|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
37-556 |
0e+00 |
|
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: 743.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLD 116
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 117 PDHPVSRHKEILRQTGARMVVVSaqhsarwassschvvtlseasigqltveddlpgfsaTPGNAAYVLFTSGSTGIPKGV 196
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 197 VLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAKAINTMGANWALLTPS 276
Cdd:cd05918 125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 277 VAQLLNPSDVPTLKILVIGGEQVTSKDWNRWPTSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVSWVVDPEDY 356
Cdd:cd05918 205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 357 HKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPAWLvdgCQGYAGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQV 436
Cdd:cd05918 285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWL---KQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 437 KVRGQRVELGEIEHHIQGCMPEANQIAVEVILLEGEKSNTILAAFLQLD-VKTGRAFPTNKAAETGSLAQVIFPvEAGKK 515
Cdd:cd05918 362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDgSSSGSGDGDSLFLEPSDEFRALVA-ELRSK 440
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1779949166 516 LAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIGASFS 556
Cdd:cd05918 441 LRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESLS 481
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
24-1563 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 631.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 24 AWNHKIPGVTNKCIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAML 103
Cdd:PRK12467 501 RWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLL 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 104 AVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSAQHSARWA-SSSCHVVTLSEAsigqltvEDDLPGFSA------- 175
Cdd:PRK12467 581 AVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPvPAGLRSLCLDEP-------ADLLCGYSGhnpeval 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 176 TPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVpSDRDR 255
Cdd:PRK12467 654 DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHL-LPPDC 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 256 HSD---LAKAINTMGANWALLTPSVAQLL----NPSDVPTLKILVIGGEQVTSKDWNRW---PTSVQLINGYGPTECCIV 325
Cdd:PRK12467 733 ARDaeaFAALMADQGVTVLKIVPSHLQALlqasRVALPRPQRALVCGGEALQVDLLARVralGPGARLINHYGPTETTVG 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 326 CTGYTTT---QAFKTGTIGTAIASVSWVVdPEDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPAwlvdGCQ 402
Cdd:PRK12467 813 VSTYELSdeeRDFGNVPIGQPLANLGLYI-LDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPF----GAD 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 403 GyagrrGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEhhiqGCMPEANQIAVEVILLEGEKSNTILAAFL 482
Cdd:PRK12467 888 G-----GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIE----ARLLAQPGVREAVVLAQPGDAGLQLVAYL 958
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 483 qldVKTGRAFPTNKAAETGSLAQVifpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIGASfsaqqlae 562
Cdd:PRK12467 959 ---VPAAVADGAEHQATRDELKAQ---------LRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAS-------- 1018
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 563 irtSGQGLKRQPSTENEKALQQLWAGVLaiDADSIGLDDSFFRLGGDSIAAMKLVGEARRA-GIHLTVADLFRNPKLEAV 641
Cdd:PRK12467 1019 ---AVQATFVAPQTELEKRLAAIWADVL--KVERVGLTDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLAGF 1093
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 642 ASlnlSLGNSSPenivafALLGETSDVTQIREEvaascntntsliediyPCSPLQEGMMALASKRPGD--YIMQSVLALH 719
Cdd:PRK12467 1094 AQ---AVAAQQQ------GAQPALPDVDRDQPL----------------PLSYAQERQWFLWQLEPGSaaYHIPQALRLK 1148
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 720 DDTDEDRFRAAWERVVQSTAVLRTRIV--------HSSKMGMLQV----VLADGIEWEQaneLEQYLEKDKSVSMGLGDS 787
Cdd:PRK12467 1149 GPLDIEALERSFDALVARHESLRTTFVqedgrtrqVIHPVGSLTLeeplLLAADKDEAQ---LKVYVEAEARQPFDLEQG 1225
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 788 -LARYALVRdVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPGFNAF-IKYL------------GEQDHE 853
Cdd:PRK12467 1226 pLLRVGLLR-LAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALpIQYAdyavwqrqwmdaGERARQ 1304
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 854 aaAAYWQGTLADCQAISfpALP-----PAVQQpVADATTAFQCP--------ALARRpSDITMSTLIRAAWALLASSYTS 920
Cdd:PRK12467 1305 --LAYWKAQLGGEQPVL--ELPtdrprPAVQS-HRGARLAFELPpalaeglrALARR-EGVTLFMLLLASFQTLLHRYSG 1378
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 921 SDDVVFGATVTGRNApvAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQ-----QATEMIPYEQtgLHETAKVSADA 995
Cdd:PRK12467 1379 QDDIRVGVPIANRNR--AETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQaaleaQAHQDLPFEQ--LVEALQPERSL 1454
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 996 RHACSFQTLLIVQPGSNGDIAhdALG-------EWRSHSDLQDFTTYAlmvqcvlADDEVQIIAS-------FDRRAIEp 1061
Cdd:PRK12467 1455 SHSPLFQVMFNHQRDDHQAQA--QLPglsveslSWESQTAQFDLTLDT-------YESSEGLQASltyatdlFEASTIE- 1524
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1062 wqvdKMLRQFSFVMQQLAtADAEAGIASIDTLTPEDRQQLWE-WN-HDVPPAIERCIHDLFADQAKARPDAPAICAWDGD 1139
Cdd:PRK12467 1525 ----RLAGHWLNLLQGLV-ADPERRLGELDLLDEAERRQILEgWNaTHTGYPLARLVHQLIEDQAAATPEAVALVFGEQE 1599
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1140 MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLASE 1219
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS 1679
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1220 ASAPL--AKDLVGTVVIVNADSALQLAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQAS 1297
Cdd:PRK12467 1680 HLQARlpLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAA 1759
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1298 TRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRT--DLASAMCRMKVNWA-FLTSTVVDLLTP----KSVPSLSIL 1370
Cdd:PRK12467 1760 DVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDpeQLIQLIERQQVTTLhFVPSMLQQLLQMdeqvEHPLSLRRV 1839
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1371 CVGGEPIRASQIVRWGSQ---VHLRQTYGSSEVSGIVSsaaLTTCSTTRDVGRASTGV--------FWIVDPNNHnrLAP 1439
Cdd:PRK12467 1840 VCGGEALEVEALRPWLERlpdTGLFNLYGPTETAVDVT---HWTCRRKDLEGRDSVPIgqpianlsTYILDASLN--PVP 1914
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1440 VGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI 1519
Cdd:PRK12467 1915 IGVAGELYLGGVGLARGYLNRPALTAERFVADP-------FGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRI 1987
|
1610 1620 1630 1640
....*....|....*....|....*....|....*....|....*.
gi 1779949166 1520 EVEEIEhqARLAE-ADVAEIAVeliQPKDGEDG-MLACFIVVEDSA 1563
Cdd:PRK12467 1988 ELGEIE--ARLREqGGVREAVV---IAQDGANGkQLVAYVVPTDPG 2028
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1116-1595 |
0e+00 |
|
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: 622.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLD 1195
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1196 PSLPHERLRLMCRKVSAKLSLASeasaplakdlvgtvvivnadsalqlahhaspitsvRPTHTAYVIFTSGSTGEPKGCR 1275
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTS-----------------------------------SPSDAAYVIFTSGSTGKPKGVV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1276 IEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTDLASAMCRMKVNWAFLTSTV 1355
Cdd:cd05918 126 IEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPSV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1356 VDLLTPKSVPSLSILCVGGEPIRASQIVRWGSQVHLRQTYGSSEVSGIVSSAALTTCSTTRDVGRASTGVFWIVDPNNHN 1435
Cdd:cd05918 206 ARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDPDNHD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1436 RLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAWRASLGLSAGqQRLYKTGDLARYKDDGSIELIGRKDNQVKLR 1515
Cdd:cd05918 286 RLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQEGSGRG-RRLYRTGDLVRYNPDGSLEYVGRKDTQVKIR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1516 GQRIEVEEIEHQARLAEADVAEIAVELIQPKDGEDG-MLACFIVVEDSASNEDELSGKRTRLDTRTQRTIGKIQDRLERD 1594
Cdd:cd05918 365 GQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSpQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRQR 444
|
.
gi 1779949166 1595 L 1595
Cdd:cd05918 445 L 445
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-1564 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 616.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLD 116
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLD 2084
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 117 PDHPVSRHKEILRQTGARMVVVSAQHSARWASSScHVVTLSeasigqLTVEDDLPGFSAT-------PGNAAYVLFTSGS 189
Cdd:PRK12316 2085 PNYPAERLAYMLEDSGAALLLTQRHLLERLPLPA-GVARLP------LDRDAEWADYPDTapavqlaGENLAYVIYTSGS 2157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 190 TGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSD-LAKAINTMGA 268
Cdd:PRK12316 2158 TGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEqLYDEMERHGV 2237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 269 NWALLTPSVAQLL--------NPsdvPTLKILVIGGEQVTSKDWNRWPTSVQ---LINGYGPTECCIVCTGYTTTQAFKT 337
Cdd:PRK12316 2238 TILDFPPVYLQQLaehaerdgRP---PAVRVYCFGGEAVPAASLRLAWEALRpvyLFNGYGPTEAVVTPLLWKCRPQDPC 2314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 338 GT----IGTAIASVSWVVDPEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgYAGRRGRLYK 413
Cdd:PRK12316 2315 GAayvpIGRALGNRRAYILDADLNLLAP-GMAGELYLGGEGLARGYLNRPGLTAERFVPDP---------FSASGERLYR 2384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 414 TGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQG--CMPEAnqiavEVILLEGeKSNTILAAFLqldvktgra 491
Cdd:PRK12316 2385 TGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAhpAVREA-----VVVAQDG-ASGKQLVAYV--------- 2449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 492 fptnkaaeTGSLAQVIFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIGASfSAQQLAEirtsgqglk 571
Cdd:PRK12316 2450 --------VPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVS-QLRQAYV--------- 2511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 572 rQPSTENEKALQQLWAGVLAIdaDSIGLDDSFFRLGGDSIAAMKLVGEARRA-GIHLTVADLFRNPKLEAVASLNLSLGN 650
Cdd:PRK12316 2512 -APQEGLEQRLAAIWQAVLKV--EQVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQT 2588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 651 SSPENIVAfallgetsdVTQIREEVAASCNTNTSLIEDIYPCSPLQEGMMALASKRPGDY--IMQSVLAL--HDDTDEDR 726
Cdd:PRK12316 2589 SRAPVLQK---------VTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQaaLEQAFDALvlRHETLRTR 2659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 727 FRAAWERVVQstaVLRTRIVHSSKMGMLQVVLADGIEWEQANELEQYLEKDKSvsmglgdSLARYALVRdVGTGKRWMVW 806
Cdd:PRK12316 2660 FVEVGEQTRQ---VILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARG-------PLLRVRLLA-LDGQEHVLVI 2728
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 807 TLHHALYDGWSLPQIANLVTEVYHGAEVGKQPGFNAFI-----------KYLGEQDHEAAAAYWQGTLADCQAISfpALP 875
Cdd:PRK12316 2729 TQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPlqyadyaawqrAWMDSGEGARQLDYWRERLGGEQPVL--ELP 2806
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 876 -----PAVQ-------QPVADATTAFQCPALARRpSDITMSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPvaGIEAM 943
Cdd:PRK12316 2807 ldrprPALQshrgarlDVALDVALSRELLALARR-EGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERL 2883
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 944 AGPTIATVPVRVRVQHSHKVSEFLHSVQQQATEM-----IPYEQtgLHETAKVSADARHACSFQTLLIVQPGSNGDIAHD 1018
Cdd:PRK12316 2884 IGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAqahqdLPFEQ--LVEALQPERSLSHSPLFQVMYNHQSGERAAAQLP 2961
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1019 ALG----EWRSHSdlqdfTTYALMVQCVLADDEVQIIASFDRRAIEPWQVDKMLRQFSFVMQQLAtADAEAGIASIDTLT 1094
Cdd:PRK12316 2962 GLHiesfAWDGAA-----TQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMV-ENPQRSVDELAMLD 3035
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1095 PEDRQQLWE-WNH-DVPPAIERCIHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFE 1172
Cdd:PRK12316 3036 AEERGQLLEaWNAtAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVE 3115
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1173 KSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLASEAsapLAKDLVGTVVIVNADSALQLAHHASPITS 1252
Cdd:PRK12316 3116 RSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSH---LRLPLAQGVQVLDLDRGDENYAEANPAIR 3192
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1253 VRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCIcVLSEEE 1332
Cdd:PRK12316 3193 TMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV-VLAGPE 3271
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1333 RRTDLASAMCRMKVNWAFLTSTVVDLLT-------PKSVPSLSILCVGGEPIRASQIVRWGSQVHLRQTYGSSEVSgiVS 1405
Cdd:PRK12316 3272 DWRDPALLVELINSEGVDVLHAYPSMLQafleeedAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEAT--IT 3349
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1406 SAALTTCSTTRD---VGRASTGVFWIVDPNNHNRlAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslglSA 1482
Cdd:PRK12316 3350 VTHWQCVEEGKDavpIGRPIANRACYILDGSLEP-VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDP--------FV 3420
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1483 GQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhqARLAEADVAEIAVELiqpkDGEDGMLACFIVVEDS 1562
Cdd:PRK12316 3421 PGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE--ARLLEHPWVREAVVL----AVDGRQLVAYVVPEDE 3494
|
..
gi 1779949166 1563 AS 1564
Cdd:PRK12316 3495 AG 3496
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
689-1082 |
6.62e-168 |
|
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: 511.84 E-value: 6.62e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 689 IYPCSPLQEGMMALASKRPGDYIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGMLQVVLADG-IEWEQA 767
Cdd:cd19545 1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESpISWTES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 768 NELEQYLEKDKSVSMGLGDSLARYALVRDvGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPGFNAFIKYL 847
Cdd:cd19545 81 TSLDEYLEEDRAAPMGLGGPLVRLALVED-PDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRFVKYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 848 GEQDHEAAAAYWQGTLADCQAISFPALPPAVQQPVADATTAFQCPALARRPSDITMSTLIRAAWALLASSYTSSDDVVFG 927
Cdd:cd19545 160 RQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSASSGVTLATVLRAAWALVLSRYTGSDDVVFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 928 ATVTGRNAPVAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATEMIPYEQTGLHETAKVSADARHACSFQTLLIV 1007
Cdd:cd19545 240 VTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDARAACNFQTLLVV 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1779949166 1008 QP-GSNGDIAHDALGEWRSHSDLQDFTTYALMVQCVLADDEVQIIASFDRRAIEPWQVDKMLRQFSFVMQQLATAD 1082
Cdd:cd19545 320 QPaLPSSTSESLELGIEEESEDLEDFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
693-1569 |
8.59e-155 |
|
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: 507.47 E-value: 8.59e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 693 SPLQEGMMALASKRPGDYIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGMLQVVLADGIEWEQANELEQ 772
Cdd:COG1020 34 LLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 773 YLEKDKSVSMGLGDSLARYALVRDVGTGKRWMVWTLHHALYDGWSLP-QIANLVTEVYHGAEVGKQPGFNAFIKY----- 846
Cdd:COG1020 114 AAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGlLLAELLRLYLAAYAGAPLPLPPLPIQYadyal 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 847 -----LGEQDHEAAAAYWQGTLADcqAISFPALP-----PAVQQPV---------ADATTAFQcpALARRpSDITMSTLI 907
Cdd:COG1020 194 wqrewLQGEELARQLAYWRQQLAG--LPPLLELPtdrprPAVQSYRgarvsfrlpAELTAALR--ALARR-HGVTLFMVL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 908 RAAWALLASSYTSSDDVVFGATVTGRNAPvaGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATEM-----IPYEQ 982
Cdd:COG1020 269 LAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAyahqdLPFER 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 983 tgLHETAKVSADARHACSFQTLLIVQ--PGSNGDIAHDALGEWRSHSDlqdFTTYALMVQCVLADDEVQIIASFDRRAIE 1060
Cdd:COG1020 347 --LVEELQPERDLSRNPLFQVMFVLQnaPADELELPGLTLEPLELDSG---TAKFDLTLTVVETGDGLRLTLEYNTDLFD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1061 PWQVDKMLRQFSFVMQQLAtADAEAGIASIDTLTPEDRQQLW-EWNH-DVPPAIERCIHDLFADQAKARPDAPAICAWDG 1138
Cdd:COG1020 422 AATIERMAGHLVTLLEALA-ADPDQPLGDLPLLTAAERQQLLaEWNAtAAPYPADATLHELFEAQAARTPDAVAVVFGDQ 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1139 DMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLAS 1218
Cdd:COG1020 501 SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQ 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1219 EASAPLAKDLVGTVVIVNADSALQLAHHAsPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQAST 1298
Cdd:COG1020 581 SALAARLPELGVPVLALDALALAAEPATN-PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGD 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1299 RTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERR--TDLASAMCRMKVNWAFLTSTVVDLL---TPKSVPSLSILCVG 1373
Cdd:COG1020 660 RVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRdpAALAELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVG 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1374 GEPIRASQIVRW---GSQVHLRQTYGSSEVSGIVSSAALTTCSTTRD---VGRASTGV-FWIVDPnnHNRLAPVGAVGEV 1446
Cdd:COG1020 740 GEALPPELVRRWrarLPGARLVNLYGPTETTVDSTYYEVTPPDADGGsvpIGRPIANTrVYVLDA--HLQPVPVGVPGEL 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1447 LVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEh 1526
Cdd:COG1020 818 YIGGAGLARGYLNRPELTAERFVADP-------FGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIE- 889
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1779949166 1527 qARLAE-ADVAEIAVeLIQPKDGEDGMLACFIVVEDSASNEDEL 1569
Cdd:COG1020 890 -AALLQhPGVREAVV-VAREDAPGDKRLVAYVVPEAGAAAAAAL 931
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
24-931 |
8.92e-140 |
|
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: 466.26 E-value: 8.92e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 24 AWNH-KIPGVTNKCIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAM 102
Cdd:COG1020 464 EWNAtAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVAL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 103 LAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSAQHSARWASSSCHVVTLSEASIGQLTVEDdlPGFSATPGNAAY 182
Cdd:COG1020 544 LAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPATN--PPVPVTPDDLAY 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 183 VLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHS--DLA 260
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDpaALA 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 261 KAINTMGANWALLTPSVAQLL---NPSDVPTLKILVIGGEQVTSKDWNRW---PTSVQLINGYGPTECCIVCTGYTTTQA 334
Cdd:COG1020 702 ELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELVRRWrarLPGARLVNLYGPTETTVDSTYYEVTPP 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 335 FKTG---TIGTAIASVS-WVVDpeDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPAwlvdgcqGYAGrrGR 410
Cdd:COG1020 782 DADGgsvPIGRPIANTRvYVLD--AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPF-------GFPG--AR 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 411 LYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCmPEANQiAVeVILLEGEKSNTILAAFLqldvktgr 490
Cdd:COG1020 851 LYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQH-PGVRE-AV-VVAREDAPGDKRLVAYV-------- 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 491 afptnkaaeTGSLAQVIFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIGAsfsaqqlaeirtsgQGL 570
Cdd:COG1020 920 ---------VPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAA--------------AAA 976
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 571 KRQPSTENEKALQQLWAGVLAIDADSIGLDDSFFRLGGDSIAAMKLVGEARRAGIHLTVADLFRNPKLEAVASLNLSLGN 650
Cdd:COG1020 977 AAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAA 1056
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 651 SSPENIVAFALLGETSDVTQIREEVAAscntntslieDIYPCSPLQEGMMALASKRPGDYIMQSVLALHDDTDEDRFRAA 730
Cdd:COG1020 1057 AAAAAPLAAAAAPLPLPPLLLSLLALL----------LALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALR 1126
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 731 WERVVQSTAVLRTRIVHSskmGMLQVVLADGIEWEQANELEQYLEKDKSVSMGLGDSLARYALVRDVGTGKRWMVWTLHH 810
Cdd:COG1020 1127 ARRAVRQEGPRLRLLVAL---AAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLL 1203
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 811 ALYDGWSLPQIANLVTEVYHGAEVGKQPGFNAFIKYLGEQDHEAAAAYWQGTLADCQAISFPALPPAVQQPVADATTAFQ 890
Cdd:COG1020 1204 LLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPAL 1283
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 1779949166 891 CPALARRPSDITMSTLIRAAWALLASSYTSSDDVVFGATVT 931
Cdd:COG1020 1284 ARARAARTARALALLLLLALLLLLALALALLLLLLLLLALL 1324
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
49-548 |
3.67e-137 |
|
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: 431.18 E-value: 3.67e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVVsaqhsarwassschvvtlseasigqltveddlpgfsaTPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCL 208
Cdd:cd05930 81 EDSGAKLVLT-------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 209 GHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHS--DLAKAINTMGANWALLTPSVAQLL----N 282
Cdd:cd05930 124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDpeALADLLAEEGITVLHLTPSLLRLLlqelE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 283 PSDVPTLKILVIGGEQVTSKDWNRWPTS---VQLINGYGPTECCIVCTGYTTTQAFKTG---TIGTAIASVS-WVVDpeD 355
Cdd:cd05930 204 LAALPSLRLVLVGGEALPPDLVRRWRELlpgARLVNLYGPTEATVDATYYRVPPDDEEDgrvPIGRPIPNTRvYVLD--E 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 356 YHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgyAGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQ 435
Cdd:cd05930 282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNP----------FGPGERMYRTGDLVRWLPDGNLEFLGRIDDQ 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 436 VKVRGQRVELGEIEHHIQGCmPEANQiAVeVILLEGEKSNTILAAFLQLDVKTgrafptnkAAETGSLAQVifpveagkk 515
Cdd:cd05930 352 VKIRGYRIELGEIEAALLAH-PGVRE-AA-VVAREDGDGEKRLVAYVVPDEGG--------ELDEEELRAH--------- 411
|
490 500 510
....*....|....*....|....*....|...
gi 1779949166 516 LAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd05930 412 LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
686-1561 |
3.08e-135 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 466.56 E-value: 3.08e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 686 IEDIYPCSPLQEGMM--ALASKRPGDYIMQSVLALhDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGM-LQVVLADG- 761
Cdd:PRK12467 2643 IEDIYPLSPMQQGMLfhTLYEGGAGDYINQMRVDV-EGLDVERFRTAWQAVIDRHEILRSGFLWDGELEEpLQVVYKQAr 2721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 762 -----IEWEQANELEQYL----EKDKSVSMGLGDS-LARYALVRdVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHG 831
Cdd:PRK12467 2722 lpfsrLDWRDRADLEQALdalaAADRQQGFDLLSApLLRLTLVR-TGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFG 2800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 832 AEVGKQPG-FNAFIKYLGEQDHEAAAAYWQGTLADCQAISF--PALPPAVQQPVA---------DATTAFQCPALARRpS 899
Cdd:PRK12467 2801 QPPPAREGrYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRlaRALYPAPAEAVAghgahylhlDATQTRQLIEFARR-H 2879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 900 DITMSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPVAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATEMIP 979
Cdd:PRK12467 2880 RVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALRE 2959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 980 YEQTGLHETAKVSADARHACsFQTLLI---------VQPGSNGDIAHDALGEwrshsdlQDFTTYALMVqCVLADDEVQI 1050
Cdd:PRK12467 2960 FEHTPLADIQRWAGQGGEAL-FDSILVfenypiseaLKQGAPSGLRFGAVSS-------REQTNYPLTL-AVGLGDTLEL 3030
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1051 IASFDRRAIEPWQVDKMLRQFSFVMQQLaTADAEAGIASIDTLTPEDRQQLWE-WNHD-VPPAIERCIHDLFADQAKARP 1128
Cdd:PRK12467 3031 EFSYDRQHFDAAAIERLAESFDRLLQAM-LNNPAARLGELPTLAAHERRQVLHaWNATaAAYPSERLVHQLIEAQVARTP 3109
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1129 DAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCR 1208
Cdd:PRK12467 3110 EAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIE 3189
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1209 KVSAKLsLASEAS--APLAKDLVGTVVIVNADSALQLAHHaSPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVT 1286
Cdd:PRK12467 3190 DSGVKL-LLTQAHllEQLPAPAGDTALTLDRLDLNGYSEN-NPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLC 3267
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1287 AHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTD-LASAMCRMKVNWA-FLTSTVVDLLT---P 1361
Cdd:PRK12467 3268 WIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEeLWQAIHAHRISIAcFPPAYLQQFAEdagG 3347
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1362 KSVPSLSILCVGGEPIRA---SQIVRWGSQVHLRQTYGSSEVsgIVSSAALTTCSTTRD------VGRASTGVFWIVDPN 1432
Cdd:PRK12467 3348 ADCASLDIYVFGGEAVPPaafEQVKRKLKPRGLTNGYGPTEA--VVTVTLWKCGGDAVCeapyapIGRPVAGRSIYVLDG 3425
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1433 NHNRlAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGQQRLYKTGDLARYKDDGSIELIGRKDNQV 1512
Cdd:PRK12467 3426 QLNP-VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP-------FSGSGGRLYRTGDLARYRADGVIEYLGRIDHQV 3497
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1513 KLRGQRIEVEEIEhqARLAEADVAEIAVELIQpkDGEDG-MLACFIVVED 1561
Cdd:PRK12467 3498 KIRGFRIELGEIE--ARLLQHPSVREAVVLAR--DGAGGkQLVAYVVPAD 3543
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
62-453 |
3.77e-135 |
|
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: 424.37 E-value: 3.77e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 62 SYSVLDGLSTKLAGYLVKI-GVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSA 140
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 141 QHSARWASSSCHVVTLS---EASIGQLTVEDDLPGFSAtPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGIT 217
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDpleLAALDDAPAPPPPDAPSG-PDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 218 DQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSD---LAKAINTMGANWALLTPSVAQLLNPSDVP---TLKI 291
Cdd:TIGR01733 160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDaalLAALIAEHPVTVLNLTPSLLALLAAALPPalaSLRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 292 LVIGGEQVTSKDWNRW---PTSVQLINGYGPTECCIVCTGYTTTQA----FKTGTIGTAIASVS-WVVDPEdyHKLAPLG 363
Cdd:TIGR01733 240 VILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTATLVDPDdaprESPVPIGRPLANTRlYVLDDD--LRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 364 SVGELLVEGPILARGYLNDAEKTAAAFIEDPAWlvdgcqgyAGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRV 443
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFA--------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRI 389
|
410
....*....|
gi 1779949166 444 ELGEIEHHIQ 453
Cdd:TIGR01733 390 ELGEIEAALL 399
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
14-1576 |
3.61e-132 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 457.32 E-value: 3.61e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 14 LEPQEMGQIWAWNHKIPGVTNKCIHDLFAEQVLAQPNAPAIcAWDGE-MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCF 92
Cdd:PRK05691 1110 LDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIAL-VWDGGsLDYAELHAQANRLAHYLRDKGVGPDVCVAIAA 1188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 93 EKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSAQHSARwASSSCHVVTLSEASIGQLTVEDDLPG 172
Cdd:PRK05691 1189 ERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLER-LPQAEGVSAIALDSLHLDSWPSQAPG 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 173 FSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSD 252
Cdd:PRK05691 1268 LHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGP 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 253 ---RDRHSdLAKAINTMGANWALLTPSVAQLL--NP--SDVPTLKILVIGGEQVTSKDWNR----WPtSVQLINGYGPTE 321
Cdd:PRK05691 1348 gehRDPQR-IAELVQQYGVTTLHFVPPLLQLFidEPlaAACTSLRRLFSGGEALPAELRNRvlqrLP-QVQLHNRYGPTE 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 322 CCIVCTgYTTTQAFKT--GTIGTAIASV-SWVVDPEdyHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlv 398
Cdd:PRK05691 1426 TAINVT-HWQCQAEDGerSPIGRPLGNVlCRVLDAE--LNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDP---- 1498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 399 DGCQGyagrrGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAVEvillegeksntil 478
Cdd:PRK05691 1499 LGEDG-----ARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA-QPGVAQAAVL------------- 1559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 479 aaflqldVKTGRAFPTNKAAETGSLAQVIFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIGasfsAQ 558
Cdd:PRK05691 1560 -------VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPV----WQ 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 559 QLAEIrtsgqglkrQPSTENEKALQQLWAGVLAIdaDSIGLDDSFFRLGGDSIAAMKLVGEARRA-GIHLTVADLFRNPK 637
Cdd:PRK05691 1629 QREHV---------EPRTELQQQIAAIWREVLGL--PRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFEASE 1697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 638 LEAVAslnlslgnsspENIVAFALLGETSDVTQIrEEVAAScntntslieDIYPCSPLQEGMMALASKRPGD--YIMQSV 715
Cdd:PRK05691 1698 LGAFA-----------EQVARIQAAGERNSQGAI-ARVDRS---------QPVPLSYSQQRMWFLWQMEPDSpaYNVGGM 1756
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 716 LALHDDTDEDRFRAAWERVVQSTAVLRTriVHSSKMGM-LQVVLADG---IEWE-----QANELEQYLEKdksvsmgLGD 786
Cdd:PRK05691 1757 ARLSGVLDVDRFEAALQALILRHETLRT--TFPSVDGVpVQQVAEDSglrMDWQdfsalPADARQQRLQQ-------LAD 1827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 787 S------------LARYALVRdVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPGFNAF-IKYL------ 847
Cdd:PRK05691 1828 SeahqpfdlergpLLRACLVK-AAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLpVQYLdysvwq 1906
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 848 ------GEQDHEaaAAYWQGTLADCQAISfpALP-----PAVQQPVADATTAFQCPALARR------PSDITMSTLIRAA 910
Cdd:PRK05691 1907 rqwlesGERQRQ--LDYWKAQLGNEHPLL--ELPadrprPPVQSHRGELYRFDLSPELAARvrafnaQRGLTLFMTMTAT 1982
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 911 WALLASSYTSSDDVVFGATVTGRNAPVAgiEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQ-----QATEMIPYEQtgL 985
Cdd:PRK05691 1983 LAALLYRYSGQRDLRIGAPVANRIRPES--EGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQtviegQSHQDLPFDH--L 2058
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 986 HETAKVSADARHACSFQTLLIVQ----------PGSNGD-IAHDALGewrshsdlqdfTTYALMVQCVLADDEVQIIASF 1054
Cdd:PRK05691 2059 VEALQPPRSAAYNPLFQVMCNVQrwefqqsrqlAGMTVEyLVNDARA-----------TKFDLNLEVTDLDGRLGCCLTY 2127
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1055 DRRAIEPWQVDKMLRQFSFVMQQLaTADAEAGIASIDTLTPEDRQQLWEWNHDVP--PAIERCIHDLFADQAKARPDAPA 1132
Cdd:PRK05691 2128 SRDLFDEPRIARMAEHWQNLLEAL-LGDPQQRLAELPLLAAAEQQQLLDSLAGEAgeARLDQTLHGLFAAQAARTPQAPA 2206
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1133 ICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSA 1212
Cdd:PRK05691 2207 LTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGI 2286
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1213 KLSLASEASAPLAKDLVGTVV--IVNADSALQLAHHASPITSVR-PTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHG 1289
Cdd:PRK05691 2287 GLLLSDRALFEALGELPAGVArwCLEDDAAALAAYSDAPLPFLSlPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVI 2366
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1290 RYLGMQASTRTLQFASYAFAGSLVELLMNLCHGgcicvlseeerrtdlASAMCRMKVNWAflTSTVVDLLTPKSVpslSI 1369
Cdd:PRK05691 2367 ERFGMRADDCELHFYSINFDAASERLLVPLLCG---------------ARVVLRAQGQWG--AEEICQLIREQQV---SI 2426
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1370 LcvGGEPIRASQIVRW----GSQVHLR---------------------------QTYGSSEVSgIVSSAALTTCSTTRDV 1418
Cdd:PRK05691 2427 L--GFTPSYGSQLAQWlagqGEQLPVRmcitggealtgehlqrirqafapqlffNAYGPTETV-VMPLACLAPEQLEEGA 2503
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1419 GRASTG------VFWIVDPNnhnrLAPV--GAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGQQRLYKT 1490
Cdd:PRK05691 2504 ASVPIGrvvgarVAYILDAD----LALVpqGATGELYVGGAGLAQGYHDRPGLTAERFVADP-------FAADGGRLYRT 2572
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1491 GDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhqARLAE-ADVAEIAVELIQPKDGEDgmLACFIVVEDSASNEDEL 1569
Cdd:PRK05691 2573 GDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIE--SRLLEhPAVREAVVLALDTPSGKQ--LAGYLVSAVAGQDDEAQ 2648
|
....*..
gi 1779949166 1570 SGKRTRL 1576
Cdd:PRK05691 2649 AALREAL 2655
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
684-1563 |
6.77e-127 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 441.32 E-value: 6.77e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 684 SLIEDIYPCSPLQEGMM--ALASKRPGDYIMQSVLALhDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGM-LQVVLAD 760
Cdd:PRK12316 4097 GEIEDIYPLSPMQQGMLfhSLYEQEAGDYINQMRVDV-QGLDVERFRAAWQAALDRHDVLRSGFVWQGELGRpLQVVHKQ 4175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 761 ------GIEWEQANELEQYLEKDKSVSMGLGDSLARYALVR----DVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYH 830
Cdd:PRK12316 4176 vslpfaELDWRGRADLQAALDALAAAERERGFDLQRAPLLRlvlvRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYS 4255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 831 GAEVGKQPG-FNAFIKYLGEQDHEAAAAYWQGTLAD-------CQAISFPALPPAvqQPVADATTAFQCPALAR-----R 897
Cdd:PRK12316 4256 GRPPAQPGGrYRDYIAWLQRQDAAASEAFWREQLAAldeptrlAQAIARADLRSA--NGYGEHVRELDATATARlrefaR 4333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 898 PSDITMSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPVAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATEM 977
Cdd:PRK12316 4334 TQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLAL 4413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 978 IPYEQTGLHETAKVSADARHACsFQTLLI---------VQPGSNGDIAHDALGEWrshsdlqDFTTYALMVQCVLADdEV 1048
Cdd:PRK12316 4414 REHEHTPLYEIQRWAGQGGEAL-FDSLLVfenypvseaLQQGAPGGLRFGEVTNH-------EQTNYPLTLAVGLGE-TL 4484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1049 QIIASFDRRAIEPWQVDKMLRQFSFVMQQLAtADAEAGIASIDTLTPEDRQQ-LWEWNH-DVPPAIERCIHDLFADQAKA 1126
Cdd:PRK12316 4485 SLQFSYDRGHFDAATIERLARHLTNLLEAMA-EDPQRRLGELQLLEKAEQQRiVALWNRtDAGYPATRCVHQLVAERARM 4563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1127 RPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLM 1206
Cdd:PRK12316 4564 TPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYM 4643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1207 CRKVSAKLSLA-SEASA--PLAKDLVGTVVIVNADSALQLAHhaSPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASS 1283
Cdd:PRK12316 4644 MEDSGAALLLTqSHLLQrlPIPDGLASLALDRDEDWEGFPAH--DPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN 4721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1284 AVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTD-LASAMCRMKVNWAFLTSTVVDLL--- 1359
Cdd:PRK12316 4722 HLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPErLYAEIHEHRVTVLVFPPVYLQQLaeh 4801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1360 --TPKSVPSLSILCVGGEPIR-ASQIVRWGS--QVHLRQTYGSSEVSGIVssaaltTCSTTRDVGRASTGVFWIVDP--- 1431
Cdd:PRK12316 4802 aeRDGEPPSLRVYCFGGEAVAqASYDLAWRAlkPVYLFNGYGPTETTVTV------LLWKARDGDACGAAYMPIGTPlgn 4875
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1432 ------NNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGQQRLYKTGDLARYKDDGSIELI 1505
Cdd:PRK12316 4876 rsgyvlDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDP-------FGAPGGRLYRTGDLARYRADGVIDYL 4948
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 1506 GRKDNQVKLRGQRIEVEEIEhqARLAEADVAEIAVELIQpkDGEDG-MLACFIVVEDSA 1563
Cdd:PRK12316 4949 GRVDHQVKIRGFRIELGEIE--ARLREHPAVREAVVIAQ--EGAVGkQLVGYVVPQDPA 5003
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
686-1579 |
1.02e-121 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 425.53 E-value: 1.02e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 686 IEDIYPCSPLQEGMM--ALASKRPGDYIMQSVLALhDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGM-LQVVLAD-- 760
Cdd:PRK12316 1553 IADIYPLSPMQQGMLfhSLYEQEAGDYINQLRVDV-QGLDPDRFRAAWQATVDRHEILRSGFLWQDGLEQpLQVIHKQve 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 761 ----GIEWEQANELEQYLEKDKSVSMGLGDSLARYALVRDV---GTGKRW-MVWTLHHALYDGWSLPQIANLVTEVYHGA 832
Cdd:PRK12316 1632 lpfaELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVlvrTGEGRHhLIYTNHHILMDGWSNAQLLGEVLQRYAGQ 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 833 EVGKQPG-FNAFIKYLGEQDHEAAAAYWQGTLAD-------CQAISFPALPPAV---QQPVADATTAfQCPALARRpSDI 901
Cdd:PRK12316 1712 PVAAPGGrYRDYIAWLQRQDAAASEAFWKEQLAAleeptrlAQAARTEDGQVGYgdhQQLLDPAQTR-ALAEFARA-QKV 1789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 902 TMSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPVAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATEMIPYE 981
Cdd:PRK12316 1790 TLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHE 1869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 982 QTGLHETAKVSADARHACsFQTLLI---------VQPGSNGDIAhdaLGEWRSHSDlqdfTTYALMVQCVLADdEVQIIA 1052
Cdd:PRK12316 1870 HTPLYDIQRWAGQGGEAL-FDSLLVfenypvaeaLKQGAPAGLV---FGRVSNHEQ----TNYPLTLAVTLGE-TLSLQY 1940
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1053 SFDRRAIEPWQVDKMLRQFSFVMQQLAtADAEAGIASIDTLTPEDRQ-QLWEWN-HDVPPAIERCIHDLFADQAKARPDA 1130
Cdd:PRK12316 1941 SYDRGHFDAAAIERLDRHLLHLLEQMA-EDAQAALGELALLDAGERQrILADWDrTPEAYPRGPGVHQRIAEQAARAPEA 2019
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1131 PAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKV 1210
Cdd:PRK12316 2020 IAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDS 2099
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1211 SAKLSLASE---ASAPLAKDLVgtVVIVNADSALQLAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTA 1287
Cdd:PRK12316 2100 GAALLLTQRhllERLPLPAGVA--RLPLDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQA 2177
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1288 HGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTD-LASAMCRMKVNWAFLTSTVVDLLTPKS--- 1363
Cdd:PRK12316 2178 AGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEqLYDEMERHGVTILDFPPVYLQQLAEHAerd 2257
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1364 --VPSLSILCVGGEPIRASQIVRWGSQ---VHLRQTYGSSEVsgIVSSAALTTCsttRDVGRASTGV----------FWI 1428
Cdd:PRK12316 2258 grPPAVRVYCFGGEAVPAASLRLAWEAlrpVYLFNGYGPTEA--VVTPLLWKCR---PQDPCGAAYVpigralgnrrAYI 2332
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1429 VDPNNHnrLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGQQRLYKTGDLARYKDDGSIELIGRK 1508
Cdd:PRK12316 2333 LDADLN--LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDP-------FSASGERLYRTGDLARYRADGVVEYLGRI 2403
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 1509 DNQVKLRGQRIEVEEIEhqARLAEADVAEIAVELIQpkDGEDG-MLACFIVVEDSAsnEDELSGKRTRLDTR 1579
Cdd:PRK12316 2404 DHQVKIRGFRIELGEIE--ARLQAHPAVREAVVVAQ--DGASGkQLVAYVVPDDAA--EDLLAELRAWLAAR 2469
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
39-548 |
2.57e-115 |
|
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: 373.07 E-value: 2.57e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 39 DLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPD 118
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 119 HPVSRHKEILRQTGARMVVVSAQHSARWASSSCHVVTLSEASigqlTVEDDLPGFSATPGNAAYVLFTSGSTGIPKGVVL 198
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALD----AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 199 EHRAVSTSCLGHGRAfGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCiCVPSDRDRHSD---LAKAINTMGANWALLTP 275
Cdd:cd12117 157 THRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGAR-LVLAPKGTLLDpdaLGALIAEEGVTVLWLTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 276 SVAQLL---NPSDVPTLKILVIGGEQVTSKDWNRW----PTsVQLINGYGPTECCIVCTGYTTTQAFKTGT---IGTAIA 345
Cdd:cd12117 235 ALFNQLadeDPECFAGLRELLTGGEVVSPPHVRRVlaacPG-LRLVNGYGPTENTTFTTSHVVTELDEVAGsipIGRPIA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 346 SVS-WVVDpeDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgyAGRRGRLYKTGDLVRYDDEG 424
Cdd:cd12117 314 NTRvYVLD--EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADP----------FGPGERLYRTGDLARWLPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 425 NLVCLGRKDSQVKVRGQRVELGEIEHHIQGCmPEANQIAVEVilLEGEKSNTILAAFLQldvktgrafptnkAAETGSLA 504
Cdd:cd12117 382 RLEFLGRIDDQVKIRGFRIELGEIEAALRAH-PGVREAVVVV--REDAGGDKRLVAYVV-------------AEGALDAA 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1779949166 505 QVifpveaGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd12117 446 EL------RAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1141-1540 |
6.48e-115 |
|
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: 369.29 E-value: 6.48e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVEL-GVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLASE 1219
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1220 ASAPLAKDLVGTVVIVNADSALQLAHHASPITS---VRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQA 1296
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPdapSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1297 STRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTD---LASAMCRMKVNWAFLTSTVVDLLTP---KSVPSLSIL 1370
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDaalLAALIAEHPVTVLNLTPSLLALLAAalpPALASLRLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1371 CVGGEPIRASQIVRW---GSQVHLRQTYGSSEVSGIVS----SAALTTCSTTRDVGRASTGV-FWIVDPnnHNRLAPVGA 1442
Cdd:TIGR01733 241 ILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTatlvDPDDAPRESPVPIGRPLANTrLYVLDD--DLRPVPVGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1443 VGEVLVEGPVLGREYIDEPDKTASTFIEAPAWraslglSAGQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVE 1522
Cdd:TIGR01733 319 VGELYIGGPGVARGYLNRPELTAERFVPDPFA------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELG 392
|
410
....*....|....*...
gi 1779949166 1523 EIEHQARlAEADVAEIAV 1540
Cdd:TIGR01733 393 EIEAALL-RHPGVREAVV 409
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1128-1576 |
2.64e-106 |
|
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: 346.44 E-value: 2.64e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMc 1207
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1208 rkvsakLslasEASAPlakdlvgTVVIVNADsalqlahhaspitsvrptHTAYVIFTSGSTGEPKGCRIEHRAASSAVTA 1287
Cdd:cd05930 80 ------L----EDSGA-------KLVLTDPD------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1288 HGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERR--TDLASAMCRMKVNWAFLT----STVVDLLTP 1361
Cdd:cd05930 125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTpsllRLLLQELEL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1362 KSVPSLSILCVGGEPIRASQIVRW---GSQVHLRQTYGSSEVSGIVSSAALTTCSTTRD---VGR--ASTGVfWIVDPNn 1433
Cdd:cd05930 205 AALPSLRLVLVGGEALPPDLVRRWrelLPGARLVNLYGPTEATVDATYYRVPPDDEEDGrvpIGRpiPNTRV-YVLDEN- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1434 hNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslglSAGQQRLYKTGDLARYKDDGSIELIGRKDNQVK 1513
Cdd:cd05930 283 -LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNP--------FGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVK 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 1514 LRGQRIEVEEIEHQARlAEADVAEIAVeLIQPKDGEDGMLACFIVVEDSAS-NEDELsgkRTRL 1576
Cdd:cd05930 354 IRGYRIELGEIEAALL-AHPGVREAAV-VAREDGDGEKRLVAYVVPDEGGElDEEEL---RAHL 412
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
41-549 |
5.19e-106 |
|
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: 347.41 E-value: 5.19e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 41 FAEQVLAQPNAPAIcAWDGE-MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDH 119
Cdd:cd17651 1 FERQAARTPDAPAL-VAEGRrLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 120 PVSRHKEILRQTGARMVVVSAQHSARWASSschVVTLSEASIGQLTVEDDLPGFSAT-PGNAAYVLFTSGSTGIPKGVVL 198
Cdd:cd17651 80 PAERLAFMLADAGPVLVLTHPALAGELAVE---LVAVTLLDQPGAAAGADAEPDPALdADDLAYVIYTSGSTGRPKGVVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 199 EHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSD--LAKAINTMGANWALLTPS 276
Cdd:cd17651 157 PHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPpaLAAWLDEQRISRVFLPTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 277 VAQLL----NPSDV--PTLKILVIGGEQVTS----KDWNRWPTSVQLINGYGPTECCIVcTGYTTTQAFK----TGTIGT 342
Cdd:cd17651 237 ALRALaehgRPLGVrlAALRYLLTGGEQLVLtedlREFCAGLPGLRLHNHYGPTETHVV-TALSLPGDPAawpaPPPIGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 343 AIASVS-WVVDPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgyAGRRGRLYKTGDLVRYD 421
Cdd:cd17651 316 PIDNTRvYVLDAAL--RPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDP----------FVPGARMYRTGDLARWL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 422 DEGNLVCLGRKDSQVKVRGQRVELGEIEHHIqgcmpeANQIAVE---VILLEGEKSNTILAAFLQLDVKTGRafptnkaa 498
Cdd:cd17651 384 PDGELEFLGRADDQVKIRGFRIELGEIEAAL------ARHPGVReavVLAREDRPGEKRLVAYVVGDPEAPV-------- 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 499 etgslaqviFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd17651 450 ---------DAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
14-865 |
5.13e-103 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 367.18 E-value: 5.13e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 14 LEPQEMGQIW-AWNHKIPGVTNK-CIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLC 91
Cdd:PRK12467 1551 LDEAERRQILeGWNATHTGYPLArLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIA 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 92 FEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSAQHSARWAS-SSCHVVTLSEASIGQLTVEDDL 170
Cdd:PRK12467 1631 VERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLpDGLRSLVLDQEDDWLEGYSDSN 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 171 PGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICV- 249
Cdd:PRK12467 1711 PAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIa 1790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 250 -PSDRDRHSDLAKAINTMGANWALLTPSVAQLL---NPSDV--PTLKILVIGGE--QVTSKD--WNRWPtSVQLINGYGP 319
Cdd:PRK12467 1791 pPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLlqmDEQVEhpLSLRRVVCGGEalEVEALRpwLERLP-DTGLFNLYGP 1869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 320 TECCIVCTGYTTTQAFKTGT----IGTAIASVSWVVDPEDYHkLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPa 395
Cdd:PRK12467 1870 TETAVDVTHWTCRRKDLEGRdsvpIGQPIANLSTYILDASLN-PVPIGVAGELYLGGVGLARGYLNRPALTAERFVADP- 1947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 396 wlvDGCQGyagrrGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQgcmpEANQIAVEVILLEGEKSN 475
Cdd:PRK12467 1948 ---FGTVG-----SRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLR----EQGGVREAVVIAQDGANG 2015
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 476 TILAAFLqldvktgraFPTNKAAETGSLAQVIFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIGASF 555
Cdd:PRK12467 2016 KQLVAYV---------VPTDPGLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASE 2086
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 556 SAQQLAeirtsgqglkrQPSTENEKALQQLWAGVLAIdaDSIGLDDSFFRLGGDSIAAMKLVGEARRAGIHLTVADLFRN 635
Cdd:PRK12467 2087 LQQAYV-----------APQSELEQRLAAIWQDVLGL--EQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQH 2153
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 636 PKLEAVASlnlslgnsspeniVAfallgetsdvtqiREEVAASCnTNTSLIEDIYPCSPLQEGMMALASKRPGDYIMQSV 715
Cdd:PRK12467 2154 QTVQSLAA-------------VA-------------QEGDGTVS-IDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVL 2206
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 716 LALHDDTDEDRFRAAWERVVQSTAVLRTRIV------HSSKMG--------MLQVVLADGIEWEQANELEQylekdKSVS 781
Cdd:PRK12467 2207 LEPREALDAELLEAALQALLVHHDALRLGFVqedggwSAMHRApeqerrplLWQVVVADKEELEALCEQAQ-----RSLD 2281
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 782 MGLGDSLAryALVRDVGTGKRWMVWTLHHALYDGWS----LPQIANLVTEVYHGAEV---GKQPGFNAFIKYLGEQDHEA 854
Cdd:PRK12467 2282 LEEGPLLR--AVLATLPDGSQRLLLVIHHLVVDGVSwrilLEDLQTAYRQLQGGQPVklpAKTSAFKAWAERLQTYAASA 2359
|
890
....*....|....*
gi 1779949166 855 A----AAYWQGTLAD 865
Cdd:PRK12467 2360 AladeLGYWQAQLQG 2374
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
39-550 |
4.87e-101 |
|
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: 331.20 E-value: 4.87e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 39 DLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPD 118
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 119 HPVSRHKEILRQTGARMVVvsaqhsarwassschvvtlseasigqltveddlpgFSATPGNAAYVLFTSGSTGIPKGVVL 198
Cdd:cd17653 81 LPSARIQAILRTSGATLLL-----------------------------------TTDSPDDLAYIIFTSGSTGIPKGVMV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 199 EHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAKAINTmganwALLTPSVA 278
Cdd:cd17653 126 PHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVARTVDA-----LMSTPSIL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 279 QLLNPSDVPTLKILVIGGEQVTSKDWNRWPTSVQLINGYGPTECCIVCTgYTTTQAFKTGTIGTAIASVS-WVVDPEDyh 357
Cdd:cd17653 201 STLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISST-MTELLPGQPVTIGKPIPNSTcYILDADL-- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 358 KLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPAWlvDGcqgyagrrGRLYKTGDLVRYDDEGNLVCLGRKDSQVK 437
Cdd:cd17653 278 QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW--PG--------SRMYRTGDYGRWTEDGGLEFLGREDNQVK 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 438 VRGQRVELGEIEHHIQGCMPEANQIAVEVillegekSNTILAAFLqldvktgrafpTNKAAETGSLAQvifpveagkKLA 517
Cdd:cd17653 348 VRGFRINLEEIEEVVLQSQPEVTQAAAIV-------VNGRLVAFV-----------TPETVDVDGLRS---------ELA 400
|
490 500 510
....*....|....*....|....*....|...
gi 1779949166 518 ERLPSYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:cd17653 401 KHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
38-548 |
9.08e-101 |
|
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: 332.70 E-value: 9.08e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 38 HDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDP 117
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 118 DHPVSRHKEILRQTGARMVVVSAQHSARWASSSCHVVTLSEASigqLTVEDDLPGFSATPGNAAYVLFTSGSTGIPKGVV 197
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEAL---AAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 198 LEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDrDRHSD---LAKAINTMGANWALLT 274
Cdd:cd17646 158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARP-GGHRDpayLAALIREHGVTTCHFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 275 PSV----AQLLNPSDVPTLKILVIGGEQVTSKDWNRW--PTSVQLINGYGPTECCIVCTGYTTTQAFKTGT--IGTAIAS 346
Cdd:cd17646 237 PSMlrvfLAEPAAGSCASLRRVFCSGEALPPELAARFlaLPGAELHNLYGPTEAAIDVTHWPVRGPAETPSvpIGRPVPN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 347 VS-WVVDpeDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawLVDGcqgyagrrGRLYKTGDLVRYDDEGN 425
Cdd:cd17646 317 TRlYVLD--DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDP--FGPG--------SRMYRTGDLARWRPDGA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 426 LVCLGRKDSQVKVRGQRVELGEIEHHIQGCmPEANQIAveVILLEGEKSNTILAAFLQLDvktgrafPTNKAAETGSLAQ 505
Cdd:cd17646 385 LEFLGRSDDQVKIRGFRVEPGEIEAALAAH-PAVTHAV--VVARAAPAGAARLVGYVVPA-------AGAAGPDTAALRA 454
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1779949166 506 vifpveagkKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd17646 455 ---------HLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
49-549 |
2.17e-99 |
|
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: 327.40 E-value: 2.17e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVvsaqhsarwassschvvtlseasigqltveddlpgfSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCL 208
Cdd:cd17649 81 EDSGAGLLL------------------------------------THHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 209 GHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDR--DRHSDLAKAINTMGANWALLTPSVAQLL----- 281
Cdd:cd17649 125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPAYLQQLaeead 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 282 --NPSDVPTLKILVIGGEQVTSKDWNRW-PTSVQLINGYGPTECCIVCTGYTTTQAFKTG----TIGTAIASVSWVVDPE 354
Cdd:cd17649 205 rtGDGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARAgasmPIGRPLGGRSAYILDA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 355 DYhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgYAGRRGRLYKTGDLVRYDDEGNLVCLGRKDS 434
Cdd:cd17649 285 DL-NPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDP---------FGAPGSRLYRTGDLARWRDDGVIEYLGRVDH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 435 QVKVRGQRVELGEIEhhiqGCMPEANQIAVEVILLEGEKSNTILAAFLQLDVktgrafptnkAAETGSLAQVIfpveaGK 514
Cdd:cd17649 355 QVKIRGFRIELGEIE----AALLEHPGVREAAVVALDGAGGKQLVAYVVLRA----------AAAQPELRAQL-----RT 415
|
490 500 510
....*....|....*....|....*....|....*
gi 1779949166 515 KLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd17649 416 ALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
40-550 |
2.88e-99 |
|
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: 328.52 E-value: 2.88e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 40 LFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDH 119
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 120 PVSRHKEILRQTGARMvVVSAQHSARWASSSCHVVTLSEASIGQLTVEdDLPGFSaTPGNAAYVLFTSGSTGIPKGVVLE 199
Cdd:cd17655 82 PEERIQYILEDSGADI-LLTQSHLQPPIAFIGLIDLLDEDTIYHEESE-NLEPVS-KSDDLAYVIYTSGSTGKPKGVMIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 200 HRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSD--LAKAINTMGANWALLTPSV 277
Cdd:cd17655 159 HRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGqaLTQYIRQNRITIIDLTPAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 278 AQLLNPSDV---PTLKILVIGGEQVTSKDWNRW----PTSVQLINGYGPTECCIVCTGYTTTQAFKTGT---IGTAIASV 347
Cdd:cd17655 239 LKLLDAADDsegLSLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDASIYQYEPETDQQVsvpIGKPLGNT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 348 S-WVVDpeDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawLVDGcqgyagrrGRLYKTGDLVRYDDEGNL 426
Cdd:cd17655 319 RiYILD--QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDP--FVPG--------ERMYRTGDLARWLPDGNI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 427 VCLGRKDSQVKVRGQRVELGEIEHHIQgcMPEANQIAVeVILLEGEKSNTILAAFLQLDvktgRAFPTnkaaetgslAQV 506
Cdd:cd17655 387 EFLGRIDHQVKIRGYRIELGEIEARLL--QHPDIKEAV-VIARKDEQGQNYLCAYIVSE----KELPV---------AQL 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1779949166 507 ifpveaGKKLAERLPSYMVPDvYFV-VTQLPITVSGKTDRKRLRE 550
Cdd:cd17655 451 ------REFLARELPDYMIPS-YFIkLDEIPLTPNGKVDRKALPE 488
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
49-548 |
3.63e-98 |
|
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: 324.63 E-value: 3.63e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVVSAQHSARWAssscHVVTLSEASIGQLTVEDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCL 208
Cdd:cd12116 81 EDAEPALVLTDDALPDRLP----AGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 209 GHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHS--DLAKAINTMGANWALLTPSVAQLL---NP 283
Cdd:cd12116 157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDpeALARLIEAHSITVMQATPATWRMLldaGW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 284 SDVPTLKILViGGE--------QVTSkdwnrwpTSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVS-WVVDpe 354
Cdd:cd12116 237 QGRAGLTALC-GGEalppdlaaRLLS-------RVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQvYVLD-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 355 DYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgYAGRRGRLYKTGDLVRYDDEGNLVCLGRKDS 434
Cdd:cd12116 307 AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDP---------FAGPGSRLYRTGDLVRRRADGRLEYLGRADG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 435 QVKVRGQRVELGEIEhhiqGCMPEANQIAVEVILLEGEKSNTILAAFLQLdvktgrafptnKAAETGSLAQVifpveaGK 514
Cdd:cd12116 378 QVKIRGHRIELGEIE----AALAAHPGVAQAAVVVREDGGDRRLVAYVVL-----------KAGAAPDAAAL------RA 436
|
490 500 510
....*....|....*....|....*....|....
