNVVFGMV--IQGWGLTETVCCGGIQRtgdLEPN--------AVGQLLKGVEMKLLDteeyk 499
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 363747658 790 ----PHlavqPSGvagELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGR 856
Cdd:PTZ00216 500 htdtPE----PRG---EILLRGPFLFKGYYKQEELTREVLDEDGW------FHTGDVGSIAANGTLRIIGR 557
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
582-874 |
3.21e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 42.78 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 582 LASEKAENHEFTPADGGSLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDI---------------VMVKT 646
Cdd:PLN02736 205 LAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVhisylplahiyervnQIVML 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 647 SFSFDASVWQLFWWSLSGASAYL-------LPPGWEKDSALIVQAIHQE--------NVTTAHFIPAMLNS-----FLDQ 706
Cdd:PLN02736 285 HYGVAVGFYQGDNLKLMDDLAALrptifcsVPRLYNRIYDGITNAVKESgglkerlfNAAYNAKKQALENGknpspMWDR 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 707 AEIERLSDRTS--LKRVFAGGEPLAPRTaARFASVLPQVSLIHGYGPTEATVdaafyVLDPERDRDRLRIPIGKPVPGAR 784
Cdd:PLN02736 365 LVFNKIKAKLGgrVRFMSSGASPLSPDV-MEFLRICFGGRVLEGYGMTETSC-----VISGMDEGDNLSGHVGSPNPACE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 785 LYVLD-PHLAV----QPSGvAGELYIAGAGVARGYLNRPALTEERFLEDPFypgermYKTGDVARWLPDGNVEFLGRTDD 859
Cdd:PLN02736 439 VKLVDvPEMNYtsedQPYP-RGEICVRGPIIFKGYYKDEVQTREVIDEDGW------LHTGDIGLWLPGGRLKIIDRKKN 511
|
330
....*....|....*.
gi 363747658 860 QVKI-RGYRIEPGEIE 874
Cdd:PLN02736 512 IFKLaQGEYIAPEKIE 527
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
1072-1292 |
4.11e-03 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 42.39 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1072 TGYNMpavlELEGKLNPERMERAFKELIKRHESLRTSFEQDAGGDPVQRIHDEVPFTLQtTVLGERTEQEAAAafikPFD 1151
Cdd:PRK09294 24 TGYTA----HLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWELVADDLLHPGIV-VVDGDAARPLPEL----QLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 1152 LSQApLFRAQIVKISDERHLLLVdMHHIISDGVSVNILIREFGELYNNR----NLPALRIQ---------YKDYAVWREG 1218
Cdd:PRK09294 95 QGVS-LLALDVVPDDGGARVTLY-IHHSIADAHHSASLLDELWSRYTDVvttgDPGPIRPQpapqsleavLAQRGIRRQA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363747658 1219 FKTGDAY-KTQEAYWLkQLEGELPVLDLPADHARPPVrsfagdkVSFTLDQEVASGLHKLARENGSTLYMVLLAA 1292
Cdd:PRK09294 173 LSGAERFmPAMYAYEL-PPTPTAAVLAKPGLPQAVPV-------TRCRLSKAQTSSLAAFGRRHRLTVNALVSAA 239
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
483-693 |
4.15e-03 |
|
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: 42.34 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 483 SLTYAELDMYASRLAAHLAARGITNESIVGVLSERSPEMLIAVL-AVLKAGGAYLPLDPAYPKERLSY------------ 549
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFyGCLYAGVVPIPIEPPDISQQLGFllgtckvrvalt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363747658 550 ---MLKDSGASLLLTQPGCSAPNFSGETLEVDMTSLASEKAENHEFT----PADGGSLAYVIYTSGSTGQPKGVAVEHRQ 622
Cdd:cd05905 94 veaCLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWgphpPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 363747658 623 AVSFLTGMQHQFPLSEDDIVMVKTSFSFDASVWQlfwWSL----SGASAYLLPPG-WEKDSALIVQAIHQENVTTA 693
Cdd:cd05905 174 LLAHCRALKEACELYESRPLVTVLDFKSGLGLWH---GCLlsvySGHHTILIPPElMKTNPLLWLQTLSQYKVRDA 246
|
|
| |