gi 1779949166 515 KLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd12116 437 HLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
49-548 |
5.95e-98 |
|
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: 322.67 E-value: 5.95e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVvsaqhsarwassschvvtlseasigqltveddlpgfsATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCL 208
Cdd:cd17652 81 ADARPALLL-------------------------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 209 GHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHS--DLAKAINTMGANWALLTPSVAQLLNPSDV 286
Cdd:cd17652 124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPgePLADLLREHRITHVTLPPAALAALPPDDL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 287 PTLKILVIGGEQVTSKDWNRWPTSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVS-WVVDpeDYHKLAPLGSV 365
Cdd:cd17652 204 PDLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRvYVLD--ARLRPVPPGVP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 366 GELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgYAGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVEL 445
Cdd:cd17652 282 GELYIAGAGLARGYLNRPGLTAERFVADP---------FGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 446 GEIEHHIQGCmpEANQIAVeVILLEGEKSNTILAAFLqldvkTGRAFPTNKAAETgsLAQvifpveagkkLAERLPSYMV 525
Cdd:cd17652 353 GEVEAALTEH--PGVAEAV-VVVRDDRPGDKRLVAYV-----VPAPGAAPTAAEL--RAH----------LAERLPGYMV 412
|
490 500
....*....|....*....|...
gi 1779949166 526 PDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd17652 413 PAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-642 |
1.39e-96 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 347.15 E-value: 1.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 35 KCIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAP 114
Cdd:PRK12467 3095 RLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 115 LDPDHPVSRHKEILRQTGARMVVVSAQHSARW-ASSSCHVVTLSEASIGQLTveDDLPGFSATPGNAAYVLFTSGSTGIP 193
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLpAPAGDTALTLDRLDLNGYS--ENNPSTRVMGENLAYVIYTSGSTGKP 3252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 194 KGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSD-LAKAINTMGANWAL 272
Cdd:PRK12467 3253 KGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEeLWQAIHAHRISIAC 3332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 273 LTPSVAQLL----NPSDVPTLKILVIGGEQVTSKDWNRWPT---SVQLINGYGPTECCIVCTGYTTTQAFKTGT----IG 341
Cdd:PRK12467 3333 FPPAYLQQFaedaGGADCASLDIYVFGGEAVPPAAFEQVKRklkPRGLTNGYGPTEAVVTVTLWKCGGDAVCEApyapIG 3412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 342 TAIASVSWVV-----DPedyhklAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgYAGRRGRLYKTGD 416
Cdd:PRK12467 3413 RPVAGRSIYVldgqlNP------VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP---------FSGSGGRLYRTGD 3477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 417 LVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAVEVILLEGEKSntiLAAFLQLDvktgrafptnk 496
Cdd:PRK12467 3478 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQ-HPSVREAVVLARDGAGGKQ---LVAYVVPA----------- 3542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 497 aAETGSLAQVIfpveaGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIGASFSAQQLAeirtsgqglkrqPST 576
Cdd:PRK12467 3543 -DPQGDWRETL-----RDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA------------PRS 3604
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 577 ENEKALQQLWAGVLAIdaDSIGLDDSFFRLGGDSIAAMKLVGEARRA-GIHLTVADLFRNPKLEAVA 642
Cdd:PRK12467 3605 EVEQQLAAIWADVLGV--EQVGVTDNFFELGGDSLLALQVLSRIRQSlGLKLSLRDLMSAPTIAELA 3669
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
36-548 |
7.63e-96 |
|
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: 317.84 E-value: 7.63e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 36 CIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPL 115
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 116 DPDHPVSRHKEILRQTGARMVVVSaqhsarwassschvvtlseasigqltveddlpgfsatPGNAAYVLFTSGSTGIPKG 195
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLTQ-------------------------------------PENLAYVIYTSGSTGKPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 196 VVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGC-ICVPSD--RDRHSDLAK-------AINT 265
Cdd:cd17644 124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATlVLRPEEmrSSLEDFVQYiqqwqltVLSL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 266 MGANWALLTPSVAQLLNPSDvPTLKILVIGGEQVTSKDWNRWPTSV----QLINGYGPTECCIVCTGYTTTQAFKTG--- 338
Cdd:cd17644 204 PPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVgnfiQLINVYGPTEATIAATVCRLTQLTERNits 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 339 -TIGTAIASVS-WVVDpeDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgYAGRRG-RLYKTG 415
Cdd:cd17644 283 vPIGRPIANTQvYILD--ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHP---------FNSSESeRLYKTG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 416 DLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQgcmpEANQI-AVEVILLEGEKSNTILAAFLqldvktgrafpt 494
Cdd:cd17644 352 DLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLS----QHNDVkTAVVIVREDQPGNKRLVAYI------------ 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 495 nkaaeTGSLAQVIFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd17644 416 -----VPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
687-1563 |
1.04e-94 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 341.55 E-value: 1.04e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 687 EDIYPCSPLQEGMMALASKRP--GDYIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGMLQVVLADGIEW 764
Cdd:PRK12316 47 AERDRLSYAQQRMWFLWQLEPqsGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 765 EQAN-------ELEQYLEKDKSVSMGLGDSLARYALVR----DVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAE 833
Cdd:PRK12316 127 EFEDcsglpeaEQEARLRDEAQRESLQPFDLCEGPLLRvrllRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 834 VGKQPGFNAF-IKY------------LGEQdhEAAAAYWQGTLADCQAISfpALP-----PAVQQPVADATTAFQCPALA 895
Cdd:PRK12316 207 TGAEPGLPALpIQYadyalwqrswleAGEQ--ERQLEYWRAQLGEEHPVL--ELPtdhprPAVPSYRGSRYEFSIDPALA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 896 R------RPSDITMSTLIRAAWALLASSYTSSDDVVFGATVTGRNApvAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHS 969
Cdd:PRK12316 283 EalrgtaRRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNR--AEVEGLIGFFVNTQVLRSVFDGRTRVATLLAG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 970 VQQ-----QATEMIPYEQtgLHETAKVSADARHACSFQTLLIVQPGSNGDIAHDALG-------EWRSHSDLQDFT--TY 1035
Cdd:PRK12316 361 VKDtvlgaQAHQDLPFER--LVEALKVERSLSHSPLFQVMYNHQPLVADIEALDTVAglefgqlEWKSRTTQFDLTldTY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1036 ----ALMVQCVLADDevqiiaSFDRRAIEpwqvdKMLRQFSFVMQQLaTADAEAGIASIDTLTPEDRQQLWE-WNHDVPP 1110
Cdd:PRK12316 439 ekggRLHAALTYATD------LFEARTVE-----RMARHWQNLLRGM-VENPQARVDELPMLDAEERGQLVEgWNATAAE 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1111 -AIERCIHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGG 1189
Cdd:PRK12316 507 yPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1190 AFLLLDPSLPHERLRLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSALQLAHHAS--PITSVRPTHTAYVIFTSGS 1267
Cdd:PRK12316 587 AYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEenPGTELNPENLAYVIYTSGS 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1268 TGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRT--DLASAMCRMK 1345
Cdd:PRK12316 667 TGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDpaKLVELINREG 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1346 VN-WAFLTSTVVDLLT---PKSVPSLSILCVGGEPIRAS---QIVRWGSQVHLRQTYGSSEvsgivsSAALTTCSTTRD- 1417
Cdd:PRK12316 747 VDtLHFVPSMLQAFLQdedVASCTSLRRIVCSGEALPADaqeQVFAKLPQAGLYNLYGPTE------AAIDVTHWTCVEe 820
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1418 ------VGRASTGV-FWIVDPNNHnrLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGqQRLYKT 1490
Cdd:PRK12316 821 ggdsvpIGRPIANLaCYILDANLE--PVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSP-------FVAG-ERMYRT 890
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 1491 GDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhqARLAEADVAEIAVELIQpkDGEDgmLACFIVVEDSA 1563
Cdd:PRK12316 891 GDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE--ARLLEHPWVREAAVLAV--DGKQ--LVGYVVLESEG 957
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-865 |
1.17e-94 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 341.17 E-value: 1.17e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 9 PRKNELEPQEMgqIWAWNHKIPGV-TNKCIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDV 87
Cdd:PRK12316 486 PMLDAEERGQL--VEGWNATAAEYpLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVL 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 88 VPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGArMVVVSAQHSARW--ASSSCHVVTLSEASIGQLT 165
Cdd:PRK12316 564 VGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGV-QLLLSQSHLGRKlpLAAGVQVLDLDRPAAWLEG 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 166 VEDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGG 245
Cdd:PRK12316 643 YSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 246 CICV--PSDRDRHSDLAKAINTMGANWALLTPSVAQLL----NPSDVPTLKILVIGGE--------QVTSKDWNrwptsV 311
Cdd:PRK12316 723 RLVVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQAFlqdeDVASCTSLRRIVCSGEalpadaqeQVFAKLPQ-----A 797
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 312 QLINGYGPTECCIVCTGYTTTQAFK-TGTIGTAIASV-SWVVDPedYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAA 389
Cdd:PRK12316 798 GLYNLYGPTEAAIDVTHWTCVEEGGdSVPIGRPIANLaCYILDA--NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAER 875
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 390 FIEDPawLVDGcqgyagrrGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHI--QGCMPEAnqiavEVI 467
Cdd:PRK12316 876 FVPSP--FVAG--------ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLleHPWVREA-----AVL 940
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 468 LLEGEKsntiLAAFLQLDVKTGRAFPTNKAAetgslaqvifpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKR 547
Cdd:PRK12316 941 AVDGKQ----LVGYVVLESEGGDWREALKAH-----------------LAASLPEYMVPAQWLALERLPLTPNGKLDRKA 999
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 548 LREIGASFSAQQLAeirtsgqglkrQPSTENEKALQQLWAGVLAIdaDSIGLDDSFFRLGGDSIAAMKLVGEARRAGIHL 627
Cdd:PRK12316 1000 LPAPEASVAQQGYV-----------APRNALERTLAAIWQDVLGV--ERVGLDDNFFELGGDSIVSIQVVSRARQAGIQL 1066
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 628 TVADLFRNpkleavaslnlslgnsspENIVAFALLGETSDVTQIREEVAASCntntsliediYPCSPLQEGMMALASKRP 707
Cdd:PRK12316 1067 SPRDLFQH------------------QTIRSLALVAKAGQATAADQGPASGE----------VALAPVQRWFFEQAIPQR 1118
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 708 GDYIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVhsSKMGMLQVVLADGIE----WEQANELEQYL-----EKDK 778
Cdd:PRK12316 1119 QHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFR--EEDGGWQQAYAAPQAgevlWQRQAASEEELlalceEAQR 1196
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 779 SVSMGLGdSLARyALVRDVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEV---GKQPGFNAFIKYLGEQDHEAA 855
Cdd:PRK12316 1197 SLDLEQG-PLLR-ALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDAdlpARTSSYQAWARRLHEHAGARA 1274
|
890
....*....|..
gi 1779949166 856 A--AYWQGTLAD 865
Cdd:PRK12316 1275 EelDYWQAQLED 1286
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1118-1567 |
1.03e-93 |
|
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: 312.21 E-value: 1.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1118 DLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPS 1197
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1198 LPHERLRLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSAlqlAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIE 1277
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDA---GPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1278 HRAASSAVTaHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCiCVLSEEERRTD---LASAMCRMKVNWAFLTST 1354
Cdd:cd12117 158 HRGVVRLVK-NTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGAR-LVLAPKGTLLDpdaLGALIAEEGVTVLWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1355 VVDLLT---PKSVPSLSILCVGGEPIRASQIVRW---GSQVHLRQTYGSSEVsgivssaalTTCSTTRDVGR-------- 1420
Cdd:cd12117 236 LFNQLAdedPECFAGLRELLTGGEVVSPPHVRRVlaaCPGLRLVNGYGPTEN---------TTFTTSHVVTEldevagsi 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1421 ------ASTGVFwIVDPnnHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAwraslglsAGQQRLYKTGDLA 1494
Cdd:cd12117 307 pigrpiANTRVY-VLDE--DGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF--------GPGERLYRTGDLA 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 1495 RYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQARLAEaDVAEIAVeLIQPKDGEDGMLACFIVVEDSASNED 1567
Cdd:cd12117 376 RWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHP-GVREAVV-VVREDAGGDKRLVAYVVAEGALDAAE 446
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
14-888 |
3.17e-93 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 336.54 E-value: 3.17e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 14 LEPQEMGQIW-AWNH-KIPGVTNKCIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLC 91
Cdd:PRK12316 3034 LDAEERGQLLeAWNAtAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVA 3113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 92 FEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVvsAQHSARWASSSCHVVTLSEASIGQLTVEDdlP 171
Cdd:PRK12316 3114 VERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL--SQSHLRLPLAQGVQVLDLDRGDENYAEAN--P 3189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 172 GFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCIcVPS 251
Cdd:PRK12316 3190 AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV-VLA 3268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 252 DRDRHSDLAKAI---NTMGANWALLTPSVAQLL----NPSDVPTLKILVIGGEQVTSKDWNRWPTSVQLINGYGPTECCI 324
Cdd:PRK12316 3269 GPEDWRDPALLVeliNSEGVDVLHAYPSMLQAFleeeDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATI 3348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 325 VCTGYTTTQAFK-TGTIGTAIASVSWVVdPEDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawLVDGcqg 403
Cdd:PRK12316 3349 TVTHWQCVEEGKdAVPIGRPIANRACYI-LDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDP--FVPG--- 3422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 404 yagrrGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEhhiqGCMPEANQIAVEVILLEGEKSntiLAAFLQ 483
Cdd:PRK12316 3423 -----ERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE----ARLLEHPWVREAVVLAVDGRQ---LVAYVV 3490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 484 LDVKTGRAFPTNKAAetgslaqvifpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIGASFSAQQLAei 563
Cdd:PRK12316 3491 PEDEAGDLREALKAH-----------------LKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-- 3551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 564 rtsgqglkrQPSTENEKALQQLWAGVLaiDADSIGLDDSFFRLGGDSIAAMKLVGEARRAGIHLTVADLFRNPKLEAVAS 643
Cdd:PRK12316 3552 ---------APVNELERRLAAIWADVL--KLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLAR 3620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 644 LnlslgnsspenivafALLGETSDVTQirEEVAASCntntsliediyPCSPLQEGMMALASKRPGDYIMQSVLALHDDTD 723
Cdd:PRK12316 3621 V---------------ARVGGGVAVDQ--GPVSGET-----------LLLPIQQQFFEEPVPERHHWNQSLLLKPREALD 3672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 724 EDRFRAAWERVVQSTAVLRTRIVHSSKMGM---LQVVLADGIEWE----QANELEQYLEKDKSvSMGLGDSLARYALVRD 796
Cdd:PRK12316 3673 AAALEAALQALVEHHDALRLRFVEDAGGWTaehLPVELGGALLWRaeldDAEELERLGEEAQR-SLDLADGPLLRALLAT 3751
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 797 VGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPGF----NAFIKYLGEQDHEAAA-------AYWQGTLAD 865
Cdd:PRK12316 3752 LADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLpaktSSFKAWAERLQEHARGealkaelAYWQEQLQG 3831
|
890 900
....*....|....*....|...
gi 1779949166 866 CQAiSFPALPPAVQQPVADATTA 888
Cdd:PRK12316 3832 VSS-ELPCDHPQGALQNRHAASV 3853
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
14-664 |
3.40e-93 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 336.54 E-value: 3.40e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 14 LEPQEMGQIWA-WNHKIPGVTNK-CIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLC 91
Cdd:PRK12316 4528 LEKAEQQRIVAlWNRTDAGYPATrCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIA 4607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 92 FEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSAQHSARWASSschvvtlseASIGQLTVE--DD 169
Cdd:PRK12316 4608 MERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIP---------DGLASLALDrdED 4678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 170 LPGFSAT-------PGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLL 242
Cdd:PRK12316 4679 WEGFPAHdpavrlhPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLI 4758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 243 YGGCICVPSDRDRHSD-LAKAINTMGANWALLTPSVAQLL-----NPSDVPTLKILVIGGEQVTSKDWNRWPTS---VQL 313
Cdd:PRK12316 4759 NGASVVIRDDSLWDPErLYAEIHEHRVTVLVFPPVYLQQLaehaeRDGEPPSLRVYCFGGEAVAQASYDLAWRAlkpVYL 4838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 314 INGYGPTECCIVCTGYTTTQAFKTGT----IGTAIASVS-WVVDpeDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAA 388
Cdd:PRK12316 4839 FNGYGPTETTVTVLLWKARDGDACGAaympIGTPLGNRSgYVLD--GQLNPLPVGVAGELYLGGEGVARGYLERPALTAE 4916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 389 AFIEDPAwlvdGCQGyagrrGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHI--QGCMPEANQIAVEV 466
Cdd:PRK12316 4917 RFVPDPF----GAPG-----GRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLreHPAVREAVVIAQEG 4987
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 467 illegeksntilAAFLQLdvkTGRAFPTNKAAETGSLAQVIFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRK 546
Cdd:PRK12316 4988 ------------AVGKQL---VGYVVPQDPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRK 5052
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 547 RLREIGASFSAQQLAeirtsgqglkrQPSTENEKALQQLWAGVLAIdaDSIGLDDSFFRLGGDSIAAMKLVGEARRA-GI 625
Cdd:PRK12316 5053 ALPQPDASLLQQAYV-----------APRSELEQQVAAIWAEVLQL--ERVGLDDNFFELGGHSLLAIQVTSRIQLElGL 5119
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1779949166 626 HLTVADLFRNPKLEAVASLNLSLGNSSPENIVAF-ALLGE 664
Cdd:PRK12316 5120 ELPLRELFQTPTLAAFVELAAAAGSGDDEKFDDLeELLSE 5159
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
710-1564 |
1.73e-92 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 334.05 E-value: 1.73e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 710 YIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVhSSKMGMLQVVLA--------DGIEWEQANELEQYLEKDKSVS 781
Cdd:PRK12467 72 YNIPTALRLRGELDVSALRRAFDALVARHESLRTRFV-QDEEGFRQVIDAslsltiplDDLANEQGRARESQIEAYINEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 782 MGLGDSLARYALVR----DVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPGFNAF-IKY---------- 846
Cdd:PRK12467 151 VARPFDLANGPLLRvrllRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALpIQYadyaiwqrsw 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 847 LGEQDHEAAAAYWQGTLADCQAISfpALP-----PAVQ-------QPVADATTAFQCPALARRpSDITMSTLIRAAWALL 914
Cdd:PRK12467 231 LEAGERERQLAYWQEQLGGEHTVL--ELPtdrprPAVPsyrgarlRVDLPQALSAGLKALAQR-EGVTLFMVLLASFQTL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 915 ASSYTSSDDVVFGATVTGRNApvAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQ-----QATEMIPYEQtgLHETA 989
Cdd:PRK12467 308 LHRYSGQSDIRIGVPNANRNR--VETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRtalgaQAHQDLPFEQ--LVEAL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 990 KVSADARHACSFQTLLIVQPgsNGDIAHDALGEWRSHSDLQDFTTYALMVQCVLADD----EVQIIASFDRRA--IEPWQ 1063
Cdd:PRK12467 384 QPERSLSHSPLFQVMFNHQN--TATGGRDREGAQLPGLTVEELSWARHTAQFDLALDtyesAQGLWAAFTYATdlFEATT 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1064 VDKMLRQFSFVMQQLaTADAEAGIASIDTLTPEDRQQLWE-WNHDVPPAIERCIHDLFADQAKARPDAPAICAWDGDMTY 1142
Cdd:PRK12467 462 IERLATHWRNLLEAI-VAEPRRRLGELPLLDAEERARELVrWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSY 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1143 GELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLASEASA 1222
Cdd:PRK12467 541 AELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLL 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1223 PLAKDLVGTVVIVNADSALQLAHHAS--PITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRT 1300
Cdd:PRK12467 621 AQLPVPAGLRSLCLDEPADLLCGYSGhnPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSM 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1301 LQFASYAFAGSLVELLMNLCHGGCICVLSEEERRT--DLASAMCRMKVN--------W-AFLTSTVVDLLTPksvpsLSI 1369
Cdd:PRK12467 701 LMVSTFAFDLGVTELFGALASGATLHLLPPDCARDaeAFAALMADQGVTvlkivpshLqALLQASRVALPRP-----QRA 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1370 LCVGGEPIRASQIVRW---GSQVHLRQTYGSSEVSGIVSSAALT---TCSTTRDVGRASTGVFWIVDPNNHNrLAPVGAV 1443
Cdd:PRK12467 776 LVCGGEALQVDLLARVralGPGARLINHYGPTETTVGVSTYELSdeeRDFGNVPIGQPLANLGLYILDHYLN-PVPVGVV 854
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1444 GEVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEE 1523
Cdd:PRK12467 855 GELYIGGAGLARGYHRRPALTAERFVPDP-------FGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGE 927
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 1779949166 1524 IEhqARLAEADVAEIAVELIQPKDGeDGMLACFIVVEDSAS 1564
Cdd:PRK12467 928 IE--ARLLAQPGVREAVVLAQPGDA-GLQLVAYLVPAAVAD 965
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
49-548 |
1.87e-92 |
|
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: 307.70 E-value: 1.87e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVVsaqhsarwassschvvtlseasigqltveddlpgfsaTPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCL 208
Cdd:cd17643 81 ADSGPSLLLT-------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 209 GHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSD---RDRhSDLAKAINTMGANWALLTPSV------AQ 279
Cdd:cd17643 124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYevaRSP-EDFARLLRDEGVTVLNQTPSAfyqlveAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 280 LLNPSDVPTLKILVIGGEQVTS---KDWN-RWPT-SVQLINGYGPTECCIVCTGYTTTQAFKTG----TIGTAIASVSW- 349
Cdd:cd17643 203 DRDGRDPLALRYVIFGGEALEAamlRPWAgRFGLdRPQLVNMYGITETTVHVTFRPLDAADLPAaaasPIGRPLPGLRVy 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 350 VVDpeDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPAwlvdgcqGYAGRrgRLYKTGDLVRYDDEGNLVCL 429
Cdd:cd17643 283 VLD--ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF-------GGPGS--RMYRTGDLARRLPDGELEYL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 430 GRKDSQVKVRGQRVELGEIEHHIQGCmPEANQIAveVILLEGEKSNTILAAFLQLDvktgrafpTNKAAETGSLAqvifp 509
Cdd:cd17643 352 GRADEQVKIRGFRIELGEIEAALATH-PSVRDAA--VIVREDEPGDTRLVAYVVAD--------DGAAADIAELR----- 415
|
490 500 510
....*....|....*....|....*....|....*....
gi 1779949166 510 veagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd17643 416 ----ALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1120-1579 |
6.35e-91 |
|
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: 304.65 E-value: 6.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1120 FADQAKARPDAPAIcAWDGD-MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSL 1198
Cdd:cd17651 1 FERQAARTPDAPAL-VAEGRrLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1199 PHERLRLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSALQLAhHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEH 1278
Cdd:cd17651 80 PAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGA-DAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1279 RAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTD--LASAMCRMKVNWAFLTSTVV 1356
Cdd:cd17651 159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPpaLAAWLDEQRISRVFLPTVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1357 DLLTPKSV------PSLSILCVGGEPIRASQIVR----WGSQVHLRQTYGSSE---VSGIVSSAALTTCSTTRDVGRAST 1423
Cdd:cd17651 239 RALAEHGRplgvrlAALRYLLTGGEQLVLTEDLRefcaGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPAPPPIGRPID 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1424 GV-FWIVDPnnHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAwraslglsAGQQRLYKTGDLARYKDDGSI 1502
Cdd:cd17651 319 NTrVYVLDA--ALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF--------VPGARMYRTGDLARWLPDGEL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 1503 ELIGRKDNQVKLRGQRIEVEEIEHqARLAEADVAEIAVeLIQPKDGEDGMLACFIVVEDSASneDELSGKRTRLDTR 1579
Cdd:cd17651 389 EFLGRADDQVKIRGFRIELGEIEA-ALARHPGVREAVV-LAREDRPGEKRLVAYVVGDPEAP--VDAAELRAALATH 461
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
37-548 |
1.15e-90 |
|
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: 302.31 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLD 116
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 117 PDHPVSRHKEILRQTGARMVVVsaqhsarwassschvvtlseasigqltveddlpgfsaTPGNAAYVLFTSGSTGIPKGV 196
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT-------------------------------------DPDDLAYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 197 VLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAKA-----INTMganwa 271
Cdd:cd12115 124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAaevtlINTV----- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 272 lltPSVA-QLLNPSDVPT-LKILVIGGEQVTS---KDWNRWPTSVQLINGYGPTECcivcTGYTT-----TQAFKTGTIG 341
Cdd:cd12115 199 ---PSAAaELLRHDALPAsVRVVNLAGEPLPRdlvQRLYARLQVERVVNLYGPSED----TTYSTvapvpPGASGEVSIG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 342 TAIA-SVSWVVDpeDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPAwlvdgcqgYAGRRgrLYKTGDLVRY 420
Cdd:cd12115 272 RPLAnTQAYVLD--RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF--------GPGAR--LYRTGDLVRW 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 421 DDEGNLVCLGRKDSQVKVRGQRVELGEIEHhiqgCMPEANQI--AVeVILLEGEKSNTILAAFLqldvktgrafptnkaa 498
Cdd:cd12115 340 RPDGLLEFLGRADNQVKVRGFRIELGEIEA----ALRSIPGVreAV-VVAIGDAAGERRLVAYI---------------- 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1779949166 499 eTGSLAQVIFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd12115 399 -VAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
14-644 |
1.19e-89 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 320.45 E-value: 1.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 14 LEPQEMGQIWAWN---HKIPGVTnkcIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPL 90
Cdd:PRK10252 437 LLPGEYAQLAQVNataVEIPETT---LSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAV 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 91 CFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSAQHSARWAssscHVVTLSEASIGQ-LTVEDD 169
Cdd:PRK10252 514 ALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFA----DVPDLTSLCYNApLAPQGA 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 170 LPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCIcV 249
Cdd:PRK10252 590 APLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKL-V 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 250 PSDRDRHSD---LAKAINTMGANWALLTPS-----VAQLLN---PSDVPTLKILVIGGEQVTSKDWNRWP--TSVQLING 316
Cdd:PRK10252 669 MAEPEAHRDplaMQQFFAEYGVTTTHFVPSmlaafVASLTPegaRQSCASLRQVFCSGEALPADLCREWQqlTGAPLHNL 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 317 YGPTECCIVCTGYTttqAFKTGTIGTAIASVS-----W-----VVDpeDYHKLAPLGSVGELLVEGPILARGYLNDAEKT 386
Cdd:PRK10252 749 YGPTEAAVDVSWYP---AFGEELAAVRGSSVPigypvWntglrILD--ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLT 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 387 AAAFIEDPAwlVDGcqgyagrrGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCMPEANQIAVEV 466
Cdd:PRK10252 824 ASRFIADPF--APG--------ERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHAC 893
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 467 ILLEGEKSN---TILAAFL------QLDVKTGRAfptnkaaetgslaqvifpveagkKLAERLPSYMVPDVYFVVTQLPI 537
Cdd:PRK10252 894 VINQAAATGgdaRQLVGYLvsqsglPLDTSALQA-----------------------QLRERLPPHMVPVVLLQLDQLPL 950
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 538 TVSGKTDRKRLreigasfSAQQLAeIRTSGqglkRQPSTENEKALQQLWAGVLAIDADSIglDDSFFRLGGDSIAAMKLV 617
Cdd:PRK10252 951 SANGKLDRKAL-------PLPELK-AQVPG----RAPKTGTETIIAAAFSSLLGCDVVDA--DADFFALGGHSLLAMKLA 1016
|
650 660
....*....|....*....|....*...
gi 1779949166 618 GEARRA-GIHLTVADLFRNPKLEAVASL 644
Cdd:PRK10252 1017 AQLSRQfARQVTPGQVMVASTVAKLATL 1044
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
47-548 |
3.99e-89 |
|
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: 298.01 E-value: 3.99e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 47 AQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKE 126
Cdd:cd05945 3 ANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 127 ILRQTGARMVVVsaqhsarwassschvvtlseasigqltVEDDLpgfsatpgnaAYVLFTSGSTGIPKGVVLEHRAVsTS 206
Cdd:cd05945 83 ILDAAKPALLIA---------------------------DGDDN----------AYIIFTSGSTGRPKGVQISHDNL-VS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 207 CLGHGRA-FGITDQSRVLQFTSYTFDFCMAEIITTLLYGGC-ICVPSDR-DRHSDLAKAINTMGANWALLTPSVAQL--- 280
Cdd:cd05945 125 FTNWMLSdFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDAtADPKQLFRFLAEHGITVWVSTPSFAAMcll 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 281 ---LNPSDVPTLKILVIGGEQV---TSKDW-NRWPTSVqLINGYGPTECCIVCTGYTTTQAFKTG----TIGTAIASVSW 349
Cdd:cd05945 205 sptFTPESLPSLRHFLFCGEVLphkTARALqQRFPDAR-IYNTYGPTEATVAVTYIEVTPEVLDGydrlPIGYAKPGAKL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 350 VVDPEDyHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgyaGRRGrlYKTGDLVRYDDEGNLVCL 429
Cdd:cd05945 284 VILDED-GRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-----------GQRA--YRTGDLVRLEADGLLFYR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 430 GRKDSQVKVRGQRVELGEIEHHIQGCMPEANQIAVEVILLEGEksnTILAAFLQLDVKTGRAFPTNKAAEtgslaqvifp 509
Cdd:cd05945 350 GRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKV---TELIAFVVPKPGAEAGLTKAIKAE---------- 416
|
490 500 510
....*....|....*....|....*....|....*....
gi 1779949166 510 veagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd05945 417 ------LAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1128-1563 |
1.78e-87 |
|
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: 293.00 E-value: 1.78e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMC 1207
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1208 RKVSAKLSLASeasaplakdlvgtvvivnadsalqlahhaspitsvrPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTA 1287
Cdd:cd17652 81 ADARPALLLTT------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1288 HGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRT--DLASAMCRMKVNWAFLTSTVVDLLTPKSVP 1365
Cdd:cd17652 125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPgePLADLLREHRITHVTLPPAALAALPPDDLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1366 SLSILCVGGEPIRASQIVRWGSQVHLRQTYGSSEVSGIVSSAALTTCSTTRDVGRASTGV-FWIVDPnnHNRLAPVGAVG 1444
Cdd:cd17652 205 DLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTrVYVLDA--RLRPVPPGVPG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1445 EVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEI 1524
Cdd:cd17652 283 ELYIAGAGLARGYLNRPGLTAERFVADP-------FGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEV 355
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1779949166 1525 EhqARLAE-ADVAEiAVELIQPKDGEDGMLACFIVVEDSA 1563
Cdd:cd17652 356 E--AALTEhPGVAE-AVVVVRDDRPGDKRLVAYVVPAPGA 392
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
34-887 |
7.60e-87 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 316.34 E-value: 7.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 34 NKCIHDLFAEQVLAQPNAPAIcAWDGE-MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAF 112
Cdd:PRK05691 2187 DQTLHGLFAAQAARTPQAPAL-TFAGQtLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAY 2265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 113 APLDPDHPVSRHKEILRQTGARMVVvsaQHSARWAssschvvTLSE--ASIGQLTVEDDLPGFSATPG----------NA 180
Cdd:PRK05691 2266 VPLDPEYPLERLHYMIEDSGIGLLL---SDRALFE-------ALGElpAGVARWCLEDDAAALAAYSDaplpflslpqHQ 2335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 181 AYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHS-DL 259
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAeEI 2415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 260 AKAINTMGANWALLTPS----VAQ-LLNPSDVPTLKILVIGGEQVTSKDWNRWPTSVQ---LINGYGPTECCIVCTGYTT 331
Cdd:PRK05691 2416 CQLIREQQVSILGFTPSygsqLAQwLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFApqlFFNAYGPTETVVMPLACLA 2495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 332 TQAFKTGT----IGTAI-ASVSWVVDpEDYhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgYAG 406
Cdd:PRK05691 2496 PEQLEEGAasvpIGRVVgARVAYILD-ADL-ALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADP---------FAA 2564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 407 RRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEhhiqGCMPEANQIAVEVILLEGEKSNTILAAFLQLDV 486
Cdd:PRK05691 2565 DGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIE----SRLLEHPAVREAVVLALDTPSGKQLAGYLVSAV 2640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 487 ktgrafptnkaAETGSLAQVIFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLreigasfSAQQLAEIRTS 566
Cdd:PRK05691 2641 -----------AGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL-------PAPDPELNRQA 2702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 567 GQglkrQPSTENEKALQQLWAGVLaiDADSIGLDDSFFRLGGDSIAAMKLVGEARRAGIHLTVADLFRNPKLEAVASLNL 646
Cdd:PRK05691 2703 YQ----APRSELEQQLAQIWREVL--NVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVAT 2776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 647 SLGNSSPENivafALLGETSDVTQIRE-----EVAASCNTNTSLIEDiyPCSPLQEGMMALAskrpgdyiMQSVLALHD- 720
Cdd:PRK05691 2777 HSEAAQAEQ----GPLQGASGLTPIQHwffdsPVPQPQHWNQALLLE--PRQALDPALLEQA--------LQALVEHHDa 2842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 721 -----DTDEDRFRAAWERVVQSTAVLRTRIvhsSKMGMLQVVLADGiewEQANELEQylekdksvsmglgDSLARYALVR 795
Cdd:PRK05691 2843 lrlrfSQADGRWQAEYRAVTAQELLWQVTV---ADFAECAALFADA---QRSLDLQQ-------------GPLLRALLVD 2903
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 796 DvGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPGFNA-----------FIKYLGEQDHEAAAAYWQGTLA 864
Cdd:PRK05691 2904 G-PQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAktsafrdwaarLQAYAGSESLREELGWWQAQLG 2982
|
890 900
....*....|....*....|...
gi 1779949166 865 DcQAISFPALPPAVQQPVADATT 887
Cdd:PRK05691 2983 G-PRAELPCDRPQGGNLNRHAQT 3004
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
37-550 |
7.94e-87 |
|
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: 291.71 E-value: 7.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLD 116
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 117 PDHPVSRHKEILRQTGARMVVVsaqhsarwassschvvtlseasigqltveddlpgfsatpgnaAYVLFTSGSTGIPKGV 196
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 197 VLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDF-CMAEIITTLLYGGCICVPSDRDRhSDLAKAINTMGANWALLTP 275
Cdd:COG0318 119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFgLTVGLLAPLLAGATLVLLPRFDP-ERVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 276 SVAQLL------NPSDVPTLKILVIGGEQVTSKDWNRW--PTSVQLINGYGPTECCIVCTG-YTTTQAFKTGTIGTAIAS 346
Cdd:COG0318 198 TMLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFeeRFGVRIVEGYGLTETSPVVTVnPEDPGERRPGSVGRPLPG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 347 VS-WVVDPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFiedpawlvdgcqgyagrRGRLYKTGDLVRYDDEGN 425
Cdd:COG0318 278 VEvRIVDEDG--RELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-----------------RDGWLRTGDLGRLDEDGY 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 426 LVCLGRKDSQVKVRGQRVELGEIEHHIQGCmPEANQIAveVILLEGEKSNTILAAFLQLdvktgrafptnKAAETGSLAQ 505
Cdd:COG0318 339 LYIVGRKKDMIISGGENVYPAEVEEVLAAH-PGVAEAA--VVGVPDEKWGERVVAFVVL-----------RPGAELDAEE 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1779949166 506 VIfpveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:COG0318 405 LR------AFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1117-1567 |
4.90e-86 |
|
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: 290.72 E-value: 4.90e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1117 HDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDP 1196
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1197 SLPHERLRLMCRKVSAKLSLASEASAPLAKdlVGTVVIVNADSALQLAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRI 1276
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLP--AGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1277 EHRAASSavtahgRYLGMQ------ASTRTLQFASYAFAGSLVELLMNLCHGGCIcVLSEEERRTD---LASAMCRMKVN 1347
Cdd:cd17646 159 THAGIVN------RLLWMQdeyplgPGDRVLQKTPLSFDVSVWELFWPLVAGARL-VVARPGGHRDpayLAALIREHGVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1348 WAFLTSTV----VDLLTPKSVPSLSILCVGGEPIRASQIVRWGSQVH--LRQTYGSSEVSGIVSSAALTTCSTTRDV--G 1419
Cdd:cd17646 232 TCHFVPSMlrvfLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGaeLHNLYGPTEAAIDVTHWPVRGPAETPSVpiG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1420 R--ASTGVFwIVDPnnHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGqQRLYKTGDLARYK 1497
Cdd:cd17646 312 RpvPNTRLY-VLDD--ALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDP-------FGPG-SRMYRTGDLARWR 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1498 DDGSIELIGRKDNQVKLRGQRIEVEEIEhqARLAEADVAEIAVELIQPKDGEDGMLACFIVVEDSASNED 1567
Cdd:cd17646 381 PDGALEFLGRSDDQVKIRGFRVEPGEIE--AALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPD 448
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
689-1080 |
2.62e-84 |
|
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: 283.33 E-value: 2.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 689 IYPCSPLQEGMM--ALASKRPGDYIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGMLQVVLADG-IEW- 764
Cdd:cd19543 1 IYPLSPMQEGMLfhSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRkLPWr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 765 ----------EQANELEQYLEKDKSVSMGLG-DSLARYALVRdVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAE 833
Cdd:cd19543 81 eldlshlseaEQEAELEALAEEDRERGFDLArAPLMRLTLIR-LGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 834 VGKQP------GFNAFIKYLGEQDHEAAAAYWQGTLAD-CQAISFPALPPAVQQPV-----------ADATTAFQcpALA 895
Cdd:cd19543 160 EGQPPslppvrPYRDYIAWLQRQDKEAAEAYWREYLAGfEEPTPLPKELPADADGSyepgevsfelsAELTARLQ--ELA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 896 RRpSDITMSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPVAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQAT 975
Cdd:cd19543 238 RQ-HGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 976 EMIPYEQTGLHETAKVSadARHACSFQTLLIVQ--PgsngdiAHDALGEWRSHSDLQ-------DFTTYALMVQCVLaDD 1046
Cdd:cd19543 317 ELREHEYVPLYEIQAWS--EGKQALFDHLLVFEnyP------VDESLEEEQDEDGLRitdvsaeEQTNYPLTVVAIP-GE 387
|
410 420 430
....*....|....*....|....*....|....
gi 1779949166 1047 EVQIIASFDRRAIEPWQVDKMLRQFSFVMQQLAT 1080
Cdd:cd19543 388 ELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAA 421
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1128-1576 |
1.81e-83 |
|
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: 281.95 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMc 1207
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1208 rkvsaklslaseasaplakdlvgtvvIVNADSALQLAHHaspitsvrPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTA 1287
Cdd:cd17649 80 --------------------------LEDSGAGLLLTHH--------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1288 HGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCIcVLSEEERRTD---LASAMCRMKVNWAFLTST-------VVD 1357
Cdd:cd17649 126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACV-VLRPDELWASadeLAEMVRELGVTVLDLPPAylqqlaeEAD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1358 LLTPKSVPSLSILCVGGEPIRASQIVRWGSQ-VHLRQTYGSSEvsGIVSSAALTTCSTTRD------VGRASTGV-FWIV 1429
Cdd:cd17649 205 RTGDGRPPSLRLYIFGGEALSPELLRRWLKApVRLFNAYGPTE--ATVTPLVWKCEAGAARagasmpIGRPLGGRsAYIL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1430 DPnnHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGQQRLYKTGDLARYKDDGSIELIGRKD 1509
Cdd:cd17649 283 DA--DLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDP-------FGAPGSRLYRTGDLARWRDDGVIEYLGRVD 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 1510 NQVKLRGQRIEVEEIEhqARLAEAD-VAEIAVeLIQPKDGEDGMLACfIVVEDSASNEDELSGKRTRL 1576
Cdd:cd17649 354 HQVKIRGFRIELGEIE--AALLEHPgVREAAV-VALDGAGGKQLVAY-VVLRAAAAQPELRAQLRTAL 417
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1128-1569 |
2.51e-82 |
|
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: 279.18 E-value: 2.51e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMC 1207
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1208 RKVSAKLSLASEASAPLAKDLVGTVVIVNADSALQlahHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTA 1287
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAA---PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1288 HGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRT--DLASAMCRMKVNWAFLTSTVVDLLT---PK 1362
Cdd:cd12116 158 MRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDpeALARLIEAHSITVMQATPATWRMLLdagWQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1363 SVPSLSILCvGGE---PIRASQIVRWGSQVHlrQTYGSSEVSgIVSSAALTTCSTTR-DVGRASTGV-FWIVDPNnhNRL 1437
Cdd:cd12116 238 GRAGLTALC-GGEalpPDLAARLLSRVGSLW--NLYGPTETT-IWSTAARVTAAAGPiPIGRPLANTqVYVLDAA--LRP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1438 APVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAwraslglSAGQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQ 1517
Cdd:cd12116 312 VPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPF-------AGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGH 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 1518 RIEVEEIEhqARLAE-ADVAEIAVELIQpkDGEDGMLACFIVVEDSAS-NEDEL 1569
Cdd:cd12116 385 RIELGEIE--AALAAhPGVAQAAVVVRE--DGGDRRLVAYVVLKAGAApDAAAL 434
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
696-1579 |
1.00e-80 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 293.10 E-value: 1.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 696 QEG--MMALASKRPGDYIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVH-----------SSKMGMLQVV----- 757
Cdd:PRK10252 14 QPGiwMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEdngevwqwvdpALTFPLPEIIdlrtq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 758 ---LADGIEWEQAnELEQYLEKDKsvsmglGDSLARYALVRdVGtGKRWmVWTL--HHALYDGWSLPQIANLVTEVYHGA 832
Cdd:PRK10252 94 pdpHAAAQALMQA-DLQQDLRVDS------GKPLVFHQLIQ-LG-DNRW-YWYQryHHLLVDGFSFPAITRRIAAIYCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 833 EVGKQPGFNAFIKYLGEQDHEAA----------AAYWQGTLADCQAI-SFPALPPAVQQPVADA-TTAFQCPA-----LA 895
Cdd:PRK10252 164 LRGEPTPASPFTPFADVVEEYQRyraseawqrdAAFWAEQRRQLPPPaSLSPAPLPGRSASADIlRLKLEFTDgafrqLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 896 RRPSDITMSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPVAGieAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQAT 975
Cdd:PRK10252 244 AQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAAL--TATGPVLNVLPLRVHIAAQETLPELATRLAAQLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 976 EM-----IPYEQtgLHETAKVSADARHAcsFQTLLIVQPGsngDIAHDALG-EWRSH-------SDLqdftTYALMVqcv 1042
Cdd:PRK10252 322 KMrrhqrYDAEQ--IVRDSGRAAGDEPL--FGPVLNIKVF---DYQLDFPGvQAQTHtlatgpvNDL----ELALFP--- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1043 ladDE-----VQIIASFDRRAIEpwQVDKMLRQFSFVMQQLAtADAEAGIASIDTLTPEDRQQLWEWN---HDVPPAIer 1114
Cdd:PRK10252 388 ---DEhgglsIEILANPQRYDEA--TLIAHAERLKALIAQFA-ADPALLCGDVDILLPGEYAQLAQVNataVEIPETT-- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1115 cIHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLL 1194
Cdd:PRK10252 460 -LSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1195 DPSLPHERLRLMCRKVSAKLSLASEASAPLAKDlvGTVVIVNADSALQLAHHASPITSVRPTHTAYVIFTSGSTGEPKGC 1274
Cdd:PRK10252 539 DTGYPDDRLKMMLEDARPSLLITTADQLPRFAD--VPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGV 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1275 RIEHRAASSavtahgRYLGMQ------ASTRTLQFASYAFAGSLVELLMNLCHGGCIcVLSEEERRTD---LASAMCRMK 1345
Cdd:PRK10252 617 MVGQTAIVN------RLLWMQnhypltADDVVLQKTPCSFDVSVWEFFWPFIAGAKL-VMAEPEAHRDplaMQQFFAEYG 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1346 VNW---------AFLTSTVVDLLtPKSVPSLSILCVGGEPIRASQIVRWGSQVH--LRQTYGSSE----VSGIVSSAALT 1410
Cdd:PRK10252 690 VTTthfvpsmlaAFVASLTPEGA-RQSCASLRQVFCSGEALPADLCREWQQLTGapLHNLYGPTEaavdVSWYPAFGEEL 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1411 TCSTTRDV--GRA--STGVFwIVDpnNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAwraslglsAGQQR 1486
Cdd:PRK10252 769 AAVRGSSVpiGYPvwNTGLR-ILD--ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF--------APGER 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1487 LYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHqARLAEADVAEI---AVELIQ--PKDGEDGMLACFIVVED 1561
Cdd:PRK10252 838 MYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDR-AMQALPDVEQAvthACVINQaaATGGDARQLVGYLVSQS 916
|
970
....*....|....*...
gi 1779949166 1562 SASNedELSGKRTRLDTR 1579
Cdd:PRK10252 917 GLPL--DTSALQAQLRER 932
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
689-1080 |
2.15e-80 |
|
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: 271.10 E-value: 2.15e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 689 IYPCSPLQEGMMALASKRPGDYIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGML-QVVLADG---IEW 764
Cdd:cd19542 1 IYPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFlQVVLKSLdppIEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 765 EQANE--LEQYLEKDKSVSMGLGDSLARYALVRDvGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPGFNA 842
Cdd:cd19542 81 VETDEdsLDALTRDLLDDPTLFGQPPHRLTLLET-SSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 843 FIKYLGEQDHEAAAAYWQGTLADCQAISFPALPPAVQQPVADATTAFQCPAL--ARRPSDITMSTLIRAAWALLASSYTS 920
Cdd:cd19542 160 YISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTRRSLAKLeaFCASLGVTLASLFQAAWALVLARYTG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 921 SDDVVFGATVTGRNAPVAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATEMIPYEQTGLHETAKVSADARHACS 1000
Cdd:cd19542 240 SRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWPSGTL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1001 FQTLLIVQP-GSNGDIAHDALGEWRShSDLQDFTTYALMVQCVLADDEVQIIASFDRRAIEPWQVDKMLRQFSFVMQQLA 1079
Cdd:cd19542 320 FNTLVSYQNfEASPESELSGSSVFEL-SAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALL 398
|
.
gi 1779949166 1080 T 1080
Cdd:cd19542 399 A 399
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
49-548 |
2.94e-80 |
|
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: 272.42 E-value: 2.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVVSaqhsarwassschvvtlseasigqltveddlpgfsatPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCL 208
Cdd:cd17650 81 EDSGAKLLLTQ-------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 209 GHGRAFGITDQS-RVLQFTSYTFDFCMAEIITTLLYGGC-ICVPSD-RDRHSDLAKAINTMGANWALLTPSVAQLL---- 281
Cdd:cd17650 124 AWRREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTlVICPDEvKLDPAALYDLILKSRITLMESTPALIRPVmayv 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 282 --NPSDVPTLKILVIGGEQVTSKDW----NRWPTSVQLINGYGPTECCIVCTGYTTTQAFKTGT----IGTAIASVS-WV 350
Cdd:cd17650 204 yrNGLDLSAMRLLIVGSDGCKAQDFktlaARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAmYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 351 VDPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawLVDGcqgyagrrGRLYKTGDLVRYDDEGNLVCLG 430
Cdd:cd17650 284 LDERL--QPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENP--FAPG--------ERMYRTGDLARWRADGNVELLG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 431 RKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQldvktgrafptnkAAETGSLAqvifpv 510
Cdd:cd17650 352 RVDHQVKIRGFRIELGEIESQLAR-HPAIDEAV--VAVREDKGGEARLCAYVV-------------AAATLNTA------ 409
|
490 500 510
....*....|....*....|....*....|....*...
gi 1779949166 511 EAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd17650 410 ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
41-439 |
7.29e-80 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 270.34 E-value: 7.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 41 FAEQVLAQPNAPAICAWDGE-MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDH 119
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 120 PVSRHKEILRQTGARMVVVS---------AQHSARWASSSCHVVTLSEASIGQLTVEDDLPGFS-------ATPGNAAYV 183
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDdalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVpppppppPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 184 LFTSGSTGIPKGVVLEHRAVSTSCLGHG----RAFGITDQSRVLQFTSYTFDF-CMAEIITTLLYGGCICVPSDRDRHSD 258
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 259 LA--KAINTMGANWALLTPSVAQLL------NPSDVPTLKILVIGGEQVTSKDWNRWP--TSVQLINGYGPTECCIVCTG 328
Cdd:pfam00501 241 AAllELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFRelFGGALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 329 YTT--TQAFKTGTIGTAIASVSW-VVDPEDyHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpawlvdgcqgya 405
Cdd:pfam00501 321 PLPldEDLRSLGSVGRPLPGTEVkIVDDET-GEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------------ 387
|
410 420 430
....*....|....*....|....*....|....
gi 1779949166 406 grrgRLYKTGDLVRYDDEGNLVCLGRKDSQVKVR 439
Cdd:pfam00501 388 ----GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
38-548 |
9.85e-79 |
|
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: 267.88 E-value: 9.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 38 HDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDP 117
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 118 DHPVSRHKEILRQTGARMVVvsaqhsarwassschvvtlseasigqltveddlpgfsATPGNAAYVLFTSGSTGIPKGVV 197
Cdd:cd17645 81 DYPGERIAYMLADSSAKILL-------------------------------------TNPDDLAYVIYTSGSTGLPKGVM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 198 LEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVpSDRDRHSDLAKA---INTMGANWALLT 274
Cdd:cd17645 124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHV-VPSERRLDLDALndyFNQEGITISFLP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 275 PSVAQLLNPSDVPTLKILVIGGEQVTSKDWNrwptSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVSWVVDPE 354
Cdd:cd17645 203 TGAAEQFMQLDNQSLRVLLTGGDKLKKIERK----GYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 355 DyHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawLVDGcqgyagrrGRLYKTGDLVRYDDEGNLVCLGRKDS 434
Cdd:cd17645 279 A-LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHP--FVPG--------ERMYRTGDLAKFLPDGNIEFLGRLDQ 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 435 QVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFlqldvktgraFPTNKAAETGSLAQVifpveagk 514
Cdd:cd17645 348 QVKIRGYRIEPGEIEPFLMN-HPLIELAA--VLAKEDADGRKYLVAY----------VTAPEEIPHEELREW-------- 406
|
490 500 510
....*....|....*....|....*....|....
gi 1779949166 515 kLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd17645 407 -LKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
350-1540 |
1.21e-78 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 289.76 E-value: 1.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 350 VVDPEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFIEDPA--WLVDGCQGYAgRRGRLYKTGDLvryddegnlv 427
Cdd:PRK05691 383 IVDPQSLEVLGD-NRVGEIWASGPSIAHGYWRNPEASAKTFVEHDGrtWLRTGDLGFL-RDGELFVTGRL---------- 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 428 clgrKDSQVkVRGQRVELGEIEHHIQGCMPEANQ--IAVEVILLEGEKSNTIlaaflqldvktgrafptnkAAETGSLAQ 505
Cdd:PRK05691 451 ----KDMLI-VRGHNLYPQDIEKTVEREVEVVRKgrVAAFAVNHQGEEGIGI-------------------AAEISRSVQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 506 VIFPVEAGKKLAERLPSYMVPDVYFVVT-----QLPITVSGKTDRK--RLR-EIGASFSAQQLAEIRTSGQGLKRQPSTE 577
Cdd:PRK05691 507 KILPPQALIKSIRQAVAEACQEAPSVVLllnpgALPKTSSGKLQRSacRLRlADGSLDSYALFPALQAVEAAQTAASGDE 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 578 NEKALQQLWAGVLAIDadSIGLDDSFFRLGGDSIAAMKLVGEAR-RAGIHLTVADLFRNPKLEAVASLnlslgnsspeni 656
Cdd:PRK05691 587 LQARIAAIWCEQLKVE--QVAADDHFFLLGGNSIAATQVVARLRdELGIDLNLRQLFEAPTLAAFSAA------------ 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 657 VAFALLGETSDVTQIreevaASCNTNTSLiediyPCSPLQEGMMALASKRP--GDYIMQSVLALHDDTDEDRFRAAWERV 734
Cdd:PRK05691 653 VARQLAGGGAAQAAI-----ARLPRGQAL-----PQSLAQNRLWLLWQLDPqsAAYNIPGGLHLRGELDEAALRASFQRL 722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 735 VQSTAVLRTR-----------IVHSSKMGMLQVVLADGIEWEQANELEQYLEKDKSVSMGLGDS-LARYALVRdVGTGKR 802
Cdd:PRK05691 723 VERHESLRTRfyerdgvalqrIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLEKGpLLRVTLVR-LDDEEH 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 803 WMVWTLHHALYDGWSL----PQIANLVTEVYHGAEVGKQP---GFNAFI----KYLGEQDHEAAAAYWQGTLADCQaisf 871
Cdd:PRK05691 802 QLLVTLHHIVADGWSLnillDEFSRLYAAACQGQTAELAPlplGYADYGawqrQWLAQGEAARQLAYWKAQLGDEQ---- 877
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 872 PALPPAVQQPVA---DATTAFQC----PALAR------RPSDITMSTLIRAAWALLASSYTSSDDVVFGatVTGRNAPVA 938
Cdd:PRK05691 878 PVLELATDHPRSarqAHSAARYSlrvdASLSEalrglaQAHQATLFMVLLAAFQALLHRYSGQGDIRIG--VPNANRPRL 955
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 939 GIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQ-----QATEMIPYEQtgLHETAkvsADARHACSFQTLLIVQ----- 1008
Cdd:PRK05691 956 ETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQatlgaQAHQDLPFEQ--LVEAL---PQAREQGLFQVMFNHQqrdls 1030
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1009 -----PGsngdIAHDALgEWRSHS---DLQDFTTyalmvqcvlADDEVQIIASFDRRA--IEPWQVDKMLRQFSFVMQQL 1078
Cdd:PRK05691 1031 alrrlPG----LLAEEL-PWHSREakfDLQLHSE---------EDRNGRLTLSFDYAAelFDAATIERLAEHFLALLEQV 1096
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1079 AtADAEAGIASIDTLTPEDRQQLWEWNHDVPPAIERCIHDLFADQAKARPDAPAIcAWDG-DMTYGELDVLSGRLAGHLV 1157
Cdd:PRK05691 1097 C-EDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIAL-VWDGgSLDYAELHAQANRLAHYLR 1174
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1158 ELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLsLASEASAPLAKDLVGTVVIVNA 1237
Cdd:PRK05691 1175 DKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVEL-LLTQSHLLERLPQAEGVSAIAL 1253
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1238 DSaLQLAHHAS--PITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVEL 1315
Cdd:PRK05691 1254 DS-LHLDSWPSqaPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWEC 1332
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1316 LMNLChGGCICVLSEEERRTD---LASAMCRMKVNWAF----LTSTVVDLLTPKSVPSLSILCVGGEPIRAS---QIVRW 1385
Cdd:PRK05691 1333 FWPLI-TGCRLVLAGPGEHRDpqrIAELVQQYGVTTLHfvppLLQLFIDEPLAAACTSLRRLFSGGEALPAElrnRVLQR 1411
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1386 GSQVHLRQTYGSSEVSGIVSSAALTTCSTTRD-VGRASTGVFWIVDPNNHNrLAPVGAVGEVLVEGPVLGREYIDEPDKT 1464
Cdd:PRK05691 1412 LPQVQLHNRYGPTETAINVTHWQCQAEDGERSpIGRPLGNVLCRVLDAELN-LLPPGVAGELCIGGAGLARGYLGRPALT 1490
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 1465 ASTFIEAPawraslgLSAGQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhqARL-AEADVAEIAV 1540
Cdd:PRK05691 1491 AERFVPDP-------LGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQ--ARLlAQPGVAQAAV 1558
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
49-548 |
2.83e-78 |
|
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: 267.99 E-value: 2.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVVsaqHSARWASSSCHVVTLSEASIGQLTVEDDLPGFSAtPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCL 208
Cdd:cd12114 81 ADAGARLVLT---DGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVA-PDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 209 GHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPsDRDRHSD---LAKAINTMGANWALLTPSVAQLL---- 281
Cdd:cd12114 157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLP-DEARRRDpahWAELIERHGVTLWNSVPALLEMLldvl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 282 --NPSDVPTLKILVIGGeqvtskDW----------NRWPtSVQLINGYGPTEccivctgytttqafktgtigTAIASVSW 349
Cdd:cd12114 236 eaAQALLPSLRLVLLSG------DWipldlparlrALAP-DARLISLGGATE--------------------ASIWSIYH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 350 VVDPED----------------YHKLAPLGS------VGELLVEGPILARGYLNDAEKTAAAFIEDPAwlvdgcqgyagr 407
Cdd:cd12114 289 PIDEVPpdwrsipygrplanqrYRVLDPRGRdcpdwvPGELWIGGRGVALGYLGDPELTAARFVTHPD------------ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 408 RGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAVEVIlleGEKSNTILAAFLQldvk 487
Cdd:cd12114 357 GERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQA-HPGVARAVVVVL---GDPGGKRLAAFVV---- 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 488 tgrafPTNKAAETGSLAQVIFpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd12114 429 -----PDNDGTPIAPDALRAF-------LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1128-1563 |
7.84e-77 |
|
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: 262.63 E-value: 7.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMC 1207
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1208 rkvsaklslaseasaplakdlvgtvvivnADSALQLahhaspiTSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTA 1287
Cdd:cd17643 81 -----------------------------ADSGPSL-------LLTDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1288 HGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRT--DLASAMCRMKVN------WAFLTSTVVDLL 1359
Cdd:cd17643 125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSpeDFARLLRDEGVTvlnqtpSAFYQLVEAADR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1360 TPKSVPSLSILCVGGEPIRASQIVRWGSQVHLRQT-----YGSSEVSGIVS----SAALTTCSTTRDVGRASTGvfWIVD 1430
Cdd:cd17643 205 DGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRPqlvnmYGITETTVHVTfrplDAADLPAAAASPIGRPLPG--LRVY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1431 P-NNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAWRASlglsagqQRLYKTGDLARYKDDGSIELIGRKD 1509
Cdd:cd17643 283 VlDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPG-------SRMYRTGDLARRLPDGELEYLGRAD 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 1510 NQVKLRGQRIEVEEIEhqARLAE-ADVAEIAVEliqPKDGEDG--MLACFIVVEDSA 1563
Cdd:cd17643 356 EQVKIRGFRIELGEIE--AALAThPSVRDAAVI---VREDEPGdtRLVAYVVADDGA 407
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1118-1579 |
9.37e-77 |
|
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: 261.86 E-value: 9.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1118 DLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPS 1197
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1198 LPHERLRLMCRKVSAKLslaseasaplakdlvgtvvIVNADSalqlahhaspitsvrPTHTAYVIFTSGSTGEPKGCRIE 1277
Cdd:cd17653 81 LPSARIQAILRTSGATL-------------------LLTTDS---------------PDDLAYIIFTSGSTGIPKGVMVP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1278 HRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTDLASamcrmKVNWAFLTSTVVD 1357
Cdd:cd17653 127 HRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVAR-----TVDALMSTPSILS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1358 LLTPKSVPSLSILCVGGEPIRASQIVRWGSQVHLRQTYGSSEVSgIVSSAALTTCSTTRDVGRA-STGVFWIVDPNnhNR 1436
Cdd:cd17653 202 TLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECT-ISSTMTELLPGQPVTIGKPiPNSTCYILDAD--LQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1437 LAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAWRAslglsagqQRLYKTGDLARYKDDGSIELIGRKDNQVKLRG 1516
Cdd:cd17653 279 PVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPG--------SRMYRTGDYGRWTEDGGLEFLGREDNQVKVRG 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 1517 QRIEVEEIEHQARLAEADVAEIAVELIQpkdgedGMLACFIVVEDSAsnedeLSGKRTRLDTR 1579
Cdd:cd17653 351 FRINLEEIEEVVLQSQPEVTQAAAIVVN------GRLVAFVTPETVD-----VDGLRSELAKH 402
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
49-548 |
4.00e-76 |
|
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: 260.80 E-value: 4.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIG-VKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEI 127
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 128 LRQTGARMVVvsaqhsarwassschvvtlseasigqltveddlpgfsATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSC 207
Cdd:cd17648 81 LEDTGARVVI-------------------------------------TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 208 LGHGRAFGITDQS--RVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSD--LAKAINTMGANWALLTPSVAQLLNP 283
Cdd:cd17648 124 TSLSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPdrFYAYINREKVTYLSGTPSVLQQYDL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 284 SDVPTLKILVIGGEQVTSKDWN--RWPTSVQLINGYGPTECCIvctgYTTTQAFKTG-----TIGTAIASVSWVVDPEDY 356
Cdd:cd17648 204 ARLPHLKRVDAAGEEFTAPVFEklRSRFAGLIINAYGPTETTV----TNHKRFFPGDqrfdkSLGRPVRNTKCYVLNDAM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 357 hKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawLVDGCQGYAGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQV 436
Cdd:cd17648 280 -KRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNP--FQTEQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 437 KVRGQRVELGEIEHHIQGC--MPEANQIAVEVILLEGEKSNTILAAFLQLdvktgrafptnkaaETGSL-AQVIFpveag 513
Cdd:cd17648 357 KIRGQRIEPGEVEAALASYpgVRECAVVAKEDASQAQSRIQKYLVGYYLP--------------EPGHVpESDLL----- 417
|
490 500 510
....*....|....*....|....*....|....*
gi 1779949166 514 KKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd17648 418 SFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1119-1595 |
8.52e-75 |
|
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: 258.03 E-value: 8.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1119 LFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSL 1198
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1199 PHERLRLMCRKVSAKLSLASEASAPLAKDLvGTVVIVNADS-----ALQLAHhaspitSVRPTHTAYVIFTSGSTGEPKG 1273
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFI-GLIDLLDEDTiyheeSENLEP------VSKSDDLAYVIYTSGSTGKPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1274 CRIEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERR--TDLASAMCRMKVNWAFL 1351
Cdd:cd17655 155 VMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLdgQALTQYIRQNRITIIDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1352 TSTVVDLLTP---KSVPSLSILCVGGEPIRASQIVRWGSQVHLRQT----YGSSEV-----SGIVSSAALTTCSTTrdVG 1419
Cdd:cd17655 235 TPAHLKLLDAaddSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTitnaYGPTETtvdasIYQYEPETDQQVSVP--IG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1420 RASTGV-FWIVDPNnhNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGqQRLYKTGDLARYKD 1498
Cdd:cd17655 313 KPLGNTrIYILDQY--GRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDP-------FVPG-ERMYRTGDLARWLP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1499 DGSIELIGRKDNQVKLRGQRIEVEEIEHQARLAEaDVAEIAVeLIQPKDGEDGMLACFIVVEDSASNEDelsgkrtrldt 1578
Cdd:cd17655 383 DGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHP-DIKEAVV-IARKDEQGQNYLCAYIVSEKELPVAQ----------- 449
|
490
....*....|....*..
gi 1779949166 1579 rtqrtigkIQDRLERDL 1595
Cdd:cd17655 450 --------LREFLAREL 458
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1120-1515 |
6.80e-73 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 250.31 E-value: 6.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1120 FADQAKARPDAPAICAWDGD-MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSL 1198
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1199 PHERLRLMCRKVSAKLSLASEA-------SAPLAKDLVGTVVIVNADSALQLAH----------HASPITSVRPTHTAYV 1261
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDAlkleellEALGKLEVVKLVLVLDRDPVLKEEPlpeeakpadvPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1262 IFTSGSTGEPKGCRIEHRAASSAVTAHGRY----LGMQASTRTLQFASYAFAGSLV-ELLMNLCHGGCICVLSEEERRTD 1336
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1337 LAS--AMCRMKVNWAFLTSTVVDLLT------PKSVPSLSILCVGGEPIRASqIVRWGSQV---HLRQTYGSSEVSGIVS 1405
Cdd:pfam00501 241 AALleLIERYKVTVLYGVPTLLNMLLeagapkRALLSSLRLVLSGGAPLPPE-LARRFRELfggALVNGYGLTETTGVVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1406 SAALTTCSTTRD--VGRASTGV-FWIVDPnNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapawraslglsa 1482
Cdd:pfam00501 320 TPLPLDEDLRSLgsVGRPLPGTeVKIVDD-ETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------------ 386
|
410 420 430
....*....|....*....|....*....|...
gi 1779949166 1483 gqQRLYKTGDLARYKDDGSIELIGRKDNQVKLR 1515
Cdd:pfam00501 387 --DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
686-1569 |
2.68e-72 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 269.35 E-value: 2.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 686 IEDIYPCSPLQEGMMALASKRPGD--YIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGMLQVVLADG-- 761
Cdd:PRK05691 3254 IEDVYPLTPMQEGLLLHTLLEPGTglYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGrt 3333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 762 ----IEW------EQANELEQYLEKDKSVsmglGDSLARYA-----LVRdVGTGKRWMVWTLHHALYDGWSLPQIANLVT 826
Cdd:PRK05691 3334 pidyLDWrglpedGQEQRLQALHKQEREA----GFDLLNQPpfhlrLIR-VDEARYWFMMSNHHILIDAWCRSLLMNDFF 3408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 827 EVYHGAEVGKQ------PGFNAFIKYLGEQDHEAAAAYWQGTLADCQ-AISFPALPPAVQQPVA--------------DA 885
Cdd:PRK05691 3409 EIYTALGEGREaqlpvpPRYRDYIGWLQRQDLAQARQWWQDNLRGFErPTPIPSDRPFLREHAGdsggmvvgdcytrlDA 3488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 886 TTAFQCPALARRpSDITMSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPVAGIEAMAGPTIATVPVRVRVQHSHK--- 962
Cdd:PRK05691 3489 ADGARLRELAQA-HQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLPAAGQrcs 3567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 963 VSEFLHSVQQQATEMIPYEQTGLHETAKVSADARHACSFQTLLIVQpgsNGDIAHDALGEWRSHSDLQD----FTTYALM 1038
Cdd:PRK05691 3568 VRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGQPLFDSLFVFE---NAPVEVSVLDRAQSLNASSDsgrtHTNFPLT 3644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1039 VQCVLADDeVQIIASFDRRAIEPWQVDKMLRQFSFVMqqLATADAEAG-IASIDTLTPEDRQQLWE----WNHDVPpaIE 1113
Cdd:PRK05691 3645 AVCYPGDD-LGLHLSYDQRYFDAPTVERLLGEFKRLL--LALVQGFHGdLSELPLLGEQERDFLLDgcnrSERDYP--LE 3719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1114 RCIHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLL 1193
Cdd:PRK05691 3720 QSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLP 3799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1194 LDPSLPHERLRLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSAL--------QLAHHASPITSVrPTHTAYVIFTS 1265
Cdd:PRK05691 3800 LDPGLPAQRLQRIIELSRTPVLVCSAACREQARALLDELGCANRPRLLvweevqagEVASHNPGIYSG-PDNLAYVIYTS 3878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1266 GSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFASYAFA------------GSLVELLMNLC--HGGCICVLSEE 1331
Cdd:PRK05691 3879 GSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDisvwqflaaplfGARVEIVPNAIahDPQGLLAHVQA 3958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1332 ERRTDLASamcrmkvnwafLTSTVVDLLTPKSVP--SLSILCVGGE---PIRASQIVRWGSQVHLRQTYGSSEVSGIVSS 1406
Cdd:PRK05691 3959 QGITVLES-----------VPSLIQGMLAEDRQAldGLRWMLPTGEampPELARQWLQRYPQIGLVNAYGPAECSDDVAF 4027
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1407 AALTTCSTtrdvgrasTGVFW-IVDPNNHNR---------LAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawra 1476
Cdd:PRK05691 4028 FRVDLAST--------RGSYLpIGSPTDNNRlylldealeLVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHP---- 4095
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1477 slgLSAGQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhqARLAE-ADVAEIAVeLIQpkDGEDG-MLA 1554
Cdd:PRK05691 4096 ---FGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIE--ARLHEqAEVREAAV-AVQ--EGVNGkHLV 4167
|
970
....*....|....*
gi 1779949166 1555 CFIVVEDSASNEDEL 1569
Cdd:PRK05691 4168 GYLVPHQTVLAQGAL 4182
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1116-1579 |
2.98e-71 |
|
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: 246.46 E-value: 2.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLD 1195
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1196 PSLPHERLRLMcrkvsaklslaseasaplakdlvgtvvivnadsalqLAHHASPITSVRPTHTAYVIFTSGSTGEPKGCR 1275
Cdd:cd12115 81 PAYPPERLRFI------------------------------------LEDAQARLVLTDPDDLAYVIYTSGSTGRPKGVA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1276 IEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTDLASAMCRMKVNwaFLTSTV 1355
Cdd:cd12115 125 IEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAAEVTLIN--TVPSAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1356 VDLLTPKSVP-SLSILCVGGEPIRAS---QIVRWGSQVHLRQTYGSSEVSGIVSSAALTT-CSTTRDVGR--ASTGVfWI 1428
Cdd:cd12115 203 AELLRHDALPaSVRVVNLAGEPLPRDlvqRLYARLQVERVVNLYGPSEDTTYSTVAPVPPgASGEVSIGRplANTQA-YV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1429 VDpnNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslglSAGQQRLYKTGDLARYKDDGSIELIGRK 1508
Cdd:cd12115 282 LD--RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDP--------FGPGARLYRTGDLVRWRPDGLLEFLGRA 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 1509 DNQVKLRGQRIEVEEIEHQARLAEAdVAEIAVELIQPKDGEDgMLACFIVVE-DSASNEDELsgkRTRLDTR 1579
Cdd:cd12115 352 DNQVKVRGFRIELGEIEAALRSIPG-VREAVVVAIGDAAGER-RLVAYIVAEpGAAGLVEDL---RRHLGTR 418
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
49-548 |
1.14e-70 |
|
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: 245.85 E-value: 1.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVVSAQHSARWASSSCHVV----TLSEASIGQLTV---EDDLpgfsatpgnaAYVLFTSGSTGIPKGVVLEHR 201
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSFNKSTILledpSISQEDTSNIDYinnSDDL----------LYIIYTSGTTGKPKGVQLEHK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 202 AVsTSCLGHGRAF-GITDQSRVLQFTSYTFDFCMAEIITTLLYGGCI-CVPSDRDRHSD-LAKAINTMGANWALLTPSVA 278
Cdd:cd17656 152 NM-VNLLHFEREKtNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyIIREETKRDVEqLFDLVKRHNIEVVFLPVAFL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 279 QLLNP-----SDVPT-LKILVIGGEQ-VTSKDWNRWPTS--VQLINGYGPTECCIVcTGYTTTQAFKTGT---IGTAIAS 346
Cdd:cd17656 231 KFIFSerefiNRFPTcVKHIITAGEQlVITNEFKEMLHEhnVHLHNHYGPSETHVV-TTYTINPEAEIPElppIGKPISN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 347 VsWVVDPEDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgyAGRRGRLYKTGDLVRYDDEGNL 426
Cdd:cd17656 310 T-WIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDP----------FDPNERMYRTGDLARYLPDGNI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 427 VCLGRKDSQVKVRGQRVELGEIEHHIQGCmPEANQiAVEVILLEGEKSNTILAAFLQLdvktgrafptnkaaetgslaQV 506
Cdd:cd17656 379 EFLGRADHQVKIRGYRIELGEIEAQLLNH-PGVSE-AVVLDKADDKGEKYLCAYFVME--------------------QE 436
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1779949166 507 IFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd17656 437 LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1115-1565 |
1.46e-69 |
|
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: 242.34 E-value: 1.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1115 CIHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLL 1194
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1195 DPSLPHERLRLMcrkvsaklslaseasaplAKDLVGTVVIVNadsalqlahhaspitsvrPTHTAYVIFTSGSTGEPKGC 1274
Cdd:cd17644 81 DPNYPQERLTYI------------------LEDAQISVLLTQ------------------PENLAYVIYTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1275 RIEHRA-ASSAVTAHGRYlGMQASTRTLQFASYAFAGSLVELLMNLCHGGCIcVLSEEERRTDLAS--AMCRMK------ 1345
Cdd:cd17644 125 MIEHQSlVNLSHGLIKEY-GITSSDRVLQFASIAFDVAAEEIYVTLLSGATL-VLRPEEMRSSLEDfvQYIQQWqltvls 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1346 ---VNWAFLTSTVVDLLTPkSVPSLSILCVGGEPIRASQIVRW----GSQVHLRQTYGSSEvsgivSSAALTTCSTTRDV 1418
Cdd:cd17644 203 lppAYWHLLVLELLLSTID-LPSSLRLVIVGGEAVQPELVRQWqknvGNFIQLINVYGPTE-----ATIAATVCRLTQLT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1419 GRASTGV----------FWIVDPNNhnRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAWraslglSAGQQRLY 1488
Cdd:cd17644 277 ERNITSVpigrpiantqVYILDENL--QPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFN------SSESERLY 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 1489 KTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhqARLAEADVAEIAVELIQPKDGEDGMLACFIVVEDSASN 1565
Cdd:cd17644 349 KTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIE--AVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESP 423
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1128-1569 |
3.10e-67 |
|
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: 234.67 E-value: 3.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMC 1207
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1208 RKVSAKLSLaseasaplakdlvgtvvivnadsalqlahhaspitsVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTA 1287
Cdd:cd17650 81 EDSGAKLLL------------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1288 HGRYLGMQA-STRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEER--RTDLASAMCRMKVNWAFLTST----VVDLLT 1360
Cdd:cd17650 125 WRREYELDSfPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKldPAALYDLILKSRITLMESTPAlirpVMAYVY 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1361 PKSV--PSLSILCVGGEPIRASQIV----RWGSQVHLRQTYGSSEV---SGIVSSAALTTC-STTRDVGRASTGV-FWIV 1429
Cdd:cd17650 205 RNGLdlSAMRLLIVGSDGCKAQDFKtlaaRFGQGMRIINSYGVTEAtidSTYYEEGRDPLGdSANVPIGRPLPNTaMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1430 DPnnHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslgLSAGQqRLYKTGDLARYKDDGSIELIGRKD 1509
Cdd:cd17650 285 DE--RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENP-------FAPGE-RMYRTGDLARWRADGNVELLGRVD 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 1510 NQVKLRGQRIEVEEIEHQarLAEAD-VAEIAVELIQPKDGEDGMlaCFIVVEDSASNEDEL 1569
Cdd:cd17650 355 HQVKIRGFRIELGEIESQ--LARHPaIDEAVVAVREDKGGEARL--CAYVVAAATLNTAEL 411
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1116-1569 |
8.26e-66 |
|
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: 230.85 E-value: 8.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLD 1195
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1196 PSLPHERLRLMCRKVSAKlslaseasaplakdlvgtVVIvnadsalqlahhaspitsvrpthTAYVIFTSGSTGEPKGCR 1275
Cdd:COG0318 81 PRLTAEELAYILEDSGAR------------------ALV-----------------------TALILYTSGTTGRPKGVM 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1276 IEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSL-VELLMNLCHGGCIcVLSEEERRTDLASAMCRMKVNWAFLTST 1354
Cdd:COG0318 120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPLLAGATL-VLLPRFDPERVLELIERERVTVLFGVPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1355 VVDLL------TPKSVPSLSILCVGGEPIRASQIVRWGS--QVHLRQTYGSSEVSGIVSSAALTTCSTTRD-VGRASTGV 1425
Cdd:COG0318 199 MLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFEErfGVRIVEGYGLTETSPVVTVNPEDPGERRPGsVGRPLPGV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1426 -FWIVDPNnhNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFieAPAWraslglsagqqrlYKTGDLARYKDDGSIEL 1504
Cdd:COG0318 279 eVRIVDED--GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF--RDGW-------------LRTGDLGRLDEDGYLYI 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 1505 IGRKDNQVKLRGQRIEVEEIEhqARLAEA-DVAEIAVELIQ-PKDGEDGMlACFIVVEDSASNEDEL 1569
Cdd:COG0318 342 VGRKKDMIISGGENVYPAEVE--EVLAAHpGVAEAAVVGVPdEKWGERVV-AFVVLRPGAELDAEEL 405
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1117-1566 |
5.79e-65 |
|
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: 227.82 E-value: 5.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1117 HDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDP 1196
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1197 SLPHERLRLMCRKVSAKLSLASeasaplAKDLvgtvvivnadsalqlahhaspitsvrpthtAYVIFTSGSTGEPKGCRI 1276
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTN------PDDL------------------------------AYVIYTSGSTGLPKGVMI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1277 EHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLsEEERRTDLA--SAMCRMK-VNWAFLTS 1353
Cdd:cd17645 125 EHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVV-PSERRLDLDalNDYFNQEgITISFLPT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1354 TVVDLLTPKSVPSLSILCVGGEPIRasQIVRWGSQvhLRQTYGSSEVSGIVSSAALTTCSTTRDVGRA--STGVFWIvdp 1431
Cdd:cd17645 204 GAAEQFMQLDNQSLRVLLTGGDKLK--KIERKGYK--LVNNYGPTENTVVATSFEIDKPYANIPIGKPidNTRVYIL--- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1432 NNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAWRAslglsagqQRLYKTGDLARYKDDGSIELIGRKDNQ 1511
Cdd:cd17645 277 DEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPG--------ERMYRTGDLAKFLPDGNIEFLGRLDQQ 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1779949166 1512 VKLRGQRIEVEEIEHQArLAEADVAEIAVELIQPKDGeDGMLACFIVVEDSASNE 1566
Cdd:cd17645 349 VKIRGYRIEPGEIEPFL-MNHPLIELAAVLAKEDADG-RKYLVAYVTAPEEIPHE 401
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1128-1560 |
2.48e-62 |
|
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: 221.58 E-value: 2.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMC 1207
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1208 RKVSAKLSLaSEASAPLAKDLVGTVVIVNADSALQLAhhASPITSVRPT-HTAYVIFTSGSTGEPKGCRIEHRAASSAVT 1286
Cdd:cd17656 82 LDSGVRVVL-TQRHLKSKLSFNKSTILLEDPSISQED--TSNIDYINNSdDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1287 AHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRT--DLASAMCRMKVNWAFLTSTVVDLL----- 1359
Cdd:cd17656 159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDveQLFDLVKRHNIEVVFLPVAFLKFIfsere 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1360 -TPKSVPSLSILCVGGEPIRASQIVR---WGSQVHLRQTYGSSEvsgivsSAALTTCSTTRD--------VGRASTGVfW 1427
Cdd:cd17656 239 fINRFPTCVKHIITAGEQLVITNEFKemlHEHNVHLHNHYGPSE------THVVTTYTINPEaeipelppIGKPISNT-W 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1428 IVDPNNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPaWRASlglsagqQRLYKTGDLARYKDDGSIELIGR 1507
Cdd:cd17656 312 IYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDP-FDPN-------ERMYRTGDLARYLPDGNIEFLGR 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 1508 KDNQVKLRGQRIEVEEIEHQArLAEADVAEIAVELIQPKDGEDGMLACFIVVE 1560
Cdd:cd17656 384 ADHQVKIRGYRIELGEIEAQL-LNHPGVSEAVVLDKADDKGEKYLCAYFVMEQ 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
40-652 |
3.77e-61 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 233.14 E-value: 3.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 40 LFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDH 119
Cdd:PRK05691 3725 LFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGL 3804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 120 PVSRHKEILRQTGARMVVVSAQHSARwasSSCHVVTLSEASIGQLTVEDDL---------PGFSATPGNAAYVLFTSGST 190
Cdd:PRK05691 3805 PAQRLQRIIELSRTPVLVCSAACREQ---ARALLDELGCANRPRLLVWEEVqagevashnPGIYSGPDNLAYVIYTSGST 3881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 191 GIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCI-CVPSD--RDRHSDLAKAINTmG 267
Cdd:PRK05691 3882 GLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVeIVPNAiaHDPQGLLAHVQAQ-G 3960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 268 ANWALLTPSVAQLLNPSD---VPTLKILVIGGEQVT---SKDW-NRWPtSVQLINGYGPTECCIVCTGYTTTQAFKTGT- 339
Cdd:PRK05691 3961 ITVLESVPSLIQGMLAEDrqaLDGLRWMLPTGEAMPpelARQWlQRYP-QIGLVNAYGPAECSDDVAFFRVDLASTRGSy 4039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 340 --IGTAIASVSWVVDPEDYhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgYAGRRGRLYKTGDL 417
Cdd:PRK05691 4040 lpIGSPTDNNRLYLLDEAL-ELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHP---------FGAPGERLYRTGDL 4109
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 418 VRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAVEVIllEGeKSNTILAAFLqldvktgraFPTNKA 497
Cdd:PRK05691 4110 ARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE-QAEVREAAVAVQ--EG-VNGKHLVGYL---------VPHQTV 4176
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 498 AETGSLAQvifpvEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR--EIGASFSAQQLAeirtsgqglkrqPS 575
Cdd:PRK05691 4177 LAQGALLE-----RIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPalDIGQLQSQAYLA------------PR 4239
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 576 TENEKALQQLWAGVLAIdaDSIGLDDSFFRLGGDSIAAMKLVGEARRAgIHLTVA--DLFRNPKLEAVASLNLSLGNSS 652
Cdd:PRK05691 4240 NELEQTLATIWADVLKV--ERVGVHDNFFELGGHSLLATQIASRVQKA-LQRNVPlrAMFECSTVEELAEYIEGLAGSA 4315
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1128-1564 |
8.80e-61 |
|
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: 217.14 E-value: 8.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMC 1207
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1208 RKVSAKLSLASEASAPLAkDLVGTVVIVNADsaLQLAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTA 1287
Cdd:cd12114 81 ADAGARLVLTDGPDAQLD-VAVFDVLILDLD--ALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1288 HGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCIcVLSEEERRTD---LASAMCRMKVN-WAFLTStVVDLL---- 1359
Cdd:cd12114 158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATL-VLPDEARRRDpahWAELIERHGVTlWNSVPA-LLEMLldvl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1360 --TPKSVPSLSILCVGGEPIRASQIVRW---GSQVHLRQTYGSSEVSgiVSSAALTTCSTTRDV-----GRASTG-VFWI 1428
Cdd:cd12114 236 eaAQALLPSLRLVLLSGDWIPLDLPARLralAPDARLISLGGATEAS--IWSIYHPIDEVPPDWrsipyGRPLANqRYRV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1429 VDPnnHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAWRaslglsagqqRLYKTGDLARYKDDGSIELIGRK 1508
Cdd:cd12114 314 LDP--RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPDGE----------RLYRTGDLGRYRPDGTLEFLGRR 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1779949166 1509 DNQVKLRGQRIEVEEIEHQArLAEADVAEIAVelIQPKDGEDGMLACFIVVEDSAS 1564
Cdd:cd12114 382 DGQVKVRGYRIELGEIEAAL-QAHPGVARAVV--VVLGDPGGKRLAAFVVPDNDGT 434
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1128-1576 |
4.19e-60 |
|
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: 214.19 E-value: 4.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVG-PEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLM 1206
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1207 CRKVSAKLSLASeasaplakdlvgtvvivnadsalqlahhaspitsvrPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVT 1286
Cdd:cd17648 81 LEDTGARVVITN------------------------------------STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1287 A-HGRYLGMQAST-RTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTD--LASAMCRMKVNWAFLTSTVVDLLTPK 1362
Cdd:cd17648 125 SlSERYFGRDNGDeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPdrFYAYINREKVTYLSGTPSVLQQYDLA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1363 SVPSLSILCVGGEPIRASQIVRwgsqvhLRQT--------YGSSEVS-GIVSSAALTTCSTTRDVGRASTGVFWIVDPNN 1433
Cdd:cd17648 205 RLPHLKRVDAAGEEFTAPVFEK------LRSRfagliinaYGPTETTvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1434 HNRLaPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAWRASLGLSAGQQRLYKTGDLARYKDDGSIELIGRKDNQVK 1513
Cdd:cd17648 279 MKRV-PVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVK 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 1514 LRGQRIEVEEIEhqARLAE-ADVAEIAV----ELIQPKDGEDGMLACFIVVEDSASNE-DELSGKRTRL 1576
Cdd:cd17648 358 IRGQRIEPGEVE--AALASyPGVRECAVvakeDASQAQSRIQKYLVGYYLPEPGHVPEsDLLSFLRAKL 424
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1124-1563 |
2.36e-59 |
|
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: 211.72 E-value: 2.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERL 1203
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1204 RLMCrkvsaklslasEASAPlakdlvgTVVIVNADSalqlahhaspitsvrpthTAYVIFTSGSTGEPKGCRIEHRAASS 1283
Cdd:cd05945 81 REIL-----------DAAKP-------ALLIADGDD------------------NAYIIFTSGSTGRPKGVQISHDNLVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1284 AVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERR--TDLASAMCRMKVNWAFLTSTVVDL--- 1358
Cdd:cd05945 125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATAdpKQLFRFLAEHGITVWVSTPSFAAMcll 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1359 ---LTPKSVPSL--SILCvgGEPIRASQIVRWGS---QVHLRQTYGSSE----VSGIVSSAALTTCSTTRDVGRASTGV- 1425
Cdd:cd05945 205 sptFTPESLPSLrhFLFC--GEVLPHKTARALQQrfpDARIYNTYGPTEatvaVTYIEVTPEVLDGYDRLPIGYAKPGAk 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1426 FWIVDPNNhnRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAWRAslglsagqqrlYKTGDLARYKDDGSIELI 1505
Cdd:cd05945 283 LVILDEDG--RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRA-----------YRTGDLVRLEADGLLFYR 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 1506 GRKDNQVKLRGQRIEVEEIEHQARLAEAdVAEIAVELIQPKDGEDGMLAcFIVVEDSA 1563
Cdd:cd05945 350 GRLDFQVKLNGYRIELEEIEAALRQVPG-VKEAVVVPKYKGEKVTELIA-FVVPKPGA 405
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
36-643 |
3.11e-59 |
|
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: 225.33 E-value: 3.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 36 CIHDLFAEQVLAQPNAPAIC----AWDG-----EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVL 106
Cdd:TIGR03443 237 AIHDIFADNAEKHPDRTCVVetpsFLDPssktrSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 107 KAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSA------QHSARWASSSCHVVTLseasIGQLTVEDD--LPGfSATPG 178
Cdd:TIGR03443 317 KAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEkagtldQLVRDYIDKELELRTE----IPALALQDDgsLVG-GSLEG 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 179 NAAYVL------------------------FTSGSTGIPKGVVLEHRAvstscLGH-----GRAFGITDQSRVLQFTSYT 229
Cdd:TIGR03443 392 GETDVLapyqalkdtptgvvvgpdsnptlsFTSGSEGIPKGVLGRHFS-----LAYyfpwmAKRFGLSENDKFTMLSGIA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 230 FDFCMAEIITTLLYGGCICVPSDRD--RHSDLAKAINTMGANWALLTPSVAQLLNP---SDVPTLKILVIGGEQVTSKDW 304
Cdd:TIGR03443 467 HDPIQRDMFTPLFLGAQLLVPTADDigTPGRLAEWMAKYGATVTHLTPAMGQLLSAqatTPIPSLHHAFFVGDILTKRDC 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 305 NRWPT---SVQLINGYGPTEC-----CIVCTGYTTTQAF--KTGTI---GTAIASVSW-VVDPEDYHKLAPLGSVGELLV 370
Cdd:TIGR03443 547 LRLQTlaeNVCIVNMYGTTETqravsYFEIPSRSSDSTFlkNLKDVmpaGKGMKNVQLlVVNRNDRTQTCGVGEVGEIYV 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 371 EGPILARGYLNDAEKTAAAFIedPAWLVD--------------GCQGYAGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQV 436
Cdd:TIGR03443 627 RAGGLAEGYLGLPELNAEKFV--NNWFVDpshwidldkennkpEREFWLGPRDRLYRTGDLGRYLPDGNVECCGRADDQV 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 437 KVRGQRVELGEIEHHI-QGCMPEANqiaveVILLEGEKSN--TILAAFL-QLDVKTGRAFPTNKAAETGSlAQVIFPVEA 512
Cdd:TIGR03443 705 KIRGFRIELGEIDTHLsQHPLVREN-----VTLVRRDKDEepTLVSYIVpQDKSDELEEFKSEVDDEESS-DPVVKGLIK 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 513 GKKLAE--------RLPSYMVPDVYFVVTQLPITVSGKTDRKRLreigaSF--SAQQLAEIRTSGQGLKRQPSTENEKAL 582
Cdd:TIGR03443 779 YRKLIKdireylkkKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL-----PFpdTAQLAAVAKNRSASAADEEFTETEREI 853
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 583 QQLWAGVLAIDADSIGLDDSFFRLGGDSIAAMKLVGEARRA-GIHLTVADLFRNPKLEAVAS 643
Cdd:TIGR03443 854 RDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKlNVELPLGLIFKSPTIKGFAK 915
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
181-544 |
3.07e-54 |
|
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: 193.27 E-value: 3.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 181 AYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHsDLA 260
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE-AAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 261 KAINTMGANWALLTPSVAQLL------NPSDVPTLKILVIGGEQVTSKDWNRWP--TSVQLINGYGPTECCIVCTGYT-T 331
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARLlkapesAGYDLSSLRALVSGGAPLPPELLERFEeaPGIKLVNGYGLTETGGTVATGPpD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 332 TQAFKTGTIGTAIASVSW-VVDPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEdpawlvdgcqGYagrrgr 410
Cdd:cd04433 162 DDARKPGSVGRPVPGVEVrIVDPDG--GELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED----------GW------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 411 lYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCmPEANQIAveVILLEGEKSNTILAAFLQLdvktgr 490
Cdd:cd04433 224 -YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGH-PGVAEAA--VVGVPDPEWGERVVAVVVL------ 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 491 afptnKAAETGSLAQVIfpveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTD 544
Cdd:cd04433 294 -----RPGADLDAEELR------AHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
39-548 |
8.87e-53 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 194.34 E-value: 8.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 39 DLFAEQvlaQPNAPAICAWDGEMSYSVLDGLSTKLAGYLvkIGVKPGDVVPLCF--EKSMWTVVAMLAVLKAGGAFAPLD 116
Cdd:PRK04813 9 EEFAQT---QPDFPAYDYLGEKLTYGQLKEDSDALAAFI--DSLKLPDKSPIIVfgHMSPEMLATFLGAVKAGHAYIPVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 117 PDHPVSRHKEILRQTGARMVVvsAQHSARWASSSCHVVTLSEasigqltVEDD-LPGFSATPGNA------AYVLFTSGS 189
Cdd:PRK04813 84 VSSPAERIEMIIEVAKPSLII--ATEELPLEILGIPVITLDE-------LKDIfATGNPYDFDHAvkgddnYYIIFTSGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 190 TGIPKGVVLEHR--------AVStsclghgrAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGC-ICVPSDR-DRHSDL 259
Cdd:PRK04813 155 TGKPKGVQISHDnlvsftnwMLE--------DFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTlVALPKDMtANFKQL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 260 AKAINTMGANWALLTPSVAQ--LLNPS----DVPTLKILVIGGE----QVTSKDWNRWPTSVqLINGYGPTECCIVCTGY 329
Cdd:PRK04813 227 FETLPQLPINVWVSTPSFADmcLLDPSfneeHLPNLTHFLFCGEelphKTAKKLLERFPSAT-IYNTYGPTEATVAVTSI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 330 TTTQ----AFKTGTIGTAIASVSWVVDPEDYHKLaPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpawlvdgcQGYa 405
Cdd:PRK04813 306 EITDemldQYKRLPIGYAKPDSPLLIIDEEGTKL-PDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF--------DGQ- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 406 grrgRLYKTGDLVRYDDeGNLVCLGRKDSQVKVRGQRVELGEIEHHIQgcmpeanqiavevillegeKSNtilaaflqlD 485
Cdd:PRK04813 376 ----PAYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNLR-------------------QSS---------Y 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1779949166 486 VKTGRAFPTNKAAETGSLAQVIFPVEAG------------KKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:PRK04813 423 VESAVVVPYNKDHKVQYLIAYVVPKEEDferefeltkaikKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
689-1082 |
1.54e-50 |
|
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: 185.34 E-value: 1.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 689 IYPCSPLQEGMMALASKRPGD--YIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGMLQVVLADGI-EW- 764
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGsvYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQvPVt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 765 --------EQANELEQYLEKDKSVSMGL-GDSLARYALVRDVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVG 835
Cdd:cd19536 81 eldltpleEQLDPLRAYKEETKIRRFDLgRAPLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 836 KQ------PGFNAFIKYLGEQ-DHEAAAAYWQGTLADCQAISFPALPPAVQQ-PVADATTAFQCPALAR-----RPSDIT 902
Cdd:cd19536 161 KPlslppaQPYRDFVAHERASiQQAASERYWREYLAGATLATLPALSEAVGGgPEQDSELLVSVPLPVRsrslaKRSGIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 903 MSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPVAGIEAMAGPTIATVPVRVRVQhSHKVSEFLHSVQQQATEMIPYEQ 982
Cdd:cd19536 241 LSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLS-EETVEDLLKRAQEQELESLSHEQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 983 tglHETAKVSADARHACSFQTLLIVQpgsNGDIAhDALGEW-RSHSDLQDF------TTYA--LMVQCVLADDEVQIIAS 1053
Cdd:cd19536 320 ---VPLADIQRCSEGEPLFDSIVNFR---HFDLD-FGLPEWgSDEGMRRGLlfsefkSNYDvnLSVLPKQDRLELKLAYN 392
|
410 420
....*....|....*....|....*....
gi 1779949166 1054 FdrRAIEPWQVDKMLRQFSFVMQQLATAD 1082
Cdd:cd19536 393 S--QVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
39-549 |
2.11e-49 |
|
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: 183.53 E-value: 2.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 39 DLFAEQVLAQPNAPAiCAWDGE-MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDP 117
Cdd:cd05936 3 DLLEEAARRFPDKTA-LIFMGRkLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 118 DHPVSRHKEILRQTGARMVVVsaqhsarwassschVVTLSEAsIGQLTVEDDLPGfsATPGNAAYVLFTSGSTGIPKGVV 197
Cdd:cd05936 82 LYTPRELEHILNDSGAKALIV--------------AVSFTDL-LAAGAPLGERVA--LTPEDVAVLQYTSGTTGVPKGAM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 198 LEHR---AVSTSCLGHGrAFGITDQSRVLQ----FTSYTFDFCMaeiITTLLYGGCIC-VPSDRDRH--SDLAK------ 261
Cdd:cd05936 145 LTHRnlvANALQIKAWL-EDLLEGDDVVLAalplFHVFGLTVAL---LLPLALGATIVlIPRFRPIGvlKEIRKhrvtif 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 262 -AINTMgaNWALLTPSVAQLLNPSdvpTLKILVIGGEQVTSKDWNRWP--TSVQLINGYGPTECCIVCTGYTTTQAFKTG 338
Cdd:cd05936 221 pGVPTM--YIALLNAPEFKKRDFS---SLRLCISGGAPLPVEVAERFEelTGVPIVEGYGLTETSPVVAVNPLDGPRKPG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 339 TIGTAIASVSW-VVDPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpaWLvdgcqgyagrrgrlyKTGDL 417
Cdd:cd05936 296 SIGIPLPGTEVkIVDDDG--EELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG--WL---------------RTGDI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 418 VRYDDEGNLVCLGRKDSQVKVRGQRVELGEIE----HHiqgcmPEANQIAveVILLEGEKSNTILAAFLQLdvktgrafp 493
Cdd:cd05936 357 GYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEevlyEH-----PAVAEAA--VVGVPDPYSGEAVKAFVVL--------- 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1779949166 494 tnKAAETGSLAQVIfpveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd05936 421 --KEGASLTEEEII------AFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
686-1101 |
7.58e-45 |
|
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: 169.44 E-value: 7.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 686 IEDIYPCSPLQEGMMALA--SKRPGDYIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGMLQVVL----- 758
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEklEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILeerpf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 759 ---------ADGIEWEQAneLEQYLEKDKSVSMGL-GDSLARYALVRdVGTGKRWMVWTLHHALYDGWSLPQIANLVTEV 828
Cdd:pfam00668 81 eleiidisdLSESEEEEA--IEAFIQRDLQSPFDLeKGPLFRAGLFR-IAENRHHLLLSMHHIIVDGVSLGILLRDLADL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 829 YHGAEVGKQ------PGFNAFIK----YLGEQDHEAAAAYWQGTLA-DCQAISFP--ALPPAVQQPVADaTTAFQCPA-- 893
Cdd:pfam00668 158 YQQLLKGEPlplppkTPYKDYAEwlqqYLQSEDYQKDAAYWLEQLEgELPVLQLPkdYARPADRSFKGD-RLSFTLDEdt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 894 -----LARRPSDITMSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPvaGIEAMAGPTIATVPVRVRVQHSHKVSEFLH 968
Cdd:pfam00668 237 eellrKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTFSELIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 969 SVQQQATEMIPYEQTGLHETAKVSA---DARHACSFQTLLIVQ--PG----------SNGDIAHDALGEWRSHSDLqdft 1033
Cdd:pfam00668 315 RVQEDLLSAEPHQGYPFGDLVNDLRlprDLSRHPLFDPMFSFQnyLGqdsqeeefqlSELDLSVSSVIEEEAKYDL---- 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 1034 tyALMVQCVLADDEVQIIAS---FDRRAIEPWQvdkmlRQFSFVMQQLAtADAEAGIASIDTLTPEDRQQL 1101
Cdd:pfam00668 391 --SLTASERGGGLTIKIDYNtslFDEETIERFA-----EHFKELLEQAI-AHPSQPLSELDLLSDAEKQKL 453
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
60-548 |
8.87e-45 |
|
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: 171.16 E-value: 8.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 60 EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVs 139
Cdd:cd17647 20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 140 aqhsarwassschvvtLSEAsiGQLTVEDDLPGFSatpgnaayvlFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQ 219
Cdd:cd17647 99 ----------------IRAA--GVVVGPDSNPTLS----------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 220 SRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRD--RHSDLAKAINTMGANWALLTPSVAQLLNPSDV---PTLKILVI 294
Cdd:cd17647 151 DKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDigTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATtpfPKLHHAFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 295 GGEQVTSKDWNRWPT---SVQLINGYGPTEC-----CIVCTGYTTTQAF--KTGTI---GTAIASVSW-VVDPEDYHKLA 360
Cdd:cd17647 231 VGDILTKRDCLRLQTlaeNVRIVNMYGTTETqravsYFEVPSRSSDPTFlkNLKDVmpaGRGMLNVQLlVVNRNDRTQIC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 361 PLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpaWLVDGC--------------QGYAGRRGRLYKTGDLVRYDDEGNL 426
Cdd:cd17647 311 GIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNN--WFVEPDhwnyldkdnnepwrQFWLGPRDRLYRTGDLGRYLPNGDC 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 427 VCLGRKDSQVKVRGQRVELGEIEHHI-QGCMPEANqiaveVILLEGEKSN--TILAAFLQLDVKTGRafpTNKAAETGSL 503
Cdd:cd17647 389 ECCGRADDQVKIRGFRIELGEIDTHIsQHPLVREN-----ITLVRRDKDEepTLVSYIVPRFDKPDD---ESFAQEDVPK 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 504 AQVIFPVEAGKK------------LAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd17647 461 EVSTDPIVKGLIgyrklikdirefLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
49-548 |
5.88e-44 |
|
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: 166.88 E-value: 5.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAIC----AWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRH 124
Cdd:cd17654 1 PDRPALIidqtTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 125 KEILRQTGARMVVVSaqhsarwasssCHVVTLSEASIGQlTVEDDLPgfsaTPGNAAYVLFTSGSTGIPKGVVLEHRAVS 204
Cdd:cd17654 81 LTVMKKCHVSYLLQN-----------KELDNAPLSFTPE-HRHFNIR----TDECLAYVIHTSGTTGTPKIVAVPHKCIL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 205 TSCLGHGRAFGITdQSRVLQFTS-YTFDFCMAEIITTLLYGGC-ICVP-SDRDRHSDLAKA------INTMGANWALLTP 275
Cdd:cd17654 145 PNIQHFRSLFNIT-SEDILFLTSpLTFDPSVVEIFLSLSSGATlLIVPtSVKVLPSKLADIlfkrhrITVLQATPTLFRR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 276 SVAQLLNP---SDVPTLKILVIGGEQVTS----KDWNRWPTSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAI-ASV 347
Cdd:cd17654 224 FGSQSIKStvlSATSSLRVLALGGEPFPSlvilSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLlGTV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 348 SWVVDPEDYHklaplgSVGELLVEGpiLARGYLNDAEKTAAafiedpawlvdgcqgyagrRGRLYKTGDLVRYDDeGNLV 427
Cdd:cd17654 304 IEVRDQNGSE------GTGQVFLGG--LNRVCILDDEVTVP-------------------KGTMRATGDFVTVKD-GELF 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 428 CLGRKDSQVKVRGQRVELGEIEHHIQGCMPEanqIAVEVILLEGEKsntiLAAFLQLDVKTGRAFPTnkaaetgslaqvi 507
Cdd:cd17654 356 FLGRKDSQIKRRGKRINLDLIQQVIESCLGV---ESCAVTLSDQQR----LIAFIVGESSSSRIHKE------------- 415
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1779949166 508 fpveagkKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd17654 416 -------LQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
54-452 |
1.70e-43 |
|
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: 166.23 E-value: 1.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 54 ICAWDG-EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLdpdHPVSRHKEI---LR 129
Cdd:cd05911 3 IDADTGkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAA---NPIYTADELahqLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 130 QTGARMVVVSAQH------SARWASSSCHVVTLSEASIGQLTVEDDLPGFSATPGNA------------AYVLFTSGSTG 191
Cdd:cd05911 80 ISKPKVIFTDPDGlekvkeAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDlppplkdgkddtAAILYSSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 192 IPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFD--FCMAEIITTLLYGGCICVpSDRDRHSDLAKAINTMGAN 269
Cdd:cd05911 160 LPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiYGLFTTLASLLNGATVII-MPKFDSELFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 270 WALLTPSVAQLL--NPS----DVPTLKILVIGGEQVTSKDWNRWPTS---VQLINGYGPTECCIVCTgYTTTQAFKTGTI 340
Cdd:cd05911 239 FLYLVPPIAAALakSPLldkyDLSSLRVILSGGAPLSKELQELLAKRfpnATIKQGYGMTETGGILT-VNPDGDDKPGSV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 341 GTAIASVSW-VVDPEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrgrlyKTGDLVR 419
Cdd:cd05911 318 GRLLPNVEAkIVDDDGKDSLGP-NEPGEICVRGPQVMKGYYNNPEATKETFDED-GWL---------------HTGDIGY 380
|
410 420 430
....*....|....*....|....*....|...
gi 1779949166 420 YDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHI 452
Cdd:cd05911 381 FDEDGYLYIVDRKKELIKYKGFQVAPAELEAVL 413
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
29-551 |
9.36e-43 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 166.06 E-value: 9.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 29 IPGVTNKCiHDLFAEQVLAQPNAPAICaWDGE------MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAM 102
Cdd:COG0365 4 VGGRLNIA-YNCLDRHAEGRGDKVALI-WEGEdgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 103 LAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSAQHS--------------ARWASSSCHVVTLSEASIGQLTVED 168
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkekvdeALEELPSLEHVIVVGRTGADVPMEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 169 DL----------PGFSATPGNA---AYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRA-FGITDQSRVLQFT-------- 226
Cdd:COG0365 162 DLdwdellaaasAEFEPEPTDAddpLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTAdigwatgh 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 227 SYTFDFCMAEIITTLLYGGcICVPSDRDRHSDLAK--AINTMGA---NWALLTPSVAQLLNPSDVPTLKILVIGGEQVTS 301
Cdd:COG0365 242 SYIVYGPLLNGATVVLYEG-RPDFPDPGRLWELIEkyGVTVFFTaptAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 302 KDWNRW--PTSVQLINGYGPTE-CCIVCTGYTTTQAfKTGTIGTAI--ASVSwVVDPEDyhKLAPLGSVGELLVEGPI-- 374
Cdd:COG0365 321 EVWEWWyeAVGVPIVDGWGQTEtGGIFISNLPGLPV-KPGSMGKPVpgYDVA-VVDEDG--NPVPPGEEGELVIKGPWpg 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 375 LARGYLNDAEKTAAAfiedpawlvdgcqgYAGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIE----- 449
Cdd:COG0365 397 MFRGYWNDPERYRET--------------YFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIEsalvs 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 450 HHiqgcmpeanqiAVE---VILLEGEKSNTILAAFLQLdvKTGrafptnkAAETGSLAQVIFpveagKKLAERLPSYMVP 526
Cdd:COG0365 463 HP-----------AVAeaaVVGVPDEIRGQVVKAFVVL--KPG-------VEPSDELAKELQ-----AHVREELGPYAYP 517
|
570 580
....*....|....*....|....*
gi 1779949166 527 DVYFVVTQLPITVSGKTDRKRLREI 551
Cdd:COG0365 518 REIEFVDELPKTRSGKIMRRLLRKI 542
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1257-1569 |
5.04e-42 |
|
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: 157.83 E-value: 5.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1257 HTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCIcVLSEEERRTD 1336
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTV-VLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1337 LASAMCRMKVNWAFLTSTVVDLL------TPKSVPSLSILCVGGEPIRASQIVRWGSQVHLR--QTYGSSEVSGIVSSAA 1408
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLlkapesAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKlvNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1409 LTTCST-TRDVGRASTGVFW-IVDPNnhNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapAWraslglsagqqr 1486
Cdd:cd04433 160 PDDDARkPGSVGRPVPGVEVrIVDPD--GGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED--GW------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1487 lYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVELI-QPKDGEDGMlACFIVVEDSASN 1565
Cdd:cd04433 224 -YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVE-AVLLGHPGVAEAAVVGVpDPEWGERVV-AVVVLRPGADLD 300
|
....
gi 1779949166 1566 EDEL 1569
Cdd:cd04433 301 AEEL 304
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
37-550 |
8.21e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 156.12 E-value: 8.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFapld 116
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVL---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 117 pdHPVS-RHKE-----ILRQTGARMVVVSAQHSARWAS------SSCHVVTLSEASIGQLTV-----EDDLPGFSAT--- 176
Cdd:PRK06187 84 --HPINiRLKPeeiayILNDAEDRVVLVDSEFVPLLAAilpqlpTVRTVIVEGDGPAAPLAPevgeyEELLAAASDTfdf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 177 ----PGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVL----QFTSYTFDFCMAeiitTLLYGGCIC 248
Cdd:PRK06187 162 pdidENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHAWGLPYL----ALMAGAKQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 249 VPsdrDRH--SDLAKAINTMGANWALLTPSVAQLL------NPSDVPTLKILVIGG--------EQVTSKdwnrwpTSVQ 312
Cdd:PRK06187 238 IP---RRFdpENLLDLIETERVTFFFAVPTIWQMLlkapraYFVDFSSLRLVIYGGaalppallREFKEK------FGID 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 313 LINGYGPTECC-IVCTGY----TTTQAFKTGTIGTAIASVSW-VVDPEDYHKLAPLGSVGELLVEGPILARGYLNDAEKT 386
Cdd:PRK06187 309 LVQGYGMTETSpVVSVLPpedqLPGQWTKRRSAGRPLPGVEArIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEAT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 387 AAAFIEDpaWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCmPEANQIAveV 466
Cdd:PRK06187 389 AETIDGG--WL---------------HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGH-PAVAEVA--V 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 467 ILLEGEKSNTILAAFLQLdvktgrafptnKAAETGSLAQVIfpveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRK 546
Cdd:PRK06187 449 IGVPDEKWGERPVAVVVL-----------KPGATLDAKELR------AFLRGRLAKFKLPKRIAFVDELPRTSVGKILKR 511
|
....
gi 1779949166 547 RLRE 550
Cdd:PRK06187 512 VLRE 515
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
48-545 |
4.56e-37 |
|
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: 146.22 E-value: 4.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 48 QPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEI 127
Cdd:cd17631 8 HPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 128 LRQTGARMVVvsaqhsarwassschvvtlseasigqltveDDLpgfsatpgnaAYVLFTSGSTGIPKGVVLEHRAVSTSC 207
Cdd:cd17631 88 LADSGAKVLF------------------------------DDL----------ALLMYTSGTTGRPKGAMLTHRNLLWNA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 208 LGHGRAFGITDQSRVLQ-FTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAkAINTMGANWALLTPSVAQLL----- 281
Cdd:cd17631 128 VNALAALDLGPDDVLLVvAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLD-LIERHRVTSFFLVPTMIQALlqhpr 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 282 -NPSDVPTLKILVIGGEQVTS---KDWNRwpTSVQLINGYGPTECCIVCTGYTTTQAF-KTGTIGTAIASVSW-VVDPED 355
Cdd:cd17631 207 fATTDLSSLRAVIYGGAPMPErllRALQA--RGVKFVQGYGMTETSPGVTFLSPEDHRrKLGSAGRPVFFVEVrIVDPDG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 356 yhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFiedpawlVDGcqgyagrrgrLYKTGDLVRYDDEGNLVCLGRKDSQ 435
Cdd:cd17631 285 --REVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-------RDG----------WFHTGDLGRLDEDGYLYIVDRKKDM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 436 VKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQLDvktgrafPTNKAAETgslaqvifpvEAGKK 515
Cdd:cd17631 346 IISGGENVYPAEVEDVLYE-HPAVAEVA--VIGVPDEKWGEAVVAVVVPR-------PGAELDED----------ELIAH 405
|
490 500 510
....*....|....*....|....*....|
gi 1779949166 516 LAERLPSYMVPDVYFVVTQLPITVSGKTDR 545
Cdd:cd17631 406 CRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1124-1561 |
1.97e-36 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 145.81 E-value: 1.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERL 1203
Cdd:PRK04813 12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1204 RLMCRKVSAKLSLASEASaPLAKDLVGTVVIVNADSALQLAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASS 1283
Cdd:PRK04813 92 EMIIEVAKPSLIIATEEL-PLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1284 AVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEE--ERRTDLASAMCRMKVN-WaflTST--VVD- 1357
Cdd:PRK04813 171 FTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDmtANFKQLFETLPQLPINvW---VSTpsFADm 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1358 -LLTP----KSVPSLS--ILCvgGE--PIR-ASQIVRWGSQVHLRQTYGSSEVSGIVSSAALT----TCSTTRDVGRAST 1423
Cdd:PRK04813 248 cLLDPsfneEHLPNLThfLFC--GEelPHKtAKKLLERFPSATIYNTYGPTEATVAVTSIEITdemlDQYKRLPIGYAKP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1424 GVFWIVDPNNHNRLaPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapawraslglSAGqQRLYKTGDLArYKDDGSIE 1503
Cdd:PRK04813 326 DSPLLIIDEEGTKL-PDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT----------FDG-QPAYHTGDAG-YLEDGLLF 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 1504 LIGRKDNQVKLRGQRIEVEEIEHQarLAEADVAEIAVELIQPKDGEDGMLACFIVVED 1561
Cdd:PRK04813 393 YQGRIDFQIKLNGYRIELEEIEQN--LRQSSYVESAVVVPYNKDHKVQYLIAYVVPKE 448
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
689-1080 |
5.15e-36 |
|
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: 142.84 E-value: 5.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 689 IYPCSPLQEGMMALASKRPGD--YIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGMLQVVLAD------ 760
Cdd:cd19547 1 VYPLAPMQEGMLFRGLFWPDSdaYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDlappwa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 761 GIEWEQ------ANELEQYLEKDKSVSMGLGD-SLARYALVRdVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAE 833
Cdd:cd19547 81 LLDWSGedpdrrAELLERLLADDRAAGLSLADcPLYRLTLVR-LGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 834 VGKQPGFNA---FIKYLGEQDHEAAAA-----YWQGTLADCQAISFPALPPAVQQPVADATTAF-----QCPALARRPSD 900
Cdd:cd19547 160 HGREPQLSPcrpYRDYVRWIRARTAQSeeserFWREYLRDLTPSPFSTAPADREGEFDTVVHEFpeqltRLVNEAARGYG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 901 ITMSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPVAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATEMIPY 980
Cdd:cd19547 240 VTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAAH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 981 EQTGLHETAKVSADARHACS--FQTLLIVQPGSNGDIAHDALGEWRSHSDLQDFTTYALMVqCVLADDEVQIIASFDRRA 1058
Cdd:cd19547 320 GHVPLAQIKSWASGERLSGGrvFDNLVAFENYPEDNLPGDDLSIQIIDLHAQEKTEYPIGL-IVLPLQKLAFHFNYDTTH 398
|
410 420
....*....|....*....|..
gi 1779949166 1059 IEPWQVDKMLRQFSFVMQQLAT 1080
Cdd:cd19547 399 FTRAQVDRFIEVFRLLTEQLCR 420
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
61-504 |
5.34e-36 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 143.50 E-value: 5.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 61 MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSa 140
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 141 qhsarwassschvvtlseasigqltveddlpgfsaTPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQS 220
Cdd:cd05907 85 -----------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 221 RVLQF--TSYTFDFCMAEIITtLLYGGCICVPSDrdrhsdlakaINTMGANWALLTP----SVAQLLNP-------SDVP 287
Cdd:cd05907 130 RHLSFlpLAHVFERRAGLYVP-LLAGARIYFASS----------AETLLDDLSEVRPtvflAVPRVWEKvyaaikvKAVP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 288 TLK-------------ILVIGGEQVtSKDWNRWPTS--VQLINGYGPTECCIVCTgYTTTQAFKTGTIGTAIASVSwvvd 352
Cdd:cd05907 199 GLKrklfdlavggrlrFAASGGAPL-PAELLHFFRAlgIPVYEGYGLTETSAVVT-LNPPGDNRIGTVGKPLPGVE---- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 353 pedyhklAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPaWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGR- 431
Cdd:cd05907 273 -------VRIADDGEILVRGPNVMLGYYKNPEATAEALDADG-WL---------------HTGDLGEIDEDGFLHITGRk 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 432 KDSQVKVRGQRVELGEIEHHIQGCmPEANQIaveVILLEGEKSntiLAAFLQLDVKTGRAFPTNKAAETGSLA 504
Cdd:cd05907 330 KDLIITSGGKNISPEPIENALKAS-PLISQA---VVIGDGRPF---LVALIVPDPEALEAWAEEHGIAYTDVA 395
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
58-549 |
7.64e-36 |
|
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: 142.05 E-value: 7.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 58 DGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVV 137
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 138 VSAqhsarwassschvvtlseasigqltveddlpgfsatpgnaAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGIT 217
Cdd:cd05934 81 VDP----------------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 218 DQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAKAINTMGANWALLTPSVAQLL-----NPSDVPTlKIL 292
Cdd:cd05934 121 EDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLlaqppSPDDRAH-RLR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 293 VIGGEQVTSKDW----NRWptSVQLINGYGPTE--CCIVCTGYTTTqafKTGTIGTAIASVS-WVVDPEDyhKLAPLGSV 365
Cdd:cd05934 200 AAYGAPNPPELHeefeERF--GVRLLEGYGMTEtiVGVIGPRDEPR---RPGSIGRPAPGYEvRIVDDDG--QELPAGEP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 366 GELLV---EGPILARGYLNDAEKTAAAFiedpawlvdgcqgyagrRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQR 442
Cdd:cd05934 273 GELVIrglRGWGFFKGYYNMPEATAEAM-----------------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGEN 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 443 VELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQLdvktgrafptnKAAETGSlaqvifPVEAGKKLAERLPS 522
Cdd:cd05934 336 ISSAEVERAILR-HPAVREAA--VVAVPDEVGEDEVKAVVVL-----------RPGETLD------PEELFAFCEGQLAY 395
|
490 500
....*....|....*....|....*..
gi 1779949166 523 YMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd05934 396 FKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
68-549 |
1.20e-35 |
|
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: 142.58 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 68 GLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGA----FAPLDPDHPVSRHKEILRQTGARMVVVSAQHS 143
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 144 ARW-----ASSSCHVVTLSEASIGQltvEDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITD 218
Cdd:cd05922 81 DRLrdalpASPDPGTVLDADGIRAA---RASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 219 QSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAKAINTMGANWALLTPSVAQLL-----NPSDVPTLKILV 293
Cdd:cd05922 158 DDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLtrlgfDPAKLPSLRYLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 294 -IGGE--QVTSKDWNRWPTSVQLINGYGPTEccivCTGYTTT-----QAFKTGTIGTAIASVSWVVDPEDYHKLAPlGSV 365
Cdd:cd05922 238 qAGGRlpQETIARLRELLPGAQVYVMYGQTE----ATRRMTYlpperILEKPGSIGLAIPGGEFEILDDDGTPTPP-GEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 366 GELLVEGPILARGYLNDAEKTAAafiedpawlvdgcqgyAGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVEL 445
Cdd:cd05922 313 GEIVHRGPNVMKGYWNDPPYRRK----------------EGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 446 GEIEH--HIQGCMPEANQIAVEVILLEGeksntiLAAFLQLDVKtgrafptnkaaetgslaqvIFPVEAGKKLAERLPSY 523
Cdd:cd05922 377 TEIEAaaRSIGLIIEAAAVGLPDPLGEK------LALFVTAPDK-------------------IDPKDVLRSLAERLPPY 431
|
490 500
....*....|....*....|....*.
gi 1779949166 524 MVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd05922 432 KVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1121-1569 |
2.30e-35 |
|
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: 141.21 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1121 ADQAKAR-PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPslp 1199
Cdd:cd17631 1 LRRRARRhPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1200 herlRLMCRKVSAklslaseasapLAKDLVGTVVIvnADSALQLahhaspitsvrpthtayviFTSGSTGEPKGCRIEHR 1279
Cdd:cd17631 78 ----RLTPPEVAY-----------ILADSGAKVLF--DDLALLM-------------------YTSGTTGRPKGAMLTHR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1280 AASSAVTAHGRYLGMQASTRTLQFAS-YAFAGSLVELLMNLCHGGCICVLSEEERRTDLAsAMCRMKVNWAFLTSTVVDL 1358
Cdd:cd17631 122 NLLWNAVNALAALDLGPDDVLLVVAPlFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLD-LIERHRVTSFFLVPTMIQA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1359 L--TPKS----VPSLSILCVGGEPIRASQIVRWGSQ-VHLRQTYGSSEVSGIVSsaALTTCSTTRDVGRASTGVFW---- 1427
Cdd:cd17631 201 LlqHPRFattdLSSLRAVIYGGAPMPERLLRALQARgVKFVQGYGMTETSPGVT--FLSPEDHRRKLGSAGRPVFFvevr 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1428 IVDPNNhnRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFieAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGR 1507
Cdd:cd17631 279 IVDPDG--REVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF--RDGW-------------FHTGDLGRLDEDGYLYIVDR 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 1508 KDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVELIQ-PKDGEDGMlaCFIVVEDSAS-NEDEL 1569
Cdd:cd17631 342 KKDMIISGGENVYPAEVE-DVLYEHPAVAEVAVIGVPdEKWGEAVV--AVVVPRPGAElDEDEL 402
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1117-1587 |
2.18e-34 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 140.63 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1117 HDLFADQAKARPDAPAICaWDGD------MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGA 1190
Cdd:COG0365 12 YNCLDRHAEGRGDKVALI-WEGEdgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1191 FLLLDPSLPHERLRLMCRKVSAKLSLASEASAPLAKDL---------------VGTVVIVNA-------------DSALQ 1242
Cdd:COG0365 91 HSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIdlkekvdealeelpsLEHVIVVGRtgadvpmegdldwDELLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1243 LAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRY-LGMQASTRTLQFA--------SYAFAGSlv 1313
Cdd:COG0365 171 AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTAdigwatghSYIVYGP-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1314 ellmnLCHGGCIcVLSEEERRTDLASAMCRM----KVNWAFLTSTVV--------DLLTPKSVPSLSILCVGGEPIRASQ 1381
Cdd:COG0365 249 -----LLNGATV-VLYEGRPDFPDPGRLWELiekyGVTVFFTAPTAIralmkagdEPLKKYDLSSLRLLGSAGEPLNPEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1382 IvRWGSQ---VHLRQTYGSSEVSGIVSSAALTT----CSTTR-----DVGrastgvfwIVDPNNHnrLAPVGAVGEVLVE 1449
Cdd:COG0365 323 W-EWWYEavgVPIVDGWGQTETGGIFISNLPGLpvkpGSMGKpvpgyDVA--------VVDEDGN--PVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1450 GPVLG--REYIDEPDKTASTFieapaWRASLGlsagqqrLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI---EVEE- 1523
Cdd:COG0365 392 GPWPGmfRGYWNDPERYRETY-----FGRFPG-------WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIgtaEIESa 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1779949166 1524 -IEHQArlaeadVAEIAVelIQPKDGEDGM-LACFIVVEDSASNEDELsgkRTRLDTRTQRTIGKI 1587
Cdd:COG0365 460 lVSHPA------VAEAAV--VGVPDEIRGQvVKAFVVLKPGVEPSDEL---AKELQAHVREELGPY 514
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
181-549 |
5.49e-34 |
|
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: 138.23 E-value: 5.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 181 AYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQ----FTSYTFDFCMaeiITTLLYGGCI-CVPSDRDR 255
Cdd:cd05909 150 AVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGCL---WLPLLSGIKVvFHPNPLDY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 256 HSdLAKAINTMGANWALLTPS----VAQLLNPSDVPTLKILVIGGEQVTSKDWNRWPTS--VQLINGYGPTECCIVCTGY 329
Cdd:cd05909 227 KK-IPELIYDKKATILLGTPTflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSPVISVN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 330 TTTQAFKTGTIGTAIASVSWVVDPEDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEdpAWlvdgcqgyagrrg 409
Cdd:cd05909 306 TPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD--GW------------- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 410 rlYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCMPEANQIAVeVILLEGEKSNTIlaaflqldvktg 489
Cdd:cd05909 371 --YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAV-VSVPDGRKGEKI------------ 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 490 RAFPTNKAAETGSLAQVIfpVEAGkklaerLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd05909 436 VLLTTTTDTDPSSLNDIL--KNAG------ISNLAKPSYIHQVEEIPLLGTGKPDYVTLK 487
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
62-481 |
5.55e-34 |
|
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: 138.52 E-value: 5.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 62 SYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSrhkEILRQ---TGARMVVV 138
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA---EIAKQvkdSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 139 SAQHSARWASSSCHVVTLSEASIGQLTVEDDL--PGFSATP------GNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGH 210
Cdd:cd05904 111 TAELAEKLASLALPVVLLDSAEFDSLSFSDLLfeADEAEPPvvvikqDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 211 GRAFGITD--QSRVL----QFTSYTFDFCMaeiITTLLYGGCICVPSDRDRHsDLAKAINTMGANWALLTPSV------A 278
Cdd:cd05904 191 VAGEGSNSdsEDVFLcvlpMFHIYGLSSFA---LGLLRLGATVVVMPRFDLE-ELLAAIERYKVTHLPVVPPIvlalvkS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 279 QLLNPSDVPTLKILVIG----GEQVTSKDWNRWPtSVQLINGYGPTE-CCIVCTGYTTTQ-AFKTGTIGTAIASV-SWVV 351
Cdd:cd05904 267 PIVDKYDLSSLRQIMSGaaplGKELIEAFRAKFP-NVDLGQGYGMTEsTGVVAMCFAPEKdRAKYGSVGRLVPNVeAKIV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 352 DPEDYHKLaPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGR 431
Cdd:cd05904 346 DPETGESL-PPNQTGELWIRGPSIMKGYLNNPEATAATIDKE-GWL---------------HTGDLCYIDEDGYLFIVDR 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1779949166 432 KDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAF 481
Cdd:cd05904 409 LKELIKYKGFQVAPAELEALLLS-HPEILDAA--VIPYPDEEAGEVPMAF 455
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1133-1569 |
1.10e-33 |
|
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: 137.34 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1133 ICAWDGD-MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVS 1211
Cdd:cd05911 3 IDADTGKeLTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1212 AKLSLASEASAPLAKD---LVGTVV-IVNADSALQLAHHASPITSVR---------------PTHTAYVIFTSGSTGEPK 1272
Cdd:cd05911 83 PKVIFTDPDGLEKVKEaakELGPKDkIIVLDDKPDGVLSIEDLLSPTlgeededlppplkdgKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1273 GCRIEHRA--ASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLseeeRRTDLASAMC---RMKVN 1347
Cdd:cd05911 163 GVCLSHRNliANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIM----PKFDSELFLDlieKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1348 WAFLTSTVV------DLLTPKSVPSLSILCVGGEPIRA---SQIVRWGSQVHLRQTYGSSEVSGIVssaaltTCSTTRDV 1418
Cdd:cd05911 239 FLYLVPPIAaalaksPLLDKYDLSSLRVILSGGAPLSKelqELLAKRFPNATIKQGYGMTETGGIL------TVNPDGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1419 GRASTGV------FWIVDPNNHNRLAPvGAVGEVLVEGPVLGREYIDEPDKTASTFIEApAWraslglsagqqrlYKTGD 1492
Cdd:cd05911 313 KPGSVGRllpnveAKIVDDDGKDSLGP-NEPGEICVRGPQVMKGYYNNPEATKETFDED-GW-------------LHTGD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1493 LARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhqARLAEAD-VAEIAVelIQPKDGEDGML-ACFIVVEDSAS-NEDEL 1569
Cdd:cd05911 378 IGYFDEDGYLYIVDRKKELIKYKGFQVAPAELE--AVLLEHPgVADAAV--IGIPDEVSGELpRAYVVRKPGEKlTEKEV 453
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
52-549 |
1.36e-33 |
|
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: 136.05 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 52 PAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQT 131
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 132 GARMVVVSAqhsarwassschvvtlseasigqltveDDLpgfsatpgnaAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHG 211
Cdd:cd05919 82 EARLVVTSA---------------------------DDI----------AYLLYSSGTTGPPKGVMHAHRDPLLFADAMA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 212 R-AFGITDQSRVLQFTSYTFDFCMAEIITTLLYGG--CICVPSDRDRHSDLAKAIN----------TMGANwalLTPSVA 278
Cdd:cd05919 125 ReALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGasAVLNPGWPTAERVLATLARfrptvlygvpTFYAN---LLDSCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 279 qlLNPSDVPTLKILVIGGEQVTSKDWNRWP--TSVQLINGYGPTEccivcTGYT----TTQAFKTGTIGTAiasVSW--- 349
Cdd:cd05919 202 --GSPDALRSLRLCVSAGEALPRGLGERWMehFGGPILDGIGATE-----VGHIflsnRPGAWRLGSTGRP---VPGyei 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 350 -VVDPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFiedpawlvdgcqgyagrRGRLYKTGDLVRYDDEGNLVC 428
Cdd:cd05919 272 rLVDEEG--HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-----------------NGGWYRTGDKFCRDADGWYTH 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 429 LGRKDSQVKVRGQRVELGEIEHHIqgCMPEANQIAVEVILLEGEKSNTiLAAFLqldvktgraFPTNKAAETGSLAQVIF 508
Cdd:cd05919 333 AGRADDMLKVGGQWVSPVEVESLI--IQHPAVAEAAVVAVPESTGLSR-LTAFV---------VLKSPAAPQESLARDIH 400
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1779949166 509 pveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd05919 401 -----RHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
37-550 |
2.38e-33 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 136.81 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVV----PLCFEksmwTVVAMLAVLKAGGA- 111
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVvvqlPNVAE----FVIVFFALFRAGAIp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 112 -FAPldPDHpvsRHKEIL---RQTGARMVVVSAQHS-------ARWASSSC----HVVTLSEA----SIGQLTVED-DLP 171
Cdd:COG1021 103 vFAL--PAH---RRAEIShfaEQSEAVAYIIPDRHRgfdyralARELQAEVpslrHVLVVGDAgeftSLDALLAAPaDLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 172 GFSATPGNAAYVLFTSGSTGIPKGVVLEH-------RAVSTSClghgrafGITDQSRVL-------QFTsytfdFCMAEI 237
Cdd:COG1021 178 EPRPDPDDVAFFQLSGGTTGLPKLIPRTHddylysvRASAEIC-------GLDADTVYLaalpaahNFP-----LSSPGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 238 ITTLLYGGCIcVPSDRDRHSDLAKAINTMGANWALLTPSVAQL-LN-----PSDVPTLKILVIGGEQVTSKDWNRWPTS- 310
Cdd:COG1021 246 LGVLYAGGTV-VLAPDPSPDTAFPLIERERVTVTALVPPLALLwLDaaersRYDLSSLRVLQVGGAKLSPELARRVRPAl 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 311 -VQLINGYGPTE--CCivctgYT----------TTQafktgtiGTAIAS---VsWVVDPEDyhKLAPLGSVGELLVEGPI 374
Cdd:COG1021 325 gCTLQQVFGMAEglVN-----YTrlddpeevilTTQ-------GRPISPddeV-RIVDEDG--NPVPPGEVGELLTRGPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 375 LARGYLNDAEKTAAAFIEDpawlvdgcqGYagrrgrlYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQG 454
Cdd:COG1021 390 TIRGYYRAPEHNARAFTPD---------GF-------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 455 CmP---EANQIAVEVILLeGEKSntilAAFLqldVKTGRAFptnkaaetgSLAQVIfpveagKKLAER-LPSYMVPDVYF 530
Cdd:COG1021 454 H-PavhDAAVVAMPDEYL-GERS----CAFV---VPRGEPL---------TLAELR------RFLRERgLAAFKLPDRLE 509
|
570 580
....*....|....*....|
gi 1779949166 531 VVTQLPITVSGKTDRKRLRE 550
Cdd:COG1021 510 FVDALPLTAVGKIDKKALRA 529
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
49-550 |
2.62e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 136.17 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVVSAQHSARWASSSCHVVT--LSEASIGQLTV--EDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVS 204
Cdd:PRK06145 96 GDAGAKLLLVDEEFDAIVALETPKIVIdaAAQADSRRLAQggLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 205 TSCLGHGRAFGITDQSRVLQFTS-YTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAkAINTMGANWALLTPSV--AQLL 281
Cdd:PRK06145 176 WKSIDHVIALGLTASERLLVVGPlYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA-AIERHRLTCAWMAPVMlsRVLT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 282 NPS----DVPTLKILVIGGEQVTS---KDWNRWPTSVQLINGYGPTEcciVCTGYTTTQAF----KTGTIGTAIASVSWV 350
Cdd:PRK06145 255 VPDrdrfDLDSLAWCIGGGEKTPEsriRDFTRVFTRARYIDAYGLTE---TCSGDTLMEAGreieKIGSTGRALAHVEIR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 351 VDPEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFIEDpaWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLG 430
Cdd:PRK06145 332 IADGAGRWLPP-NMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--WF---------------RSGDVGYLDEEGFLYLTD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 431 RKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQLdvktgrafptnKAAETGSLAQVIFPV 510
Cdd:PRK06145 394 RKKDMIISGGENIASSEVERVIYE-LPEVAEAA--VIGVHDDRWGERITAVVVL-----------NPGATLTLEALDRHC 459
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1779949166 511 EAgkklaeRLPSYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:PRK06145 460 RQ------RLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
37-485 |
3.54e-33 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 137.54 E-value: 3.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDG----EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAF 112
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 113 APLDPDHPVSRHKEILRQTGARMVVVSAQH------SARWASSSC-HVVTLSEASIGQ----LTVED--------DLPGF 173
Cdd:COG1022 93 VPIYPTSSAEEVAYILNDSGAKVLFVEDQEqldkllEVRDELPSLrHIVVLDPRGLRDdprlLSLDEllalgrevADPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 174 ------SATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQF--TSYTFDFCMAeiITTLLYGG 245
Cdd:COG1022 173 learraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlpLAHVFERTVS--YYALAAGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 246 CICVPSDRDR-HSDL-------------------AKAINTMGA---------NWALltpSVAQ-----LLNPSDVPT--- 288
Cdd:COG1022 251 TVAFAESPDTlAEDLrevkptfmlavprvwekvyAGIQAKAEEagglkrklfRWAL---AVGRryaraRLAGKSPSLllr 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 289 ---------------------LKILVIGGEQVtSKDWNRWPTS--VQLINGYGPTECCIVCTGyTTTQAFKTGTIGTAIA 345
Cdd:COG1022 328 lkhaladklvfsklrealggrLRFAVSGGAAL-GPELARFFRAlgIPVLEGYGLTETSPVITV-NRPGDNRIGTVGPPLP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 346 SVSWVVDPEdyhklaplgsvGELLVEGPILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGN 425
Cdd:COG1022 406 GVEVKIAED-----------GEILVRGPNVMKGYYKNPEATAEAFDAD-GWL---------------HTGDIGELDEDGF 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 426 LVCLGRKDSQVKVR-GQRVELGEIEHHIQGCmPEANQIAVeviLLEGEKSntiLAAFLQLD 485
Cdd:COG1022 459 LRITGRKKDLIVTSgGKNVAPQPIENALKAS-PLIEQAVV---VGDGRPF---LAALIVPD 512
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
33-550 |
1.30e-32 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 134.88 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 33 TNKCIHDLFAEQVLAQPNAPAICAWDG-EMSYSVLDGLSTKLAGYLVKIGVKPGDVVplCFEKSMWT--VVAMLAVLKAG 109
Cdd:PRK06087 21 GDASLADYWQQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRV--AFQLPGWCefTIIYLACLKVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 110 GAFAPLDPDHPVSRHKEILRQTGARM--------------VVVSAQHSARwasSSCHVV-------TLSEASIGQLtVED 168
Cdd:PRK06087 99 AVSVPLLPSWREAELVWVLNKCQAKMffaptlfkqtrpvdLILPLQNQLP---QLQQIVgvdklapATSSLSLSQI-IAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 169 DLPGFSATPGNA---AYVLFTSGSTGIPKGVVLEHRAVstscLGHGRAFgitdqSRVLQFTSYTFDFCMAE--------- 236
Cdd:PRK06087 175 YEPLTTAITTHGdelAAVLFTSGTEGLPKGVMLTHNNI----LASERAY-----CARLNLTWQDVFMMPAPlghatgflh 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 237 -IITTLLYGGCIcVPSDRDRHSDLAKAINTMGANWAL-LTPSVAQLLN-----PSDVPTLKILVIGGEQVTSKDWNR-WP 308
Cdd:PRK06087 246 gVTAPFLIGARS-VLLDIFTPDACLALLEQQRCTCMLgATPFIYDLLNllekqPADLSALRFFLCGGTTIPKKVAREcQQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 309 TSVQLINGYGPTECC---IVCTGYTTTQAFktGTIGTAIASVSW-VVDpeDYHKLAPLGSVGELLVEGPILARGYLNDAE 384
Cdd:PRK06087 325 RGIKLLSVYGSTESSphaVVNLDDPLSRFM--HTDGYAAAGVEIkVVD--EARKTLPPGCEGEEASRGPNVFMGYLDEPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 385 KTAAAFIEDpAWlvdgcqgyagrrgrlYKTGDLVRYDDEGNLVCLGRKdSQVKVR-GQRVELGEIEHHIQGCmPEANQIA 463
Cdd:PRK06087 401 LTARALDEE-GW---------------YYSGDLCRMDEAGYIKITGRK-KDIIVRgGENISSREVEDILLQH-PKIHDAC 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 464 veVILLEGEKSNTILAAFLQLdvktgrafptnKAAE-TGSLAQVIFPVEagkklAERLPSYMVPDVYFVVTQLPITVSGK 542
Cdd:PRK06087 463 --VVAMPDERLGERSCAYVVL-----------KAPHhSLTLEEVVAFFS-----RKRVAKYKYPEHIVVIDKLPRTASGK 524
|
....*...
gi 1779949166 543 TDRKRLRE 550
Cdd:PRK06087 525 IQKFLLRK 532
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
875-1571 |
7.34e-31 |
|
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: 132.88 E-value: 7.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 875 PPAVQQPVADATTAFQCPALARR-PSDITMSTLIRAAWALLASSYTSSDDVVFGAtvtgrNAPVAGIEAMagptiatvpV 953
Cdd:TIGR03443 19 LRPANNRLVEATYSLQLPSAEVTaGGGSTPFIILLAAFAALVYRLTGDEDIVLGT-----SSNKSGRPFV---------L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 954 RVRVQHSHKVSEFLHSVQQQATEMIPYEQTGLHETA----KVSADARHACSFQTLLIVQPGSngdiahdalgewrSHSDL 1029
Cdd:TIGR03443 85 RLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSehiqAAKKLERTPPLFRLAFQDAPDN-------------QQTTY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1030 QDFTTYALMVQCVLADDEVQIIASFDRRAIEPWQVDKMLRQFSFVMQQlATADAEAGIASIDTLTPEDRQQLWEWNHDVP 1109
Cdd:TIGR03443 152 STGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSA-ASSNPDEPIGKVSLITPSQKSLLPDPTKDLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1110 PAIER-CIHDLFADQAKARPDAPAIC----AWDGD-----MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVV 1179
Cdd:TIGR03443 231 WSGFRgAIHDIFADNAEKHPDRTCVVetpsFLDPSsktrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1180 AMLAVLKAGGAFLLLDPSLPHER---------------------LRLMCRK-VSAKLSLASEASA-PLAKD--LVGTVVI 1234
Cdd:TIGR03443 311 AVMGVLKAGATFSVIDPAYPPARqtiylsvakpraliviekagtLDQLVRDyIDKELELRTEIPAlALQDDgsLVGGSLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1235 VNADSALQ-LAHHASPITSV--RPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGS 1311
Cdd:TIGR03443 391 GGETDVLApYQALKDTPTGVvvGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPI 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1312 LVELLMNLCHGGCICVLSEEERRTD--LASAMCRMKVNWAFLTSTVVDLLTPKSV---PSLSILCVGGEPIRASQIVRWG 1386
Cdd:TIGR03443 471 QRDMFTPLFLGAQLLVPTADDIGTPgrLAEWMAKYGATVTHLTPAMGQLLSAQATtpiPSLHHAFFVGDILTKRDCLRLQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1387 S---QVHLRQTYGSSEVSGIVS-------SAALTTCSTTRDVGRASTGV----FWIVDPNNHNRLAPVGAVGEVLVEGPV 1452
Cdd:TIGR03443 551 TlaeNVCIVNMYGTTETQRAVSyfeipsrSSDSTFLKNLKDVMPAGKGMknvqLLVVNRNDRTQTCGVGEVGEIYVRAGG 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1453 LGREYIDEPDKTASTFI----------------EAPAWRAS-LGLsagQQRLYKTGDLARYKDDGSIELIGRKDNQVKLR 1515
Cdd:TIGR03443 631 LAEGYLGLPELNAEKFVnnwfvdpshwidldkeNNKPEREFwLGP---RDRLYRTGDLGRYLPDGNVECCGRADDQVKIR 707
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 1516 GQRIEVEEIE-HQARlaEADVAEiAVELIQPKDGEDGMLACFIVVEDSASNEDELSG 1571
Cdd:TIGR03443 708 GFRIELGEIDtHLSQ--HPLVRE-NVTLVRRDKDEEPTLVSYIVPQDKSDELEEFKS 761
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1128-1564 |
8.51e-31 |
|
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: 127.97 E-value: 8.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAIC----AWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERL 1203
Cdd:cd17654 1 PDRPALIidqtTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1204 RLMCRKVSAKLSLASEASAPLAKDLVGTVVivnaDSALQLAHHaspitsvrpthTAYVIFTSGSTGEPKGCRIEHRAASS 1283
Cdd:cd17654 81 LTVMKKCHVSYLLQNKELDNAPLSFTPEHR----HFNIRTDEC-----------LAYVIHTSGTTGTPKIVAVPHKCILP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1284 AVTaHGRYLGMQASTRTLQFASYA-FAGSLVELLMNLCHGGCIcVLSEEERRTD---LASAM-CRMKVNWAFLTSTVVDL 1358
Cdd:cd17654 146 NIQ-HFRSLFNITSEDILFLTSPLtFDPSVVEIFLSLSSGATL-LIVPTSVKVLpskLADILfKRHRITVLQATPTLFRR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1359 LTPKSVP--------SLSILCVGGEPIRASQIVR-W---GSQVHLRQTYGSSEVSGIVSSAALTTCSTTRDVGRASTG-V 1425
Cdd:cd17654 224 FGSQSIKstvlsatsSLRVLALGGEPFPSLVILSsWrgkGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGtV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1426 FWIVDPNNHNrlapvgAVGEVLVEGpVLGREYIDEPDKTA-STFieapawraslglsagqqrlYKTGDLARYKDdGSIEL 1504
Cdd:cd17654 304 IEVRDQNGSE------GTGQVFLGG-LNRVCILDDEVTVPkGTM-------------------RATGDFVTVKD-GELFF 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1505 IGRKDNQVKLRGQRIEVEEIEHQARLAEAdVAEIAVELIqpkdgEDGMLACFIVVEDSAS 1564
Cdd:cd17654 357 LGRKDSQIKRRGKRINLDLIQQVIESCLG-VESCAVTLS-----DQQRLIAFIVGESSSS 410
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
50-550 |
9.42e-31 |
|
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: 127.41 E-value: 9.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 50 NAPAICAWDGEMSYSVLDGLSTKLAGYLV-KIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVvsaqhsarwassschvvtlseasigqltveddlpgfsatpgNAAYVLFTSGSTGIPKGVVLEHRAVSTSCL 208
Cdd:cd05941 81 TDSEPSLVL-----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 209 GHGRAFGITDQSRVLQ----------FTSytfdfcmaeIITTLLYGG-CICVP---SDRDRHSDLAKAIN------TMga 268
Cdd:cd05941 120 ALVDAWRWTEDDVLLHvlplhhvhglVNA---------LLCPLFAGAsVEFLPkfdPKEVAISRLMPSITvfmgvpTI-- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 269 nWALLTPSVAQLLNPSDVPT------LKILVIGGEQVTSKDWNRWP--TSVQLINGYGPTEccivcTGYTTTQAFK---- 336
Cdd:cd05941 189 -YTRLLQYYEAHFTDPQFARaaaaerLRLMVSGSAALPVPTLEEWEaiTGHTLLERYGMTE-----IGMALSNPLDgerr 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 337 TGTIGTAIASVSWVVDPEDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpawlvdgcqGYagrrgrlYKTGD 416
Cdd:cd05941 263 PGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDD---------GW-------FKTGD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 417 LVRYDDEGNLVCLGR-KDSQVKVRGQRVELGEIEHHIQGcMPEANQIAVEVILLE--GEKsntiLAAFLQLdvktgrafp 493
Cdd:cd05941 327 LGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLA-HPGVSECAVIGVPDPdwGER----VVAVVVL--------- 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 494 tNKAAETGSLAQVIfpveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:cd05941 393 -RAGAAALSLEELK------EWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
37-550 |
2.17e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 127.71 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLD 116
Cdd:PRK07656 7 LPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 117 PDHPVSRHKEILRQTGARMVVVSAQH--SARWASSSC----HVVTLS-----EASIGQLTVEDDL----PGFSA---TPG 178
Cdd:PRK07656 87 TRYTADEAAYILARGDAKALFVLGLFlgVDYSATTRLpaleHVVICEteeddPHTEKMKTFTDFLaagdPAERApevDPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 179 NAAYVLFTSGSTGIPKGVVLEHRavstSCLGHGRAF----GITDQSRVLQFTSYTFDFCM-AEIITTLLYGGCIcVPSdr 253
Cdd:PRK07656 167 DVADILFTSGTTGRPKGAMLTHR----QLLSNAADWaeylGLTEGDRYLAANPFFHVFGYkAGVNAPLMRGATI-LPL-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 254 dRHSDLAKAINTMGANWALLTPSVAQL---------LNPSDVPTLKILVIGGEQVtskdwnrwPtsVQLIN--------- 315
Cdd:PRK07656 240 -PVFDPDEVFRLIETERITVLPGPPTMynsllqhpdRSAEDLSSLRLAVTGAASM--------P--VALLErfeselgvd 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 316 ----GYGPTECCIVCTGYTTTQAFKT--GTIGTAIASVSWVVDPEDYHKLaPLGSVGELLVEGPILARGYLNDAEKTAAA 389
Cdd:PRK07656 309 ivltGYGLSEASGVTTFNRLDDDRKTvaGTIGTAIAGVENKIVNELGEEV-PVGEVGELLVRGPNVMKGYYDDPEATAAA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 390 FIEDpawlvdgcqgyagrrGRLYkTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEhHIQGCMPEANQIAVEVILL 469
Cdd:PRK07656 388 IDAD---------------GWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVE-EVLYEHPAVAEAAVIGVPD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 470 E--GEksntilaaflqldvkTGRAFPTNKAAETGSLAQVIfpveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKR 547
Cdd:PRK07656 451 ErlGE---------------VGKAYVVLKPGAELTEEELI------AYCREHLAKYKVPRSIEFLDELPKNATGKVLKRA 509
|
...
gi 1779949166 548 LRE 550
Cdd:PRK07656 510 LRE 512
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
39-548 |
3.27e-30 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 126.67 E-value: 3.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 39 DLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVV----PLCFEksmwTVVAMLAVLKAGGAFAP 114
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVvvqlPNVAE----FVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 115 LDPDHpvsRHKEIL---RQTGARMVVVSAQHS-------ARWASSSCHVVtlseasigqltveddlpgfsatpgnaAYVL 184
Cdd:cd05920 95 ALPSH---RRSELSafcAHAEAVAYIVPDRHAgfdhralARELAESIPEV--------------------------ALFL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 185 FTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAE--IITTLLYGGCICVPSDRDRHSDLAkA 262
Cdd:cd05920 146 LSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPDPSPDAAFP-L 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 263 INTMGANWALLTPSVAQLL------NPSDVPTLKILVIGGEQVTSKDWNRWPT--SVQLINGYGPTECCIVCTGYTTTQA 334
Cdd:cd05920 225 IEREGVTVTALVPALVSLWldaaasRRADLSSLRLLQVGGARLSPALARRVPPvlGCTLQQVFGMAEGLLNYTRLDDPDE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 335 FKTGTIGTAIASV--SWVVDpEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFIEDpawlvdgcqGYagrrgrlY 412
Cdd:cd05920 305 VIIHTQGRPMSPDdeIRVVD-EEGNPVPP-GEEGELLTRGPYTIRGYYRAPEHNARAFTPD---------GF-------Y 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 413 KTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAVeVIL---LEGEKSntilAAFLqldvktg 489
Cdd:cd05920 367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR-HPAVHDAAV-VAMpdeLLGERS----CAFV------- 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 490 raFPTNKAAETGSLAQviFPVEAGkklaerLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd05920 434 --VLRDPPPSAAQLRR--FLRERG------LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
37-550 |
4.30e-30 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 127.31 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDGE--MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAP 114
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 115 LDPDHPVSRHKEILRQTGARMVVVS-------AQHSARWASSSCHVVTLSEASIGQLTVEDDL-----PGFSATPG---N 179
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLIDadgphdrAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAateptPATSTPEGlrpD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 180 AAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQ-SRVLQFTSYTFDFCMAEIITTLLYGGCICVPSdRDRHS- 257
Cdd:PRK05852 178 DAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRdATVAVMPLYHGHGLIAALLATLASGGAVLLPA-RGRFSa 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 258 -DLAKAINTMGANWALLTPSVAQLL--------NPSDVPTLKILVIGGEQVTSKDWNRWPT--SVQLINGYGPTECC--- 323
Cdd:PRK05852 257 hTFWDDIKAVGATWYTAVPTIHQILleraatepSGRKPAALRFIRSCSAPLTAETAQALQTefAAPVVCAFGMTEAThqv 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 324 ----IVCTGYTTTQAFKTGTIGTAIASVSWVVDPeDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFIEdpAWLvd 399
Cdd:PRK05852 337 tttqIEGIGQTENPVVSTGLVGRSTGAQIRIVGS-DGLPLPA-GAVGEVWLRGTTVVRGYLGDPTITAANFTD--GWL-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 400 gcqgyagrrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCmPEANQIAVEVI--LLEGEksnTI 477
Cdd:PRK05852 411 -------------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASH-PNVMEAAVFGVpdQLYGE---AV 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 478 LAAFlqldVKTGRAFPTnkaaetgslaqvifPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:PRK05852 474 AAVI----VPRESAPPT--------------AEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
60-548 |
4.36e-30 |
|
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: 125.28 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 60 EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVS 139
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 140 AQhsarwassschvvtlseasigqltvEDDLpgfsatpgnaAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQ 219
Cdd:cd05935 81 SE-------------------------LDDL----------ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 220 SRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAKAINTMGAN-WALLTPSVAQLLNP-----SDVPTLKILV 293
Cdd:cd05935 126 DVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTfWTNIPTMLVDLLATpefktRDLSSLKVLT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 294 IGG----EQVTSKDWNRwpTSVQLINGYGPTECCiVCTGYTTTQAFKTGTIGTAIASV-SWVVDPEDYHKLAPlGSVGEL 368
Cdd:cd05935 206 GGGapmpPAVAEKLLKL--TGLRFVEGYGLTETM-SQTHTNPPLRPKLQCLGIP*FGVdARVIDIETGRELPP-NEVGEI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 369 LVEGPILARGYLNDAEKTAAAFIEDpawlvdgcqgyAGRrgRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEI 448
Cdd:cd05935 282 VVRGPQIFKGYWNRPEETEESFIEI-----------KGR--RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 449 EHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQLDvktgrafPTNKAAETgslaqvifPVEAGKKLAERLPSYMVPDV 528
Cdd:cd05935 349 EAKLYK-HPAI*EVC--VISVPDERVGEEVKAFIVLR-------PEYRGKVT--------EEDIIEWAREQMAAYKYPRE 410
|
490 500
....*....|....*....|
gi 1779949166 529 YFVVTQLPITVSGKTDRKRL 548
Cdd:cd05935 411 VEFVDELPRSASGKILWRLL 430
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
62-548 |
1.63e-29 |
|
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: 123.71 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 62 SYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSAQ 141
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 142 HSARwassscHVVTLSEASIGqLTVEDDLPGFSATPGNA-AYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQS 220
Cdd:TIGR01923 81 LEEK------DFQADSLDRIE-AAGRYETSLSASFNMDQiATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 221 RVLQFTSYTFDFCMAEIITTLLYGGCICVPsdrDRHSDLAKAINTMGANWALLTPSVAQLLNPSDVP--TLKILVIGGEq 298
Cdd:TIGR01923 154 NWLLSLPLYHISGLSILFRWLIEGATLRIV---DKFNQLLEMIANERVTHISLVPTQLNRLLDEGGHneNLRKILLGGS- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 299 vtskdwnrwPTSVQLI-----------NGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVSWVVDPEDyhklapLGSVGE 367
Cdd:TIGR01923 230 ---------AIPAPLIeeaqqyglpiyLSYGMTETCSQVTTATPEMLHARPDVGRPLAGREIKIKVDN------KEGHGE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 368 LLVEGPILARGYLNDAEKTAAAFIedpawlvdgcQGYagrrgrlYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGE 447
Cdd:TIGR01923 295 IMVKGANLMKGYLYQGELTPAFEQ----------QGW-------FNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 448 IEH------HIQ--GCMP----EANQIAVEVILLEGEKSNTILAAFLQldvktgrafptnkaaetgslaqvifpveagkk 515
Cdd:TIGR01923 358 IETvlyqhpGIQeaVVVPkpdaEWGQVPVAYIVSESDISQAKLIAYLT-------------------------------- 405
|
490 500 510
....*....|....*....|....*....|...
gi 1779949166 516 laERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:TIGR01923 406 --EKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
42-554 |
5.97e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 122.99 E-value: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 42 AEQVLAQPNAPAI--CAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDH 119
Cdd:PRK09088 2 AFHARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 120 PVSRHKEILRQTGARMVVvsaqHSARWASSSCHVVTLSeASIGQLTVEDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLE 199
Cdd:PRK09088 82 SASELDALLQDAEPRLLL----GDDAVAAGRTDVEDLA-AFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 200 HRAVSTSCLGHGRAFGITDQSRVLqftsytFDFCMAEII-------TTLLYGGCICVPSDRDRHSDLAKAIN-TMGANWA 271
Cdd:PRK09088 157 ERNLQQTAHNFGVLGRVDAHSSFL------CDAPMFHIIglitsvrPVLAVGGSILVSNGFEPKRTLGRLGDpALGITHY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 272 LLTPSVAQLL------NPSDVPTLKILVIGGEQVTSKDWNRW-PTSVQLINGYGPTECCIV--CTGYTTTQAFKTGTIGT 342
Cdd:PRK09088 231 FCVPQMAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWlDDGIPMVDGFGMSEAGTVfgMSVDCDVIRAKAGAAGI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 343 AIASV-SWVVDPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpAWlvdgcqgyagrrgrlYKTGDLVRYD 421
Cdd:PRK09088 311 PTPTVqTRVVDDQG--NDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGD-GW---------------FRTGDIARRD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 422 DEGNLVCLGRKDSQVKVRGQRVELGEIE-----H-HIQGC----MPEANQiavevilleGEksntilaaflqldvkTGRA 491
Cdd:PRK09088 373 ADGFFWVVDRKKDMFISGGENVYPAEIEavladHpGIRECavvgMADAQW---------GE---------------VGYL 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 492 FPTNKAAETGSLAQVIfpveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIGAS 554
Cdd:PRK09088 429 AIVPADGAPLDLERIR------SHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
59-549 |
1.01e-28 |
|
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: 122.48 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 59 GEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVV 138
Cdd:cd05959 28 GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 139 SAQHSARWAS----SSCHVVTL-----SEASIGQLTVEDDLPGFS------AT-PGNAAYVLFTSGSTGIPKGVVLEHRA 202
Cdd:cd05959 108 SGELAPVLAAaltkSEHTLVVLivsggAGPEAGALLLAELVAAEAeqlkpaAThADDPAFWLYSSGSTGRPKGVVHLHAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 203 VSTSCLGHGR-AFGITDQSRVLQ----FTSYTFD----FCMAEIITTLLYGGcicvpsdRDRHSDLAKAINTMganwall 273
Cdd:cd05959 188 IYWTAELYARnVLGIREDDVCFSaaklFFAYGLGnsltFPLSVGATTVLMPE-------RPTPAAVFKRIRRY------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 274 TPSV--------AQLLNPSDVP-----TLKILVIGGEQVTSKDWNRWPT--SVQLINGYGPTECC-IVCTgyTTTQAFKT 337
Cdd:cd05959 254 RPTVffgvptlyAAMLAAPNLPsrdlsSLRLCVSAGEALPAEVGERWKArfGLDILDGIGSTEMLhIFLS--NRPGRVRY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 338 GTIGTAIASVSWVVDPEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFiedpawlvdgcQGYagrrgrLYKTGDL 417
Cdd:cd05959 332 GTTGKPVPGYEVELRDEDGGDVAD-GEPGELYVRGPSSATMYWNNRDKTRDTF-----------QGE------WTRTGDK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 418 VRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQG--CMPEANQIAVE-----------VILLEGEKSNTILAAFLQL 484
Cdd:cd05959 394 YVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQhpAVLEAAVVGVEdedgltkpkafVVLRPGYEDSEALEEELKE 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1779949166 485 DVKtgrafptnkaaetgslaqvifpveagkklaERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd05959 474 FVK------------------------------DRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
62-550 |
3.12e-28 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 119.79 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 62 SYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLdpdHPVSRHKE---ILRQTGARMVVV 138
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFREHElafILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 139 SAqhsaRWASSSchvvtlseasigqltveddlpgFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITD 218
Cdd:cd05903 80 PE----RFRQFD----------------------PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 219 QSRVL------QFTSYTFDFCMAEIITTllyggcicvPSDRDRHSDLAKA---INTMGANWAL-LTPSVAQLLN-----P 283
Cdd:cd05903 134 GDVFLvaspmaHQTGFVYGFTLPLLLGA---------PVVLQDIWDPDKAlalMREHGVTFMMgATPFLTDLLNaveeaG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 284 SDVPTLKILVIGGEQV----TSKDWNRWPTSVqlINGYGPTECCIVCTGYTTTQAFKT-GTIGTAIASVSWVVDPEDYHK 358
Cdd:cd05903 205 EPLSRLRTFVCGGATVprslARRAAELLGAKV--CSAYGSTECPGAVTSITPAPEDRRlYTDGRPLPGVEIKVVDDTGAT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 359 LAPlGSVGELLVEGPILARGYLNDAEKTAAAFIEdpAWlvdgcqgyagrrgrlYKTGDLVRYDDEGNLVCLGRKDSQVKV 438
Cdd:cd05903 283 LAP-GVEGELLSRGPSVFLGYLDRPDLTADAAPE--GW---------------FRTGDLARLDEDGYLRITGRSKDIIIR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 439 RGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQLdvKTGRAFPTNKAAETGSLAQVifpveAGKKLAE 518
Cdd:cd05903 345 GGENIPVLEVEDLLLG-HPGVIEAA--VVALPDERLGERACAVVVT--KSGALLTFDELVAYLDRQGV-----AKQYWPE 414
|
490 500 510
....*....|....*....|....*....|..
gi 1779949166 519 RLpsymvpdvyFVVTQLPITVSGKTDRKRLRE 550
Cdd:cd05903 415 RL---------VHVDDLPRTPSGKVQKFRLRE 437
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1118-1569 |
7.23e-28 |
|
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: 119.20 E-value: 7.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1118 DLFADQAKARPDAPAiCAWDGD-MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDP 1196
Cdd:cd05936 3 DLLEEAARRFPDKTA-LIFMGRkLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1197 SLPHERLRLMCRKvsaklslaSEASAplakdlvgTVVIVNADSALQLAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRI 1276
Cdd:cd05936 82 LYTPRELEHILND--------SGAKA--------LIVAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1277 EHRAASSAVTAHGRYLG--MQASTRTLQ----FASYAFAgslVELLMNLCHGGCIcVLSEEERRTDLASAMCRMKVNW-- 1348
Cdd:cd05936 146 THRNLVANALQIKAWLEdlLEGDDVVLAalplFHVFGLT---VALLLPLALGATI-VLIPRFRPIGVLKEIRKHRVTIfp 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1349 -------AFLTSTVVDLLTPKSVPslsiLCV-GGEPIRASQIVRWG--SQVHLRQTYGSSEVSGIvssaalTTCSTTRDV 1418
Cdd:cd05936 222 gvptmyiALLNAPEFKKRDFSSLR----LCIsGGAPLPVEVAERFEelTGVPIVEGYGLTETSPV------VAVNPLDGP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1419 GRA-STGVFW------IVDPNNHnrLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapAWraslglsagqqrlYKTG 1491
Cdd:cd05936 292 RKPgSIGIPLpgtevkIVDDDGE--ELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVD--GW-------------LRTG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1492 DLARYKDDGSIELIGRKDNQVKLRGQRI---EVEEI--EHQArlaeadVAEIAVELI-QPKDGEdgMLACFIVVEDSAS- 1564
Cdd:cd05936 355 DIGYMDEDGYFFIVDRKKDMIIVGGFNVyprEVEEVlyEHPA------VAEAAVVGVpDPYSGE--AVKAFVVLKEGASl 426
|
....*
gi 1779949166 1565 NEDEL 1569
Cdd:cd05936 427 TEEEI 431
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
49-550 |
7.93e-28 |
|
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: 119.72 E-value: 7.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEM--SYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKE 126
Cdd:cd05926 1 PDAPALVVPGSTPalTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 127 ILRQTGARMVVVS---------AQHSARWA-------SSSCHVVtLSEASIGQLTVEDDLPGFS--ATPGNAAYVLFTSG 188
Cdd:cd05926 81 YLADLGSKLVLTPkgelgpasrAASKLGLAilelaldVGVLIRA-PSAESLSNLLADKKNAKSEgvPLPDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 189 STGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTS-YTFDFCMAEIITTLLYGGCICVPSDRDRH---SDLAKAin 264
Cdd:cd05926 160 TTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPlFHVHGLVASLLSTLAAGGSVVLPPRFSAStfwPDVRDY-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 265 tmGANWALLTPSVAQLL------NPSDV-PTLKILVIGGEQVTSKDWNRWPTS--VQLINGYGPTEccivctgyTTTQAF 335
Cdd:cd05926 238 --NATWYTAVPTIHQILlnrpepNPESPpPKLRFIRSCSASLPPAVLEALEATfgAPVLEAYGMTE--------AAHQMT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 336 ---------KTGTIGTAIASVSWVVDPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPaWLvdgcqgyag 406
Cdd:cd05926 308 snplppgprKPGSVGKPVGVEVRILDEDG--EILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG-WF--------- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 407 rrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCmPEANQIAveVILLEGEKSNTILAAFLQLdv 486
Cdd:cd05926 376 ------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH-PAVLEAV--AFGVPDEKYGEEVAAAVVL-- 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 487 ktgrafptnKAAETGSLAQVIfpveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:cd05926 445 ---------REGASVTEEELR------AFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1141-1570 |
1.50e-27 |
|
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: 117.92 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLASEA 1220
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1221 SAPlakdlvgtvvivnadsalqlahhaspitsvrpthtAYVIFTSGSTGEPKGCRIEHRAassaVTAH--GRYLGMQAST 1298
Cdd:cd05971 88 DDP-----------------------------------ALIIYTSGTTGPPKGALHAHRV----LLGHlpGVQFPFNLFP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1299 RT--LQF--ASYAFAGSLVELLMNLCHGGcICVLSEEERRTDLASA---MCRMKVNWAFLTSTVVDLL----TPKSVPSL 1367
Cdd:cd05971 129 RDgdLYWtpADWAWIGGLLDVLLPSLYFG-VPVLAHRMTKFDPKAAldlMSRYGVTTAFLPPTALKMMrqqgEQLKHAQV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1368 SILCV--GGEPIrASQIVRWGSQ---VHLRQTYGSSEVSGIVSSAALTTCSTTRDVGRASTG-VFWIVDpNNHNRLAPvG 1441
Cdd:cd05971 208 KLRAIatGGESL-GEELLGWAREqfgVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGhRVAIVD-DNGTPLPP-G 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1442 AVGEVLVE--GPVLGREYIDEPDKTASTFieAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI 1519
Cdd:cd05971 285 EVGEIAVElpDPVAFLGYWNNPSATEKKM--AGDW-------------LLTGDLGRKDSDGYFWYVGRDDDVITSSGYRI 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 1520 EVEEIEHqARLAEADVAEIAVELI-QPKDGEdgMLACFIVVEDSASNEDELS 1570
Cdd:cd05971 350 GPAEIEE-CLLKHPAVLMAAVVGIpDPIRGE--IVKAFVVLNPGETPSDALA 398
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1093-1559 |
5.32e-27 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 117.85 E-value: 5.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1093 LTPEDRQQ-----LWewnHDvppaieRCIHDLFADQAKARPDAPAICAWDGD------MTYGELDVLSGRLAGHLVELGV 1161
Cdd:PRK13295 7 LLPPRRAAsiaagHW---HD------RTINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1162 GPEDIVPlCFEKSMWTVVAM-LAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLAS--------EASA----PLAKDL 1228
Cdd:PRK13295 78 GRGDVVS-CQLPNWWEFTVLyLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPktfrgfdhAAMArrlrPELPAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1229 vGTVVIVNADSALQLAHHAS------------PITSVR--PTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGM 1294
Cdd:PRK13295 157 -RHVVVVGGDGADSFEALLItpaweqepdapaILARLRpgPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1295 QASTRTLQFASYAF-AGSLVELLMNLCHGGCIcVLSEEERRTDLASAMCRMKVNW-----AFLT--STVVDlLTPKSVPS 1366
Cdd:PRK13295 236 GADDVILMASPMAHqTGFMYGLMMPVMLGATA-VLQDIWDPARAAELIRTEGVTFtmastPFLTdlTRAVK-ESGRPVSS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1367 LSILCVGGEPIRASQIVRwgsqvhLRQTYGSSEVS--GIVSSAALTTCSTTRDVGRAST--GVFW------IVDPNNHNr 1436
Cdd:PRK13295 314 LRTFLCAGAPIPGALVER------ARAALGAKIVSawGMTENGAVTLTKLDDPDERASTtdGCPLpgvevrVVDADGAP- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1437 lAPVGAVGEVLVEGPVLGREYIDEPDKTAStfiEAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGR-KDnqVKLR 1515
Cdd:PRK13295 387 -LPAGQIGRLQVRGCSNFGGYLKRPQLNGT---DADGW-------------FDTGDLARIDADGYIRISGRsKD--VIIR 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1779949166 1516 G-QRIEVEEIEhQARLAEADVAEIAVelIQPKDGEDGMLACFIVV 1559
Cdd:PRK13295 448 GgENIPVVEIE-ALLYRHPAIAQVAI--VAYPDERLGERACAFVV 489
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1116-1569 |
5.67e-27 |
|
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: 117.08 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLD 1195
Cdd:cd05959 6 ATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1196 PSLPHERLRLMCRKVSAKLSLASEASAPLAKDLVGT------VVIV-----NADSALQLAH---HASPITSVRPTHT--- 1258
Cdd:cd05959 86 TLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKsehtlvVLIVsggagPEAGALLLAElvaAEAEQLKPAATHAddp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1259 AYVIFTSGSTGEPKGcrIEHRAAS---SAVTAHGRYLGMQA-----STRTLQFAsYAFAGSLVELLMNlchgGCICVLSE 1330
Cdd:cd05959 166 AFWLYSSGSTGRPKG--VVHLHADiywTAELYARNVLGIREddvcfSAAKLFFA-YGLGNSLTFPLSV----GATTVLMP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1331 EERRTDL-ASAMCRMKVNWAFLTSTVVDLLT-----PKSVPSLSILCV-GGEPIRASQIVRWgsqvhlRQTYGSSEVSGI 1403
Cdd:cd05959 239 ERPTPAAvFKRIRRYRPTVFFGVPTLYAAMLaapnlPSRDLSSLRLCVsAGEALPAEVGERW------KARFGLDILDGI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1404 VSSAALTT-CSTT-RDVGRASTGV------FWIVDPNNHNrlAPVGAVGEVLVEGPVLGREYIDEPDKTASTFieapawr 1475
Cdd:cd05959 313 GSTEMLHIfLSNRpGRVRYGTTGKpvpgyeVELRDEDGGD--VADGEPGELYVRGPSSATMYWNNRDKTRDTF------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1476 aslglsagQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVELIQPKDGEDGMLAc 1555
Cdd:cd05959 384 --------QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVE-SALVQHPAVLEAAVVGVEDEDGLTKPKA- 453
|
490
....*....|....*...
gi 1779949166 1556 FIVV----EDSASNEDEL 1569
Cdd:cd05959 454 FVVLrpgyEDSEALEEEL 471
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
62-453 |
8.88e-27 |
|
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: 117.00 E-value: 8.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 62 SYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLD--PDHPVSRHK--------EILRQ- 130
Cdd:cd05906 41 SYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvpPTYDEPNARlrklrhiwQLLGSp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 131 ---TGARMVVVSAQHSARWASSSCHVVTLSEASigqlTVEDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSC 207
Cdd:cd05906 121 vvlTDAELVAEFAGLETLSGLPGIRVLSIEELL----DTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 208 LGHGRAFGITDQSRVLQFTSytFDFCMAEIITTL--LYGGC--ICVPSDR------------DRHsdlaKAINTMGANWA 271
Cdd:cd05906 197 AGKIQHNGLTPQDVFLNWVP--LDHVGGLVELHLraVYLGCqqVHVPTEEiladplrwldliDRY----RVTITWAPNFA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 272 --LLTPSVAQLLNPS-DVPTLKILVIGGEQVTSKdwnrwpTSVQLIN--------------GYGPTECC------IVCTG 328
Cdd:cd05906 271 faLLNDLLEEIEDGTwDLSSLRYLVNAGEAVVAK------TIRRLLRllepyglppdairpAFGMTETCsgviysRSFPT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 329 YTTTQAFKTGTIGTAIASVSW-VVDPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpAWlvdgcqgyagr 407
Cdd:cd05906 345 YDHSQALEFVSLGRPIPGVSMrIVDDEG--QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED-GW----------- 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1779949166 408 rgrlYKTGDLVrYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQ 453
Cdd:cd05906 411 ----FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVE 451
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
181-562 |
1.10e-26 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 119.26 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 181 AYVLFTSGSTGIPKGVVLEHR-------AVSTsclghgrAFGITDQSRVLQ----FTSYTFdfcmaeIITT---LLYG-G 245
Cdd:PRK08633 785 ATIIFSSGSEGEPKGVMLSHHnilsnieQISD-------VFNLRNDDVILSslpfFHSFGL------TVTLwlpLLEGiK 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 246 CICVPSDRDRHSdLAKAINTMGANWALLTPSVAQL------LNPSDVPTLKILVIGGEQVTS--KDWNRWPTSVQLINGY 317
Cdd:PRK08633 852 VVYHPDPTDALG-IAKLVAKHRATILLGTPTFLRLylrnkkLHPLMFASLRLVVAGAEKLKPevADAFEEKFGIRILEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 318 GPTECCIV---------CTGYTTTQAFKTGTIGTAIASVSW-VVDPEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTA 387
Cdd:PRK08633 931 GATETSPVasvnlpdvlAADFKRQTGSKEGSVGMPLPGVAVrIVDPETFEELPP-GEDGLILIGGPQVMKGYLGDPEKTA 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 388 AAFIEdpawlVDGCqgyagrrgRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCMPEANQIAVeVI 467
Cdd:PRK08633 1010 EVIKD-----IDGI--------GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFA-VT 1075
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 468 LLEGEKSNTILAAFLqldvktgrafpTNKAAETGSLAQVIfpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKR 547
Cdd:PRK08633 1076 AVPDEKKGEKLVVLH-----------TCGAEDVEELKRAI--------KESGLPNLWKPSRYFKVEALPLLGSGKLDLKG 1136
|
410
....*....|....*
gi 1779949166 548 LREIgasfsAQQLAE 562
Cdd:PRK08633 1137 LKEL-----ALALLG 1146
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1116-1540 |
1.59e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 116.05 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLD 1195
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1196 PSLPHERLRLMCRKVSAKLSLASEASAPLAKDL------VGTVVIVNADSALQL---AHHASPITSVRPTH--------- 1257
Cdd:PRK06187 88 IRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAIlpqlptVRTVIVEGDGPAAPLapeVGEYEELLAAASDTfdfpdiden 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1258 TAYVIF-TSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLseeeRRTD 1336
Cdd:PRK06187 168 DAAAMLyTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIP----RRFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1337 lASAMCRM----KVNWAFLTSTVV-DLLT-----PKSVPSLSILCVGGEPIRASQIVRWGSQVH--LRQTYGSSEVSGIV 1404
Cdd:PRK06187 244 -PENLLDLieteRVTFFFAVPTIWqMLLKaprayFVDFSSLRLVIYGGAALPPALLREFKEKFGidLVQGYGMTETSPVV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1405 SSAALTTCSTTRDVGRASTGVFW------IVDPNNhNRLAPVG-AVGEVLVEGPVLGREYIDEPDKTASTFieAPAWras 1477
Cdd:PRK06187 323 SVLPPEDQLPGQWTKRRSAGRPLpgvearIVDDDG-DELPPDGgEVGEIIVRGPWLMQGYWNRPEATAETI--DGGW--- 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 1478 lglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI---EVEEI--EHqarlaeADVAEIAV 1540
Cdd:PRK06187 397 ----------LHTGDVGYIDEDGYLYITDRIKDVIISGGENIyprELEDAlyGH------PAVAEVAV 448
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1090-1524 |
2.46e-26 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 115.62 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1090 IDTLT-PEDRQQLWE----WNhdvppaiERCIHDLFADQAKARPDAPAICAWDG-DMTYGELDVLSGRLAGHLVELGVGP 1163
Cdd:PRK06087 1 KVTLTfNEQRRAAYRqqgyWG-------DASLADYWQQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1164 EDIVplCFEKSMWT--VVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLA---------SEASAPLAKDL--VG 1230
Cdd:PRK06087 74 GDRV--AFQLPGWCefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkqtrpVDLILPLQNQLpqLQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1231 TVVIVN----ADSALQLAH---HASPITSVRPTHT---AYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRT 1300
Cdd:PRK06087 152 QIVGVDklapATSSLSLSQiiaDYEPLTTAITTHGdelAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1301 LQFASYAFA-GSLVELLMNLCHGGCIcVLSEEERRTDLASAMCRMKVNWAF-LTSTVVDLLT-----PKSVPSLSILCVG 1373
Cdd:PRK06087 232 MMPAPLGHAtGFLHGVTAPFLIGARS-VLLDIFTPDACLALLEQQRCTCMLgATPFIYDLLNllekqPADLSALRFFLCG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1374 GEPIrASQIVR--WGSQVHLRQTYGSSEVS--GIVSSAALTTCSTTRDvGRASTGV-FWIVDpNNHNRLAPvGAVGEVLV 1448
Cdd:PRK06087 311 GTTI-PKKVARecQQRGIKLLSVYGSTESSphAVVNLDDPLSRFMHTD-GYAAAGVeIKVVD-EARKTLPP-GCEGEEAS 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 1449 EGPVLGREYIDEPDKTASTfIEAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI---EVEEI 1524
Cdd:PRK06087 387 RGPNVFMGYLDEPELTARA-LDEEGW-------------YYSGDLCRMDEAGYIKITGRKKDIIVRGGENIssrEVEDI 451
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1116-1569 |
5.11e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 114.23 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLD 1195
Cdd:PRK07656 7 LPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1196 PSLPHERLRLMCRKVSAKLSLASEA------SAPLAKDLVGTVVIVNADSALQ-----------LAHHASPITS--VRPT 1256
Cdd:PRK07656 87 TRYTADEAAYILARGDAKALFVLGLflgvdySATTRLPALEHVVICETEEDDPhtekmktftdfLAAGDPAERApeVDPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1257 HTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQ----FASYAFAGSLVELLMNlchGGCICVLS--- 1329
Cdd:PRK07656 167 DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAanpfFHVFGYKAGVNAPLMR---GATILPLPvfd 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1330 --------EEERRTDLAS--AMcrmkvnWAFLtstvvdLLTPKSVP----SLSILCVGGEPIRASQIVRwgsqvhLRQT- 1394
Cdd:PRK07656 244 pdevfrliETERITVLPGppTM------YNSL------LQHPDRSAedlsSLRLAVTGAASMPVALLER------FESEl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1395 --------YGSSEVSGIVssaalTTCSTTRD-------VGRASTGV-FWIVDPnnHNRLAPVGAVGEVLVEGPVLGREYI 1458
Cdd:PRK07656 306 gvdivltgYGLSEASGVT-----TFNRLDDDrktvagtIGTAIAGVeNKIVNE--LGEEVPVGEVGELLVRGPNVMKGYY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1459 DEPDKTASTfIEAPAWraslglsagqqrLYkTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEI 1538
Cdd:PRK07656 379 DDPEATAAA-IDADGW------------LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVE-EVLYEHPAVAEA 443
|
490 500 510
....*....|....*....|....*....|....*
gi 1779949166 1539 AVelIQPKD---GEDGmlACFIVVEDSAS-NEDEL 1569
Cdd:PRK07656 444 AV--IGVPDerlGEVG--KAYVVLKPGAElTEEEL 474
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1141-1562 |
6.74e-26 |
|
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: 114.15 E-value: 6.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMcrkvsakLSLASEA 1220
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIY-------LGVAKPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1221 saplakdlvGTVVIVNADsalqlahhaspiTSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRT 1300
Cdd:cd17647 95 ---------GLIVIRAAG------------VVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1301 LQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTD--LASAMCRMKVNWAFLTSTVVDLLTPKSV---PSLSILCVGGE 1375
Cdd:cd17647 154 TMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPgrLAEWMAKYGATVTHLTPAMGQLLTAQATtpfPKLHHAFFVGD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1376 PIRASQIVRWGS---QVHLRQTYGSSEVSGIVSSAALTTCSTT-------RDVGRASTGV----FWIVDPNNHNRLAPVG 1441
Cdd:cd17647 234 ILTKRDCLRLQTlaeNVRIVNMYGTTETQRAVSYFEVPSRSSDptflknlKDVMPAGRGMlnvqLLVVNRNDRTQICGIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1442 AVGEVLVEGPVLGREYIDEPDKTASTFI-----------------EAPaWRA-SLGLsagQQRLYKTGDLARYKDDGSIE 1503
Cdd:cd17647 314 EVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvepdhwnyldkdnNEP-WRQfWLGP---RDRLYRTGDLGRYLPNGDCE 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 1504 LIGRKDNQVKLRGQRIEVEEIEhqARLAEADVAEIAVELIQPKDGEDGMLACFIVVEDS 1562
Cdd:cd17647 390 CCGRADDQVKIRGFRIELGEID--THISQHPLVRENITLVRRDKDEEPTLVSYIVPRFD 446
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
62-549 |
7.38e-26 |
|
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: 112.43 E-value: 7.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 62 SYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAP----LDPDHPVSRhkeiLRQTGARMVV 137
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPlttlLGPKDIEYR----LEAAGAKAIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 138 VSAQhsarwassschvvtlseasigqltveddlpgfsatpgNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGIT 217
Cdd:cd05972 78 TDAE-------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 218 DQSRVL--------QFTSYTFDFCMAEIITTLLYGGcicVPSDRDRHSDLAK--AINTMGANWALLTPSVAQLLNPSDVP 287
Cdd:cd05972 121 PDDIHWniadpgwaKGAWSSFFGPWLLGATVFVYEG---PRFDAERILELLEryGVTSFCGPPTAYRMLIKQDLSSYKFS 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 288 TLKILVIGGEQVTSKDWNRW--PTSVQLINGYGPTECCIVCtGYTTTQAFKTGTIGTAIASVSWVVDPEDYHKLAPlGSV 365
Cdd:cd05972 198 HLRLVVSAGEPLNPEVIEWWraATGLPIRDGYGQTETGLTV-GNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPP-GEE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 366 GELLVE-GPI-LARGYLNDAEKTAAAFiedpawlvdgcqgyagrRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQR- 442
Cdd:cd05972 276 GDIAIKlPPPgLFLGYVGDPEKTEASI-----------------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRi 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 443 ----VELGEIEHhiqgcmPEANQIAV-----EVIlleGEksntILAAFLqldVKTGRAFPTNKAAEtgslaqvifpvEAG 513
Cdd:cd05972 339 gpfeVESALLEH------PAVAEAAVvgspdPVR---GE----VVKAFV---VLTSGYEPSEELAE-----------ELQ 391
|
490 500 510
....*....|....*....|....*....|....*.
gi 1779949166 514 KKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd05972 392 GHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1141-1564 |
9.61e-26 |
|
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: 112.47 E-value: 9.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKlslasea 1220
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1221 saplakdlvgtvVIVNADSALQLAHHAspitsvRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRT 1300
Cdd:cd05903 76 ------------VFVVPERFRQFDPAA------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1301 LQFASYA-FAGSLVELLMNLCHGGCICVLS-----------EEERRTDLASAMcrmkvnwAFLTSTV-VDLLTPKSVPSL 1367
Cdd:cd05903 138 LVASPMAhQTGFVYGFTLPLLLGAPVVLQDiwdpdkalalmREHGVTFMMGAT-------PFLTDLLnAVEEAGEPLSRL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1368 SILCVGGEPIRASqIVRWGSQV---HLRQTYGSSEVSGIVSSA--ALTTCSTTRDvGRASTGVFWIVDPNNHNRLAPvGA 1442
Cdd:cd05903 211 RTFVCGGATVPRS-LARRAAELlgaKVCSAYGSTECPGAVTSItpAPEDRRLYTD-GRPLPGVEIKVVDDTGATLAP-GV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1443 VGEVLVEGPVLGREYIDEPDKTASTFIEapAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVE 1522
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRPDLTADAAPE--GW-------------FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVL 352
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1779949166 1523 EIEhQARLAEADVAEIAVelIQPKDGEDGMLAC-FIVVEDSAS 1564
Cdd:cd05903 353 EVE-DLLLGHPGVIEAAV--VALPDERLGERACaVVVTKSGAL 392
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
60-549 |
1.06e-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: 112.14 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 60 EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPdhpvsrhkeILRQTGARMvvvs 139
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFA---------LFGPEALEY---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 140 aqhsaRWASSSCHVVTLSEAsigqltveDDLpgfsatpgnaAYVLFTSGSTGIPKGVVLEHRAVstscLGHgrafgitdq 219
Cdd:cd05971 73 -----RLSNSGASALVTDGS--------DDP----------ALIIYTSGTTGPPKGALHAHRVL----LGH--------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 220 SRVLQFTSYTF---DFCM------AEI-------ITTLLYGgcICVPSDRDRHSDlAKAINTMGANW----ALLTPSVAQ 279
Cdd:cd05971 117 LPGVQFPFNLFprdGDLYwtpadwAWIgglldvlLPSLYFG--VPVLAHRMTKFD-PKAALDLMSRYgvttAFLPPTALK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 280 LLNPSDVPT------LKILVIGGEQVTSKD--WNRWPTSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAI-ASVSWV 350
Cdd:cd05971 194 MMRQQGEQLkhaqvkLRAIATGGESLGEELlgWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIpGHRVAI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 351 VDPEDYHklAPLGSVGELLVE--GPILARGYLNDAEKTAAAFIEDpaWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVC 428
Cdd:cd05971 274 VDDNGTP--LPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD--WL---------------LTGDLGRKDSDGYFWY 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 429 LGRKDSQVKVRGQRVELGEIEHhiqgCMPEANQIA-VEVILLEGEKSNTILAAFLQLdvktgrafptnKAAETGS--LAQ 505
Cdd:cd05971 335 VGRDDDVITSSGYRIGPAEIEE----CLLKHPAVLmAAVVGIPDPIRGEIVKAFVVL-----------NPGETPSdaLAR 399
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1779949166 506 vifpvEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd05971 400 -----EIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
689-1081 |
2.85e-25 |
|
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: 110.60 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 689 IYPCSPLQEGMM---ALASKrpGD-YIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSskmGM---LQVVL--A 759
Cdd:cd19544 1 IYPLAPLQEGILfhhLLAEE--GDpYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWE---GLsepVQVVWrqA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 760 D-GIEW----EQANELEQYLEK--DKSVSMGLGDS-LARYALVRDVGTGKRWMVWTLHHALYDGWSLpQIanLVTEV--- 828
Cdd:cd19544 76 ElPVEEltldPGDDALAQLRARfdPRRYRLDLRQApLLRAHVAEDPANGRWLLLLLFHHLISDHTSL-EL--LLEEIqai 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 829 --YHGAEVGKQPGFNAFIKY-LGEQDHEAAAAYWQGTLADcqaISFPALP---PAVQQ---PVADATTAFQcPALARRPS 899
Cdd:cd19544 153 laGRAAALPPPVPYRNFVAQaRLGASQAEHEAFFREMLGD---VDEPTAPfglLDVQGdgsDITEARLALD-AELAQRLR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 900 D------ITMSTLIRAAWALLASSYTSSDDVVFGaTV-TGRNAPVAGIEAMAGPTIATVPVRVRVQHShKVSEFLHSVQQ 972
Cdd:cd19544 229 AqarrlgVSPASLFHLAWALVLARCSGRDDVVFG-TVlSGRMQGGAGADRALGMFINTLPLRVRLGGR-SVREAVRQTHA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 973 QATEMIPYEQTGLhetakvsADArHACS--------FQTLLIV--QPGSNGDIAHDALGEWRSHSDlQDFTTYALMVqCV 1042
Cdd:cd19544 307 RLAELLRHEHASL-------ALA-QRCSgvpaptplFSALLNYrhSAAAAAAAALAAWEGIELLGG-EERTNYPLTL-SV 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1779949166 1043 laDD-------EVQIIASfdrraIEPWQVDKMLRQfsfVMQQLATA 1081
Cdd:cd19544 377 --DDlgdgfslTAQVVAP-----IDAERVCAYMET---ALEQLVDA 412
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1118-1593 |
6.39e-25 |
|
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: 110.49 E-value: 6.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1118 DLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIV----PLCFEksmwTVVAMLAVLKAGGAFLL 1193
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVvvqlPNVAE----FVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1194 LDPSLPHERLRLMCRKVSAKLSLASEASAPLAkdlvgtvvivNADSALQLAH-HASPitsvrpthtAYVIFTSGSTGEPK 1272
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIVPDRHAGFD----------HRALARELAEsIPEV---------ALFLLSGGTTGTPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1273 GCRIEHRAASSAVTAHGRYLGMQASTRTLQF--ASYAFAGSLVELLMNLCHGGCIcVLSEEERRTDLASAMCRMKVNWAF 1350
Cdd:cd05920 156 LIPRTHNDYAYNVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRV-VLAPDPSPDAAFPLIEREGVTVTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1351 LTSTVVDLLT------PKSVPSLSILCVGGEPIRASQIVRWGSQ--VHLRQTYGSSEvsGIVSSAAL-----TTCSTTrd 1417
Cdd:cd05920 235 LVPALVSLWLdaaasrRADLSSLRLLQVGGARLSPALARRVPPVlgCTLQQVFGMAE--GLLNYTRLddpdeVIIHTQ-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1418 vGR--ASTGVFWIVDPnnHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapawraslglsagqQRLYKTGDLAR 1495
Cdd:cd05920 311 -GRpmSPDDEIRVVDE--EGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP--------------DGFYRTGDLVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1496 YKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQARL--AEADVAEIAVEliqpkDGEDGMLAC-FIVVEDSASNEDELsgk 1572
Cdd:cd05920 374 RTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRhpAVHDAAVVAMP-----DELLGERSCaFVVLRDPPPSAAQL--- 445
|
490 500
....*....|....*....|...
gi 1779949166 1573 RTRLdtrTQRTIG--KIQDRLER 1593
Cdd:cd05920 446 RRFL---RERGLAayKLPDRIEF 465
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
39-550 |
6.41e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 111.63 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 39 DLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDP- 117
Cdd:PRK05605 36 DLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 118 ------DHPVSRHK--------------EILRQTGARMVVVSAQHSA------RWA----------------SSSCHVV- 154
Cdd:PRK05605 116 ytahelEHPFEDHGarvaivwdkvaptvERLRRTTPLETIVSVNMIAampllqRLAlrlpipalrkaraaltGPAPGTVp 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 155 --TLSEASIGQLTVEDDLPgfSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLgHGRAF--GITDQ-SRVLQ----F 225
Cdd:PRK05605 196 weTLVDAAIGGDGSDVSHP--RPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAA-QGKAWvpGLGDGpERVLAalpmF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 226 TSYTFDFCMAeiittllyggcicvpsdrdrhsdLAKAIntmGANWALL-TPSVAQLLN------PS---DVPTL--KILV 293
Cdd:PRK05605 273 HAYGLTLCLT-----------------------LAVSI---GGELVLLpAPDIDLILDamkkhpPTwlpGVPPLyeKIAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 294 IGGEQ-------------------VTSKDWNRwPTSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVSW-VVDP 353
Cdd:PRK05605 327 AAEERgvdlsgvrnafsgamalpvSTVELWEK-LTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVrIVDP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 354 EDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpaWlvdgcqgyagrrgrlYKTGDLVRYDDEGNLVCLGRKD 433
Cdd:PRK05605 406 EDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--W---------------FRTGDVVVMEEDGFIRIVDRIK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 434 SQVKVRGQRVELGEIEHHIQGcMPEANQIAVeVILLEGEKSNTILAAFLqldVKTGRAFPtnkaaetgslaqvifpvEAG 513
Cdd:PRK05605 469 ELIITGGFNVYPAEVEEVLRE-HPGVEDAAV-VGLPREDGSEEVVAAVV---LEPGAALD-----------------PEG 526
|
570 580 590
....*....|....*....|....*....|....*....
gi 1779949166 514 KK--LAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:PRK05605 527 LRayCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
690-1079 |
6.88e-25 |
|
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: 109.42 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 690 YPCSPLQEGMMAL--ASKRPGDYIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKmGMLQVVLAD------- 760
Cdd:cd19066 2 IPLSPMQRGMWFLkkLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAG-RYEQVVLDKtvrfrie 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 761 ----GIEWEQANELEQYLEKDKSVSMGL-GDSLARYALVRDVGTGKRWmVWTLHHALYDGWSLPQIANLVTEVYHGAEVG 835
Cdd:cd19066 81 iidlRNLADPEARLLELIDQIQQTIYDLeRGPLVRVALFRLADERDVL-VVAIHHIIVDGGSFQILFEDISSVYDAAERQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 836 KQ---PGFNAFI-------KYLGEQDHEAAAAYWQGTLAD-CQAISFPALPPAVQQPVADATTAFQC--PALARRPSDI- 901
Cdd:cd19066 160 KPtlpPPVGSYAdyaawleKQLESEAAQADLAYWTSYLHGlPPPLPLPKAKRPSQVASYEVLTLEFFlrSEETKRLREVa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 902 -----TMSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPvaGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATE 976
Cdd:cd19066 240 resgtTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 977 MIP----YEQTGLHETAKVSADARHAcSFQTLLIVQpgsNGDIAHDALGEWRshSDLQDFTT-----YALMVQCV-LADD 1046
Cdd:cd19066 318 AIEhqrvPFIELVRHLGVVPEAPKHP-LFEPVFTFK---NNQQQLGKTGGFI--FTTPVYTSsegtvFDLDLEASeDPDG 391
|
410 420 430
....*....|....*....|....*....|...
gi 1779949166 1047 EVQIIASFDRRAIEPWQVDKMLRQFSFVMQQLA 1079
Cdd:cd19066 392 DLLLRLEYSRGVYDERTIDRFAERYMTALRQLI 424
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1114-1569 |
1.52e-24 |
|
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: 109.52 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1114 RCIHDLFADQAKARPDAPAICAWDGD--MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAF 1191
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1192 LLLDPSLPHERLRL------MCRKVSAKLSLASEASAplakDLVGTVVIVNADSALQLAHHASPIT---SVRPTHTAYVI 1262
Cdd:cd05923 81 ALINPRLKAAELAEliergeMTAAVIAVDAQVMDAIF----QSGVRVLALSDLVGLGEPESAGPLIedpPREPEQPAFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1263 FTSGSTGEPKGCRIEHRAASSAVTA-----------HGRYLGMQASTRTLQFASYafagslveLLMNLCHGGCICVLsEE 1331
Cdd:cd05923 157 YTSGTTGLPKGAVIPQRAAESRVLFmstqaglrhgrHNVVLGLMPLYHVIGFFAV--------LVAALALDGTYVVV-EE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1332 ERRTDLASAMCRMKVNWAFLTSTVVDLL------TPKSVPSLSILCVGGEPIRASQIVRWGSQVHLRQT--YGSSEVSGI 1403
Cdd:cd05923 228 FDPADALKLIEQERVTSLFATPTHLDALaaaaefAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVniYGTTEAMNS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1404 VSSAALTTCSTTRDVGRASTGVFWIVDPNNHnrLAPVGAVGEVLV--EGPVLGREYIDEPDKTASTFieapawraslgls 1481
Cdd:cd05923 308 LYMRDARTGTEMRPGFFSEVRIVRIGGSPDE--ALANGEEGELIVaaAADAAFTGYLNQPEATAKKL------------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1482 agQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQARLAeADVAEIAVelIQPKDGEDG--MLACFIVV 1559
Cdd:cd05923 373 --QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRH-PGVTEVVV--IGVADERWGqsVTACVVPR 447
|
490
....*....|
gi 1779949166 1560 EDSASnEDEL 1569
Cdd:cd05923 448 EGTLS-ADEL 456
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
47-458 |
1.55e-24 |
|
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: 110.02 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 47 AQPNAPAICAWDGE------MSYSVLDGLSTKLAGYLVKIGvKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHP 120
Cdd:cd05931 5 ARPDRPAYTFLDDEggreetLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 121 vSRHKE----ILRQTGARMVVVSAQHSA---RWASSSCHVVTLSEASIGQLTVE--DDLPGFSATPGNAAYVLFTSGSTG 191
Cdd:cd05931 84 -GRHAErlaaILADAGPRVVLTTAAALAavrAFAASRPAAGTPRLLVVDLLPDTsaADWPPPSPDPDDIAYLQYTSGSTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 192 IPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICV---PSD--RDRHSDLaKAINTM 266
Cdd:cd05931 163 TPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVlmsPAAflRRPLRWL-RLISRY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 267 GANWalltpSVA-----QL---------LNPSDVPTLKILVIGGEQVTSKDWNRW----------PTSVQliNGYGPTEC 322
Cdd:cd05931 242 RATI-----SAApnfayDLcvrrvrdedLEGLDLSSWRVALNGAEPVRPATLRRFaeafapfgfrPEAFR--PSYGLAEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 323 CIVCTGYTTTQAFKT------------------GTIGTAIASVSWV--------VDPEDyHKLAPLGSVGELLVEGPILA 376
Cdd:cd05931 315 TLFVSGGPPGTGPVVlrvdrdalagravavaadDPAARELVSCGRPlpdqevriVDPET-GRELPDGEVGEIWVRGPSVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 377 RGYLNDAEKTAAAFIEDPawlvdgcqgyAGRRGRLYKTGDL-VRYDDEgnLVCLGRKDSQVKVRGQRVELGEIEHHIQGC 455
Cdd:cd05931 394 SGYWGRPEATAETFGALA----------ATDEGGWLRTGDLgFLHDGE--LYITGRLKDLIIVRGRNHYPQDIEATAEEA 461
|
...
gi 1779949166 456 MPE 458
Cdd:cd05931 462 HPA 464
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1139-1540 |
4.03e-24 |
|
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: 107.68 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1139 DMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLAS 1218
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1219 EasaplakdlvgtvvivnadsalqlahhaspitsvrPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQAST 1298
Cdd:cd05907 85 D-----------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1299 RTLQF--ASYAFAGSLVELLMnLCHGGCICVLSEEER-RTDLA------------------SAMCRMKVNWafLTSTVVD 1357
Cdd:cd05907 130 RHLSFlpLAHVFERRAGLYVP-LLAGARIYFASSAETlLDDLSevrptvflavprvwekvyAAIKVKAVPG--LKRKLFD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1358 LLtpkSVPSLSILCVGGEPIRASqIVRW--GSQVHLRQTYGSSEVSGIVssaaltTCSTTRDVGRASTGvfwIVDPNNHN 1435
Cdd:cd05907 207 LA---VGGRLRFAASGGAPLPAE-LLHFfrALGIPVYEGYGLTETSAVV------TLNPPGDNRIGTVG---KPLPGVEV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1436 RLAPVGavgEVLVEGPVLGREYIDEPDKTASTFiEAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLR 1515
Cdd:cd05907 274 RIADDG---EILVRGPNVMLGYYKNPEATAEAL-DADGW-------------LHTGDLGEIDEDGFLHITGRKKDLIITS 336
|
410 420
....*....|....*....|....*.
gi 1779949166 1516 -GQRIEVEEIEHQARLAEAdVAEIAV 1540
Cdd:cd05907 337 gGKNISPEPIENALKASPL-ISQAVV 361
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1148-1550 |
5.00e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 107.53 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1148 LSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGA----FLLLDPSLPHERLRLMCRKVSAKLSLASEAsap 1223
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1224 lAKDLVGTVVIVNAD-----SALQLAHHASPITSVRPTH--TAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQA 1296
Cdd:cd05922 79 -AADRLRDALPASPDpgtvlDADGIRAARASAPAHEVSHedLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1297 STRTLQFASYAFAGSLVELLMNLCHGGCIcVLSE---------EERRTDLASAMCRMKVNWAFLTSTVVDlltPKSVPSL 1367
Cdd:cd05922 158 DDRALTVLPLSYDYGLSVLNTHLLRGATL-VLTNdgvlddafwEDLREHGATGLAGVPSTYAMLTRLGFD---PAKLPSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1368 SILCVGGEPIRASQIVRW-----GSQVHLrqTYGSSEvsgivSSAALTTCSTTR------DVGRASTGVFWIVDPNNHNR 1436
Cdd:cd05922 234 RYLTQAGGRLPQETIARLrellpGAQVYV--MYGQTE-----ATRRMTYLPPERilekpgSIGLAIPGGEFEILDDDGTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1437 LAPvGAVGEVLVEGPVLGREYIDepdktastfieAPAWRASLGLSAGqqRLYkTGDLARYKDDGSIELIGRKDNQVKLRG 1516
Cdd:cd05922 307 TPP-GEPGEIVHRGPNVMKGYWN-----------DPPYRRKEGRGGG--VLH-TGDLARRDEDGFLFIVGRRDRMIKLFG 371
|
410 420 430
....*....|....*....|....*....|....
gi 1779949166 1517 QRIEVEEIEHQARlAEADVAEIAVELIQPKDGED 1550
Cdd:cd05922 372 NRISPTEIEAAAR-SIGLIIEAAAVGLPDPLGEK 404
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
35-562 |
8.55e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 107.94 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 35 KCIHDLFAEQVLAQPNAPAICA--WDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVV----PLCFEksmWTVVAMlAVLKA 108
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVgiwaPNCAE---WLLTQF-ATARI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 109 GGAFAPLDPDHPVSRHKEILRQTGARMVVVSAqhsaRWASSSCHVV------TLSEASIGQLTVED-------------D 169
Cdd:PRK12583 94 GAILVNINPAYRASELEYALGQSGVRWVICAD----AFKTSDYHAMlqellpGLAEGQPGALACERlpelrgvvslapaP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 170 LPGFSA-----------------------TPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLqfT 226
Cdd:PRK12583 170 PPGFLAwhelqargetvsrealaerqaslDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLC--V 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 227 SYTFDFCMAEIITTLL---YGGCICVPSDRDRHSDLAKAINTMGAN--WALLTPSVAQLLNPS----DVPTLKILVIGGE 297
Cdd:PRK12583 248 PVPLYHCFGMVLANLGcmtVGACLVYPNEAFDPLATLQAVEEERCTalYGVPTMFIAELDHPQrgnfDLSSLRTGIMAGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 298 ----QVTSKDWNRWPTSVQLInGYGPTECCIVC--TGYTTTQAFKTGTIGTAIASV-SWVVDPEDyhKLAPLGSVGELLV 370
Cdd:PRK12583 328 pcpiEVMRRVMDEMHMAEVQI-AYGMTETSPVSlqTTAADDLERRVETVGRTQPHLeVKVVDPDG--ATVPRGEIGELCT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 371 EGPILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEH 450
Cdd:PRK12583 405 RGYSVMKGYWNNPEATAESIDED-GWM---------------HTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 451 HIqgcMPEANQIAVEVILLEGEKSNTILAAFLQLDvktgrafPTNKAAEtgslaqvifpVEAGKKLAERLPSYMVPDVYF 530
Cdd:PRK12583 469 FL---FTHPAVADVQVFGVPDEKYGEEIVAWVRLH-------PGHAASE----------EELREFCKARIAHFKVPRYFR 528
|
570 580 590
....*....|....*....|....*....|..
gi 1779949166 531 VVTQLPITVSGKTDRKRLREIgasfSAQQLAE 562
Cdd:PRK12583 529 FVDEFPMTVTGKVQKFRMREI----SIEELAL 556
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
183-545 |
2.21e-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: 103.49 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 183 VLFTSGSTGIPKGVVLEHRAvstsclghgrAFGITD--QSRVLQFTS---------YTFDFCMAEIITTLLYGGCICVPS 251
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKT----------FFAVPDilQKEGLNWVVgdvtylplpATHIGGLWWILTCLIHGGLCVTGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 252 DRDRHSDLAKAINTMGANWALLTPSV-AQLLNP-----SDVPTLKILVIGGEQVTSKDWN--RWPTSVQLINGYGPTECC 323
Cdd:cd17635 76 ENTTYKSLFKILTTNAVTTTCLVPTLlSKLVSElksanATVPSLRLIGYGGSRAIAADVRfiEATGLTNTAQVYGLSETG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 324 IVCTGYTTTQAFKTGTIGTAIASVSWVVDPEDYHKlAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpaWLvdgcqg 403
Cdd:cd17635 156 TALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIA-GPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG--WV------ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 404 yagrrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAVEVIllegekSNTILAAFLQ 483
Cdd:cd17635 227 ---------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEG-VSGVQECACYEI------SDEEFGELVG 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 484 LDVKTGRAFPTNKAaetgslaqvifpveAGKKLAER--LPSYMVPDVYFVVTQLPITVSGKTDR 545
Cdd:cd17635 291 LAVVASAELDENAI--------------RALKHTIRreLEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
48-550 |
2.38e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 106.66 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 48 QPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVV----PLC--FeksmwtVVAMLAVLKAGGAFAPLDPdhpV 121
Cdd:PRK06178 46 RPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVavflPNCpqF------HIVFFGILKLGAVHVPVSP---L 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 122 SRHKEI---LRQTGARMVV-------VSAQHSARWASSSCHVVTLSEASIGQLTVE----------------DDLPGFSA 175
Cdd:PRK06178 117 FREHELsyeLNDAGAEVLLaldqlapVVEQVRAETSLRHVIVTSLADVLPAEPTLPlpdslraprlaaagaiDLLPALRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 176 TPGNA----------AYVLFTSGSTGIPKGVVLEHR-AVSTSCLGHGRAFGITDQSRVLQFTSytfDFCMAEIITTLLY- 243
Cdd:PRK06178 197 CTAPVplpppaldalAALNYTGGTTGMPKGCEHTQRdMVYTAAAAYAVAVVGGEDSVFLSFLP---EFWIAGENFGLLFp 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 244 --GGCICVPSDR-DRHSDLAkAINTMGANWALLT-PSVAQLLN-PS----DVPTLKILviggeQVTS--KDWN-----RW 307
Cdd:PRK06178 274 lfSGATLVLLARwDAVAFMA-AVERYRVTRTVMLvDNAVELMDhPRfaeyDLSSLRQV-----RVVSfvKKLNpdyrqRW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 308 P--TSVQLING-YGPTEcciVCTGYTTTQAFKTGTI--------------GTAIAsvswVVDpEDYHKLAPLGSVGELLV 370
Cdd:PRK06178 348 RalTGSVLAEAaWGMTE---THTCDTFTAGFQDDDFdllsqpvfvglpvpGTEFK----ICD-FETGELLPLGAEGEIVV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 371 EGPILARGYLNDAEKTAAAFIEdpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIE- 449
Cdd:PRK06178 420 RTPSLLKGYWNKPEATAEALRD--GWL---------------HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEa 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 450 ---HH--IQGCM------PEANQIAVevillegeksntilaAFLQLdvktgRAFPTNKAAETGSLAqvifpveagkklAE 518
Cdd:PRK06178 483 llgQHpaVLGSAvvgrpdPDKGQVPV---------------AFVQL-----KPGADLTAAALQAWC------------RE 530
|
570 580 590
....*....|....*....|....*....|..
gi 1779949166 519 RLPSYMVPDVYfVVTQLPITVSGKTDRKRLRE 550
Cdd:PRK06178 531 NMAVYKVPEIR-IVDALPMTATGKVRKQDLQA 561
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
49-424 |
3.74e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 105.81 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLV-KIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEI 127
Cdd:PRK08314 24 PDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 128 LRQTGARMVVVSAQHSARWASSSC-----HVVT-------------------LSEASIGQLTVEDDL------------P 171
Cdd:PRK08314 104 VTDSGARVAIVGSELAPKVAPAVGnlrlrHVIVaqysdylpaepeiavpawlRAEPPLQALAPGGVVawkealaaglapP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 172 GFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICV-- 249
Cdd:PRK08314 184 PHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVlm 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 250 PS-DRDRHSDLAK--------AINTMGANWaLLTPSVAQllnpSDVPTLKILVIGG----EQVTSKDWNRwpTSVQLING 316
Cdd:PRK08314 264 PRwDREAAARLIEryrvthwtNIPTMVVDF-LASPGLAE----RDLSSLRYIGGGGaampEAVAERLKEL--TGLDYVEG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 317 YGPTECcIVCTGYTTTQAFKTGTIGTAIASV-SWVVDPEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFIEdpa 395
Cdd:PRK08314 337 YGLTET-MAQTHSNPPDRPKLQCLGIPTFGVdARVIDPETLEELPP-GEVGEIVVHGPQVFKGYWNRPEATAEAFIE--- 411
|
410 420
....*....|....*....|....*....
gi 1779949166 396 wlVDGcqgyagrrGRLYKTGDLVRYDDEG 424
Cdd:PRK08314 412 --IDG--------KRFFRTGDLGRMDEEG 430
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
47-443 |
5.29e-23 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 105.37 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 47 AQPNAPAICAWDG----------EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGgAFAPL- 115
Cdd:PRK09274 18 ERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAG-AVPVLv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 116 DPDHPVSRHKEILRQTGARMVV-VSAQHSAR----WA-SSSCHVVTLSE---------ASIGQLTVEDDLPGFSATPGNA 180
Cdd:PRK09274 97 DPGMGIKNLKQCLAEAQPDAFIgIPKAHLARrlfgWGkPSVRRLVTVGGrllwggttlATLLRDGAAAPFPMADLAPDDM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 181 AYVLFTSGSTGIPKGVVLEHR--AVSTSCLGHgrAFGITDQSR--------VLqftsytFDFCMaeiittllyGGCICVP 250
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGmfEAQIEALRE--DYGIEPGEIdlptfplfAL------FGPAL---------GMTSVIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 251 ---------SDRDRhsdLAKAIN-----TMGANWALLTPsVAQ--LLNPSDVPTLKILVIGGEQVTSKDWNRW----PTS 310
Cdd:PRK09274 240 dmdptrpatVDPAK---LFAAIErygvtNLFGSPALLER-LGRygEANGIKLPSLRRVISAGAPVPIAVIERFramlPPD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 311 VQLINGYGPTECCIVCTGYTTTQAFKTGTI---------GTAIASVSWVV-----DP----EDYHKLAPlGSVGELLVEG 372
Cdd:PRK09274 316 AEILTPYGATEALPISSIESREILFATRAAtdngagicvGRPVDGVEVRIiaisdAPipewDDALRLAT-GEIGEIVVAG 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 373 PILARGYLNDAEKTAAAFIEDpawlvdgcqgyaGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRV 443
Cdd:PRK09274 395 PMVTRSYYNRPEATRLAKIPD------------GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
37-548 |
7.35e-23 |
|
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: 104.51 E-value: 7.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDG--EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAP 114
Cdd:cd05923 3 VFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 115 LDPDHPVSRHKEILRQTGARMVV--VSAQHSARWASSSCHVVTLS-EASIGQLTVEDDLPGFSAT-PGNAAYVLFTSGST 190
Cdd:cd05923 83 INPRLKAAELAELIERGEMTAAViaVDAQVMDAIFQSGVRVLALSdLVGLGEPESAGPLIEDPPRePEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 191 GIPKGVVLEHRAVSTSCL-----------GHGRAFGITDQSRVLQFtsytfdfcMAEIITTLLYGGCICVPSDRDRhSDL 259
Cdd:cd05923 163 GLPKGAVIPQRAAESRVLfmstqaglrhgRHNVVLGLMPLYHVIGF--------FAVLVAALALDGTYVVVEEFDP-ADA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 260 AKAINTMGANWALLTPS------VAQLLNPSDVPTLKILVIGGEQVTSKDWNRWPTSVQ--LINGYGPTEccivCTGYTT 331
Cdd:cd05923 234 LKLIEQERVTSLFATPThldalaAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPgeKVNIYGTTE----AMNSLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 332 TQAFKTGTIGTA--IASVSWVVDPEDYHKLAPLGSVGELLVEGPILA--RGYLNDAEKTAAAfiedpawLVDGcqgyagr 407
Cdd:cd05923 310 MRDARTGTEMRPgfFSEVRIVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKK-------LQDG------- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 408 rgrLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEhHIQGCMPEANQIAveVILLEGEKSNTILAAFlqldVK 487
Cdd:cd05923 376 ---WYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIE-RVLSRHPGVTEVV--VIGVADERWGQSVTAC----VV 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 488 TGRAFPTNKAAETGSLAQvifpveagkklaeRLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:cd05923 446 PREGTLSADELDQFCRAS-------------ELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1129-1540 |
7.65e-23 |
|
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: 103.52 E-value: 7.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1129 DAPAICAWDGDMTYGELDVLSGRLAGHLVELG-VGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRlmc 1207
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1208 rkvsaklslaseasaplakdlvgtVVIVNADSALqlahhaspitSVRPthtAYVIFTSGSTGEPKGCRIEHRAASSAVTA 1287
Cdd:cd05941 78 ------------------------YVITDSEPSL----------VLDP---ALILYTSGTTGRPKGVVLTHANLAANVRA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1288 ----------------------HGRYLGMQASTrtlqfasyaFAGSLVELLMNLChggcicvLSEEERRTDLASAMCRMK 1345
Cdd:cd05941 121 lvdawrwteddvllhvlplhhvHGLVNALLCPL---------FAGASVEFLPKFD-------PKEVAISRLMPSITVFMG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1346 V---------NWAFlTSTVVDLLTPKSVPSLSILCVGGEPIRASQIVRWGS---QVHLRQtYGSSEVsGIVSSAALTTCS 1413
Cdd:cd05941 185 VptiytrllqYYEA-HFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAitgHTLLER-YGMTEI-GMALSNPLDGER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1414 TTRDVGRASTGV-FWIVDPNNhNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapawraslglsagqQRLYKTGD 1492
Cdd:cd05941 262 RPGTVGMPLPGVqARIVDEET-GEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTD--------------DGWFKTGD 326
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1779949166 1493 LARYKDDGSIELIGR-KDNQVKLRGQRIEVEEIEHQArLAEADVAEIAV 1540
Cdd:cd05941 327 LGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVL-LAHPGVSECAV 374
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
39-561 |
9.51e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 104.44 E-value: 9.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 39 DLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPD 118
Cdd:PRK06164 14 SLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 119 HPVSRHKEILRQTGARMVVV--------------SAQHSARWASSSCHVVTLSEASI-----GQLTVEDDLPGFSATPG- 178
Cdd:PRK06164 94 YRSHEVAHILGRGRARWLVVwpgfkgidfaailaAVPPDALPPLRAIAVVDDAADATpapapGARVQLFALPDPAPPAAa 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 179 -------NAAYVLFT-SGSTGIPKGVVLEHRAVstscLGHG----RAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGG- 245
Cdd:PRK06164 174 geraadpDAGALLFTtSGTTSGPKLVLHRQATL----LRHAraiaRAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAp 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 246 CICVPSdrdrhSDLAKAINTMG--------ANWALLTPSVAQLLNPSDVPTLKILVIGGEQVTSKDWNRWPTS--VQLIN 315
Cdd:PRK06164 250 LVCEPV-----FDAARTARALRrhrvthtfGNDEMLRRILDTAGERADFPSARLFGFASFAPALGELAALARArgVPLTG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 316 GYGPTECCIVCTGYTTTQAFKT-----GTIGTAIASVSwVVDPEDyHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAF 390
Cdd:PRK06164 325 LYGSSEVQALVALQPATDPVSVrieggGRPASPEARVR-ARDPQD-GALLPDGESGEIEIRAPSLMRGYLDNPDATARAL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 391 IEDpawlvdgcqGYagrrgrlYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCmPEANQIAVEVILLE 470
Cdd:PRK06164 403 TDD---------GY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL-PGVAAAQVVGATRD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 471 GeksNTILAAFLQLDvktgrafPTNKAAETGSLAQvifpveagkkLAERLPSYMVPDVYFVVTQLPITVSG---KTDRKR 547
Cdd:PRK06164 466 G---KTVPVAFVIPT-------DGASPDEAGLMAA----------CREALAGFKVPARVQVVEAFPVTESAngaKIQKHR 525
|
570
....*....|....
gi 1779949166 548 LREIGASFSAQQLA 561
Cdd:PRK06164 526 LREMAQARLAAERA 539
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1124-1512 |
1.22e-22 |
|
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: 103.85 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPA-ICAWDGD-MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDP-SLPH 1200
Cdd:cd05904 15 ASAHPSRPAlIDAATGRaLTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPlSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1201 ERLRLMcrKVS-AKLSLASEASAPLAKDLVGTVVIVnaDSALQLAHHASPITS-----------VRPTHTAYVIFTSGST 1268
Cdd:cd05904 95 EIAKQV--KDSgAKLAFTTAELAEKLASLALPVVLL--DSAEFDSLSFSDLLFeadeaeppvvvIKQDDVAALLYSSGTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1269 GEPKGCRIEHR--AASSAVTAHGRYLGMQASTRTL----QFASYAFAGSLVELLMNlchGGCICVLseeeRRTDLASAMC 1342
Cdd:cd05904 171 GRSKGVMLTHRnlIAMVAQFVAGEGSNSDSEDVFLcvlpMFHIYGLSSFALGLLRL---GATVVVM----PRFDLEELLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1343 ---RMKVNWAFLTSTVVDLLTPKS------VPSLSILCVGGEPIRASQIVRWGS---QVHLRQTYGSSEVSGIVSSAALT 1410
Cdd:cd05904 244 aieRYKVTHLPVVPPIVLALVKSPivdkydLSSLRQIMSGAAPLGKELIEAFRAkfpNVDLGQGYGMTESTGVVAMCFAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1411 TCSTTR--DVGRASTGV-FWIVDPNNhNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapawraslglsagqQRL 1487
Cdd:cd05904 324 EKDRAKygSVGRLVPNVeAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK--------------EGW 388
|
410 420 430
....*....|....*....|....*....|..
gi 1779949166 1488 YKTGDLARYKDDGSI-------ELIGRKDNQV 1512
Cdd:cd05904 389 LHTGDLCYIDEDGYLfivdrlkELIKYKGFQV 420
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1116-1540 |
1.87e-22 |
|
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: 103.30 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIV----PLCFEksmwTVVAMLAVLKAGGAF 1191
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVvvqlPNVAE----FVIVFFALFRAGAIP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1192 LLLDPSlpHERLRL--MCRKVSAKLSLASEASA-----PLAKDLVG------TVVIVN-ADSALQLAH-HASPITSVRP- 1255
Cdd:COG1021 103 VFALPA--HRRAEIshFAEQSEAVAYIIPDRHRgfdyrALARELQAevpslrHVLVVGdAGEFTSLDAlLAAPADLSEPr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1256 THTAYVIF---TSGSTGEPKG---------CRIEHRAASSAVTAHGRYLGMQAstrtlqfASYAFAGSLVELLMNLCHGG 1323
Cdd:COG1021 181 PDPDDVAFfqlSGGTTGLPKLiprthddylYSVRASAEICGLDADTVYLAALP-------AAHNFPLSSPGVLGVLYAGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1324 CIcVLSEEERRTDLASAMCRMKVNwafLTSTVVDLL---------TPKSVPSLSILCVGG---EPIRASQIV-RWGSQvh 1390
Cdd:COG1021 254 TV-VLAPDPSPDTAFPLIERERVT---VTALVPPLAllwldaaerSRYDLSSLRVLQVGGaklSPELARRVRpALGCT-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1391 LRQTYGSSEvsGIVSSAAL-----TTCSTtrdVGRA-STG-VFWIVDPNnhNRLAPVGAVGEVLVEGPVLGREYIDEPDK 1463
Cdd:COG1021 328 LQQVFGMAE--GLVNYTRLddpeeVILTT---QGRPiSPDdEVRIVDED--GNPVPPGEVGELLTRGPYTIRGYYRAPEH 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 1464 TASTFIEapawraslglsagqQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQArLAEADVAEIAV 1540
Cdd:COG1021 401 NARAFTP--------------DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLL-LAHPAVHDAAV 462
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1094-1596 |
1.21e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 101.23 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1094 TPEDRQQLWEWNHDVPPAIE---RCIHDLFaDQAKAR-PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPL 1169
Cdd:PRK05605 9 AFADKPWLQSYAPWTPHDLDygdTTLVDLY-DNAVARfGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1170 CFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLASEASAPLAKDLVG-----TVVIVNADSAL--- 1241
Cdd:PRK05605 88 VLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRttpleTIVSVNMIAAMpll 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1242 -QLA---------------HHASPIT---------------------SVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSA 1284
Cdd:PRK05605 168 qRLAlrlpipalrkaraalTGPAPGTvpwetlvdaaiggdgsdvshpRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1285 VtAHGRY----LGMQASTrtlQFAS----YAFAGSLVELLMNLChGGCICVLSEEErrTDLA-SAMCRMKVNW----AFL 1351
Cdd:PRK05605 248 A-AQGKAwvpgLGDGPER---VLAAlpmfHAYGLTLCLTLAVSI-GGELVLLPAPD--IDLIlDAMKKHPPTWlpgvPPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1352 TSTVVDLLTPKSVP------SLSilcvGGEPIRASQIVRWGSQV--HLRQTYGSSEVSGIVSSAALttcSTTRDVGRA-- 1421
Cdd:PRK05605 321 YEKIAEAAEERGVDlsgvrnAFS----GAMALPVSTVELWEKLTggLLVEGYGLTETSPIIVGNPM---SDDRRPGYVgv 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1422 ---STGVfWIVDPNNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFieAPAWraslglsagqqrlYKTGDLARYKD 1498
Cdd:PRK05605 394 pfpDTEV-RIVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF--LDGW-------------FRTGDVVVMEE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1499 DGSIELIGRKDNQVKLRGQRI---EVEEIehqarLAEA-DVAEIAVELIQPKDGEDGMLACFIVVEDSASNEDEL-SGKR 1573
Cdd:PRK05605 458 DGFIRIVDRIKELIITGGFNVypaEVEEV-----LREHpGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLrAYCR 532
|
570 580 590
....*....|....*....|....*....|....*.
gi 1779949166 1574 TRLdTRTQ--RT-----------IGKIQDRLERDLV 1596
Cdd:PRK05605 533 EHL-TRYKvpRRfyhvdelprdqLGKVRRREVREEL 567
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
61-549 |
1.42e-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: 99.51 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 61 MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGG-------AFAPldpdhPVSRHKeiLRQTGA 133
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAvyqplftAFGP-----KAIEHR--LRTSGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 134 RMVVVSAQHSARWASSschvvtlseasigqLTVEddlpgfsatpgnaayvLFTSGSTGIPKGVVLEHRAVSTSCLGHGRA 213
Cdd:cd05973 74 RLVVTDAANRHKLDSD--------------PFVM----------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 214 FGITDQSRVLQFTS--------YTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAkAINTMGAnwalltPSVAQLL--NP 283
Cdd:cd05973 124 VDLRPEDSFWNAADpgwayglyYAITGPLALGHPTILLEGGFSVESTWRVIERLG-VTNLAGS------PTAYRLLmaAG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 284 SDVPT-----LKILVIGGEQVTSK--DWNRWPTSVQLINGYGPTEC-CIVCTGYTTTQAFKTGTIGTAIASVSWVVDPED 355
Cdd:cd05973 197 AEVPArpkgrLRRVSSAGEPLTPEviRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 356 YHKLAPlGSVGELLVE---GPILA-RGYLNDAEKTAAafiedpawlvdgcqgyagrrGRLYKTGDLVRYDDEGNLVCLGR 431
Cdd:cd05973 277 GDELGP-GEPGRLAIDianSPLMWfRGYQLPDTPAID--------------------GGYYLTGDTVEFDPDGSFSFIGR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 432 KDSQVKVRGQR-----VELGEIEHhiqgcmPEANQIAVE--------------VILLEGEKSNTILAAFLQLDVKTgraf 492
Cdd:cd05973 336 ADDVITMSGYRigpfdVESALIEH------PAVAEAAVIgvpdpertevvkafVVLRGGHEGTPALADELQLHVKK---- 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 493 ptnkaaetgslaqvifpveagkklaeRLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd05973 406 --------------------------RLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1131-1570 |
1.43e-21 |
|
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: 99.84 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1131 PAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKV 1210
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1211 SAKLslaseasaplakdlvgtvVIVNADSAlqlahhaspitsvrpthtAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGR 1290
Cdd:cd05919 82 EARL------------------VVTSADDI------------------AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1291 -YLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTD-LASAMCRMKVNWAFLTST----VVDL--LTPK 1362
Cdd:cd05919 126 eALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAErVLATLARFRPTVLYGVPTfyanLLDScaGSPD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1363 SVPSLSILCVGGEPIRASQIVRWgsqvhlRQTYGSSEVSGIVSSAALTTCSTTR--DVGRASTG--VFW----IVDPNNH 1434
Cdd:cd05919 206 ALRSLRLCVSAGEALPRGLGERW------MEHFGGPILDGIGATEVGHIFLSNRpgAWRLGSTGrpVPGyeirLVDEEGH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1435 NrlAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKL 1514
Cdd:cd05919 280 T--IPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNG--GW-------------YRTGDKFCRDADGWYTHAGRADDMLKV 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 1515 RGQRIEVEEIEhQARLAEADVAEIAVelIQPKDGEDGM-LACFIVVEDSASNEDELS 1570
Cdd:cd05919 343 GGQWVSPVEVE-SLIIQHPAVAEAAV--VAVPESTGLSrLTAFVVLKSPAAPQESLA 396
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
51-549 |
3.71e-21 |
|
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: 98.32 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 51 APAICAWDGEMSYSVLDGLSTKLAGYLV-KIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLdpdHPVSRHKE--- 126
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVAT---MPLLRPKElay 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 127 ILRQTgARMVVVSAqhsarwassschvvtlseasiGQLTVEDDLpgfsatpgnaAYVLFTSGSTGIPKGVVLEHRAVSTS 206
Cdd:cd05958 78 ILDKA-RITVALCA---------------------HALTASDDI----------CILAFTSGTTGAPKATMHFHRDPLAS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 207 CLGHGR-AFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAKAIN-----------TMGANWALLT 274
Cdd:cd05958 126 ADRYAVnVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIArykptvlftapTAYRAMLAHP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 275 PSVAQLLNPsdvptLKILVIGGEQVTSKDWNRW--PTSVQLINGYGPTECCIVCTGYTTTQAfKTGTIGTAIASV-SWVV 351
Cdd:cd05958 206 DAAGPDLSS-----LRKCVSAGEALPAALHRAWkeATGIPIIDGIGSTEMFHIFISARPGDA-RPGATGKPVPGYeAKVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 352 DpeDYHKLAPLGSVGELLVEGPIlarGYLNDAEKTAAAFIEDpAWLVdgcqgyagrrgrlykTGDLVRYDDEGNLVCLGR 431
Cdd:cd05958 280 D--DEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQG-GWNI---------------TGDTYSRDPDGYFRHQGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 432 KDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQLdvktgrafptnkAAETGSLAQvifPVE 511
Cdd:cd05958 339 SDDMIVSGGYNIAPPEVEDVLLQ-HPAVAECA--VVGHPDESRGVVVKAFVVL------------RPGVIPGPV---LAR 400
|
490 500 510
....*....|....*....|....*....|....*....
gi 1779949166 512 AGKKLAER-LPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd05958 401 ELQDHAKAhIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1121-1582 |
5.60e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 98.34 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1121 ADQAKARPDAPAI--CAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSL 1198
Cdd:PRK09088 2 AFHARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1199 PHERLRLMCRKVSAKLSLASEASAPLAKDLVG-TVVIVNADsalqlAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIE 1277
Cdd:PRK09088 82 SASELDALLQDAEPRLLLGDDAVAAGRTDVEDlAAFIASAD-----ALEPADTPSIPPERVSLILFTSGTSGQPKGVMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1278 HRAASSAVTAHGRYLGMQASTRTL----QFASYAFAGSLVELLMnlcHGGCICVLSE-EERRTDLASAMCRMKVNWAFLT 1352
Cdd:PRK09088 157 ERNLQQTAHNFGVLGRVDAHSSFLcdapMFHIIGLITSVRPVLA---VGGSILVSNGfEPKRTLGRLGDPALGITHYFCV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1353 STVVDLL------TPKSVPSLSILCVGGEPIRASQIVRWGSQ-VHLRQTYGSSE---VSGIVSSAALTTcSTTRDVGRAS 1422
Cdd:PRK09088 234 PQMAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWLDDgIPMVDGFGMSEagtVFGMSVDCDVIR-AKAGAAGIPT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1423 TGVFW-IVDpnNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEApAWraslglsagqqrlYKTGDLARYKDDGS 1501
Cdd:PRK09088 313 PTVQTrVVD--DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGD-GW-------------FRTGDIARRDADGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1502 IELIGRKDNQVKLRGQRIEVEEIEhqARLAE-ADVAEIAV-ELIQPKDGEDGMlaCFIVVEDSASNedELSGKRTRLDTR 1579
Cdd:PRK09088 377 FWVVDRKKDMFISGGENVYPAEIE--AVLADhPGIRECAVvGMADAQWGEVGY--LAIVPADGAPL--DLERIRSHLSTR 450
|
...
gi 1779949166 1580 TQR 1582
Cdd:PRK09088 451 LAK 453
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
60-551 |
9.17e-21 |
|
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: 98.37 E-value: 9.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 60 EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHpvsRHKEILRQTG---ARMV 136
Cdd:cd17642 44 NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNiskPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 137 VVSA---QHSARWASSSCHVVTL----------SEASIGQLTVEDDLPGFSA---TPGNA------AYVLFTSGSTGIPK 194
Cdd:cd17642 121 FCSKkglQKVLNVQKKLKIIKTIiildskedykGYQCLYTFITQNLPPGFNEydfKPPSFdrdeqvALIMNSSGSTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 195 GVVLEHRAVSTScLGHGR--AFG--ITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDLaKAINTMGANW 270
Cdd:cd17642 201 GVQLTHKNIVAR-FSHARdpIFGnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFL-RSLQDYKVQS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 271 ALLTPSVAQLLNPS------DVPTLKILVIGG--------EQVtsKDWNRWPTSVQlinGYGPTEccivctgytTTQAF- 335
Cdd:cd17642 279 ALLVPTLFAFFAKStlvdkyDLSNLHEIASGGaplskevgEAV--AKRFKLPGIRQ---GYGLTE---------TTSAIl 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 336 -------KTGTIGTAIASVSW-VVDPeDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagr 407
Cdd:cd17642 345 itpegddKPGAVGKVVPFFYAkVVDL-DTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKD-GWL---------- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 408 rgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHhiqgcmpeanqiavevILLEGEKsntILAAFLqldvk 487
Cdd:cd17642 413 -----HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELES----------------ILLQHPK---IFDAGV----- 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1779949166 488 TGRAFPtnkaaETGSLAQVIFPVEAGKKLAERLPSYMVPD-----------VYFvVTQLPITVSGKTDRKRLREI 551
Cdd:cd17642 464 AGIPDE-----DAGELPAAVVVLEAGKTMTEKEVMDYVASqvstakrlrggVKF-VDEVPKGLTGKIDRRKIREI 532
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
35-550 |
1.26e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 98.03 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 35 KCIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLV-KIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFA 113
Cdd:PRK08751 25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 114 PLDPDHPVSRHKEILRQTGARMVVV-----SAQHSARWASSSCHVVT--------LSEASIGQLTV-------------- 166
Cdd:PRK08751 105 NVNPLYTPRELKHQLIDSGASVLVVidnfgTTVQQVIADTPVKQVITtglgdmlgFPKAALVNFVVkyvkklvpeyring 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 167 ------------EDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSR------VLQFTSY 228
Cdd:PRK08751 185 airfrealalgrKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEegcevvITALPLY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 229 TFDFCMAEIITTLLYGGC---ICVPSD---------RDRHSDLAkAINTMgANWALLTPSVAQLlnpsDVPTLKILVIGG 296
Cdd:PRK08751 265 HIFALTANGLVFMKIGGCnhlISNPRDmpgfvkelkKTRFTAFT-GVNTL-FNGLLNTPGFDQI----DFSSLKMTLGGG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 297 EQVTSKDWNRWP--TSVQLINGYGPTECC-IVCTGYTTTQAFkTGTIGTAIASVSWVVDpEDYHKLAPLGSVGELLVEGP 373
Cdd:PRK08751 339 MAVQRSVAERWKqvTGLTLVEAYGLTETSpAACINPLTLKEY-NGSIGLPIPSTDACIK-DDAGTVLAIGEIGELCIKGP 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 374 ILARGYLNDAEKTAAAfIEDPAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIq 453
Cdd:PRK08751 417 QVMKGYWKRPEETAKV-MDADGWL---------------HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVI- 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 454 GCMPEANQIAveVILLEGEKSNTILAAFLqldVKTGRAFptnkAAEtgslaqvifpvEAGKKLAERLPSYMVPDVYFVVT 533
Cdd:PRK08751 480 AMMPGVLEVA--AVGVPDEKSGEIVKVVI---VKKDPAL----TAE-----------DVKAHARANLTGYKQPRIIEFRK 539
|
570
....*....|....*..
gi 1779949166 534 QLPITVSGKTDRKRLRE 550
Cdd:PRK08751 540 ELPKTNVGKILRRELRD 556
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1116-1520 |
1.42e-20 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 98.25 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAICAWDG----DMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAF 1191
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1192 LLLDPSLPHERLRLMCRKVSAKLSLASEAS-----APLAKDL--VGTVVIVNADSALQL-------------AHHASP-- 1249
Cdd:COG1022 93 VPIYPTSSAEEVAYILNDSGAKVLFVEDQEqldklLEVRDELpsLRHIVVLDPRGLRDDprllsldellalgREVADPae 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1250 ----ITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTL----------QFASYAFagslvel 1315
Cdd:COG1022 173 learRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLsflplahvfeRTVSYYA------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1316 lmnLCHGGCICVLSEEER-RTDL-------------------ASAMCRMK---------VNWAFLTSTVV--DLLTPKSV 1364
Cdd:COG1022 246 ---LAAGATVAFAESPDTlAEDLrevkptfmlavprvwekvyAGIQAKAEeagglkrklFRWALAVGRRYarARLAGKSP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1365 PS------------------------LSILCVGGEPIrASQIVRW--GSQVHLRQTYGSSEVSGIVSsaalttcsttrdv 1418
Cdd:COG1022 323 SLllrlkhaladklvfsklrealggrLRFAVSGGAAL-GPELARFfrALGIPVLEGYGLTETSPVIT------------- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1419 grastgvfwiVDPNNHNRLAPVGAV-----------GEVLVEGPVLGREYIDEPDKTASTFiEAPAWraslglsagqqrl 1487
Cdd:COG1022 389 ----------VNRPGDNRIGTVGPPlpgvevkiaedGEILVRGPNVMKGYYKNPEATAEAF-DADGW------------- 444
|
490 500 510
....*....|....*....|....*....|....*....
gi 1779949166 1488 YKTGDLARYKDDGSIELIGRKDNQVKLRG------QRIE 1520
Cdd:COG1022 445 LHTGDIGELDEDGFLRITGRKKDLIVTSGgknvapQPIE 483
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1116-1540 |
2.44e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 96.88 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGA----- 1190
Cdd:PRK07798 5 IADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVpvnvn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1191 --------FLLLDPS----LPHER--------LRLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSALQLAHHASPi 1250
Cdd:PRK07798 85 yryvedelRYLLDDSdavaLVYERefaprvaeVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPERDFGERSP- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1251 tsvrptHTAYVIFTSGSTGEPKGC---------------RIEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVEL 1315
Cdd:PRK07798 164 ------DDLYLLYTGGTTGMPKGVmwrqedifrvllggrDFATGEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQWAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1316 LMNLCHGGCICVLSEEE-RRTDLASAMCRMKVNWAFLTSTV-----VDLLTPKS---VPSLSILCVGGEPIRAS---QIV 1383
Cdd:PRK07798 238 FAALFSGQTVVLLPDVRfDADEVWRTIEREKVNVITIVGDAmarplLDALEARGpydLSSLFAIASGGALFSPSvkeALL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1384 RWGSQVHLRQTYGSSEV----SGIVSSAALTTCSTTRDVGrASTGVFwivDPNnHNRLAP-VGAVGEVLVEGPV-LGreY 1457
Cdd:PRK07798 318 ELLPNVVLTDSIGSSETgfggSGTVAKGAVHTGGPRFTIG-PRTVVL---DED-GNPVEPgSGEIGWIARRGHIpLG--Y 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1458 IDEPDKTASTFIEAPAWRASLglsagqqrlykTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAE 1537
Cdd:PRK07798 391 YKDPEKTAETFPTIDGVRYAI-----------PGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVE-EALKAHPDVAD 458
|
...
gi 1779949166 1538 IAV 1540
Cdd:PRK07798 459 ALV 461
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
51-449 |
2.82e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 96.21 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 51 APAICAWDGEMSYSVLDGLSTKLAGylvkiGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQ 130
Cdd:PRK07787 16 ADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILAD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 131 TGARMVVVSAQhsarWASSSCHVVTLSeasigqLTVEDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGH 210
Cdd:PRK07787 91 SGAQAWLGPAP----DDPAGLPHVPVR------LHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 211 GRAFGITDQ--------------------------SRVLQFTSYTFDFCMAEIIT--TLLYGgcicVPsdrdrhsdlaka 262
Cdd:PRK07787 161 AEAWQWTADdvlvhglplfhvhglvlgvlgplrigNRFVHTGRPTPEAYAQALSEggTLYFG----VP------------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 263 inTMganWALLT--PSVAQLLNPSdvptlKILVIGGEQVTSKDWNRWP--TSVQLINGYGPTECCIVctgyTTTQA---F 335
Cdd:PRK07787 225 --TV---WSRIAadPEAARALRGA-----RLLVSGSAALPVPVFDRLAalTGHRPVERYGMTETLIT----LSTRAdgeR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 336 KTGTIGTAIASVSWVVDPEDYHKLAPLG-SVGELLVEGPILARGYLNDAEKTAAAFIEDpAWlvdgcqgyagrrgrlYKT 414
Cdd:PRK07787 291 RPGWVGLPLAGVETRLVDEDGGPVPHDGeTVGELQVRGPTLFDGYLNRPDATAAAFTAD-GW---------------FRT 354
|
410 420 430
....*....|....*....|....*....|....*.
gi 1779949166 415 GDLVRYDDEGNLVCLGRKDSQ-VKVRGQRVELGEIE 449
Cdd:PRK07787 355 GDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIE 390
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
27-549 |
3.14e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 96.63 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 27 HKIPGVTNKCIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVL 106
Cdd:PRK07059 15 AEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 107 KAGGAFAPLDPDHPVSRHKEILRQTGARMVVV------SAQHSARwASSSCHVVTlseASIGQL-------------TVE 167
Cdd:PRK07059 95 RAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVlenfatTVQQVLA-KTAVKHVVV---ASMGDLlgfkghivnfvvrRVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 168 DDLPGFS-----------------------ATPGNAAYVLFTSGSTGIPKGVVLEHRA----VSTSCLGHGRAFGITDQS 220
Cdd:PRK07059 171 KMVPAWSlpghvrfndalaegarqtfkpvkLGPDDVAFLQYTGGTTGVSKGATLLHRNivanVLQMEAWLQPAFEKKPRP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 221 RVLQFTS-----YTFDFCMAEIITTLLYGGCICVPSDRDRHS---DLAK-------AINTMgANWALLTPSVAQLlnpsD 285
Cdd:PRK07059 251 DQLNFVCalplyHIFALTVCGLLGMRTGGRNILIPNPRDIPGfikELKKyqvhifpAVNTL-YNALLNNPDFDKL----D 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 286 VPTLKILVIGGEQVTSKDWNRW--PTSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVSWVVDPEDYHKLaPLG 363
Cdd:PRK07059 326 FSKLIVANGGGMAVQRPVAERWleMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDL-PLG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 364 SVGELLVEGPILARGYLNDAEKTAAAFIEDpawlvdgcqGYagrrgrlYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRV 443
Cdd:PRK07059 405 EPGEICIRGPQVMAGYWNRPDETAKVMTAD---------GF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 444 ELGEIEHHIQGCmpeANQIAVEVILLEGEKSNTILAAFLqldVKTGRAFptnkaaetgSLAQVIfpveagKKLAERLPSY 523
Cdd:PRK07059 469 YPNEIEEVVASH---PGVLEVAAVGVPDEHSGEAVKLFV---VKKDPAL---------TEEDVK------AFCKERLTNY 527
|
570 580
....*....|....*....|....*.
gi 1779949166 524 MVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:PRK07059 528 KRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
49-551 |
3.89e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 96.08 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLV-KIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEI 127
Cdd:PRK06839 16 PDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 128 LRQTGARMVVVSAQHSARWA-----SSSCHVVTLSEASigqlTVEDDLP-GFSATPGNAAYVL-FTSGSTGIPKGVVLEH 200
Cdd:PRK06839 96 LKDSGTTVLFVEKTFQNMALsmqkvSYVQRVISITSLK----EIEDRKIdNFVEKNESASFIIcYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 201 RAVSTSCLGHGRAFGITDQSRVLQFTSYtfdFCMAEI----ITTLLYGGCICVPsDRDRHSDLAKAINTMGANWALLTPS 276
Cdd:PRK06839 172 ENMFWNALNNTFAIDLTMHDRSIVLLPL---FHIGGIglfaFPTLFAGGVIIVP-RKFEPTKALSMIEKHKVTVVMGVPT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 277 VAQ-LLNPSDVPTlkilviggeqvTSKDWNRW------PTSVQLI-----------NGYGPTEccivctgyTTTQAF--- 335
Cdd:PRK06839 248 IHQaLINCSKFET-----------TNLQSVRWfynggaPCPEELMrefidrgflfgQGFGMTE--------TSPTVFmls 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 336 ------KTGTIGTAIASVSWVVDPEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFiedpawlvdgcqgyagRRG 409
Cdd:PRK06839 309 eedarrKVGSIGKPVLFCDYELIDENKNKVEV-GEVGELLIRGPNVMKEYWNRPDATEETI----------------QDG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 410 RLYkTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQLdvktg 489
Cdd:PRK06839 372 WLC-TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINK-LSDVYEVA--VVGRQHVKWGEIPIAFIVK----- 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 490 rafptnkaaETGSlaqVIFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREI 551
Cdd:PRK06839 443 ---------KSSS---VLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1122-1533 |
4.32e-20 |
|
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: 96.15 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1122 DQAKARPDAPAICAWDGD------MTYGELDVLSGRLAGHLVELGvGPEDIVPLCFEKSMWTVVAMLAVLKAGG-AFLLL 1194
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEggreetLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAiAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1195 DPSLPH--ERLRLMCRKVSAKLSLASEASAPLAKD------LVGTVVIVNADSALQLAHHASPITSVRPTHTAYVIFTSG 1266
Cdd:cd05931 80 PPTPGRhaERLAAILADAGPRVVLTTAAALAAVRAfaasrpAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1267 STGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTlqfasyafaGS---------LVELLMNLCHGGCICVLSE------- 1330
Cdd:cd05931 160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVV---------VSwlplyhdmgLIGGLLTPLYSGGPSVLMSpaaflrr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1331 ---------EERRT-----DLASAMCRMKVNWAFLTStvVDLLtpksvpSLSILCVGGEPIRASQIVRW---GSQVHLRQ 1393
Cdd:cd05931 231 plrwlrlisRYRATisaapNFAYDLCVRRVRDEDLEG--LDLS------SWRVALNGAEPVRPATLRRFaeaFAPFGFRP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1394 T-----YGSSEVSGIVSSAALTTCSTTRDVGRASTGVFW--------------------------IVDPNNHNRLAPvGA 1442
Cdd:cd05931 303 EafrpsYGLAEATLFVSGGPPGTGPVVLRVDRDALAGRAvavaaddpaarelvscgrplpdqevrIVDPETGRELPD-GE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1443 VGEVLVEGPVLGREYIDEPDKTASTFieapawRASLGLSAGqqRLYKTGDLArYKDDGSIELIGRKDNQVKLRGQRIEVE 1522
Cdd:cd05931 382 VGEIWVRGPSVASGYWGRPEATAETF------GALAATDEG--GWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQ 452
|
490
....*....|.
gi 1779949166 1523 EIEHQARLAEA 1533
Cdd:cd05931 453 DIEATAEEAHP 463
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1118-1540 |
4.43e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 95.72 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1118 DLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPS 1197
Cdd:PRK06145 6 ASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1198 LPHERLRLMCRKVSAKLSLASEASAPLAKDLVGTVVI---VNADSALQLAHH--ASPITSVRPTHTAYVIFTSGSTGEPK 1272
Cdd:PRK06145 86 LAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVIdaaAQADSRRLAQGGleIPPQAAVAPTDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1273 GCRIEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSL-VELLMNLCHGGCICVLSEEERRTDLAS-AMCRMKVNW-- 1348
Cdd:PRK06145 166 GVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFdLPGIAVLWVGGTLRIHREFDPEAVLAAiERHRLTCAWma 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1349 AFLTSTVVDLLTPK--SVPSLSILCVGGEPIRASQIVRWGS---QVHLRQTYGSSE-VSGIVSSAALTTCSTTRDVGRAS 1422
Cdd:PRK06145 246 PVMLSRVLTVPDRDrfDLDSLAWCIGGGEKTPESRIRDFTRvftRARYIDAYGLTEtCSGDTLMEAGREIEKIGSTGRAL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1423 TGVfWIVDPNNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapAWraslglsagqqrlYKTGDLARYKDDGSI 1502
Cdd:PRK06145 326 AHV-EIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYG--DW-------------FRSGDVGYLDEEGFL 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 1779949166 1503 ELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAV 1540
Cdd:PRK06145 390 YLTDRKKDMIISGGENIASSEVE-RVIYELPEVAEAAV 426
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
40-554 |
7.41e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 95.60 E-value: 7.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 40 LFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDH 119
Cdd:PRK06155 26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 120 PVSRHKEILRQTGARMVVVSAQHSARWAS------SSCHVVTLSEASIGQLTVEDD----------LPGFSATPGNAAYV 183
Cdd:PRK06155 106 RGPQLEHILRNSGARLLVVEAALLAALEAadpgdlPLPAVWLLDAPASVSVPAGWStaplppldapAPAAAVQPGDTAAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 184 LFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSrVLQFTSYTFDF-CMAEIITTLLyGGCICVPSDRDRHSDLAKA 262
Cdd:PRK06155 186 LYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD-VLYTTLPLFHTnALNAFFQALL-AGATYVLEPRFSASGFWPA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 263 INTMGANWALLTPSVAQLL-----NPSD-VPTLKILVIGGEQVTSKDWNRWPTSVQLINGYGPTECCIVCtgYTTTQAFK 336
Cdd:PRK06155 264 VRRHGATVTYLLGAMVSILlsqpaRESDrAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVI--AVTHGSQR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 337 TGTIGTAIASV-SWVVDPEDyhKLAPLGSVGELLV---EGPILARGYLNDAEKTAAAfiedpaWlvdgcqgyagrRGRLY 412
Cdd:PRK06155 342 PGSMGRLAPGFeARVVDEHD--QELPDGEPGELLLradEPFAFATGYFGMPEKTVEA------W-----------RNLWF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 413 KTGDLVRYDDEGNLVCLGR-KDSqVKVRGQRVELGEIEHHIQG--CMPEANQIAVEVILLEGEksntILAAFLqldVKTG 489
Cdd:PRK06155 403 HTGDRVVRDADGWFRFVDRiKDA-IRRRGENISSFEVEQVLLShpAVAAAAVFPVPSELGEDE----VMAAVV---LRDG 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1779949166 490 RAfptnkaaetgslaqvIFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIGAS 554
Cdd:PRK06155 475 TA---------------LEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVT 524
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
72-550 |
7.42e-20 |
|
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: 95.39 E-value: 7.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 72 KLAGYLVKIGVKPGDVVPLCfeksMWT----VVAMLAVLKAGGAFAPLDPD-HP-----VSRHKE--------------- 126
Cdd:cd12119 37 RLANALRRLGVKPGDRVATL----AWNthrhLELYYAVPGMGAVLHTINPRlFPeqiayIINHAEdrvvfvdrdflplle 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 127 -ILRQTGARMVVVSAQHSARWASSSCHVVTLSEASIGQLTVEDDLPGFsatPGNAAYVL-FTSGSTGIPKGVVLEHRAVS 204
Cdd:cd12119 113 aIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDF---DENTAAAIcYTSGTTGNPKGVVYSHRSLV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 205 TSCLG--HGRAFGITDQSRVLQFT------SYTFDFcmaeiiTTLLYGGCICVPSDRDRHSDLAKAINTMGANWALLTPS 276
Cdd:cd12119 190 LHAMAalLTDGLGLSESDVVLPVVpmfhvnAWGLPY------AAAMVGAKLVLPGPYLDPASLAELIEREGVTFAAGVPT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 277 VAQLL------NPSDVPTLKILVIGGEQV---TSKDWNRwpTSVQLINGYGPTECC-IVCTGYTTTQAFKTG-------- 338
Cdd:cd12119 264 VWQGLldhleaNGRDLSSLRRVVIGGSAVprsLIEAFEE--RGVRVIHAWGMTETSpLGTVARPPSEHSNLSedeqlalr 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 339 -TIGTAIASVSW-VVDPEDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFiEDpAWLvdgcqgyagrrgrlyKTGD 416
Cdd:cd12119 342 aKQGRPVPGVELrIVDDDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEALT-ED-GWL---------------RTGD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 417 LVRYDDEGNLVCLGR-KDSqVKVRGQRVELGEIEHHIQGCmPEANQIAV---------E-----VILLEGEksntilaaf 481
Cdd:cd12119 405 VATIDEDGYLTITDRsKDV-IKSGGEWISSVELENAIMAH-PAVAEAAVigvphpkwgErplavVVLKEGA--------- 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 482 lQLDVKTGRAFptnkaaetgslaqvifpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:cd12119 474 -TVTAEELLEF-----------------------LADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
61-551 |
8.63e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 95.29 E-value: 8.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 61 MSYSVLDGLSTKLA-GYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVS 139
Cdd:PLN02574 67 ISYSELQPLVKSMAaGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 140 AQHSARWASSSCHVVTLSE-----------ASIGQLTVEDdlPGFSATP----GNAAYVLFTSGSTGIPKGVVLEHR--- 201
Cdd:PLN02574 147 PENVEKLSPLGVPVIGVPEnydfdskriefPKFYELIKED--FDFVPKPvikqDDVAAIMYSSGTTGASKGVVLTHRnli 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 202 -AVSTSCLGHGRAFGITDQSRVLQFTSYTFD-FCMAEIITTLLYGGCICVPSDRDRHSDLAKAINTMGANWALLTPSVAQ 279
Cdd:PLN02574 225 aMVELFVRFEASQYEYPGSDNVYLAALPMFHiYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 280 LLNPSDVP-------TLKILVIGGEQVTSK---DWNRWPTSVQLINGYGPTECCIVCT-GYTTTQAFKTGTIGTAIASV- 347
Cdd:PLN02574 305 ALTKKAKGvcgevlkSLKQVSCGAAPLSGKfiqDFVQTLPHVDFIQGYGMTESTAVGTrGFNTEKLSKYSSVGLLAPNMq 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 348 SWVVDPEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLV 427
Cdd:PLN02574 385 AKVVDWSTGCLLPP-GNCGELWIQGPGVMKGYLNNPKATQSTIDKD-GWL---------------RTGDIAYFDEDGYLY 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 428 CLGRKDSQVKVRGQRVELGEIEhHIQGCMPEANQIAveVILLEGEKSNTILAAFLqldVKtgrafptnKAAETGSLAQVI 507
Cdd:PLN02574 448 IVDRLKEIIKYKGFQIAPADLE-AVLISHPEIIDAA--VTAVPDKECGEIPVAFV---VR--------RQGSTLSQEAVI 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1779949166 508 FPVEagKKLAerlPSYMVPDVYFvVTQLPITVSGKTDRKRLREI 551
Cdd:PLN02574 514 NYVA--KQVA---PYKKVRKVVF-VQSIPKSPAGKILRRELKRS 551
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1141-1569 |
1.11e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 93.51 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLASea 1220
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1221 saplakdlvgtvvivnadsalqlahhaspitsvrpthTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRT 1300
Cdd:cd05934 83 -------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1301 LQF--------ASYAFAGSLVellmnlchGGCICVLSEEERRTDLASAMCRMKVNWAFLTSTVVDLL--TPKSV-----P 1365
Cdd:cd05934 126 LTVlplfhinaQAVSVLAALS--------VGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLlaQPPSPddrahR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1366 SLSILCVGGEPIRASQIV-RWGsqVHLRQTYGSSEVSGIVSSAALTTCSTTrDVGRASTGV-FWIVDPnnHNRLAPVGAV 1443
Cdd:cd05934 198 LRAAYGAPNPPELHEEFEeRFG--VRLLEGYGMTETIVGVIGPRDEPRRPG-SIGRPAPGYeVRIVDD--DGQELPAGEP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1444 GEVLV---EGPVLGREYIDEPDKTAStfieapAWRASLglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIE 1520
Cdd:cd05934 273 GELVIrglRGWGFFKGYYNMPEATAE------AMRNGW---------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1779949166 1521 VEEIEhQARLAEADVAEIAVELIQPKDGEDGMLACFIVVEDSASNEDEL 1569
Cdd:cd05934 338 SAEVE-RAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEEL 385
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
39-557 |
1.53e-19 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 94.29 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 39 DLFAEQvlAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGD--VVPLCFEKSMWtvVAMLAVLKAGgaFAPLD 116
Cdd:PRK10946 29 DILTRH--AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDtaLVQLGNVAEFY--ITFFALLKLG--VAPVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 117 P--DHPVSRHKEILRQTGARMVVVSAQHS-----------ARWASSSCHVVTLSEASIGQLT--VEDDLPGFSATPGNAA 181
Cdd:PRK10946 103 AlfSHQRSELNAYASQIEPALLIADRQHAlfsdddflntlVAEHSSLRVVLLLNDDGEHSLDdaINHPAEDFTATPSPAD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 182 YVLF---TSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAE--IITTLLYGGCICVPSDR--- 253
Cdd:PRK10946 183 EVAFfqlSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYPMSSpgALGVFLAGGTVVLAPDPsat 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 254 ------DRHSdlakaINTMganwALLTPSVAQLLNPSDVP-------TLKILVIGGEQVTSKDWNRWPTSV--QLINGYG 318
Cdd:PRK10946 263 lcfpliEKHQ-----VNVT----ALVPPAVSLWLQAIAEGgsraqlaSLKLLQVGGARLSETLARRIPAELgcQLQQVFG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 319 PTECcIVCtgYT----------TTQafktgtiGTAIASVS--WVVDpEDYHKLAPlGSVGELLVEGPILARGYLNDAEKT 386
Cdd:PRK10946 334 MAEG-LVN--YTrlddsderifTTQ-------GRPMSPDDevWVAD-ADGNPLPQ-GEVGRLMTRGPYTFRGYYKSPQHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 387 AAAFIEDpawlvdgcqGYagrrgrlYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEH----HiqgcmPE---A 459
Cdd:PRK10946 402 ASAFDAN---------GF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENlllrH-----PAvihA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 460 NQIAVEVILLeGEKSntilAAFLqldVKTgrafptnkaaetgslaQVIFPVEAGKKLAER-LPSYMVPDVYFVVTQLPIT 538
Cdd:PRK10946 461 ALVSMEDELM-GEKS----CAFL---VVK----------------EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLT 516
|
570
....*....|....*....
gi 1779949166 539 VSGKTDRKRLREIGASFSA 557
Cdd:PRK10946 517 AVGKVDKKQLRQWLASRAS 535
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
693-881 |
1.56e-19 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 89.71 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 693 SPLQEGMMALASKRPgDYIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTR-----------IVHSSKMGMLQVVLADG 761
Cdd:COG4908 2 SPAQKRFLFLEPGSN-AYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRfveedgepvqrIDPDADLPLEVVDLSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 762 IEWEQANELEQYLEKDKSVSMGLGDS-LARYALVRdVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPG- 839
Cdd:COG4908 81 PEPEREAELEELVAEEASRPFDLARGpLLRAALIR-LGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPPPl 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 840 ------FNAFI----KYLGEQDHEAAAAYWQGTLADcqAISFPALPPAVQQP 881
Cdd:COG4908 160 pelpiqYADYAawqrAWLQSEALEKQLEYWRQQLAG--APPVLELPTDRPRP 209
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1128-1569 |
2.78e-19 |
|
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: 93.15 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAICAWDGDM--TYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRL 1205
Cdd:cd05926 1 PDAPALVVPGSTPalTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1206 MCRKVSAKLSLASE----ASAPLAKDLVGTVV--------IVNADSALQLAHH------ASPITSVRPTHTAYVIFTSGS 1267
Cdd:cd05926 81 YLADLGSKLVLTPKgelgPASRAASKLGLAILelaldvgvLIRAPSAESLSNLladkknAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1268 TGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFAS-YAFAGSLVELLMNLCHGGCIcVLSEEERRTDLASAMCRMKV 1346
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPlFHVHGLVASLLSTLAAGGSV-VLPPRFSASTFWPDVRDYNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1347 NWafLTstvvdlltpkSVPSL-SILCVGGEPIRAS-----QIVRWGS-----QVHLR----------QTYGSSEVSGIVS 1405
Cdd:cd05926 240 TW--YT----------AVPTIhQILLNRPEPNPESpppklRFIRSCSaslppAVLEAleatfgapvlEAYGMTEAAHQMT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1406 SAAL-TTCSTTRDVGRASTGVFWIVDPNnhNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPaWraslglsagq 1484
Cdd:cd05926 308 SNPLpPGPRKPGSVGKPVGVEVRILDED--GEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG-W---------- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1485 qrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHqARLAEADVAEIAVELI-QPKDGEDgmLACFIV-VEDS 1562
Cdd:cd05926 375 ---FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDG-VLLSHPAVLEAVAFGVpDEKYGEE--VAAAVVlREGA 448
|
....*..
gi 1779949166 1563 ASNEDEL 1569
Cdd:cd05926 449 SVTEEEL 455
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
60-545 |
3.59e-19 |
|
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: 92.51 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 60 EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPD-HPVSRHkeilrqtgarmvvv 138
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEfTADEVH-------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 139 saqhsarwassscHVVTLSEASIGQLTVEDDLpgfsatpgnaAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITD 218
Cdd:cd05914 73 -------------HILNHSEAKAIFVSDEDDV----------ALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 219 QSRVLQFTSYTFDF-CMAEIITTLLYGGCIC----VPSDR-----------------------DRHSDLAKAINTMGANW 270
Cdd:cd05914 130 GDKILSILPLHHIYpLTFTLLLPLLNGAHVVfldkIPSAKiialafaqvtptlgvpvplviekIFKMDIIPKLTLKKFKF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 271 ALLTP--------SVAQLLNPSDVPTLKILVIGGEQVtSKDWNRWPTSVQL--INGYGPTECC-IVCtgYTTTQAFKTGT 339
Cdd:cd05914 210 KLAKKinnrkirkLAFKKVHEAFGGNIKEFVIGGAKI-NPDVEEFLRTIGFpyTIGYGMTETApIIS--YSPPNRIRLGS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 340 IGTAIASVSWVVDPEDyhklaPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrgrlyKTGDLVR 419
Cdd:cd05914 287 AGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKD-GWF---------------HTGDLGK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 420 YDDEGNLVCLGRKDSQ-VKVRGQRVELGEIEHHIQGcMPeANQIAvEVILLEGEKSNTILAAFLQLDVKTGRafptNKAA 498
Cdd:cd05914 346 IDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINN-MP-FVLES-LVVVQEKKLVALAYIDPDFLDVKALK----QRNI 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1779949166 499 ETGSLAQVIfpveagKKLAERLPSY-MVPDVYFVVTQLPITVSGKTDR 545
Cdd:cd05914 419 IDAIKWEVR------DKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
42-569 |
3.65e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 93.30 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 42 AEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPV 121
Cdd:PRK07786 24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 122 SRHKEILRQTGARMVVVSAQHSARWASSSCHVVTLSEASIGQLTVEDDLPGF-----SATPGNA---------AYVLFTS 187
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYedllaEAGPAHApvdipndspALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 188 GSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFC-MAEIITTLLYGGCICV-PSDRDRHSDLAKAINT 265
Cdd:PRK07786 184 GTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAgIGSMLPGLLLGAPTVIyPLGAFDPGQLLDVLEA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 266 MGANWALLTPS------VAQLLNPSDvptLKILVIGgeqvtskdWNRWPTS-------------VQLINGYGPTECC-IV 325
Cdd:PRK07786 264 EKVTGIFLVPAqwqavcAEQQARPRD---LALRVLS--------WGAAPASdtllrqmaatfpeAQILAAFGQTEMSpVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 326 CTGYTTTQAFKTGTIGTAIASVSWVVDPEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFieDPAWlvdgcqgya 405
Cdd:PRK07786 333 CMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPV-GEVGEIVYRAPTLMSGYWNNPEATAEAF--AGGW--------- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 406 grrgrlYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQLD 485
Cdd:PRK07786 401 ------FHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLAS-HPDIVEVA--VIGRADEKWGEVPVAVAAVR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 486 vktgrafPTNKAAETGSLAQVifpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREigaSFSAQQLAEIRT 565
Cdd:PRK07786 472 -------NDDAALTLEDLAEF---------LTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE---RYGACVNVERRS 532
|
....
gi 1779949166 566 SGQG 569
Cdd:PRK07786 533 ASAG 536
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
62-551 |
5.20e-19 |
|
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: 91.79 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 62 SYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPL----DPDHPVSRhkeiLRQTGARMVV 137
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLfsafGPEAIRDR----LENSEAKVLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 138 VSAQHSARwassschvvtlseasigqltveddlpgfsATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGIT 217
Cdd:cd05969 78 TTEELYER-----------------------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 218 DQSRVlqftsytfdFCMAE----------IITTLLYGGCICVPSDRDRHSDLAKAINTMGANWALLTPSVAQLLNPS--- 284
Cdd:cd05969 129 PDDIY---------WCTADpgwvtgtvygIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgde 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 285 -----DVPTLKILVIGGEQVTSK--DWNRWPTSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVSWVVDPEDYH 357
Cdd:cd05969 200 larkyDLSSLRFIHSVGEPLNPEaiRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 358 KLAPlGSVGELLVEG--PILARGYLNDAEKTAAAFIEdpawlvdgcqGYagrrgrlYKTGDLVRYDDEGNLVCLGRKDSQ 435
Cdd:cd05969 280 ELPP-GTKGILALKPgwPSMFRGIWNDEERYKNSFID----------GW-------YLTGDLAYRDEDGYFWFVGRADDI 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 436 VKVRGQRVELGEIEHHI--QGCMPEANQIAVEVILLeGEksntILAAFLQLdvKTGRAfPTNKAAEtgslaqvifpvEAG 513
Cdd:cd05969 342 IKTSGHRVGPFEVESALmeHPAVAEAGVIGKPDPLR-GE----IIKAFISL--KEGFE-PSDELKE-----------EII 402
|
490 500 510
....*....|....*....|....*....|....*...
gi 1779949166 514 KKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREI 551
Cdd:cd05969 403 NFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
1141-1586 |
5.36e-19 |
|
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: 91.74 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSL-PHERLRLMCRKVSAKLSlase 1219
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLtENERTNQLEDLDVQLLL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1220 ASAPLakDLVGTVVIVNADSALQLAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTR 1299
Cdd:TIGR01923 77 TDSLL--EEKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1300 TLQFASYAFAGSLVELLMNLCHGGCICVLSeeeRRTDLASAMCRMKVNWAFLTSTVVDLLTPKSVPSLSILCV--GGEPI 1377
Cdd:TIGR01923 155 WLLSLPLYHISGLSILFRWLIEGATLRIVD---KFNQLLEMIANERVTHISLVPTQLNRLLDEGGHNENLRKIllGGSAI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1378 RASQIVRWGSQ-VHLRQTYGSSEvsgivSSAALTTCSTTRDVGRASTGVfwiVDPNNHNRL--APVGAVGEVLVEGPVLG 1454
Cdd:TIGR01923 232 PAPLIEEAQQYgLPIYLSYGMTE-----TCSQVTTATPEMLHARPDVGR---PLAGREIKIkvDNKEGHGEIMVKGANLM 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1455 REYIDEPDKTASTFieapawraslglsagQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEAD 1534
Cdd:TIGR01923 304 KGYLYQGELTPAFE---------------QQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIE-TVLYQHPG 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 1535 VAEIAVelIQPKDGEDGMLACFIVVedsaSNEDELSGKrtrLDTRTQRTIGK 1586
Cdd:TIGR01923 368 IQEAVV--VPKPDAEWGQVPVAYIV----SESDISQAK---LIAYLTEKLAK 410
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1124-1550 |
6.02e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 92.80 E-value: 6.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIV----PLC--FeksmwtVVAMLAVLKAGGAFLLLDP- 1196
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVavflPNCpqF------HIVFFGILKLGAVHVPVSPl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1197 ----SLPHE-------------RLRLMCRKVSAKLS------------LASEASAPLAKDLVGTVVIVN--AD--SALQL 1243
Cdd:PRK06178 117 frehELSYElndagaevllaldQLAPVVEQVRAETSlrhvivtsladvLPAEPTLPLPDSLRAPRLAAAgaIDllPALRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1244 AHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHR-AASSAVTAHGRYLGMQASTRTLQF-ASYAFAGSLVELLMNLCH 1321
Cdd:PRK06178 197 CTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRdMVYTAAAAYAVAVVGGEDSVFLSFlPEFWIAGENFGLLFPLFS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1322 GGCICVLSeeerRTDLASAMC---RMKVNWAFLT-STVVDLL-TPKSVP-SLSILcvggEPIRASQIV---------RW- 1385
Cdd:PRK06178 277 GATLVLLA----RWDAVAFMAaveRYRVTRTVMLvDNAVELMdHPRFAEyDLSSL----RQVRVVSFVkklnpdyrqRWr 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1386 ---GSqVHLRQTYGSSEVSgivSSAALTTCSTTRD---------VGRASTG-VFWIVDPNNHnRLAPVGAVGEVLVEGPV 1452
Cdd:PRK06178 349 altGS-VLAEAAWGMTETH---TCDTFTAGFQDDDfdllsqpvfVGLPVPGtEFKICDFETG-ELLPLGAEGEIVVRTPS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1453 LGREYIDEPDKTASTFIEapAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIE-----HQ 1527
Cdd:PRK06178 424 LLKGYWNKPEATAEALRD--GW-------------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEallgqHP 488
|
490 500 510
....*....|....*....|....*....|
gi 1779949166 1528 ARLAEADVA-------EIAVELIQPKDGED 1550
Cdd:PRK06178 489 AVLGSAVVGrpdpdkgQVPVAFVQLKPGAD 518
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1141-1594 |
7.06e-19 |
|
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: 91.24 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGG----AFLLLDPSLPHERLRlmcrkvsaklsl 1216
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAvyvpLTTLLGPKDIEYRLE------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1217 ASEASAplakdlvgtvVIVNADSalqlahhaspitsvrpthTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQA 1296
Cdd:cd05972 70 AAGAKA----------IVTDAED------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1297 STRTLQFASYAFA-GSLVELLMNLCHGgcICVLSEEERRTDLASA---MCRMKVNWAFLTSTVVDLLTPKSVPS-----L 1367
Cdd:cd05972 122 DDIHWNIADPGWAkGAWSSFFGPWLLG--ATVFVYEGPRFDAERIlelLERYGVTSFCGPPTAYRMLIKQDLSSykfshL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1368 SILCVGGEPIRASQIVRWGSQVHL--RQTYGSSEVSgivssaalTTCSTTRD-------VGRASTG--VFwIVDPNNhnR 1436
Cdd:cd05972 200 RLVVSAGEPLNPEVIEWWRAATGLpiRDGYGQTETG--------LTVGNFPDmpvkpgsMGRPTPGydVA-IIDDDG--R 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1437 LAPVGAVGE--VLVEGPVLGREYIDEPDKTASTFIEApaWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKL 1514
Cdd:cd05972 269 ELPPGEEGDiaIKLPPPGLFLGYVGDPEKTEASIRGD--Y-------------YLTGDRAYRDEDGYFWFVGRADDIIKS 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1515 RGQRI---EVEE--IEHQArlaeadVAEIAVelIQPKDGEDG-MLACFIVV----EDSASNEDELSGK-RTRLDTRT--- 1580
Cdd:cd05972 334 SGYRIgpfEVESalLEHPA------VAEAAV--VGSPDPVRGeVVKAFVVLtsgyEPSEELAEELQGHvKKVLAPYKypr 405
|
490 500
....*....|....*....|...
gi 1779949166 1581 --------QRTI-GKIQDRLERD 1594
Cdd:cd05972 406 eiefveelPKTIsGKIRRVELRD 428
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1140-1540 |
9.68e-19 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 91.00 E-value: 9.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1140 MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLrlmcrkvsaklslase 1219
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKEREL---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1220 asAPLAKDLVGTVVIVNA---DSALqlahhaspitsvrpthtayVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQA 1296
Cdd:cd05935 66 --EYILNDSGAKVAVVGSeldDLAL-------------------IPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1297 STRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTDLASAMCRMKVN-WAFLTSTVVDLL-TPK----SVPSLSIL 1370
Cdd:cd05935 125 SDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTfWTNIPTMLVDLLaTPEfktrDLSSLKVL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1371 CVGGEPIRASQIVRWGSQVHLR--QTYGSSE-VSGIVSSAALTTCSTTrdVGRASTGV-FWIVDPNNHNRLaPVGAVGEV 1446
Cdd:cd05935 205 TGGGAPMPPAVAEKLLKLTGLRfvEGYGLTEtMSQTHTNPPLRPKLQC--LGIP*FGVdARVIDIETGREL-PPNEVGEI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1447 LVEGPVLGREYIDEPDKTASTFIEapawraslglsAGQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI---EVEE 1523
Cdd:cd05935 282 VVRGPQIFKGYWNRPEETEESFIE-----------IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVwpaEVEA 350
|
410
....*....|....*..
gi 1779949166 1524 IEHQARlAEADVAEIAV 1540
Cdd:cd05935 351 KLYKHP-AI*EVCVISV 366
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
349-644 |
9.85e-19 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 88.65 E-value: 9.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 349 WVVDPEDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPAwlvdGCQGYAGRRGRLYKTGDLVRYDDEGNLvc 428
Cdd:COG3433 23 AIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPF----IPVPYPAQPGRQADDLRLLLRRGLGPG-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 429 lGRKDSQVKVRGQRVELGEIEHHIQGCMPEANQIAVEVILLEGEKSNTILAAflqldvktgrafptnkAAETGSLAQVIF 508
Cdd:COG3433 97 -GGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIV----------------GAVAALDGLAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 509 PVEAgkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLReigasfSAQQLAEIRTSGQGLKRQPSTENEKALQQLWAG 588
Cdd:COG3433 160 AALA---ALDKVPPDVVAASAVVALDALLLLALKVVARAAP------ALAAAEALLAAASPAPALETALTEEELRADVAE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1779949166 589 VLAIDADSIGLDDSFFRLGGDSIAAMKLVGEARRAGIHLTVADLFRNPKLEAVASL 644
Cdd:COG3433 231 LLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWAL 286
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
49-551 |
2.01e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 90.41 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAvLKAGGAFAPLDPDHpVSRHkEIL 128
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHA-LQQLGAVAVLLNTR-LSRE-ELL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQ---TGARMVVVSAQHSARWASSSchVVTLSEASIGQLTVEDDLPGFSATpgNAAYVLFTSGSTGIPKGVVLE-----H 200
Cdd:PRK03640 93 WQlddAEVKCLITDDDFEAKLIPGI--SVKFAELMNGPKEEAEIQEEFDLD--EVATIMYTSGTTGKPKGVIQTygnhwW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 201 RAVStSCLGhgraFGITDQSRVLQ----FTSYTFDFCMAEIIttllYGGCICVPSDRDrhsdlAKAIN---------TMG 267
Cdd:PRK03640 169 SAVG-SALN----LGLTEDDCWLAavpiFHISGLSILMRSVI----YGMRVVLVEKFD-----AEKINkllqtggvtIIS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 268 ANWALLTPSVAQLLNPSDVPTLKILVIGG--------EQVTSKDwnrwptsVQLINGYGPTECCI-VCTGYTTTQAFKTG 338
Cdd:PRK03640 235 VVSTMLQRLLERLGEGTYPSSFRCMLLGGgpapkpllEQCKEKG-------IPVYQSYGMTETASqIVTLSPEDALTKLG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 339 TIGTAIASVSwvVDPEDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEdpAWLvdgcqgyagrrgrlyKTGDLV 418
Cdd:PRK03640 308 SAGKPLFPCE--LKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD--GWF---------------KTGDIG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 419 RYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFlqldVKTGRAFPTNKAA 498
Cdd:PRK03640 369 YLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS-HPGVAEAG--VVGVPDDKWGQVPVAF----VVKSGEVTEEELR 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 499 ETGSlaqvifpveagkklaERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREI 551
Cdd:PRK03640 442 HFCE---------------EKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1258-1571 |
2.28e-18 |
|
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: 88.47 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1258 TAYVIFTSGSTGEPKGCRIEHRAAsSAVTAHGRYLGMQASTR--TLQFASYAFAGSLVELLMNLCHGGCICVLSE----- 1330
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTF-FAVPDILQKEGLNWVVGdvTYLPLPATHIGGLWWILTCLIHGGLCVTGGEnttyk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1331 ---EERRTDLASAMCRMKVNWAFLTSTVVDLLtpKSVPSLSILCVGGE-PIRA-SQIVRWGSQVHLRQTYGSSEVSgivs 1405
Cdd:cd17635 82 slfKILTTNAVTTTCLVPTLLSKLVSELKSAN--ATVPSLRLIGYGGSrAIAAdVRFIEATGLTNTAQVYGLSETG---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1406 saALTTCSTTRD------VGRASTGV-FWIVdpNNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapAWrasl 1478
Cdd:cd17635 156 --TALCLPTDDDsieinaVGRPYPGVdVYLA--ATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID--GW---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1479 glsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVELIqpKDGEDGMLACFIV 1558
Cdd:cd17635 226 ---------VNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECACYEI--SDEEFGELVGLAV 293
|
330
....*....|...
gi 1779949166 1559 VEDSASNEDELSG 1571
Cdd:cd17635 294 VASAELDENAIRA 306
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1141-1569 |
2.43e-18 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 89.87 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLASEa 1220
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1221 saplakdlvgtvvivnadsalQLAHHASPITSvrpthtAYVIFTSGSTGEPKGcrIEHraASSAVTAH---GRY-LGMQA 1296
Cdd:cd05969 81 ---------------------ELYERTDPEDP------TLLHYTSGTTGTPKG--VLH--VHDAMIFYyftGKYvLDLHP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1297 STRTLQFASYAF-AGSLVELLMNLCHGGCICVLSEEERRTDLASAMCRMKVNWAFLTSTVVDLLTPKSV--------PSL 1367
Cdd:cd05969 130 DDIYWCTADPGWvTGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDelarkydlSSL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1368 SILCVGGEPIRAsQIVRWGSQVH---LRQTYGSSEVSGIVSSAALTTCSTTRDVGRASTGVFWIVDPNNHNRLAPvGAVG 1444
Cdd:cd05969 210 RFIHSVGEPLNP-EAIRWGMEVFgvpIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPP-GTKG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1445 EVLVEG--PVLGREYIDEPDKTASTFIEApaWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI--- 1519
Cdd:cd05969 288 ILALKPgwPSMFRGIWNDEERYKNSFIDG--W-------------YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVgpf 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 1520 EVEE--IEHQArlaeadVAEIAVelIQPKDGEDG-MLACFIVVEDSASNEDEL 1569
Cdd:cd05969 353 EVESalMEHPA------VAEAGV--IGKPDPLRGeIIKAFISLKEGFEPSDEL 397
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
49-550 |
4.26e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 89.66 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVV-SAQHSARW------ASSSCHVVTLSEASIG-----QLTVEDDLPGFS-ATPGNAAYVLFTSGSTGIPKG 195
Cdd:PRK06188 106 EDAGISTLIVdPAPFVERAlallarVPSLKHVLTLGPVPDGvdllaAAAKFGPAPLVAaALPPDIAGLAYTGGTTGKPKG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 196 VVLEHRAVSTSCLGHGRAFGITDQSRVLQFT-----SYTFdfcmaeIITTLLYGGCICVPSDRDRHSDLAkAINTMGANW 270
Cdd:PRK06188 186 VMGTHRSIATMAQIQLAEWEWPADPRFLMCTplshaGGAF------FLPTLLRGGTVIVLAKFDPAEVLR-AIEEQRITA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 271 ALLTPSV--AQLLNP----SDVPTLKILVIGGEQVT----SKDWNRW-PTSVQLingYGPTECCIVCT-----GYTTTQA 334
Cdd:PRK06188 259 TFLVPTMiyALLDHPdlrtRDLSSLETVYYGASPMSpvrlAEAIERFgPIFAQY---YGQTEAPMVITylrkrDHDPDDP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 335 FKTGTIGTAIASVSWVV-DPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpaWLvdgcqgyagrrgrlyK 413
Cdd:PRK06188 336 KRLTSCGRPTPGLRVALlDEDG--REVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG--WL---------------H 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 414 TGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQLdvktgRAFP 493
Cdd:PRK06188 397 TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAE-HPAVAQVA--VIGVPDEKWGEAVTAVVVL-----RPGA 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 494 TNKAAETgslaqvifpVEAGKklaERLPSYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:PRK06188 469 AVDAAEL---------QAHVK---ERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
174-550 |
7.18e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 89.44 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 174 SATPGNAAYVLFTSGSTGIPKGVVLEHR----------AVSTSCLGHGRAFGITDqsrVLQFTSYTFDF-CMAeiitTLL 242
Cdd:PRK05677 203 NPQADDVAVLQYTGGTTGVAKGAMLTHRnlvanmlqcrALMGSNLNEGCEILIAP---LPLYHIYAFTFhCMA----MML 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 243 YGG-CICVPSDRDRHS---DLAK-------AINTMGAnwALLTPSVAQLLnpsDVPTLKILVIGGEQVTSKDWNRWP--T 309
Cdd:PRK05677 276 IGNhNILISNPRDLPAmvkELGKwkfsgfvGLNTLFV--ALCNNEAFRKL---DFSALKLTLSGGMALQLATAERWKevT 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 310 SVQLINGYGPTECCIVCTGyTTTQAFKTGTIGTAIASVSWVVDPEDYHKLaPLGSVGELLVEGPILARGYLNDAEKTAAA 389
Cdd:PRK05677 351 GCAICEGYGMTETSPVVSV-NPSQAIQVGTIGIPVPSTLCKVIDDDGNEL-PLGEVGELCVKGPQVMKGYWQRPEATDEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 390 FIEDpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEhHIQGCMPEANQIAveVILL 469
Cdd:PRK05677 429 LDSD-GWL---------------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELE-DVLAALPGVLQCA--AIGV 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 470 EGEKSNTILAAFLQldVKTGRAFPTNKAAEtgslaqvifpveagkKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:PRK05677 490 PDEKSGEAIKVFVV--VKPGETLTKEQVME---------------HMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
.
gi 1779949166 550 E 550
Cdd:PRK05677 553 D 553
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
25-551 |
7.20e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 89.11 E-value: 7.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 25 WNHKIP-GVTN-------KCIHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVK-IGVKPGDVVPLCFEKS 95
Cdd:PRK12492 6 WNDKRPaGVPStidlaayKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 96 MWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSAQHSARWAS--SSCHVVTLSEASIGQL--------- 164
Cdd:PRK12492 86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEvlPDTGIEYLIEAKMGDLlpaakgwlv 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 165 -TVEDD---------LP-------------GFSATP-----GNAAYVLFTSGSTGIPKGVVLEHRAVST------SCLGH 210
Cdd:PRK12492 166 nTVVDKvkkmvpayhLPqavpfkqalrqgrGLSLKPvpvglDDIAVLQYTGGTTGLAKGAMLTHGNLVAnmlqvrACLSQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 211 GRAFG---ITDQSRVL-----QFTSYTFDF-CMAEIITTllyGGCICVPSDRDrhsdLAKAINTMGaNW---ALL---TP 275
Cdd:PRK12492 246 LGPDGqplMKEGQEVMiaplpLYHIYAFTAnCMCMMVSG---NHNVLITNPRD----IPGFIKELG-KWrfsALLglnTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 276 SVAQLLNPS----DVPTLKILVIGGEQVTSKDWNRWP--TSVQLINGYGPTECC-IVCTGYTTTQAfKTGTIGTAIASVS 348
Cdd:PRK12492 318 FVALMDHPGfkdlDFSALKLTNSGGTALVKATAERWEqlTGCTIVEGYGLTETSpVASTNPYGELA-RLGTVGIPVPGTA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 349 WVVDPEDYHKLaPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVC 428
Cdd:PRK12492 397 LKVIDDDGNEL-PLGERGELCIKGPQVMKGYWQQPEATAEALDAE-GWF---------------KTGDIAVIDPDGFVRI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 429 LGRKDSQVKVRGQRVELGEIEHHIQGCMPEANQIAVEVIllegeksntilaaflqlDVKTGRAFPTNKAAETGSLAqvif 508
Cdd:PRK12492 460 VDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVP-----------------DERSGEAVKLFVVARDPGLS---- 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1779949166 509 pVEAGKKLA-ERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREI 551
Cdd:PRK12492 519 -VEELKAYCkENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1107-1582 |
9.53e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 88.91 E-value: 9.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1107 DVPPAI-ERCIhdlfaDQAKARPDAPAICAWDG--DMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLA 1183
Cdd:PRK05857 11 QLPSTVlDRVF-----EQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1184 VLKAGGAFLLLDPSLPH---ERLRLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSALQLAHHASPITSVRP-THTA 1259
Cdd:PRK05857 86 CAKLGAIAVMADGNLPIaaiERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLaGNAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1260 Y-------VIFTSGSTGEPKGCRIEHR---AASSAVTAHG-RYLGMQASTRTLQFASYAFAGSLVELLMNLCHGG-CIcv 1327
Cdd:PRK05857 166 QgsedplaMIFTSGTTGEPKAVLLANRtffAVPDILQKEGlNWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGlCV-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1328 lSEEERRTDLASAMCRMKVNWAFLTSTVVDLL------TPKSVPSLSILCVGGEPIRASQiVRW--GSQVHLRQTYGSSE 1399
Cdd:PRK05857 244 -TGGENTTSLLEILTTNAVATTCLVPTLLSKLvselksANATVPSLRLVGYGGSRAIAAD-VRFieATGVRTAQVYGLSE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1400 VSGIVSSAALTTCSTTR----DVGRASTGV-FWIVDPNNHNRLAPVGA----VGEVLVEGPVLGREYIDEPDKTASTFIE 1470
Cdd:PRK05857 322 TGCTALCLPTDDGSIVKieagAVGRPYPGVdVYLAATDGIGPTAPGAGpsasFGTLWIKSPANMLGYWNNPERTAEVLID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1471 apAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhqaRLAE--ADVAEIAVELIqpKDG 1548
Cdd:PRK05857 402 --GW-------------VNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD---RIAEgvSGVREAACYEI--PDE 461
|
490 500 510
....*....|....*....|....*....|....
gi 1779949166 1549 EDGMLACFIVVEDSASNEDELSGKRTRLDTRTQR 1582
Cdd:PRK05857 462 EFGALVGLAVVASAELDESAARALKHTIAARFRR 495
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1125-1540 |
1.22e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 88.12 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1125 KARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPL----CFEKSMWTVVAMLAVLK-------------- 1186
Cdd:PRK06188 23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALlslnRPEVLMAIGAAQLAGLRrtalhplgslddha 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1187 -----AGGAFLLLDPSLPHERLRLMCRKVSAKLSLASEASAPLAKDLVgtvvivnadSALQLAHHASPITSVRPTHTAYV 1261
Cdd:PRK06188 103 yvledAGISTLIVDPAPFVERALALLARVPSLKHVLTLGPVPDGVDLL---------AAAAKFGPAPLVAAALPPDIAGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1262 IFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFA--SYAfAGSLVelLMNLCHGGCICVLSEEErrtdlAS 1339
Cdd:PRK06188 174 AYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTplSHA-GGAFF--LPTLLRGGTVIVLAKFD-----PA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1340 AMCRM----KVNWAFLTSTVVDLLT--PKS----VPSLSILCVGGEPIRASQIV----RWGSQvhLRQTYGSSEVSGIVS 1405
Cdd:PRK06188 246 EVLRAieeqRITATFLVPTMIYALLdhPDLrtrdLSSLETVYYGASPMSPVRLAeaieRFGPI--FAQYYGQTEAPMVIT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1406 -----------SAALTTCsttrdvGRASTGV-FWIVDPNnhNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFieAPA 1473
Cdd:PRK06188 324 ylrkrdhdpddPKRLTSC------GRPTPGLrVALLDED--GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF--RDG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 1474 WraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQarLAE-ADVAEIAV 1540
Cdd:PRK06188 394 W-------------LHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDV--LAEhPAVAQVAV 446
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1122-1524 |
1.28e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 88.42 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1122 DQAKARPDAPAICA---WDGD-------MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAF 1191
Cdd:PRK09274 14 RAAQERPDQLAVAVpggRGADgklaydeLSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1192 LLLDPSLPHERLRLMCRKVSAK----LSLASEASA--PLAKDLVGTVVIVNADSA----------LQLAHHASPITSVRP 1255
Cdd:PRK09274 94 VLVDPGMGIKNLKQCLAEAQPDafigIPKAHLARRlfGWGKPSVRRLVTVGGRLLwggttlatllRDGAAAPFPMADLAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1256 THTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLqfASY-AFAgslvelLMNLCHGGCiCVLSEeerr 1334
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDL--PTFpLFA------LFGPALGMT-SVIPD---- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1335 TDLA-----------SAMCRMKVNWAFLTSTVVDLLT------PKSVPSLSILCVGGEPI------RASQIVRWGSQVHl 1391
Cdd:PRK09274 241 MDPTrpatvdpaklfAAIERYGVTNLFGSPALLERLGrygeanGIKLPSLRRVISAGAPVpiavieRFRAMLPPDAEIL- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1392 rQTYGSSE---VSGIVSSAALttcSTTRD---------VGRASTGVFW----IVD-PNNH---NRLAPVGAVGEVLVEGP 1451
Cdd:PRK09274 320 -TPYGATEalpISSIESREIL---FATRAatdngagicVGRPVDGVEVriiaISDaPIPEwddALRLATGEIGEIVVAGP 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 1452 VLGREYIDEPDKTASTFIEAPA---WraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQR---IEVEEI 1524
Cdd:PRK09274 396 MVTRSYYNRPEATRLAKIPDGQgdvW-------------HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTlytIPCERI 461
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
185-549 |
2.15e-17 |
|
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: 85.79 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 185 FTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRV-LQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAKAI 263
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcIPVPLFHCFGSVLGVLACLTHGATMVFPSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 264 NTMGANWALLTPS--VAQLLNPS----DVPTLKILVIGGEQVTSKDWNRwptSVQLIN------GYGPTECCIVCTGYTT 331
Cdd:cd05917 89 EKEKCTALHGVPTmfIAELEHPDfdkfDLSSLRTGIMAGAPCPPELMKR---VIEVMNmkdvtiAYGMTETSPVSTQTRT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 332 TQAF--KTGTIGTAIASV-SWVVDPEDyHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpawlvdgcqgyagrr 408
Cdd:cd05917 166 DDSIekRVNTVGRIMPHTeAKIVDPEG-GIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD--------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 409 gRLYKTGDLVRYDDEGNLVCLGR-KDsqVKVRG-QRVELGEIE-----HHiqgcmpeanQIA-VEVILLEGEKSNTILAA 480
Cdd:cd05917 230 -GWLHTGDLAVMDEDGYCRIVGRiKD--MIIRGgENIYPREIEeflhtHP---------KVSdVQVVGVPDERYGEEVCA 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 481 FLQLdvktgrafptnKAAETGSLAQVIfpveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:cd05917 298 WIRL-----------KEGAELTEEDIK------AYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1124-1500 |
2.45e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 87.32 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPAICAWDGDMTYGELDVLSGRLAGHLV-ELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHER 1202
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1203 LRLMCRKVSAKLSLASEASAPLAKDLVGTV----VIV----NADSA---------LQLAHHASPITSVR----------- 1254
Cdd:PRK08314 100 LAHYVTDSGARVAIVGSELAPKVAPAVGNLrlrhVIVaqysDYLPAepeiavpawLRAEPPLQALAPGGvvawkealaag 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1255 ---PTHTAY-----VI-FTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFASY----AFAGSlvellMN--L 1319
Cdd:PRK08314 180 lapPPHTAGpddlaVLpYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLfhvtGMVHS-----MNapI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1320 CHGGCICVLSEEERRTdLASAMCRMKV-NWAFLTSTVVDLL-TPK----SVPSLSILCVGGEPIRASQIVRwgsqvhLRQ 1393
Cdd:PRK08314 255 YAGATVVLMPRWDREA-AARLIERYRVtHWTNIPTMVVDFLaSPGlaerDLSSLRYIGGGGAAMPEAVAER------LKE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1394 TYGSSEVSGI-VSSAALTTCSTTRD------VGRASTGV-FWIVDPNNHNRLaPVGAVGEVLVEGPVLGREYIDEPDKTA 1465
Cdd:PRK08314 328 LTGLDYVEGYgLTETMAQTHSNPPDrpklqcLGIPTFGVdARVIDPETLEEL-PPGEVGEIVVHGPQVFKGYWNRPEATA 406
|
410 420 430
....*....|....*....|....*....|....*
gi 1779949166 1466 STFIEapawraslglsAGQQRLYKTGDLARYKDDG 1500
Cdd:PRK08314 407 EAFIE-----------IDGKRFFRTGDLGRMDEEG 430
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
34-551 |
3.42e-17 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 87.03 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 34 NKCIHDLFAEQVLAQPNAPAICAWDGE------MSYSVLDGLSTKLAGYLVKIGVKPGDVVPlCFEKSMWTVVAM-LAVL 106
Cdd:PRK13295 23 DRTINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVS-CQLPNWWEFTVLyLACS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 107 KAGGAFAPLdpdHPVSRHKEI---LRQTGARMVVVSAQ-----HSARWAS------SSCHVVT------------LSEAS 160
Cdd:PRK13295 102 RIGAVLNPL---MPIFRERELsfmLKHAESKVLVVPKTfrgfdHAAMARRlrpelpALRHVVVvggdgadsfealLITPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 161 IGQltvEDDLPGFSAT----PGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSytfdfcMAE 236
Cdd:PRK13295 179 WEQ---EPDAPAILARlrpgPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASP------MAH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 237 iITTLLYGgcICVPS------------DRDRHSDLakaINTMGANWALL-TPSVAQLLN-----PSDVPTLKILVIGGEQ 298
Cdd:PRK13295 250 -QTGFMYG--LMMPVmlgatavlqdiwDPARAAEL---IRTEGVTFTMAsTPFLTDLTRavkesGRPVSSLRTFLCAGAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 299 ----VTSKDWNRWPTSVqlINGYGPTECCIVCTGYTTTQAFKTGTI-GTAIASVSW-VVDPEDyhKLAPLGSVGELLVEG 372
Cdd:PRK13295 324 ipgaLVERARAALGAKI--VSAWGMTENGAVTLTKLDDPDERASTTdGCPLPGVEVrVVDADG--APLPAGQIGRLQVRG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 373 PILARGYLndaektaaafiEDPAWLVDGCQGYagrrgrlYKTGDLVRYDDEGNLVCLGR-KDsqVKVRG-QRVELGEIE- 449
Cdd:PRK13295 400 CSNFGGYL-----------KRPQLNGTDADGW-------FDTGDLARIDADGYIRISGRsKD--VIIRGgENIPVVEIEa 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 450 ---HHiqgcmPEANQIAVEVILLE--GEKSNtilaaflqldvktgrAFPTNKAAETGSLAQVIFPVEAgKKLAERlpsYM 524
Cdd:PRK13295 460 llyRH-----PAIAQVAIVAYPDErlGERAC---------------AFVVPRPGQSLDFEEMVEFLKA-QKVAKQ---YI 515
|
570 580
....*....|....*....|....*..
gi 1779949166 525 vPDVYFVVTQLPITVSGKTDRKRLREI 551
Cdd:PRK13295 516 -PERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
73-449 |
4.29e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 86.78 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 73 LAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVV--SAQH-------- 142
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTdeTCSSwyeelqnd 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 143 ---SARW---ASSSCHVVT------LSEASIGQLTVEDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGH 210
Cdd:PLN02860 125 rlpSLMWqvfLESPSSSVFiflnsfLTTEMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 211 GRAFGITDQSRVLqftsYTFDFC----MAEIITTLLYGGC------------------------ICVPSdrdRHSDLAkA 262
Cdd:PLN02860 205 IAIVGYGEDDVYL----HTAPLChiggLSSALAMLMVGAChvllpkfdakaalqaikqhnvtsmITVPA---MMADLI-S 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 263 INTMGANWAlLTPSVAQLLNpsdvptlkilviGGEQVTS---KDWNRWPTSVQLINGYGPTECC---IVCTGYTTTQAFK 336
Cdd:PLN02860 277 LTRKSMTWK-VFPSVRKILN------------GGGSLSSrllPDAKKLFPNAKLFSAYGMTEACsslTFMTLHDPTLESP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 337 TGTIGTAIASVSWVVDPedYH-----KLAP----------LGSVGELLVEGPILARGYLNDAEKTAAAFIEDpAWLvdgc 401
Cdd:PLN02860 344 KQTLQTVNQTKSSSVHQ--PQgvcvgKPAPhvelkigldeSSRVGRILTRGPHVMLGYWGQNSETASVLSND-GWL---- 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1779949166 402 qgyagrrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIE 449
Cdd:PLN02860 417 -----------DTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVE 453
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1141-1526 |
4.36e-17 |
|
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: 86.57 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDP----SLPHERLRLMCR-------- 1208
Cdd:cd05906 41 SYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptyDEPNARLRKLRHiwqllgsp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1209 KVSAKLSLASEAsAPLAKDLV--GTVVIVNADSALQLAHHASPItsVRPTHTAYVIFTSGSTGEPKGCRIEHR---AASS 1283
Cdd:cd05906 121 VVLTDAELVAEF-AGLETLSGlpGIRVLSIEELLDTAADHDLPQ--SRPDDLALLMLTSGSTGFPKAVPLTHRnilARSA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1284 AVTAHGRYlgmQASTRTLQFASYAFAGSLVEL-LMNLCHGgciC---------VLSEEERRTDLASAMcRMKVNWA--FL 1351
Cdd:cd05906 198 GKIQHNGL---TPQDVFLNWVPLDHVGGLVELhLRAVYLG---CqqvhvpteeILADPLRWLDLIDRY-RVTITWApnFA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1352 TSTVVDLL---TPKS--VPSLSILCVGGEPIRASQIVRWGSQVH--------LRQTYGSSE-VSGIVSSAALTTCSTTR- 1416
Cdd:cd05906 271 FALLNDLLeeiEDGTwdLSSLRYLVNAGEAVVAKTIRRLLRLLEpyglppdaIRPAFGMTEtCSGVIYSRSFPTYDHSQa 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1417 ----DVGRASTGV-FWIVDPNnhNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEApAWraslglsagqqrlYKTG 1491
Cdd:cd05906 351 lefvSLGRPIPGVsMRIVDDE--GQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED-GW-------------FRTG 414
|
410 420 430
....*....|....*....|....*....|....*
gi 1779949166 1492 DLArYKDDGSIELIGRKDNQVKLRGQRIEVEEIEH 1526
Cdd:cd05906 415 DLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEA 448
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1118-1564 |
4.43e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 86.72 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1118 DLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIV----PLCFEKSMW---------TVVAM--- 1181
Cdd:PRK06164 14 SLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVavwlPNCIEWVVLflacarlgaTVIAVntr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1182 -----LAVL--KAGGAFLLLDPSL-------------PHERLRLmcRKVSAKLSLASEASAPLAKDLVgtvviVNADSAL 1241
Cdd:PRK06164 94 yrsheVAHIlgRGRARWLVVWPGFkgidfaailaavpPDALPPL--RAIAVVDDAADATPAPAPGARV-----QLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1242 QLAHHASPITSVRPTHTAYVIFTSGSTGEPKgcRIEHRaaSSAVTAHG----RYLGMQASTRTLQFASYAFAGSLVELLM 1317
Cdd:PRK06164 167 PAPPAAAGERAADPDAGALLFTTSGTTSGPK--LVLHR--QATLLRHAraiaRAYGYDPGAVLLAALPFCGVFGFSTLLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1318 NLCHGGCICVLSE-EERRTdlASAMCRMKVNWAFLTSTVVDLL-----TPKSVPSLSILCVGGEPIRASQIVRWGSQ--V 1389
Cdd:PRK06164 243 ALAGGAPLVCEPVfDAART--ARALRRHRVTHTFGNDEMLRRIldtagERADFPSARLFGFASFAPALGELAALARArgV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1390 HLRQTYGSSEVSGIVSSAALTTCSTTRDVG----RASTGVFWIVDPNNhNRLAPVGAVGEVLVEGPVLGREYIDEPDKTA 1465
Cdd:PRK06164 321 PLTGLYGSSEVQALVALQPATDPVSVRIEGggrpASPEARVRARDPQD-GALLPDGESGEIEIRAPSLMRGYLDNPDATA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1466 STfIEAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHqaRLAEAD-VAEIAVELIQ 1544
Cdd:PRK06164 400 RA-LTDDGY-------------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEH--ALEALPgVAAAQVVGAT 463
|
490 500
....*....|....*....|
gi 1779949166 1545 pKDGEDGMLAcFIVVEDSAS 1564
Cdd:PRK06164 464 -RDGKTVPVA-FVIPTDGAS 481
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
37-436 |
5.42e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 86.48 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAfapld 116
Cdd:PRK07798 5 IADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 117 pdhPVS---RHKE-----ILRQTGARMVVVSAQHSARWA------SSSCHVVTLSEASIGQ-----------LTVEDDLP 171
Cdd:PRK07798 80 ---PVNvnyRYVEdelryLLDDSDAVALVYEREFAPRVAevlprlPKLRTLVVVEDGSGNDllpgavdyedaLAAGSPER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 172 GFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGhGRAFG----ITDQSRVLQFT-----SYTFDFC-------MA 235
Cdd:PRK07798 157 DFGERSPDDLYLLYTGGTTGMPKGVMWRQEDIFRVLLG-GRDFAtgepIEDEEELAKRAaagpgMRRFPAPplmhgagQW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 236 EIITTLLYGGCICVPSDR--DRHsDLAKAINTMGANWALLT------PSVAQLLNPS--DVPTLKILVIGGEQVTS--KD 303
Cdd:PRK07798 236 AAFAALFSGQTVVLLPDVrfDAD-EVWRTIEREKVNVITIVgdamarPLLDALEARGpyDLSSLFAIASGGALFSPsvKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 304 -WNRWPTSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVSWVVDpEDYHKLAPlGS--VGELLVEGPIlARGYL 380
Cdd:PRK07798 315 aLLELLPNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRTVVLD-EDGNPVEP-GSgeIGWIARRGHI-PLGYY 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1779949166 381 NDAEKTAAAFIEdpawlvdgcqgYAGRRGRLykTGDLVRYDDEGNLVCLGRkDSQV 436
Cdd:PRK07798 392 KDPEKTAETFPT-----------IDGVRYAI--PGDRARVEADGTITLLGR-GSVC 433
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
8-542 |
9.19e-17 |
|
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: 85.71 E-value: 9.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 8 PPRKNELEpqEMGQIW-AWnhkIPGVTNKCIHDLFAEQVLAQPNAPAICaWDGEM-------SYSVLDGLSTKLAGYLVK 79
Cdd:cd17634 30 QKVKNTSF--APGAPSiKW---FEDATLNLAANALDRHLRENGDRTAII-YEGDDtsqsrtiSYRELHREVCRFAGTLLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 80 IGVKPGDVV----PLCFEksmwTVVAMLAVLKAGGAFAPL----DPDHPVSRhkeiLRQTGARMVVVS------------ 139
Cdd:cd17634 104 LGVKKGDRVaiymPMIPE----AAVAMLACARIGAVHSVIfggfAPEAVAGR----IIDSSSRLLITAdggvragrsvpl 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 140 ---AQHSARWASSSCH---VVTLSEASIG---------QLTVEDDLPGFSATPGNAA---YVLFTSGSTGIPKGVVLEHR 201
Cdd:cd17634 176 kknVDDALNPNVTSVEhviVLKRTGSDIDwqegrdlwwRDLIAKASPEHQPEAMNAEdplFILYTSGTTGKPKGVLHTTG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 202 avstsclGHGRAfgitdqsrVLQFTSYTFDFCMAEIITT------------LLYGGCIC---------VPS--DRDRhsd 258
Cdd:cd17634 256 -------GYLVY--------AATTMKYVFDYGPGDIYWCtadvgwvtghsyLLYGPLACgattllyegVPNwpTPAR--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 259 LAKAINTMGANWALLTPSVAQLLNPS--------DVPTLKILVIGGEQVTSKDWnRWPTSV------QLINGYGPTECC- 323
Cdd:cd17634 318 MWQVVDKHGVNILYTAPTAIRALMAAgddaiegtDRSSLRILGSVGEPINPEAY-EWYWKKigkekcPVVDTWWQTETGg 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 324 IVCTGYTTTQAFKTGTIGTAIASVS-WVVDPEDyhKLAPLGSVGELLVEGPI--LARGYLNDaektaaafieDPAWLvdg 400
Cdd:cd17634 397 FMITPLPGAIELKAGSATRPVFGVQpAVVDNEG--HPQPGGTEGNLVITDPWpgQTRTLFGD----------HERFE--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 401 cQGYAGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAA 480
Cdd:cd17634 462 -QTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVA-HPKVAEAA--VVGIPHAIKGQAPYA 537
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 481 FLQLdvKTGRAFPTNKAAETGSlaqvifpveagkKLAERLPSYMVPDVYFVVTQLPITVSGK 542
Cdd:cd17634 538 YVVL--NHGVEPSPELYAELRN------------WVRKEIGPLATPDVVHWVDSLPKTRSGK 585
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
691-1039 |
1.24e-16 |
|
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: 84.35 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 691 PCSPLQEGMMALASKRPGD--YIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGMLQVVLADG------- 761
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGpaYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGpaplevr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 762 IEWEQANELEQYLEKDKSVSMGLGDSLARYALVR----DVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQ 837
Cdd:cd19539 83 DLSDPDSDRERRLEELLRERESRGFDLDEEPPIRavlgRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 838 P----------GFNAFIK-YLGEQDHEAAAAYWQGTLADCQAISFP---------ALPPAVQQPVADATTAFQCPALARR 897
Cdd:cd19539 163 AplpelrqqykEYAAWQReALAAPRAAELLDFWRRRLRGAEPTALPtdrprpagfPYPGADLRFELDAELVAALRELAKR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 898 psdiTMSTL---IRAAWALLASSYTSSDDVVFGATVTGRNAPvaGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQA 974
Cdd:cd19539 243 ----ARSSLfmvLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKAL 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 975 TEM-----IPYEQtgLHETAKVSADARHACSFQTLLIVQPGSNGDIAHDALGEWRSHSDLQDFTTYALMV 1039
Cdd:cd19539 317 VDAqrhqeLPFQQ--LVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNL 384
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
46-433 |
3.33e-16 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 83.77 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 46 LAQPNAPAICAWDGE-MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHpvsRH 124
Cdd:PRK07514 13 FADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAY---TL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 125 KEI---LRQTGARMVV-----------VSAQHSARwassscHVVTLSEASIGQLT--VEDDLPGFSATPGNA---AYVLF 185
Cdd:PRK07514 90 AELdyfIGDAEPALVVcdpanfawlskIAAAAGAP------HVETLDADGTGSLLeaAAAAPDDFETVPRGAddlAAILY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 186 TSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQ----FtsYTFDFCMAeIITTLLYGG-CICVPS-DRDRHSD- 258
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHalpiF--HTHGLFVA-TNVALLAGAsMIFLPKfDPDAVLAl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 259 LAKAINTMGanwalltpsvaqllnpsdVPTLKI-----------------LVIGG------EqvTSKDWnRWPTSVQLIN 315
Cdd:PRK07514 241 MPRATVMMG------------------VPTFYTrllqeprltreaaahmrLFISGsapllaE--THREF-QERTGHAILE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 316 GYGPTEccivcTGYTTTQAF----KTGTIGTAIASVSW-VVDPEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAF 390
Cdd:PRK07514 300 RYGMTE-----TNMNTSNPYdgerRAGTVGFPLPGVSLrVTDPETGAELPP-GEIGMIEVKGPNVFKGYWRMPEKTAEEF 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1779949166 391 IEDpawlvdgcqGYagrrgrlYKTGDLVRYDDEGNLVCLGR-KD 433
Cdd:PRK07514 374 RAD---------GF-------FITGDLGKIDERGYVHIVGRgKD 401
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1127-1587 |
4.07e-16 |
|
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: 83.78 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1127 RPDAPAICaWDGDM-------TYGELDVLSGRLAGHLVELGVGPEDIV----PLCFEksmwTVVAMLAVLKAG------- 1188
Cdd:cd17634 66 NGDRTAII-YEGDDtsqsrtiSYRELHREVCRFAGTLLDLGVKKGDRVaiymPMIPE----AAVAMLACARIGavhsvif 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1189 ---------------GAFLLLDPSLPHERLRLMCRKVSAKLSLASEASAP---LAKDLVGtvVIVNADSALQLAHH---- 1246
Cdd:cd17634 141 ggfapeavagriidsSSRLLITADGGVRAGRSVPLKKNVDDALNPNVTSVehvIVLKRTG--SDIDWQEGRDLWWRdlia 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1247 -ASP---ITSVRPTHTAYVIFTSGSTGEPKGcriehraassAVTAHGRYLgmQASTRTLQFASYAFAGSLVELLMN---- 1318
Cdd:cd17634 219 kASPehqPEAMNAEDPLFILYTSGTTGKPKG----------VLHTTGGYL--VYAATTMKYVFDYGPGDIYWCTADvgwv 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1319 -----LCHGGCIC----VLSEEERRTDLASAMCRM----KVNWAFLTSTVVDLLTPK--------SVPSLSILCVGGEPI 1377
Cdd:cd17634 287 tghsyLLYGPLACgattLLYEGVPNWPTPARMWQVvdkhGVNILYTAPTAIRALMAAgddaiegtDRSSLRILGSVGEPI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1378 RaSQIVRW------GSQVHLRQTYGSSEVSGIVSS------AALTTCSTTRDVGRASTgvfwIVDPNNHNrlAPVGAVGE 1445
Cdd:cd17634 367 N-PEAYEWywkkigKEKCPVVDTWWQTETGGFMITplpgaiELKAGSATRPVFGVQPA----VVDNEGHP--QPGGTEGN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1446 VLVEGPVLG--REYIDEPDKTASTFieapaWRASLGlsagqqrLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEE 1523
Cdd:cd17634 440 LVITDPWPGqtRTLFGDHERFEQTY-----FSTFKG-------MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAE 507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 1524 IEhQARLAEADVAEIAVELIqPKDGEDGMLACFIVVEDSASNEDELsgkRTRLDTRTQRTIGKI 1587
Cdd:cd17634 508 IE-SVLVAHPKVAEAAVVGI-PHAIKGQAPYAYVVLNHGVEPSPEL---YAELRNWVRKEIGPL 566
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1124-1569 |
4.73e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 83.44 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERL 1203
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1204 RLMCRKVSAKLSLASEASAPLAKDL---VG--TVVIVNADSAL----------QLAHHASPITSVRPT-HTAYVIFTSGS 1267
Cdd:PRK07788 139 AEVAAREGVKALVYDDEFTDLLSALppdLGrlRAWGGNPDDDEpsgstdetldDLIAGSSTAPLPKPPkPGGIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1268 TGEPKGCRiehRAASSAVTAHGRYLG---MQASTRTLQFASYAFAGSLVELLMNLCHgGCICVLSeeeRRTDLASAM--- 1341
Cdd:PRK07788 219 TGTPKGAP---RPEPSPLAPLAGLLSrvpFRAGETTLLPAPMFHATGWAHLTLAMAL-GSTVVLR---RRFDPEATLedi 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1342 ----CRMKVNWAFLTSTVVDLLtPKSVP-----SLSILCVGGEPIRASQIVRwgsqVH------LRQTYGSSEVS--GIV 1404
Cdd:PRK07788 292 akhkATALVVVPVMLSRILDLG-PEVLAkydtsSLKIIFVSGSALSPELATR----ALeafgpvLYNLYGSTEVAfaTIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1405 SSAALTTCSTTrdVGRASTGV-FWIVDPnNHNRLaPVGAVGEVLVEGPVLGREYIDEPDKtastfieapawraslglsag 1483
Cdd:PRK07788 367 TPEDLAEAPGT--VGRPPKGVtVKILDE-NGNEV-PRGVVGRIFVGNGFPFEGYTDGRDK-------------------- 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1484 qQR---LYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI---EVEEIehqarLAE-ADVAEIAVelIQPKDGEDGM-LAC 1555
Cdd:PRK07788 423 -QIidgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVfpaEVEDL-----LAGhPDVVEAAV--IGVDDEEFGQrLRA 494
|
490
....*....|....*
gi 1779949166 1556 FIVVEDSAS-NEDEL 1569
Cdd:PRK07788 495 FVVKAPGAAlDEDAI 509
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
72-550 |
4.81e-16 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 83.49 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 72 KLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSAQHSARWASSSC 151
Cdd:PLN02330 67 RFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 152 HVVTLSEASIGQLTVEDDLPGFSATPGNAA-----------YVLFTSGSTGIPKGVVLEHR-----------AVSTSCLG 209
Cdd:PLN02330 147 PVIVLGEEKIEGAVNWKELLEAADRAGDTSdneeilqtdlcALPFSSGTTGISKGVMLTHRnlvanlcsslfSVGPEMIG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 210 HGRAFGITDQSRVLQFTSytfdFCMAeiitTLLYGGCICVPSDRDRHSDLaKAINTMGANWALLTPSVAQLL--NPS--- 284
Cdd:PLN02330 227 QVVTLGLIPFFHIYGITG----ICCA----TLRNKGKVVVMSRFELRTFL-NALITQEVSFAPIVPPIILNLvkNPIvee 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 285 -DVPTLKILVI-------GGEQVTSKDwNRWPtSVQLINGYGPTE-CCIVCTGYTTTQAF---KTGTIGTAIASVSW-VV 351
Cdd:PLN02330 298 fDLSKLKLQAImtaaaplAPELLTAFE-AKFP-GVQVQEAYGLTEhSCITLTHGDPEKGHgiaKKNSVGFILPNLEVkFI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 352 DPEDYHKLaPLGSVGELLVEGPILARGYLNDAEKTAAAfIEDPAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGR 431
Cdd:PLN02330 376 DPDTGRSL-PKNTPGELCVRSQCVMQGYYNNKEETDRT-IDEDGWL---------------HTGDIGYIDDDGDIFIVDR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 432 KDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQLDvktgrafPTNKAAETGSLAQVIFPVE 511
Cdd:PLN02330 439 IKELIKYKGFQVAPAELEAILLT-HPSVEDAA--VVPLPDEEAGEIPAACVVIN-------PKAKESEEDILNFVAANVA 508
|
490 500 510
....*....|....*....|....*....|....*....
gi 1779949166 512 AGKKlaerlpsymVPDVYFVVTqLPITVSGKTDRKRLRE 550
Cdd:PLN02330 509 HYKK---------VRVVQFVDS-IPKSLSGKIMRRLLKE 537
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1130-1559 |
6.07e-16 |
|
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: 82.53 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1130 APAICAWDGDMTYGELDVLSGRLAGHLV-ELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPherlrlmcr 1208
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLR--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1209 kvsaklslASEASAPLAKDLVGTVVIVNADSALQlahhaspitsvrptHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAH 1288
Cdd:cd05958 72 --------PKELAYILDKARITVALCAHALTASD--------------DICILAFTSGTTGAPKATMHFHRDPLASADRY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1289 GRY-LGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTDLASAMCRMKVNWAFLTSTVVDL---LTPKSV 1364
Cdd:cd05958 130 AVNvLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAmlaHPDAAG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1365 PSLSIL--CV-GGEPIRASQIVRWgsqvhlRQTYGSSEVSGIVSSAALTTCSTTRD----VGRASTGV----FWIVDpnN 1433
Cdd:cd05958 210 PDLSSLrkCVsAGEALPAALHRAW------KEATGIPIIDGIGSTEMFHIFISARPgdarPGATGKPVpgyeAKVVD--D 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1434 HNRLAPVGAVGEVLVEGPVlGREYIDepDKTASTFIEApAWRAslglsagqqrlykTGDLARYKDDGSIELIGRKDNQVK 1513
Cdd:cd05958 282 EGNPVPDGTIGRLAVRGPT-GCRYLA--DKRQRTYVQG-GWNI-------------TGDTYSRDPDGYFRHQGRSDDMIV 344
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1779949166 1514 LRGQRIEVEEIEhQARLAEADVAEIAVelIQPKDGEDGMLA-CFIVV 1559
Cdd:cd05958 345 SGGYNIAPPEVE-DVLLQHPAVAECAV--VGHPDESRGVVVkAFVVL 388
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
62-550 |
6.32e-16 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 82.93 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 62 SYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPldPDHPVSRHKEILR--QTGARMVVVS 139
Cdd:cd05970 49 TFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP--ATHQLTAKDIVYRieSADIKMIVAI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 140 A----QHSARWASSSCHVVTLsEASIGQLTVE---------DDLPGFSATPGNAAY--------VLFTSGSTGIPKGVvl 198
Cdd:cd05970 127 AedniPEEIEKAAPECPSKPK-LVWVGDPVPEgwidfrkliKNASPDFERPTANSYpcgedillVYFSSGTTGMPKMV-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 199 EHraVSTSCLGH-------------GRAFGITDqsrvlqfTSYtfdfcmAEIITTLLYG----GCICVPSDRDRHSdlAK 261
Cdd:cd05970 204 EH--DFTYPLGHivtakywqnvregGLHLTVAD-------TGW------GKAVWGKIYGqwiaGAAVFVYDYDKFD--PK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 262 AINTMGANWALLT----PSVAQLL-----NPSDVPTLKILVIGGEQVTSKDWNRWP--TSVQLINGYGPTECcIVCTGYT 330
Cdd:cd05970 267 ALLEKLSKYGVTTfcapPTIYRFLiredlSRYDLSSLRYCTTAGEALNPEVFNTFKekTGIKLMEGFGQTET-TLTIATF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 331 TTQAFKTGTIGTAiaSVSWVVDPEDYH-KLAPLGSVGELLV---EG-PI-LARGYLNDAEKTAAAFIEdpawlvdgcqGY 404
Cdd:cd05970 346 PWMEPKPGSMGKP--APGYEIDLIDREgRSCEAGEEGEIVIrtsKGkPVgLFGGYYKDAEKTAEVWHD----------GY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 405 agrrgrlYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIE----HH-------IQGCMPEANQIAVE--VILLEG 471
Cdd:cd05970 414 -------YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVEsaliQHpavlecaVTGVPDPIRGQVVKatIVLAKG 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 472 EKSNTILAAFLQLDVKtgrafptnkaaetgslaQVIFPveagkklaerlpsYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:cd05970 487 YEPSEELKKELQDHVK-----------------KVTAP-------------YKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1140-1593 |
7.02e-16 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 82.18 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1140 MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGA----FLLLDPSLPHERLRlmcrkvsakls 1215
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVyqplFTAFGPKAIEHRLR----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1216 lASEASaplakdlvgtVVIVNADSALQLAhhaspitsvrpTHTAYVIFTSGSTGEPKGCRIEHRAAsSAVTAHGRY-LGM 1294
Cdd:cd05973 70 -TSGAR----------LVVTDAANRHKLD-----------SDPFVMMFTSGTTGLPKGVPVPLRAL-AAFGAYLRDaVDL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1295 QASTRTLQFAS--------YAFAGSLVE-LLMNLCHGG----CICVLSEEERRTDLASAmcrmkvnwafltSTVVDLLTP 1361
Cdd:cd05973 127 RPEDSFWNAADpgwayglyYAITGPLALgHPTILLEGGfsveSTWRVIERLGVTNLAGS------------PTAYRLLMA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1362 KSVP-------SLSILCVGGEPIrASQIVRW-----GSQVHlrQTYGSSEVSGIVSSA-ALTTCSTTRDVGRASTGVFWI 1428
Cdd:cd05973 195 AGAEvparpkgRLRRVSSAGEPL-TPEVIRWfdaalGVPIH--DHYGQTELGMVLANHhALEHPVHAGSAGRAMPGWRVA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1429 VDPNNHNRLAPvGAVGEVLVE---GPVLG-REYIDEPDKTASTfieapawraslglsagqqRLYKTGDLARYKDDGSIEL 1504
Cdd:cd05973 272 VLDDDGDELGP-GEPGRLAIDianSPLMWfRGYQLPDTPAIDG------------------GYYLTGDTVEFDPDGSFSF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1505 IGRKDNQVKLRGQRI---EVEE--IEHQArlaeadVAEIAVeLIQPKDGEDGMLACFIVV----EDSASNEDELSGK-RT 1574
Cdd:cd05973 333 IGRADDVITMSGYRIgpfDVESalIEHPA------VAEAAV-IGVPDPERTEVVKAFVVLrgghEGTPALADELQLHvKK 405
|
490 500 510
....*....|....*....|....*....|.
gi 1779949166 1575 RLDTRTQ-RTI-----------GKIQDRLER 1593
Cdd:cd05973 406 RLSAHAYpRTIhfvdelpktpsGKIQRFLLR 436
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1116-1525 |
7.53e-16 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 82.63 E-value: 7.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAICAWDGD--MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLL 1193
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1194 LDPSLPHERLRLMCRKVSAKLSLA-----SEASAPLAKDLVGTV------------VIVNADSALQLAHHASPITSVRPT 1256
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLIdadgpHDRAEPTTRWWPLTVnvggdsgpsggtLSVHLDAATEPTPATSTPEGLRPD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1257 hTAYVIFTSGSTGEPKGCRIEHraASSAVTAHGRYLGMQASTRTLQFAS---YAFAGSLVELLMNLCHGGCICV-----L 1328
Cdd:PRK05852 178 -DAMIMFTGGTTGLPKMVPWTH--ANIASSVRAIITGYRLSPRDATVAVmplYHGHGLIAALLATLASGGAVLLpargrF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1329 SEEERRTDLASAmcrmKVNWAFLTSTVVDLL--------TPKSVPSLSILCVGGEPI--RASQIVRWGSQVHLRQTYGSS 1398
Cdd:PRK05852 255 SAHTFWDDIKAV----GATWYTAVPTIHQILleraatepSGRKPAALRFIRSCSAPLtaETAQALQTEFAAPVVCAFGMT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1399 EVSGIVSSAALTTCSTTRD-------VGRASTGVFWIVDPNNHNrlAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEa 1471
Cdd:PRK05852 331 EATHQVTTTQIEGIGQTENpvvstglVGRSTGAQIRIVGSDGLP--LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD- 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 1472 pAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIE 1525
Cdd:PRK05852 408 -GW-------------LRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVE 447
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
61-449 |
1.11e-15 |
|
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: 81.88 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 61 MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLcFEKSMWT-VVAMLAVLKAGgafapldpdhpvsrhkeilrqtgarMVVVS 139
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAI-FAETRAEwLITALGCWSQN-------------------------IPIVT 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 140 A---------QHSARWASSScHVVTLSEAsigqltveDDLpgfsatpgnaAYVLFTSGSTGIPKGVVLEHRAVSTSCLGH 210
Cdd:cd17639 60 VyatlgedalIHSLNETECS-AIFTDGKP--------DDL----------ACIMYTSGSTGNPKGVMLTHGNLVAGIAGL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 211 GRAFG--ITDQSRVLQF--TSYTFDFcMAEIIttLLYGGC------------------------------ICVPS--DRD 254
Cdd:cd17639 121 GDRVPelLGPDDRYLAYlpLAHIFEL-AAENV--CLYRGGtigygsprtltdkskrgckgdltefkptlmVGVPAiwDTI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 255 RHSDLAKaINTMGAN-----WALLTPSVAQLLNPSDVPTLKILVIGG-EQVT--------------SKDWNRWPTSV--Q 312
Cdd:cd17639 198 RKGVLAK-LNPMGGLkrtlfWTAYQSKLKALKEGPGTPLLDELVFKKvRAALggrlrymlsggaplSADTQEFLNIVlcP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 313 LINGYGPTE-CCivCTGYTTTQAFKTGTIGTAIASVSW-VVDPEDY----HKLAPLGsvgELLVEGPILARGYLNDAEKT 386
Cdd:cd17639 277 VIQGYGLTEtCA--GGTVQDPGDLETGRVGPPLPCCEIkLVDWEEGgystDKPPPRG---EILIRGPNVFKGYYKNPEKT 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 387 AAAFIEDpawlvdgcqgyagrrgRLYKTGDLVRYDDEGNLVCLGRKDSQVKVR-GQRVELGEIE 449
Cdd:cd17639 352 KEAFDGD----------------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLE 399
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
37-550 |
1.17e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 81.90 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAP-- 114
Cdd:PRK08316 13 IGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPvn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 115 --LDPDhpvsrhkE---ILRQTGARMVVVSA--------------QHSARWAssscHVVTLSEASIGQLTVEDDLPGFSA 175
Cdd:PRK08316 93 fmLTGE-------ElayILDHSGARAFLVDPalaptaeaalallpVDTLILS----LVLGGREAPGGWLDFADWAEAGSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 176 TPGNA-------AYVLFTSGSTGIPKGVVLEHRAV---STSCLghgRAFGITDQSRVLQ----FTSYTFD-FCMaeiitT 240
Cdd:PRK08316 162 AEPDVeladddlAQILYTSGTESLPKGAMLTHRALiaeYVSCI---VAGDMSADDIPLHalplYHCAQLDvFLG-----P 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 241 LLYGGCICVPSDRDRHSDLAKAINTMGANWALLTPSV-AQLLN-----PSDVPTLKILVIGG----EQVTSKDWNRWPtS 310
Cdd:PRK08316 234 YLYVGATNVILDAPDPELILRTIEAERITSFFAPPTVwISLLRhpdfdTRDLSSLRKGYYGAsimpVEVLKELRERLP-G 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 311 VQLINGYGPTEccivcTGYTTT------QAFKTGTIGTAIASV-SWVVDpEDYHKLAPlGSVGELLVEGPILARGYLNDA 383
Cdd:PRK08316 313 LRFYNCYGQTE-----IAPLATvlgpeeHLRRPGSAGRPVLNVeTRVVD-DDGNDVAP-GEVGEIVHRSPQLMLGYWDDP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 384 EKTAAAFiedpawlvdgcqgyagrRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHhiqgCMPEANQIA 463
Cdd:PRK08316 386 EKTAEAF-----------------RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE----ALYTHPAVA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 464 -VEVILLEGEKSNTILAAFLQLdvktgrafptnKAAETGSLAQVIfpveagKKLAERLPSYMVPDVYFVVTQLPITVSGK 542
Cdd:PRK08316 445 eVAVIGLPDPKWIEAVTAVVVP-----------KAGATVTEDELI------AHCRARLAGFKVPKRVIFVDELPRNPSGK 507
|
....*...
gi 1779949166 543 TDRKRLRE 550
Cdd:PRK08316 508 ILKRELRE 515
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1124-1590 |
1.69e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 81.19 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPAICAWDGDMTYGELDVLSGRLAGhlvelGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERL 1203
Cdd:PRK07787 10 AAAADIADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1204 RLMCRKVSAKLSLASEASAPLAKDLVGtvVIVNADSAlqlahHASPitSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASS 1283
Cdd:PRK07787 85 RHILADSGAQAWLGPAPDDPAGLPHVP--VRLHARSW-----HRYP--EPDPDAPALIVYTSGTTGPPKGVVLSRRAIAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1284 AVTA----------------------HGRYLGMQASTR-------TLQFASYAFAGSLVE---LLMnlchgGCICVLSEE 1331
Cdd:PRK07787 156 DLDAlaeawqwtaddvlvhglplfhvHGLVLGVLGPLRignrfvhTGRPTPEAYAQALSEggtLYF-----GVPTVWSRI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1332 ERRTDLASAM--CRMKVNW-AFLTSTVVDLLTPKSvpslsilcvGGEPIrasqivrwgsqvhlrQTYGSSEvsgivssaA 1408
Cdd:PRK07787 231 AADPEAARALrgARLLVSGsAALPVPVFDRLAALT---------GHRPV---------------ERYGMTE--------T 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1409 LTTCSTTRD-------VGRASTGV-FWIVDPNNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEaPAWraslgl 1480
Cdd:PRK07787 279 LITLSTRADgerrpgwVGLPLAGVeTRLVDEDGGPVPHDGETVGELQVRGPTLFDGYLNRPDATAAAFTA-DGW------ 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1481 sagqqrlYKTGDLARYKDDGSIELIGRKD-NQVKLRGQRIEVEEIEhQARLAEADVAEIAVelIQPKDGEDGMLACFIVV 1559
Cdd:PRK07787 352 -------FRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIE-TALLGHPGVREAAV--VGVPDDDLGQRIVAYVV 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1779949166 1560 EDSASNEDELSG---------KRTR----LDTRTQRTIGKIQDR 1590
Cdd:PRK07787 422 GADDVAADELIDfvaqqlsvhKRPRevrfVDALPRNAMGKVLKK 465
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1123-1549 |
1.75e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 81.21 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1123 QAKARPDAPA-ICAWDGD-MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSL-P 1199
Cdd:PRK13390 6 HAQIAPDRPAvIVAETGEqVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLtA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1200 HERLRLMCRK------VSAKLS-LASEASAPLAKDLV-GTVVIVNADSALQLAHHASPITSvRPThTAYVIFTSGSTGEP 1271
Cdd:PRK13390 86 PEADYIVGDSgarvlvASAALDgLAAKVGADLPLRLSfGGEIDGFGSFEAALAGAGPRLTE-QPC-GAVMLYSSGTTGFP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1272 KGCRIE------HRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCIcVLSEEERRTDLASAMCRMK 1345
Cdd:PRK13390 164 KGIQPDlpgrdvDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTV-VLAKRFDAQATLGHVERYR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1346 VNWAFLTSTVV--------DLLTPKSVPSLS--ILCVGGEPIRASQ-IVRWGSQVhLRQTYGSSEVSGIVSSAALTTCST 1414
Cdd:PRK13390 243 ITVTQMVPTMFvrllkldaDVRTRYDVSSLRavIHAAAPCPVDVKHaMIDWLGPI-VYEYYSSTEAHGMTFIDSPDWLAH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1415 TRDVGRASTGVFWIVDPNNHNrlAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEA-PAWRAslglsagqqrlykTGDL 1493
Cdd:PRK13390 322 PGSVGRSVLGDLHICDDDGNE--LPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhPFWTT-------------VGDL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 1494 ARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQARLAEA--DVAEIAVEliQPKDGE 1549
Cdd:PRK13390 387 GSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAvhDVAVIGVP--DPEMGE 442
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
55-449 |
1.84e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 81.57 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 55 CAWDGE----MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSrhkEILRQ 130
Cdd:PLN02246 41 CLIDGAtgrvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPA---EIAKQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 131 ---TGARMVVVSAQHSARWASSSCH----VVTLSEA-----SIGQLTV--EDDLPGFSATPGNAAYVLFTSGSTGIPKGV 196
Cdd:PLN02246 118 akaSGAKLIITQSCYVDKLKGLAEDdgvtVVTIDDPpegclHFSELTQadENELPEVEISPDDVVALPYSSGTTGLPKGV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 197 VLEHRAVSTSCL----GHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDLAKAINTMGANWAL 272
Cdd:PLN02246 198 MLTHKGLVTSVAqqvdGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 273 LTPS--VAQLLNPS----DVPTLKIlVIGGEQVTSKDWN-----RWPTSVqLINGYGPTECCIV---CTGYTTTQ-AFKT 337
Cdd:PLN02246 278 FVPPivLAIAKSPVvekyDLSSIRM-VLSGAAPLGKELEdafraKLPNAV-LGQGYGMTEAGPVlamCLAFAKEPfPVKS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 338 GTIGTAI--ASVSwVVDPEDYHKLaPLGSVGELLVEGPILARGYLNDAEKTAAAfIEDPAWLvdgcqgyagrrgrlyKTG 415
Cdd:PLN02246 356 GSCGTVVrnAELK-IVDPETGASL-PRNQPGEICIRGPQIMKGYLNDPEATANT-IDKDGWL---------------HTG 417
|
410 420 430
....*....|....*....|....*....|....
gi 1779949166 416 DLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIE 449
Cdd:PLN02246 418 DIGYIDDDDELFIVDRLKELIKYKGFQVAPAELE 451
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
178-544 |
1.95e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 80.12 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 178 GNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGhGRAFG--------ITDQSRVLQFTSYTFDFC-------MAEIITTLL 242
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMG-GADFGtgeftpseDAHKAAAAAAGTVMFPAPplmhgtgSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 243 YGGCICVPSDRDRHSDLAKAINTMGANW------ALLTPSVAQL--LNPSDVPTLKILVIGGEQVTSKDWNRWPTSVQ-- 312
Cdd:cd05924 82 GGQTVVLPDDRFDPEEVWRTIEKHKVTSmtivgdAMARPLIDALrdAGPYDLSSLFAISSGGALLSPEVKQGLLELVPni 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 313 -LINGYGPTECCIVCTGYTTTQAFKTGTIgTAIASVSWVVDPeDYHKLAP-LGSVGELLVEGPIlARGYLNDAEKTAAAF 390
Cdd:cd05924 162 tLVDAFGSSETGFTGSGHSAGSGPETGPF-TRANPDTVVLDD-DGRVVPPgSGGVGWIARRGHI-PLGYYGDEAKTAETF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 391 IEdpawlVDGCqgyagrrgRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcmpEANQIAVEVILLE 470
Cdd:cd05924 239 PE-----VDGV--------RYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKS---HPAVYDVLVVGRP 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 471 GEKSNTILAAFLQLDvktGRAFPTNKAAETGslaqvifpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTD 544
Cdd:cd05924 303 DERWGQEVVAVVQLR---EGAGVDLEELREH--------------CRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
70-550 |
2.00e-15 |
|
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: 80.47 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 70 STKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDpdhpvSR--HKEILRQtgarmvvvsaqhsarwa 147
Cdd:cd05912 11 VSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN-----TRltPNELAFQ----------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 148 ssschvvtLSEASIGQltveDDlpgfsatpgnAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSR------ 221
Cdd:cd05912 69 --------LKDSDVKL----DD----------IATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNwlcalp 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 222 --------------VLQFTSYTFDFCMAEIITTLLYGGcicvpsdrdrhsdlakAINTMGANWALLTPSVAQLLNPSDvP 287
Cdd:cd05912 127 lfhisglsilmrsvIYGMTVYLVDKFDAEQVLHLINSG----------------KVTIISVVPTMLQRLLEILGEGYP-N 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 288 TLKILVIGG--------EQVTSKDwnrwptsVQLINGYGPTECCI-VCTGYTTTQAFKTGTIGTAIASVswvvDPEDYHK 358
Cdd:cd05912 190 NLRCILLGGgpapkpllEQCKEKG-------IPVYQSYGMTETCSqIVTLSPEDALNKIGSAGKPLFPV----ELKIEDD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 359 LAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpaWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKV 438
Cdd:cd05912 259 GQPPYEVGEILLKGPNVTKGYLNRPDATEESFENG--WF---------------KTGDIGYLDEEGFLYVLDRRSDLIIS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 439 RGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFLQLDVKTgrafptnkaaetgSLAQVIfpveagKKLAE 518
Cdd:cd05912 322 GGENIYPAEIEEVLLS-HPAIKEAG--VVGIPDDKWGQVPVAFVVSERPI-------------SEEELI------AYCSE 379
|
490 500 510
....*....|....*....|....*....|..
gi 1779949166 519 RLPSYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:cd05912 380 KLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
181-449 |
2.10e-15 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 81.25 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 181 AYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFG-ITDQSRVLQFTSYTFDFCMAEIITTLLY---GGC---ICVPSDR 253
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGpLLHPGKELVVTALPLYHIFALTVNCLLFielGGQnllITNPRDI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 254 DRH-SDLAK-------AINTMgANWALLTPSVAQLlnpsDVPTLKILVIGGEQVTSKDWNRWP--TSVQLINGYGPTECC 323
Cdd:PRK08974 289 PGFvKELKKypftaitGVNTL-FNALLNNEEFQEL----DFSSLKLSVGGGMAVQQAVAERWVklTGQYLLEGYGLTECS 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 324 IVCTGYTTTQAFKTGTIGTAIASVS-WVVDPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAfIEDpAWLVdgcq 402
Cdd:PRK08974 364 PLVSVNPYDLDYYSGSIGLPVPSTEiKLVDDDG--NEVPPGEPGELWVKGPQVMLGYWQRPEATDEV-IKD-GWLA---- 435
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1779949166 403 gyagrrgrlykTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIE 449
Cdd:PRK08974 436 -----------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIE 471
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1132-1550 |
2.11e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 81.10 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1132 AICAWDGD-MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKV 1210
Cdd:PRK08276 3 VIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1211 SAKLSLASEASAPLAKDLV--------------GTVVIVNADSALQLAHHASPITSVRP-THTAYvifTSGSTGEPKGCR 1275
Cdd:PRK08276 83 GAKVLIVSAALADTAAELAaelpagvplllvvaGPVPGFRSYEEALAAQPDTPIADETAgADMLY---SSGTTGRPKGIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1276 IE------HRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTDLAsAMCRMKVNWA 1349
Cdd:PRK08276 160 RPlpgldpDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEEALA-LIERYRVTHS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1350 FLTSTV-VDLLT-PKSV------PSLSILCVGGEP----IRASQIVRWGSQVHlrQTYGSSEVSGIvssaaltTCSTTRD 1417
Cdd:PRK08276 239 QLVPTMfVRMLKlPEEVrarydvSSLRVAIHAAAPcpveVKRAMIDWWGPIIH--EYYASSEGGGV-------TVITSED 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1418 -------VGRASTGVFWIVDPNNhNRLaPVGAVGEVLVEGPVLGREYIDEPDKTAStfieapAWRAslglsagqQRLYKT 1490
Cdd:PRK08276 310 wlahpgsVGKAVLGEVRILDEDG-NEL-PPGEIGTVYFEMDGYPFEYHNDPEKTAA------ARNP--------HGWVTV 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 1491 GDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHqARLAEADVAEIAV-------------ELIQPKDGED 1550
Cdd:PRK08276 374 GDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIEN-LLVTHPKVADVAVfgvpdeemgervkAVVQPADGAD 445
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
48-551 |
2.67e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 80.59 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 48 QPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLcFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEI 127
Cdd:PRK07638 14 QPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAIL-LENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 128 LRQTGARMVVVSAQHSARWASSSCHVVTLSEAsigQLTVEDDLPGFSAT--PGNAA-YVLFTSGSTGIPKGVVLEHRAVS 204
Cdd:PRK07638 93 LAISNADMIVTERYKLNDLPDEEGRVIEIDEW---KRMIEKYLPTYAPIenVQNAPfYMGFTSGSTGKPKAFLRAQQSWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 205 TSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICvpsdrdrhsdLAKAINTMGANWALLTPSVAQLLNps 284
Cdd:PRK07638 170 HSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVH----------LMRKFIPNQVLDKLETENISVMYT-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 285 dVPT---------------LKILVIGGeqvtskDW---------NRWPtSVQLINGYGPTECCIVCTGYTTTQAFKTGTI 340
Cdd:PRK07638 238 -VPTmleslykenrvienkMKIISSGA------KWeaeakekikNIFP-YAKLYEFYGASELSFVTALVDEESERRPNSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 341 GTAIASVSWVVDPEDYHKLAPlGSVGELLVEGPILARGYLNDAekTAAAFIEDPAWLVDGCQGYAGRRGRLYKTGdlvry 420
Cdd:PRK07638 310 GRPFHNVQVRICNEAGEEVQK-GEIGTVYVKSPQFFMGYIIGG--VLARELNADGWMTVRDVGYEDEEGFIYIVG----- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 421 dDEGNLVCLGrkdsqvkvrGQRVELGEIEHHIQGCmPEANQIAVEVILLE--GEKSNTILAAflQLDVKTGRAFptnkaa 498
Cdd:PRK07638 382 -REKNMILFG---------GINIFPEEIESVLHEH-PAVDEIVVIGVPDSywGEKPVAIIKG--SATKQQLKSF------ 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 499 etgslaqvifpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREI 551
Cdd:PRK07638 443 -----------------CLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSW 478
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1123-1564 |
3.79e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 80.29 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1123 QAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLV-ELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHE 1201
Cdd:PRK06839 11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1202 RLRLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSALQLAH--HASPITSVRPTHTA-YVI-FTSGSTGEPKGCRIE 1277
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEieDRKIDNFVEKNESAsFIIcYTSGTTGKPKGAVLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1278 ---------HRAASSAVTAHGRYLGMqastrtlqFASYAFAGSLVELLMNLCHGGCICV-----------LSEEERRTdl 1337
Cdd:PRK06839 171 qenmfwnalNNTFAIDLTMHDRSIVL--------LPLFHIGGIGLFAFPTLFAGGVIIVprkfeptkalsMIEKHKVT-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1338 aSAMCRMKVNWAFLTStvVDLLTPkSVPSLSILCVGGEP-----IRASQI--VRWGsqvhlrQTYGSSEVSGIVssAALT 1410
Cdd:PRK06839 241 -VVMGVPTIHQALINC--SKFETT-NLQSVRWFYNGGAPcpeelMREFIDrgFLFG------QGFGMTETSPTV--FMLS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1411 TCSTTRDVGRASTGVFW----IVDPNNHNrlAPVGAVGEVLVEGPVLGREYIDEPDKTASTFieapawraslglsagQQR 1486
Cdd:PRK06839 309 EEDARRKVGSIGKPVLFcdyeLIDENKNK--VEVGEVGELLIRGPNVMKEYWNRPDATEETI---------------QDG 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 1487 LYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVELIQ-PKDGEdgMLACFIVVEDSAS 1564
Cdd:PRK06839 372 WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVE-QVINKLSDVYEVAVVGRQhVKWGE--IPIAFIVKKSSSV 447
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
62-552 |
4.71e-15 |
|
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: 79.78 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 62 SYSVLDGLSTKLAGYLVKI-GVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDhpvsrhkeilrQTGARMVvvsa 140
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYN-----------LSGDPLI---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 141 qhsarwassscHVVTLSEASigQLTVEDDLPgfsatpgnaAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQS 220
Cdd:cd05937 72 -----------HCLKLSGSR--FVIVDPDDP---------AILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 221 RVLQ----FTSYTFDFCMaeiITTLLYGGCICVpSDRDRHSDLAKAINTMGANWALLTPSVAQ-LLN--PS-DVPTLKIL 292
Cdd:cd05937 130 RTYTcmplYHGTAAFLGA---CNCLMSGGTLAL-SRKFSASQFWKDVRDSGATIIQYVGELCRyLLStpPSpYDRDHKVR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 293 VIGGEQVTSKDWNRW------PTSVQLingYGPTECCIVCTGYTTTqAFKTGTIGTAIASVSWV---------VDPED-- 355
Cdd:cd05937 206 VAWGNGLRPDIWERFrerfnvPEIGEF---YAATEGVFALTNHNVG-DFGAGAIGHHGLIRRWKfenqvvlvkMDPETdd 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 356 --------YHKLAPLGSVGELLVEGPILAR----GYLNDAEKTAAAFIEDpawlvdgcqgyAGRRGRLY-KTGDLVRYDD 422
Cdd:cd05937 282 pirdpktgFCVRAPVGEPGEMLGRVPFKNReafqGYLHNEDATESKLVRD-----------VFRKGDIYfRTGDLLRQDA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 423 EGNLVCLGRKDSQVKVRGQRVELGEIEHHIqGCMPEANQIAVEVILLEGEKsntilaaflqldvktGRAFPTNKAAETGS 502
Cdd:cd05937 351 DGRWYFLDRLGDTFRWKSENVSTTEVADVL-GAHPDIAEANVYGVKVPGHD---------------GRAGCAAITLEESS 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 503 LAQVIFPVEAGKKLA-ERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIG 552
Cdd:cd05937 415 AVPTEFTKSLLASLArKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEG 465
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
50-549 |
4.81e-15 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 80.46 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 50 NAPAICAWDGEMSYSVLDGlSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLkAGGAFAPL-DPDHPVSRHKEIL 128
Cdd:PRK06060 21 DRPAFYAADVVTHGQIHDG-AARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACL-ARGVMAFLaNPELHRDDHALAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVVSAQHSARWASSSchVVT----LSEASIGQLTVEDDLPGFSAtpgnaAYVLFTSGSTGIPKGVVleHRavs 204
Cdd:PRK06060 99 RNTEPALVVTSDALRDRFQPSR--VAEaaelMSEAARVAPGGYEPMGGDAL-----AYATYTSGTTGPPKAAI--HR--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 205 tsclgHGRAFGITDQ--SRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDrHSDLAKAINTMGANWALLT----PSV- 277
Cdd:PRK06060 167 -----HADPLTFVDAmcRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATG-GSAVINSAPVTPEAAAILSarfgPSVl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 278 -------AQLL---NPSDVPTLKILVIGGEQVT---SKDWNRWPTSVQLINGYGPTEccivcTGYT----TTQAFKTGTI 340
Cdd:PRK06060 241 ygvpnffARVIdscSPDSFRSLRCVVSAGEALElglAERLMEFFGGIPILDGIGSTE-----VGQTfvsnRVDEWRLGTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 341 GTaiasvswVVDPEDYHKLAPLGSV------GELLVEGPILARGYLNDAEktaaAFIEDPAWLvdgcqgyagrrgrlyKT 414
Cdd:PRK06060 316 GR-------VLPPYEIRVVAPDGTTagpgveGDLWVRGPAIAKGYWNRPD----SPVANEGWL---------------DT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 415 GDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQgcmpEANQIA-VEVILLEGEKSNTILAAFLqldvktgraFP 493
Cdd:PRK06060 370 RDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLII----EDEAVAeAAVVAVRESTGASTLQAFL---------VA 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1779949166 494 TNKAAETGSLAQVIFpveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:PRK06060 437 TSGATIDGSVMRDLH-----RGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
37-563 |
5.52e-15 |
|
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: 80.23 E-value: 5.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAIcAWDGE------MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGG 110
Cdd:cd05968 63 VEQLLDKWLADTRTRPAL-RWEGEdgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 111 AFAPL----DPDHPVSRhkeiLRQTGARMVV-----------VSAQHSARWASSSC----HVVTLSEASIGQL-TVEDDL 170
Cdd:cd05968 142 IVVPIfsgfGKEAAATR----LQDAEAKALItadgftrrgreVNLKEEADKACAQCptveKVVVVRHLGNDFTpAKGRDL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 171 --PGFSATPGNAA---------YVLFTSGSTGIPKGVVLEHRAVSTSC---LGHGraFGITDQSRVLQFTSYTFDFCMAE 236
Cdd:cd05968 218 syDEEKETAGDGAertesedplMIIYTSGTTGKPKGTVHVHAGFPLKAaqdMYFQ--FDLKPGDLLTWFTDLGWMMGPWL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 237 IITTLLYGGCIC----VPS--DRDRHSDLAKA--INTMGanwalLTPSVAQLLNP--------SDVPTLKILVIGGEQVT 300
Cdd:cd05968 296 IFGGLILGATMVlydgAPDhpKADRLWRMVEDheITHLG-----LSPTLIRALKPrgdapvnaHDLSSLRVLGSTGEPWN 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 301 SKDWN-----RWPTSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVSWVVDPEDYHKLAPlgSVGELLVEGPI- 374
Cdd:cd05968 371 PEPWNwlfetVGKGRNPIINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP--EVGELVLLAPWp 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 375 -LARGylndaektaaaFIEDPAWLVDGcqgYAGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHI- 452
Cdd:cd05968 449 gMTRG-----------FWRDEDRYLET---YWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLn 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 453 -QGCMPEANQIAVEVIlLEGEKsnTILAAFLQLDVktgrafptnkaAETGSLAQvifpvEAGKKLAERLPSYMVPDVYFV 531
Cdd:cd05968 515 aHPAVLESAAIGVPHP-VKGEA--IVCFVVLKPGV-----------TPTEALAE-----ELMERVADELGKPLSPERILF 575
|
570 580 590
....*....|....*....|....*....|..
gi 1779949166 532 VTQLPITVSGKTDRKRLReigASFSAQQLAEI 563
Cdd:cd05968 576 VKDLPKTRNAKVMRRVIR---AAYLGKELGDL 604
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1123-1569 |
6.46e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 79.62 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1123 QAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHER 1202
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1203 LRLMCRKVSAKLSLASEASAplAKDLVGTVVIVNADSALQLAhHASPITSVRPTHTAYVIFTSGSTGEPKGCRIE----- 1277
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFE--AKLIPGISVKFAELMNGPKE-EAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTygnhw 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1278 HRAASSAVTahgryLGMQASTRTLqFASYAFAGSLVELLMNLCHGGCICVLSE---EERRTDL--ASAMCRMKVNWAFLT 1352
Cdd:PRK03640 168 WSAVGSALN-----LGLTEDDCWL-AAVPIFHISGLSILMRSVIYGMRVVLVEkfdAEKINKLlqTGGVTIISVVSTMLQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1353 STVVDLLTPKSVPSLSILCVGGEPIRAS---QIVRWGSQVHlrQTYGSSEV-SGIVssaALTTCSTTRDVGRASTGVF-- 1426
Cdd:PRK03640 242 RLLERLGEGTYPSSFRCMLLGGGPAPKPlleQCKEKGIPVY--QSYGMTETaSQIV---TLSPEDALTKLGSAGKPLFpc 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1427 --WIVDpnnHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapAWraslglsagqqrlYKTGDLARYKDDGSIEL 1504
Cdd:PRK03640 317 elKIEK---DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD--GW-------------FKTGDIGYLDEEGFLYV 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1779949166 1505 IGRKDNQVKLRGQRIEVEEIEHqARLAEADVAEIAVelIQPKDGEDGMLACFIVVEDSASNEDEL 1569
Cdd:PRK03640 379 LDRRSDLIISGGENIYPAEIEE-VLLSHPGVAEAGV--VGVPDDKWGQVPVAFVVKSGEVTEEEL 440
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
173-473 |
7.38e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 79.47 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 173 FSATPGNAAYVLFTSGSTGIPKGVVLEHR---AVSTSCLghgRAFGITDQSRVLQFT----SYTFDFCMaeiITTLLYGG 245
Cdd:PRK06334 178 SDKDPEDVAVILFTSGTEKLPKGVPLTHAnllANQRACL---KFFSPKEDDVMMSFLppfhAYGFNSCT---LFPLLSGV 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 246 CICVPSDRDRHSDLAKAINTMGANWALLTPSVAQLL------NPSDVPTLKILVIGGE-------QVTSKDWnrwpTSVQ 312
Cdd:PRK06334 252 PVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYIlktakkQESCLPSLRFVVIGGDafkdslyQEALKTF----PHIQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 313 LINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVSWVVDPEDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIE 392
Cdd:PRK06334 328 LRQGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELG 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 393 DPAWLVDGCQGYAGRRGRLYKTGDLVRYddegnlvclgrkdsqVKVRGQRVELGEIEH-HIQGCMPEANQIAVEVIL--L 469
Cdd:PRK06334 408 GETWYVTGDLGYVDRHGELFLKGRLSRF---------------VKIGAEMVSLEALESiLMEGFGQNAADHAGPLVVcgL 472
|
....
gi 1779949166 470 EGEK 473
Cdd:PRK06334 473 PGEK 476
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
41-550 |
7.42e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 79.69 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 41 FAEQVLAQ-PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDH 119
Cdd:PRK06710 29 YVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 120 PVSRHKEILRQTGARMV---------VVSAQHSARWA------------------------SSSCHVVTLSEASIGQL-- 164
Cdd:PRK06710 109 TERELEYQLHDSGAKVIlcldlvfprVTNVQSATKIEhvivtriadflpfpknllypfvqkKQSNLVVKVSESETIHLwn 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 165 TVEDDLPGFSATP----GNAAYVLFTSGSTGIPKGVVLEHR-AVSTSCLGHGRAFGITD-QSRVLQFTSYTFDFCMAEII 238
Cdd:PRK06710 189 SVEKEVNTGVEVPcdpeNDLALLQYTGGTTGFPKGVMLTHKnLVSNTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMTAVM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 239 TTLLYGG--CICVPSdrdrhSDLAKAINTMGANWALLTPSV---------AQLLNPSDVPTLKILVIGGEQVTSKDWNRW 307
Cdd:PRK06710 269 NLSIMQGykMVLIPK-----FDMKMVFEAIKKHKVTLFPGAptiyiallnSPLLKEYDISSIRACISGSAPLPVEVQEKF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 308 P--TSVQLINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVSWVVDPEDYHKLAPLGSVGELLVEGPILARGYLNDAEK 385
Cdd:PRK06710 344 EtvTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 386 TAAAfIEDpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHhiqgcmpeanqiave 465
Cdd:PRK06710 424 TAAV-LQD-GWL---------------HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEE--------------- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 466 vILLEGEKSNTILAAFLQLDVK--TGRAFPTNKAAETGSLAQVifpveagKKLAER-LPSYMVPDVYFVVTQLPITVSGK 542
Cdd:PRK06710 472 -VLYEHEKVQEVVTIGVPDPYRgeTVKAFVVLKEGTECSEEEL-------NQFARKyLAAYKVPKVYEFRDELPKTTVGK 543
|
....*...
gi 1779949166 543 TDRKRLRE 550
Cdd:PRK06710 544 ILRRVLIE 551
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-436 |
2.04e-14 |
|
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: 77.89 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 60 EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGarmvvvs 139
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 140 aqhsarwassschvvtlSEASIGQLTVEDDlpgfsatpgnaAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQ 219
Cdd:cd05910 75 -----------------PDAFIGIPKADEP-----------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 220 SRVLQftsyTFD----FCMAEIITTLLYGGCICVPSDRDRhSDLAKAINTMGANWALLTPSVAQLL------NPSDVPTL 289
Cdd:cd05910 127 EVDLA----TFPlfalFGPALGLTSVIPDMDPTRPARADP-QKLVGAIRQYGVSIVFGSPALLERVarycaqHGITLPSL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 290 KILVIGGEQVTSKDWNRW----PTSVQLINGYGPTECCIVCT-----GYTTTQAFKTG----TIGTAIASVSWVV---DP 353
Cdd:cd05910 202 RRVLSAGAPVPIALAARLrkmlSDEAEILTPYGATEALPVSSigsreLLATTTAATSGgagtCVGRPIPGVRVRIieiDD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 354 EDYH-----KLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDPawlvdgcqgyagRRGRLYKTGDLVRYDDEGNLVC 428
Cdd:cd05910 282 EPIAewddtLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN------------SEGFWHRMGDLGYLDDEGRLWF 349
|
....*...
gi 1779949166 429 LGRKDSQV 436
Cdd:cd05910 350 CGRKAHRV 357
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
72-472 |
2.37e-14 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 77.89 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 72 KLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVV-------SAQHSA 144
Cdd:cd05932 18 RLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgklddwkAMAPGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 145 RWASSSCHVVTLSEA----------SIGQLTVEDDLPGfsatPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAF 214
Cdd:cd05932 98 PEGLISISLPPPSAAncqyqwddliAQHPPLEERPTRF----PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 215 GITDQSRVLQFTSYTFDFCMAEIITTLLYGGC-ICVPSDRDRH-SDLAKAINTMGAN----WALLTPSVAQLLNPSDVPT 288
Cdd:cd05932 174 GTEENDRMLSYLPLAHVTERVFVEGGSLYGGVlVAFAESLDTFvEDVQRARPTLFFSvprlWTKFQQGVQDKIPQQKLNL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 289 L-KILVIG---------------------GEQVTSKDWNRWPTSVQL--INGYGPTECC---IVCTGYTTtqafKTGTIG 341
Cdd:cd05932 254 LlKIPVVNslvkrkvlkglgldqcrlagcGSAPVPPALLEWYRSLGLniLEAYGMTENFaysHLNYPGRD----KIGTVG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 342 TAIASVSWVVDPEdyhklaplgsvGELLVEGPILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrgrlyKTGDLVRYD 421
Cdd:cd05932 330 NAGPGVEVRISED-----------GEILVRSPALMMGYYKDPEATAEAFTAD-GFL---------------RTGDKGELD 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 422 DEGNLVCLGRKDSQVKV-RGQRVELGEIEHHIqgcmpeANQIAVEVILLEGE 472
Cdd:cd05932 383 ADGNLTITGRVKDIFKTsKGKYVAPAPIENKL------AEHDRVEMVCVIGS 428
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1118-1509 |
2.41e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 77.61 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1118 DLFADqAKARPDAPAICAWDGD-MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLL-- 1194
Cdd:PRK07514 7 DALRA-AFADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLnt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1195 --------------DPSLpherlrLMCRkvsaklSLASEASAPLAKDL-VGTVVIVNAD---SALQLAHHASP--ITSVR 1254
Cdd:PRK07514 86 aytlaeldyfigdaEPAL------VVCD------PANFAWLSKIAAAAgAPHVETLDADgtgSLLEAAAAAPDdfETVPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1255 -PTHTAYVIFTSGSTGEPKGCRIEHR-AASSAVTAHgRYLGMQASTRTLQ----FASYA-FAGSLVELLmnlcHGGCICV 1327
Cdd:PRK07514 154 gADDLAAILYTSGTTGRSKGAMLSHGnLLSNALTLV-DYWRFTPDDVLIHalpiFHTHGlFVATNVALL----AGASMIF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1328 LSeeerRTDLASAMCRMKvnwaflTSTV--------VDLL-----TPKSVPSLSILCVGGEPIRASQIVRWGSQVHLR-- 1392
Cdd:PRK07514 229 LP----KFDPDAVLALMP------RATVmmgvptfyTRLLqeprlTREAAAHMRLFISGSAPLLAETHREFQERTGHAil 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1393 QTYGSSEVSGIVSSA------ALTtcsttrdVGRASTGV-FWIVDPNNHNRLaPVGAVGEVLVEGPVLGREYIDEPDKTA 1465
Cdd:PRK07514 299 ERYGMTETNMNTSNPydgerrAGT-------VGFPLPGVsLRVTDPETGAEL-PPGEIGMIEVKGPNVFKGYWRMPEKTA 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1779949166 1466 STFiEAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGR-KD 1509
Cdd:PRK07514 371 EEF-RADGF-------------FITGDLGKIDERGYVHIVGRgKD 401
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
580-640 |
6.53e-14 |
|
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: 67.59 E-value: 6.53e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 580 KALQQLWAGVLAIDADSIGLDDSFFRLGGDSIAAMKLVGEARRA-GIHLTVADLFRNPKLEA 640
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
183-542 |
7.32e-14 |
|
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: 74.84 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 183 VLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSY--TFDFcMAEIITTLLYGGCIcVPSDRDRHSDLA 260
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFfhTFGY-KAGIVACLLTGATV-VPVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 261 KAINTMGANWALLTPSVAQ--LLNPS----DVPTLKILVIGGEQVTSKDWNRWPTSVQLIN---GYGPTECcIVCTGYTT 331
Cdd:cd17638 83 EAIERERITVLPGPPTLFQslLDHPGrkkfDLSSLRAAVTGAATVPVELVRRMRSELGFETvltAYGLTEA-GVATMCRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 332 TQAFKT--GTIGTAIASVSwvvdpedyhklAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrg 409
Cdd:cd17638 162 GDDAETvaTTCGRACPGFE-----------VRIADDGEVLVRGYNVMQGYLDDPEATAEAIDAD-GWL------------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 410 rlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTIlaaflqldvktG 489
Cdd:cd17638 218 ---HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAE-HPGVAQVA--VIGVPDERMGEV-----------G 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 490 RAFPTNKAAETGSLAQVIfpveAGKKlaERLPSYMVPDVYFVVTQLPITVSGK 542
Cdd:cd17638 281 KAFVVARPGVTLTEEDVI----AWCR--ERLANYKVPRFVRFLDELPRNASGK 327
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1120-1582 |
7.81e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 76.23 E-value: 7.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1120 FADQAKAR-PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLlldPSl 1198
Cdd:PRK07470 12 FLRQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWV---PT- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1199 pheRLRLMCRKVsAKLSLASEASAPL---------------AKDLVGTVVIVNAD-----SALQLAHHASPITSVRPTHT 1258
Cdd:PRK07470 88 ---NFRQTPDEV-AYLAEASGARAMIchadfpehaaavraaSPDLTHVVAIGGARagldyEALVARHLGARVANAAVDHD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1259 --AYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLgMQASTRtlQFASYAFA----GSLVELLMNLCHGGCICVLSEEe 1332
Cdd:PRK07470 164 dpCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLADL-MPGTTE--QDASLVVAplshGAGIHQLCQVARGAATVLLPSE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1333 rRTDLASA---MCRMKVNWAFLTSTVVDLLTPK-SV-----PSLSILCVGGEPI-RASQ---IVRWGSQvhLRQTYGSSE 1399
Cdd:PRK07470 240 -RFDPAEVwalVERHRVTNLFTVPTILKMLVEHpAVdrydhSSLRYVIYAGAPMyRADQkraLAKLGKV--LVQYFGLGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1400 VSGIVS-------------SAALTTCsttrdvGRASTGVFWIVDPNNHNRLAPvGAVGEVLVEGPVLGREYIDEPDKTAS 1466
Cdd:PRK07470 317 VTGNITvlppalhdaedgpDARIGTC------GFERTGMEVQIQDDEGRELPP-GETGEICVIGPAVFAGYYNNPEANAK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1467 TFIEapAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQArLAEADVAEIAVELI-QP 1545
Cdd:PRK07470 390 AFRD--GW-------------FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKL-LTHPAVSEVAVLGVpDP 453
|
490 500 510
....*....|....*....|....*....|....*...
gi 1779949166 1546 KDGEDGMLACfiVVEDSAS-NEDELsgkRTRLDTRTQR 1582
Cdd:PRK07470 454 VWGEVGVAVC--VARDGAPvDEAEL---LAWLDGKVAR 486
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1139-1595 |
9.37e-14 |
|
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: 76.03 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1139 DMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLL---------LDPSLPHERLRLM-CR 1208
Cdd:cd17642 44 NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPtndiynereLDHSLNISKPTIVfCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1209 KVSAKLSLASEASAPLAK---------DLVG-----TVVIVNADSALQlAHHASPITSVRPTHTAYVIFTSGSTGEPKGC 1274
Cdd:cd17642 124 KKGLQKVLNVQKKLKIIKtiiildskeDYKGyqclyTFITQNLPPGFN-EYDFKPPSFDRDEQVALIMNSSGSTGLPKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1275 RIEHRAAsSAVTAHGR--YLGMQAS--TRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTDLaSAMCRMKVNWAF 1350
Cdd:cd17642 203 QLTHKNI-VARFSHARdpIFGNQIIpdTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFL-RSLQDYKVQSAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1351 LTSTVVDLLtPKS-------VPSLSILCVGGEPIR---ASQIVRWGSQVHLRQTYGSSEvsgiVSSAALTTCSTtrDVGR 1420
Cdd:cd17642 281 LVPTLFAFF-AKStlvdkydLSNLHEIASGGAPLSkevGEAVAKRFKLPGIRQGYGLTE----TTSAILITPEG--DDKP 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1421 ASTGVFW------IVDPNNHNRLAPvGAVGEVLVEGPVLGREYIDEPDKTaSTFIEAPAWraslglsagqqrlYKTGDLA 1494
Cdd:cd17642 354 GAVGKVVpffyakVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEAT-KALIDKDGW-------------LHSGDIA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1495 RYKDDGSIELIGRKDNQVKLRGQRIEVEEIE----HQARLAEADVAEIAveliqpkDGEDGML-ACFIVVE--------- 1560
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELEsillQHPKIFDAGVAGIP-------DEDAGELpAAVVVLEagktmteke 491
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1779949166 1561 ------DSASNEDELSGKRTRLDTRTQRTIGKIQDRLERDL 1595
Cdd:cd17642 492 vmdyvaSQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
72-449 |
9.64e-14 |
|
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: 75.47 E-value: 9.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 72 KLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQtgarmvvvsaqhsarwasssc 151
Cdd:cd17640 17 DFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNH--------------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 152 hvvtlSEASIgqLTVEDDlpgfsatPGNAAYVLFTSGSTGIPKGVVLEHRAVstsclghgrAFGITDQSRVLQ------F 225
Cdd:cd17640 76 -----SESVA--LVVEND-------SDDLATIIYTSGTTGNPKGVMLTHANL---------LHQIRSLSDIVPpqpgdrF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 226 TSYTFDFCMAEII--TTLLYGGCICV-PSDRDRHSDLAKAINTMGANWALLTPSV-----AQLLNPSdvPTLKILVI--- 294
Cdd:cd17640 133 LSILPIWHSYERSaeYFIFACGCSQAyTSIRTLKDDLKRVKPHYIVSVPRLWESLysgiqKQVSKSS--PIKQFLFLffl 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 295 -----------GGEQVTSKDWNRWPTSVQLINGYGPTECC-IVCTGytTTQAFKTGTIGTAIASVSW-VVDPEDYHKLAP 361
Cdd:cd17640 211 sggifkfgisgGGALPPHVDTFFEAIGIEVLNGYGLTETSpVVSAR--RLKCNVRGSVGRPLPGTEIkIVDPEGNVVLPP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 362 lGSVGELLVEGPILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGR-KDSQVKVRG 440
Cdd:cd17640 289 -GEKGIVWVRGPQVMKGYYKNPEATSKVLDSD-GWF---------------NTGDLGWLTCGGELVLTGRaKDTIVLSNG 351
|
....*....
gi 1779949166 441 QRVELGEIE 449
Cdd:cd17640 352 ENVEPQPIE 360
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
49-414 |
1.14e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 75.50 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPA-ICAWDGE-MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKE 126
Cdd:PRK13391 11 PDKPAvIMASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 127 ILRQTGARMVVVSAQHS--ARWASSSCHVVTL------SEASIGQLTVEDDLPGFSATPGN----AAYVLFTSGSTGIPK 194
Cdd:PRK13391 91 IVDDSGARALITSAAKLdvARALLKQCPGVRHrlvldgDGELEGFVGYAEAVAGLPATPIAdeslGTDMLYSSGTTGRPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 195 GVV--LEHRAVSTSC----LGHgRAFGITDQSRVLQ----FTSYTFDFCMaeiiTTLLYGGCICVPSDRDRHSDLAkAIN 264
Cdd:PRK13391 171 GIKrpLPEQPPDTPLpltaFLQ-RLWGFRSDMVYLSpaplYHSAPQRAVM----LVIRLGGTVIVMEHFDAEQYLA-LIE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 265 TMGANWALLTPS--VAQLLNPS------DVPTLKILVIGGEQVtskdwnrwPTSV--QLINGYGPteccIVCTGYTTTQA 334
Cdd:PRK13391 245 EYGVTHTQLVPTmfSRMLKLPEevrdkyDLSSLEVAIHAAAPC--------PPQVkeQMIDWWGP----IIHEYYAATEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 335 FKTgtigTAIASVSWVVDP--------------EDYHKLAPLGSVGELLVEGPILARgYLNDAEKTAAAFIEDPAWLVDG 400
Cdd:PRK13391 313 LGF----TACDSEEWLAHPgtvgramfgdlhilDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGTWSTVG 387
|
410
....*....|....
gi 1779949166 401 CQGYAGRRGRLYKT 414
Cdd:PRK13391 388 DIGYVDEDGYLYLT 401
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
177-551 |
1.21e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 76.29 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 177 PGNAAYVLFTSGSTGIPKGVVLEH--------------------RAVSTSCLGHgrAFGIT--------DQSRVLQFTS- 227
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHksllanveqiktiadftpndRFMSALPLFH--SFGLTvglftpllTGAEVFLYPSp 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 228 --YtfdfcmaEIITTLLYggcicvpsdrDRHSDLAKAINTMGANWAlltpsvaQLLNPSDVPTLKILVIGGEQVTSKDWN 305
Cdd:PRK08043 442 lhY-------RIVPELVY----------DRNCTVLFGTSTFLGNYA-------RFANPYDFARLRYVVAGAEKLQESTKQ 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 306 RWPTS--VQLINGYGPTECCIVCTgYTTTQAFKTGTIGTAIasvswvvdPEDYHKLAPLGSV---GELLVEGPILARGYL 380
Cdd:PRK08043 498 LWQDKfgLRILEGYGVTECAPVVS-INVPMAAKPGTVGRIL--------PGMDARLLSVPGIeqgGRLQLKGPNIMNGYL 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 381 NdaektaaafIEDPAWLV----DGCQGYagRRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCM 456
Cdd:PRK08043 569 R---------VEKPGVLEvptaENARGE--MERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVS 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 457 PEANQiavevillegeksntilAAFLQLDVKTGRA---FPTNKAAETGSLAQVifPVEAGkklaerLPSYMVPDVYFVVT 533
Cdd:PRK08043 638 PDKQH-----------------ATAIKSDASKGEAlvlFTTDSELTREKLQQY--AREHG------VPELAVPRDIRYLK 692
|
410
....*....|....*...
gi 1779949166 534 QLPITVSGKTDRKRLREI 551
Cdd:PRK08043 693 QLPLLGSGKPDFVTLKSM 710
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1121-1582 |
1.59e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 75.20 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1121 ADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPH 1200
Cdd:PRK07786 24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1201 ERLRLMCRKVSAKLSLASEASAPLA---KDLV---GTVVIVNADS---------ALQLAHHASPITSVRPTHTAYVIFTS 1265
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAPVAtavRDIVpllSTVVVAGGSSddsvlgyedLLAEAGPAHAPVDIPNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1266 GSTGEPKGcriehraassAVTAHgryLGMQASTRTLQFASYAFAGSLVELL-MNLCH----GGCICVLseeerrtdLASA 1340
Cdd:PRK07786 184 GTTGRPKG----------AVLTH---ANLTGQAMTCLRTNGADINSDVGFVgVPLFHiagiGSMLPGL--------LLGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1341 MCRMKVNWAFLTSTVVDLLTPKSVPSLSILCVGGEPIRASQIVR----------WG----SQVHLRQTYGSSEVSGIVSS 1406
Cdd:PRK07786 243 PTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARprdlalrvlsWGaapaSDTLLRQMAATFPEAQILAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1407 AALT-----TCSTTRD--------VGRA-STGVFWIVDPNNHNrlAPVGAVGEVLVEGPVLGREYIDEPDKTASTFieAP 1472
Cdd:PRK07786 323 FGQTemspvTCMLLGEdairklgsVGKViPTVAARVVDENMND--VPVGEVGEIVYRAPTLMSGYWNNPEATAEAF--AG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1473 AWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHqARLAEADVAEIAVelIQPKDGEDGM 1552
Cdd:PRK07786 399 GW-------------FHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVEN-VLASHPDIVEVAV--IGRADEKWGE 462
|
490 500 510
....*....|....*....|....*....|
gi 1779949166 1553 LACFIVVEDSASNEDELSGKRTRLDTRTQR 1582
Cdd:PRK07786 463 VPVAVAAVRNDDAALTLEDLAEFLTDRLAR 492
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
181-550 |
2.13e-13 |
|
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: 73.13 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 181 AYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPsdrDRHSDLA 260
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLL---ERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 261 KAINTMGANWALLTPsvAQLLN-------PSDVPTLKILVIGG--------EQVTSKDWNRWPTsvqlingYGPTE-CCI 324
Cdd:cd17630 80 EDLAPPGVTHVSLVP--TQLQRlldsgqgPAALKSLRAVLLGGapippellERAADRGIPLYTT-------YGMTEtASQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 325 VCTGytTTQAFKTGTIGTAIASVSWVVDPEdyhklaplgsvGELLVEGPILARGYLNDAEKTAAAfieDPAWlvdgcqgy 404
Cdd:cd17630 151 VATK--RPDGFGRGGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQLVPEFN---EDGW-------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 405 agrrgrlYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIE------HHIQGCM------PEANQIAVEVILLEGE 472
Cdd:cd17630 207 -------FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEaalaahPAVRDAFvvgvpdEELGQRPVAVIVGRGP 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 473 KSNTILAAFLQldvktgrafptnkaaetgslaqvifpveagkklaERLPSYMVPDVYFVVTQLPITVSGKTDRKRLRE 550
Cdd:cd17630 280 ADPAELRAWLK----------------------------------DKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1139-1535 |
2.30e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 74.93 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1139 DMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGG-------AFLlldPSLPHERL-------- 1203
Cdd:PRK04319 73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAivgplfeAFM---EEAVRDRLedseakvl 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1204 ----RLMCRKVSAKLslaseasaPLAKdlvgTVVIVNADSAL--------QLAHHASP---ITSVRPTHTAYVIFTSGST 1268
Cdd:PRK04319 150 ittpALLERKPADDL--------PSLK----HVLLVGEDVEEgpgtldfnALMEQASDefdIEWTDREDGAILHYTSGST 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1269 GEPKGCRIEHraasSAVTAH---GRY-LGMQAS------------TRTlqfaSYA-FAgslvellmNLCHGGCICVLSEE 1331
Cdd:PRK04319 218 GKPKGVLHVH----NAMLQHyqtGKYvLDLHEDdvywctadpgwvTGT----SYGiFA--------PWLNGATNVIDGGR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1332 ERRTDLASAMCRMKVN-W-----AF--LTSTVVDLLTPKSVPSL-SILCVgGEPIRAsQIVRWGSQVH-LR--QTYGSSE 1399
Cdd:PRK04319 282 FSPERWYRILEDYKVTvWytaptAIrmLMGAGDDLVKKYDLSSLrHILSV-GEPLNP-EVVRWGMKVFgLPihDNWWMTE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1400 VSG--IVSSAALttcsttrDV-----GRASTGV-FWIVDpNNHNRLAPvGAVGE-VLVEG-PVLGREYIDEPDKTASTFi 1469
Cdd:PRK04319 360 TGGimIANYPAM-------DIkpgsmGKPLPGIeAAIVD-DQGNELPP-NRMGNlAIKKGwPSMMRGIWNNPEKYESYF- 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 1470 eAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI---EVEE--IEHQArLAEADV 1535
Cdd:PRK04319 430 -AGDW-------------YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVgpfEVESklMEHPA-VAEAGV 485
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
49-548 |
3.68e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 73.88 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVVVSAQHSARWASSSCHVVTLSEASIGQltveDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVStscl 208
Cdd:PRK13383 129 RAHHISTVVADNEFAERIAGADDAVAVIDPATAGA----EESGGRPAVAAPGRIVLLTSGTTGKPKGVPRAPQLRS---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 209 GHGRAFGITDQSRVLQFTSYTFDFCM------AEIITTLLYGGCICVPSDRDRHSDLAKAINTMGANWALLTPSVAQLLN 282
Cdd:PRK13383 201 AVGVWVTILDRTRLRTGSRISVAMPMfhglglGMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 283 PSD-------VPTLKILVIGGEQVTSKDWNRWPTSVQ--LINGYGPTECCIVCTGYTTTQAFKTGTIGTAIASVSWVVDP 353
Cdd:PRK13383 281 LPPrvrarnpLPQLRVVMSSGDRLDPTLGQRFMDTYGdiLYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILD 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 354 EDYHKLAPLgSVGELLVEGPILARGYLNDAEKTaaafiedpawLVDGcqgyagrrgrLYKTGDLVRYDDEGNLVCLGRKD 433
Cdd:PRK13383 361 RNNRPVGPR-VTGRIFVGGELAGTRYTDGGGKA----------VVDG----------MTSTGDMGYLDNAGRLFIVGRED 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 434 SQVKVRGQRVELGEIEHHIqGCMPEANQIAveVILLEGEKSNTILAAFLQLDVKTGrafptnkaaetgslaqvifpVEAG 513
Cdd:PRK13383 420 DMIISGGENVYPRAVENAL-AAHPAVADNA--VIGVPDERFGHRLAAFVVLHPGSG--------------------VDAA 476
|
490 500 510
....*....|....*....|....*....|....*...
gi 1779949166 514 K---KLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:PRK13383 477 QlrdYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1116-1586 |
4.00e-13 |
|
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: 74.06 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAIcAWDGD------MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGG 1189
Cdd:cd05968 63 VEQLLDKWLADTRTRPAL-RWEGEdgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1190 AFLLLDPSLPHERLRLMCRKVSAKL--------------SLASEASAPLAKDL-VGTVVIVNADSALQLAHHASPI--TS 1252
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKAlitadgftrrgrevNLKEEADKACAQCPtVEKVVVVRHLGNDFTPAKGRDLsyDE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1253 VRPTHTAY-----------VIFTSGSTGEPKGCRIEH-----RAASSAvtAHGryLGMQASTRTLQFASYAFAGSLVELL 1316
Cdd:cd05968 222 EKETAGDGaertesedplmIIYTSGTTGKPKGTVHVHagfplKAAQDM--YFQ--FDLKPGDLLTWFTDLGWMMGPWLIF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1317 MNLCHGGCIcVLSEEERRTDLASAMCRM----KVNWAFLTSTVVDLLTPK--------SVPSLSILCVGGEPIRASQ--- 1381
Cdd:cd05968 298 GGLILGATM-VLYDGAPDHPKADRLWRMvedhEITHLGLSPTLIRALKPRgdapvnahDLSSLRVLGSTGEPWNPEPwnw 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1382 --IVRWGSQVHLRQTYGSSEVSGIVSSAALTTCSTTRDVGRASTGVFWIVDPNNHNRLAPvgAVGEVLVEGPVLG--REY 1457
Cdd:cd05968 377 lfETVGKGRNPIINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP--EVGELVLLAPWPGmtRGF 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1458 IDEPDKTASTFieapaWRASLGlsagqqrLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAE 1537
Cdd:cd05968 455 WRDEDRYLETY-----WSRFDN-------VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIE-SVLNAHPAVLE 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1538 IA-VELIQPKDGEDgmLACFIVVEDsasNEDELSGKRTRLDTRTQRTIGK 1586
Cdd:cd05968 522 SAaIGVPHPVKGEA--IVCFVVLKP---GVTPTEALAEELMERVADELGK 566
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1119-1564 |
4.18e-13 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 74.02 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1119 LFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSL 1198
Cdd:PRK13382 48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1199 PHERLR-LMCRKVSAKLSLASEASAPLAKDLVG----TVVIVNADSALQLAH------HASPITSVRPTHTAYVIFTSGS 1267
Cdd:PRK13382 128 AGPALAeVVTREGVDTVIYDEEFSATVDRALADcpqaTRIVAWTDEDHDLTVevliaaHAGQRPEPTGRKGRVILLTSGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1268 TGEPKGCRieHRAASSAVTA----------HGRYLGMQAST-RTLQFASYAFAGSLvellmnlchgGCICV--------- 1327
Cdd:PRK13382 208 TGTPKGAR--RSGPGGIGTLkaildrtpwrAEEPTVIVAPMfHAWGFSQLVLAASL----------ACTIVtrrrfdpea 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1328 ---LSEEERrtdlASAMCRMKVNWAFLTSTVVDLLTPKSVPSLSILCVGGEPIRaSQIV-----RWGSQVHlrQTYGSSE 1399
Cdd:PRK13382 276 tldLIDRHR----ATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMR-PDVViafmdQFGDVIY--NNYNATE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1400 VSGIVSS--AALTTCSTTrdVGRASTG-VFWIVDPnNHNRLaPVGAVGEVLVEGPVLGREYIDEPDKtasTFIEapawra 1476
Cdd:PRK13382 349 AGMIATAtpADLRAAPDT--AGRPAEGtEIRILDQ-DFREV-PTGEVGTIFVRNDTQFDGYTSGSTK---DFHD------ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1477 slGLSAgqqrlykTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHqARLAEADVAEIAVelIQPKDGEDGM-LAC 1555
Cdd:PRK13382 416 --GFMA-------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEK-TLATHPDVAEAAV--IGVDDEQYGQrLAA 483
|
....*....
gi 1779949166 1556 FIVVEDSAS 1564
Cdd:PRK13382 484 FVVLKPGAS 492
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1116-1549 |
4.53e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 74.58 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPAICawD---GDMTYGELdvLSGRLA-GHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAF 1191
Cdd:PRK08633 617 LAEAWIDTAKRNWSRLAVA--DstgGELSYGKA--LTGALAlARLLKRELKDEENVGILLPPSVAGALANLALLLAGKVP 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1192 LLLDPSLPHERLR-----------LMCRKVSAKLSL---ASEASAP----LAKDLVGTVVIVNADSALQLAH-------H 1246
Cdd:PRK08633 693 VNLNYTASEAALKsaieqaqiktvITSRKFLEKLKNkgfDLELPENvkviYLEDLKAKISKVDKLTALLAARllparllK 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1247 ASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQ----FASYAFagsLVELLMNLCHG 1322
Cdd:PRK08633 773 RLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGL---TVTLWLPLLEG 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1323 -GCICVLSEEERRTdLASAMCRMKVNWAFLTSTVVDL------LTPKSVPSLSILCVGGE----PIRASQIVRWGsqVHL 1391
Cdd:PRK08633 850 iKVVYHPDPTDALG-IAKLVAKHRATILLGTPTFLRLylrnkkLHPLMFASLRLVVAGAEklkpEVADAFEEKFG--IRI 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1392 RQTYGSSEVSGIVS---------SAALTTCSTTRDVGRASTGV-FWIVDPNNHNRLaPVGAVGEVLVEGPVLGREYIDEP 1461
Cdd:PRK08633 927 LEGYGATETSPVASvnlpdvlaaDFKRQTGSKEGSVGMPLPGVaVRIVDPETFEEL-PPGEDGLILIGGPQVMKGYLGDP 1005
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1462 DKTASTFIEAPAwraslglsagqQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI---EVEEiEHQARLAEADVAEI 1538
Cdd:PRK08633 1006 EKTAEVIKDIDG-----------IGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVplgAVEE-ELAKALGGEEVVFA 1073
|
490
....*....|.
gi 1779949166 1539 AVELIQPKDGE 1549
Cdd:PRK08633 1074 VTAVPDEKKGE 1084
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1243-1525 |
5.27e-13 |
|
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: 73.16 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1243 LAHHASPITSV--RPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQF-ASYAFAGSLVELLMNL 1319
Cdd:cd17640 73 LNHSESVALVVenDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSIlPIWHSYERSAEYFIFA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1320 CHGGCIC----VLSEEERRT--DLASAMCRMkvnWAFLTSTVVDLLTPKSVPSLSI---LCVGGE---PIR-----ASQI 1382
Cdd:cd17640 153 CGCSQAYtsirTLKDDLKRVkpHYIVSVPRL---WESLYSGIQKQVSKSSPIKQFLflfFLSGGIfkfGISgggalPPHV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1383 VRW--GSQVHLRQTYGSSEVSGIVSsAALTTCSTTRDVGRASTGV-FWIVDPNNHNRLAPvGAVGEVLVEGPVLGREYID 1459
Cdd:cd17640 230 DTFfeAIGIEVLNGYGLTETSPVVS-ARRLKCNVRGSVGRPLPGTeIKIVDPEGNVVLPP-GEKGIVWVRGPQVMKGYYK 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 1460 EPDKTaSTFIEAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGR-KDNQVKLRGQRIEVEEIE 1525
Cdd:cd17640 308 NPEAT-SKVLDSDGW-------------FNTGDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIE 360
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1139-1569 |
6.35e-13 |
|
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: 72.76 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1139 DMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLrlmcrkvsaklslas 1218
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNEL--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1219 easaplakdlvgTVVIVNADSALQlahhaspitsvrptHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQAST 1298
Cdd:cd05912 66 ------------AFQLKDSDVKLD--------------DIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1299 RTLQFASYAFAGSLVELLMNLCHGGCICVL---SEEERRTDLASAmcrmKVNWAFLTSTVVDLL---TPKSVPSlSILCV 1372
Cdd:cd05912 120 NWLCALPLFHISGLSILMRSVIYGMTVYLVdkfDAEQVLHLINSG----KVTIISVVPTMLQRLleiLGEGYPN-NLRCI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1373 --GGEPIRAS---QIVRWGSQVHlrQTYGSSEV-SGIVSSAALTTCSTTRDVGRASTGV-FWIVDPNNhnrlaPVGAVGE 1445
Cdd:cd05912 195 llGGGPAPKPlleQCKEKGIPVY--QSYGMTETcSQIVTLSPEDALNKIGSAGKPLFPVeLKIEDDGQ-----PPYEVGE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1446 VLVEGPVLGREYIDEPDKTASTFieAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIE 1525
Cdd:cd05912 268 ILLKGPNVTKGYLNRPDATEESF--ENGW-------------FKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE 332
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1779949166 1526 HQArLAEADVAEIAVelIQPKDGEDGMLACFIVVEDSASNEDEL 1569
Cdd:cd05912 333 EVL-LSHPAIKEAGV--VGIPDDKWGQVPVAFVVSERPISEEEL 373
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
43-548 |
8.40e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 73.12 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 43 EQVLAQPNAPAICAWDG--EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHP 120
Cdd:PRK05857 22 EQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 121 ---VSRHKEILRQT------GARmVVVSAQHSARWASSSCHVVTLSEASIGQLTVEDDLPgfSATPGNAA----YVLFTS 187
Cdd:PRK05857 102 iaaIERFCQITDPAaalvapGSK-MASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASL--AGNADQGSedplAMIFTS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 188 GSTGIPKGVVLEHRAVstsclghgraFGITDQSR---------VLQFTSY-----TFDFCMAEIITTLLYGG-CIcvpSD 252
Cdd:PRK05857 179 GTTGEPKAVLLANRTF----------FAVPDILQkeglnwvtwVVGETTYsplpaTHIGGLWWILTCLMHGGlCV---TG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 253 RDRHSDLAKAINTMGANWALLTPS-----VAQL-LNPSDVPTLKILVIGGEQVTSKDWnRW--PTSVQLINGYGPTE--C 322
Cdd:PRK05857 246 GENTTSLLEILTTNAVATTCLVPTllsklVSELkSANATVPSLRLVGYGGSRAIAADV-RFieATGVRTAQVYGLSEtgC 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 323 CIVC--TGYTTTQAFKTGTIGTAIASVSWVVDPED-----YHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEdpA 395
Cdd:PRK05857 325 TALClpTDDGSIVKIEAGAVGRPYPGVDVYLAATDgigptAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID--G 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 396 WLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAVEVILLE--GEK 473
Cdd:PRK05857 403 WV---------------NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEG-VSGVREAACYEIPDEefGAL 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 474 SNTILAAFLQLDVKTGRAFPTNKAA----ETGSLAQvifpveagkklaerlPSYMVpdvyfVVTQLPITVSGKTDRKRL 548
Cdd:PRK05857 467 VGLAVVASAELDESAARALKHTIAArfrrESEPMAR---------------PSTIV-----IVTDIPRTQSGKVMRASL 525
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1095-1561 |
1.09e-12 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 72.72 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1095 PEDRQQLWE----WNhDVPpaiercIHDLFADQAkaRPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPED--IVP 1168
Cdd:PRK10946 9 PEEFARRYRekgyWQ-DLP------LTDILTRHA--ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDtaLVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1169 LCFEKSMWtvVAMLAVLKAGGAFLLLDPSlpHERLRLM--CRKVSAKLSLASEASAPLAKDL-----------VGTVVIV 1235
Cdd:PRK10946 80 LGNVAEFY--ITFFALLKLGVAPVNALFS--HQRSELNayASQIEPALLIADRQHALFSDDDflntlvaehssLRVVLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1236 NADSALQLAHH-ASPITSVRPTHT-----AYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQF--ASYA 1307
Cdd:PRK10946 156 NDDGEHSLDDAiNHPAEDFTATPSpadevAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCAlpAAHN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1308 FAGSLVELLMNLCHGGCIcVLSEEERRTDLASAMCRMKVNWAFLTSTVVDL-LTPKSVP-------SLSILCVGGEPIRA 1379
Cdd:PRK10946 236 YPMSSPGALGVFLAGGTV-VLAPDPSATLCFPLIEKHQVNVTALVPPAVSLwLQAIAEGgsraqlaSLKLLQVGGARLSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1380 SQIVRWGSQV--HLRQTYGSSEvsGIVSSAAL----TTCSTTRdvGR--ASTGVFWIVDpNNHNRLaPVGAVGEVLVEGP 1451
Cdd:PRK10946 315 TLARRIPAELgcQLQQVFGMAE--GLVNYTRLddsdERIFTTQ--GRpmSPDDEVWVAD-ADGNPL-PQGEVGRLMTRGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1452 VLGREYIDEPDKTASTFIEapawraslglsagqQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQArLA 1531
Cdd:PRK10946 389 YTFRGYYKSPQHNASAFDA--------------NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLL-LR 453
|
490 500 510
....*....|....*....|....*....|.
gi 1779949166 1532 EADVAEIAveLIQPKDGEDGMLAC-FIVVED 1561
Cdd:PRK10946 454 HPAVIHAA--LVSMEDELMGEKSCaFLVVKE 482
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
183-550 |
1.20e-12 |
|
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: 72.50 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 183 VLFTSGSTGIPKgvVLEHravSTSCLGHGRAfgiTDQSRVLQFTSYTFDFCMAE----------IITTLLYGGCICVpsd 252
Cdd:cd05928 179 IYFTSGTTGSPK--MAEH---SHSSLGLGLK---VNGRYWLDLTASDIMWNTSDtgwiksawssLFEPWIQGACVFV--- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 253 rdrHS----DLAKAINTMgANWALLT----PSVAQLLNPSDV-----PTLKILVIGGEQVTSKDWNRWP--TSVQLINGY 317
Cdd:cd05928 248 ---HHlprfDPLVILKTL-SSYPITTfcgaPTVYRMLVQQDLssykfPSLQHCVTGGEPLNPEVLEKWKaqTGLDIYEGY 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 318 GPTECCIVCTGYTTtQAFKTGTIGTAIASVS-WVVDpeDYHKLAPLGSVGELLVE-GPI----LARGYLNDAEKTAAAFi 391
Cdd:cd05928 324 GQTETGLICANFKG-MKIKPGSMGKASPPYDvQIID--DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATI- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 392 edpawlvdgcqgyagrRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQR-----VELGEIEHhiqgcmPEANQIAV-- 464
Cdd:cd05928 400 ----------------RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRigpfeVESALIEH------PAVVESAVvs 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 465 --EVILLEGEKSNTILAA-FLQLDvktgrafptnkaaetgslaqvifPVEAGKKLAERLPSYMVPDVY-----FvVTQLP 536
Cdd:cd05928 458 spDPIRGEVVKAFVVLAPqFLSHD-----------------------PEQLTKELQQHVKSVTAPYKYprkveF-VQELP 513
|
410
....*....|....
gi 1779949166 537 ITVSGKTDRKRLRE 550
Cdd:cd05928 514 KTVTGKIQRNELRD 527
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1140-1525 |
1.50e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 71.72 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1140 MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPherlrlmcrkvsaklslase 1219
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMG-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1220 asaplAKDLVGTVVIVNADSAlqlahhaspITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTR 1299
Cdd:cd05910 63 -----RKNLKQCLQEAEPDAF---------IGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1300 TLQ----FASYAFAGSLVELLMNLCHGGCICVLSEEerrtdLASAMCRMKVNWAFLTSTVVDLLT------PKSVPSLSI 1369
Cdd:cd05910 129 DLAtfplFALFGPALGLTSVIPDMDPTRPARADPQK-----LVGAIRQYGVSIVFGSPALLERVArycaqhGITLPSLRR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1370 LCVGGEPIRASQIVRWGSQVH----LRQTYGSSE---VSGIVSSAALTTCSTTRD------VGRASTGVFWIVDPNNHNR 1436
Cdd:cd05910 204 VLSAGAPVPIALAARLRKMLSdeaeILTPYGATEalpVSSIGSRELLATTTAATSggagtcVGRPIPGVRVRIIEIDDEP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1437 LA--------PVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPawraslglsaGQQRLYKTGDLARYKDDGSIELIGRK 1508
Cdd:cd05910 284 IAewddtlelPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN----------SEGFWHRMGDLGYLDDEGRLWFCGRK 353
|
410
....*....|....*..
gi 1779949166 1509 DNQVKLRGQRIEVEEIE 1525
Cdd:cd05910 354 AHRVITTGGTLYTEPVE 370
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
149-432 |
1.64e-12 |
|
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: 71.86 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 149 SSCHVVTLSEASIgqLTVEDDLPGFS-----------------ATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLG-- 209
Cdd:cd05927 70 AIEYILNHAEISI--VFCDAGVKVYSleefeklgkknkvppppPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGvf 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 210 --HGRAFGITDQSRVLQFT--SYTFDFCMaeIITTLLYGGCI-----------------------CVPSDRDR-HSDLAK 261
Cdd:cd05927 148 kiLEILNKINPTDVYISYLplAHIFERVV--EALFLYHGAKIgfysgdirlllddikalkptvfpGVPRVLNRiYDKIFN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 262 AINTMG------ANWAL-----------LTPS----------VAQLLNPSdvptLKILVIGGEQVTSK--DWNRWPTSVQ 312
Cdd:cd05927 226 KVQAKGplkrklFNFALnyklaelrsgvVRASpfwdklvfnkIKQALGGN----VRLMLTGSAPLSPEvlEFLRVALGCP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 313 LINGYGPTECCIVCTGyTTTQAFKTGTIGTAIASVSW-VVD-PE-DYHKLAPLGSvGELLVEGPILARGYLNDAEKTAAA 389
Cdd:cd05927 302 VLEGYGQTECTAGATL-TLPGDTSVGHVGGPLPCAEVkLVDvPEmNYDAKDPNPR-GEVCIRGPNVFSGYYKDPEKTAEA 379
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1779949166 390 FIEDpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGRK 432
Cdd:cd05927 380 LDED-GWL---------------HTGDIGEWLPNGTLKIIDRK 406
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
49-549 |
1.68e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPA-ICAWDGE-MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKE 126
Cdd:PRK13390 11 PDRPAvIVAETGEqVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 127 ILRQTGARMVVVSAQHSARWASSSCHVvTLSEASIGQLtveDDLPGFSATPGNA----------AYVLFTSGSTGIPKGV 196
Cdd:PRK13390 91 IVGDSGARVLVASAALDGLAAKVGADL-PLRLSFGGEI---DGFGSFEAALAGAgprlteqpcgAVMLYSSGTTGFPKGI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 197 V--LEHRAVST---SCLGHGRA-FGITDQ----SRVLQFTSYTFDFCmaEIITTLlyGGCIcVPSDRDRHSDLAKAINTM 266
Cdd:PRK13390 167 QpdLPGRDVDApgdPIVAIARAfYDISESdiyySSAPIYHAAPLRWC--SMVHAL--GGTV-VLAKRFDAQATLGHVERY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 267 GANWALLTPSV--------AQLLNPSDVPTLKILVIGGEQVtskdwnrwPTSVQ--LINGYGPteccIVCTGYTTTQAF- 335
Cdd:PRK13390 242 RITVTQMVPTMfvrllkldADVRTRYDVSSLRAVIHAAAPC--------PVDVKhaMIDWLGP----IVYEYYSSTEAHg 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 336 -----------KTGTIGTAIASVSWVVDpEDYHKLaPLGSVGELLVEGPILARGYLNDAEKTAAAfiEDPA---WLVdgc 401
Cdd:PRK13390 310 mtfidspdwlaHPGSVGRSVLGDLHICD-DDGNEL-PAGRIGTVYFERDRLPFRYLNDPEKTAAA--QHPAhpfWTT--- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 402 qgyagrrgrlykTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQgCMPEANQIAveVILLEGEKSNTILAAF 481
Cdd:PRK13390 383 ------------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALT-MHPAVHDVA--VIGVPDPEMGEQVKAV 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 482 LQLdvkTGRAFPTNKAAEtgslaqvifpvEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:PRK13390 448 IQL---VEGIRGSDELAR-----------ELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
177-544 |
1.81e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 72.69 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 177 PGNAAYVLFTSGSTGIPKGVVLEHRAVSTSC--LGHGRAFGITDqsRVLQ----FTSytFDFCMAEIITTL------LYg 244
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRaqVAARIDFSPED--KVFNalpvFHS--FGLTGGLVLPLLsgvkvfLY- 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 245 gcicvPSDRDRHS--DLAKAIN--------TMGANWAlltpsvaQLLNPSDVPTLKILVIGGEQV---TSKDW-NRWptS 310
Cdd:PRK06814 867 -----PSPLHYRIipELIYDTNatilfgtdTFLNGYA-------RYAHPYDFRSLRYVFAGAEKVkeeTRQTWmEKF--G 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 311 VQLINGYGPTECCIVcTGYTTTQAFKTGTIGTAIASVSWVVDPedyhkLAPLGSVGELLVEGPILARGYLnDAEKTAAaf 390
Cdd:PRK06814 933 IRILEGYGVTETAPV-IALNTPMHNKAGTVGRLLPGIEYRLEP-----VPGIDEGGRLFVRGPNVMLGYL-RAENPGV-- 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 391 IEDPA--WlvdgcqgyagrrgrlYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCMPEANQIAV---- 464
Cdd:PRK06814 1004 LEPPAdgW---------------YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVsipd 1068
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 465 ----EVILLEGEKSNTILAAFLqldvktgRAFPTNKAAETgslaqvifpveagkklaerlpsyMVPDVYFVVTQLPITVS 540
Cdd:PRK06814 1069 arkgERIILLTTASDATRAAFL-------AHAKAAGASEL-----------------------MVPAEIITIDEIPLLGT 1118
|
....
gi 1779949166 541 GKTD 544
Cdd:PRK06814 1119 GKID 1122
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
49-551 |
1.89e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 71.88 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEIL 128
Cdd:PRK07788 63 PDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 129 RQTGARMVV--------VSAQHS--ARWASSSCHVVTLSEASIGQLTVEDDLPGFSATP-----GNAAYVLFTSGSTGIP 193
Cdd:PRK07788 143 AREGVKALVyddeftdlLSALPPdlGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPlpkppKPGGIVILTSGTTGTP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 194 KGVVleHRAVST-SCLGhgrafGITDQ-----SRVLQFTSYTFD---FCMAEIITTLlygGCICVPSdrdRHSDLAKA-- 262
Cdd:PRK07788 223 KGAP--RPEPSPlAPLA-----GLLSRvpfraGETTLLPAPMFHatgWAHLTLAMAL---GSTVVLR---RRFDPEATle 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 263 -INTMGANWALLTPSV--------AQLLNPSDVPTLKILVIGGEQVTSKDWNRwptsVQ------LINGYGPTECCIVCT 327
Cdd:PRK07788 290 dIAKHKATALVVVPVMlsrildlgPEVLAKYDTSSLKIIFVSGSALSPELATR----ALeafgpvLYNLYGSTEVAFATI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 328 GYTTTQAFKTGTIGTAIASVSWVVDPEDyHKLAPLGSVGELLVEGPILARGYLNDAEKTaaafiedpawLVDGcqgyagr 407
Cdd:PRK07788 366 ATPEDLAEAPGTVGRPPKGVTVKILDEN-GNEVPRGVVGRIFVGNGFPFEGYTDGRDKQ----------IIDG------- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 408 rgrLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAveVILLEGEKSNTILAAFL----- 482
Cdd:PRK07788 428 ---LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAG-HPDVVEAA--VIGVDDEEFGQRLRAFVvkapg 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 483 -QLDVKTGRAFPTNKAAEtgslaqvifpveagkklaerlpsYMVP-DVYFvVTQLPITVSGKTDRKRLREI 551
Cdd:PRK07788 502 aALDEDAIKDYVRDNLAR-----------------------YKVPrDVVF-LDELPRNPTGKVLKRELREM 548
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
710-976 |
2.40e-12 |
|
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: 70.85 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 710 YIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTR----------IVHSSKMGMLQVV-LADGIEWEQANELEQYLEKDK 778
Cdd:cd19531 24 YNIPGALRLRGPLDVAALERALNELVARHEALRTTfvevdgepvqVILPPLPLPLPVVdLSGLPEAEREAEAQRLAREEA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 779 SVSMGLG-DSLARYALVRdVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPGFNAF-IKY---------- 846
Cdd:cd19531 104 RRPFDLArGPLLRATLLR-LGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPPLpIQYadyavwqrew 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 847 LGEQDHEAAAAYWQGTLADCQAIsfPALP-----PAVQQPVAdATTAFQCP--------ALARRpSDITMSTLIRAAWAL 913
Cdd:cd19531 183 LQGEVLERQLAYWREQLAGAPPV--LELPtdrprPAVQSFRG-ARVRFTLPaeltaalrALARR-EGATLFMTLLAAFQV 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 914 LASSYTSSDDVVFGATVTGRNAPvaGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATE 976
Cdd:cd19531 259 LLHRYSGQDDIVVGTPVAGRNRA--ELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALE 319
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
41-542 |
2.47e-12 |
|
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: 71.53 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 41 FAEQVLA---QPNAPAICAWDG----EMSYSVLDGLSTKLAGYLVKIGVKPGD----VVPLCFEksmwTVVAMLAVLKAG 109
Cdd:cd05943 72 YAENLLRhadADDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDrvagYLPNIPE----AVVAMLATASIG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 110 GA----------------FAPLDP--------------DHPV-SRHKEILRQ--TGARMVVVSAQHSARW--ASSSCHVV 154
Cdd:cd05943 148 AIwsscspdfgvpgvldrFGQIEPkvlfavdaytyngkRHDVrEKVAELVKGlpSLLAVVVVPYTVAAGQpdLSKIAKAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 155 TLSEAsigQLTVEDDLPGFSATPGNAA-YVLFTSGSTGIPK-------GVVLEHRAvstsclGHGRAFGITDQSRVLQFT 226
Cdd:cd05943 228 TLEDF---LATGAAGELEFEPLPFDHPlYILYSSGTTGLPKcivhgagGTLLQHLK------EHILHCDLRPGDRLFYYT 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 227 SytfdfCM-----------AEIITTLLYGGCICVPSDrDRHSDLAKA--INTMGANWALLTPSVAQLLNPS---DVPTLK 290
Cdd:cd05943 299 T-----CGwmmwnwlvsglAVGATIVLYDGSPFYPDT-NALWDLADEegITVFGTSAKYLDALEKAGLKPAethDLSSLR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 291 ILVIGGEQVTSK--DW--NRWPTSVQLINGYGPTECCIVCTGYTTTQAFKTGTI-----GTAIasVSWvvdpeDYHKLAP 361
Cdd:cd05943 373 TILSTGSPLKPEsfDYvyDHIKPDVLLASISGGTDIISCFVGGNPLLPVYRGEIqcrglGMAV--EAF-----DEEGKPV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 362 LGSVGELLVEGPILAR--GYLNDAEKT---AAAFIEDPAwlvdgcqgyagrrgrLYKTGDLVRYDDEGNLVCLGRKDSQV 436
Cdd:cd05943 446 WGEKGELVCTKPFPSMpvGFWNDPDGSryrAAYFAKYPG---------------VWAHGDWIEITPRGGVVILGRSDGTL 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 437 KVRGQRVELGEIEHHIQGCMPEANQIAVEvilLEGEKSNTILAAFLQLdvktgrafpTNKAAETGSLAQVIfpveaGKKL 516
Cdd:cd05943 511 NPGGVRIGTAEIYRVVEKIPEVEDSLVVG---QEWKDGDERVILFVKL---------REGVELDDELRKRI-----RSTI 573
|
570 580
....*....|....*....|....*.
gi 1779949166 517 AERLPSYMVPDVYFVVTQLPITVSGK 542
Cdd:cd05943 574 RSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1113-1279 |
2.78e-12 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 71.44 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1113 ERCIHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFL 1192
Cdd:PRK08279 36 KRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1193 LLDPSLPHERLRLMCRKVSAK--------LSLASEASAPLAKDLVGTVV----------IVNADSALQLAHHASPIT--S 1252
Cdd:PRK08279 116 LLNTQQRGAVLAHSLNLVDAKhlivgeelVEAFEEARADLARPPRLWVAggdtlddpegYEDLAAAAAGAPTTNPASrsG 195
|
170 180
....*....|....*....|....*..
gi 1779949166 1253 VRPTHTAYVIFTSGSTGEPKGCRIEHR 1279
Cdd:PRK08279 196 VTAKDTAFYIYTSGTTGLPKAAVMSHM 222
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1125-1564 |
3.30e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 71.03 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1125 KARPDAPAI--CAWDGDMTYGELDVLSGRLAGHLVE-LGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHE 1201
Cdd:PLN02574 50 HNHNGDTALidSSTGFSISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1202 RLRLMCRKVSAKLSLAS----EASAPLAKDLVGTVVIVNADS-ALQLAHHASPITS---------VRPTHTAYVIFTSGS 1267
Cdd:PLN02574 130 EIKKRVVDCSVGLAFTSpenvEKLSPLGVPVIGVPENYDFDSkRIEFPKFYELIKEdfdfvpkpvIKQDDVAAIMYSSGT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1268 TGEPKGCRIEHRAASSAVTAHGRYLGMQastrtlqfasYAFAGS---------------LVELLMNLCHGGCICVLSEEE 1332
Cdd:PLN02574 210 TGASKGVVLTHRNLIAMVELFVRFEASQ----------YEYPGSdnvylaalpmfhiygLSLFVVGLLSLGSTIVVMRRF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1333 RRTDLASAMCRMKVNWAFLTSTVVDLLTPKSVP-------SLSILCVGGEPIRASQI---VRWGSQVHLRQTYGSSEvsg 1402
Cdd:PLN02574 280 DASDMVKVIDRFKVTHFPVVPPILMALTKKAKGvcgevlkSLKQVSCGAAPLSGKFIqdfVQTLPHVDFIQGYGMTE--- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1403 ivSSAALTTCSTTRDVGR-ASTGvfwIVDPNNHNR--------LAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEaPA 1473
Cdd:PLN02574 357 --STAVGTRGFNTEKLSKySSVG---LLAPNMQAKvvdwstgcLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDK-DG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1474 WraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhqARLAE----ADVAEIAVEliqpkDGE 1549
Cdd:PLN02574 431 W-------------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLE--AVLIShpeiIDAAVTAVP-----DKE 490
|
490
....*....|....*
gi 1779949166 1550 DGMLACFIVVEDSAS 1564
Cdd:PLN02574 491 CGEIPVAFVVRRQGS 505
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
37-424 |
5.25e-12 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 70.67 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLD 116
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 117 pdhpVSRHKEIL----RQTGARMVVVSAQHSARWASSSCHVVTLSEASIGQLTVEDDLPGFSA----------------- 175
Cdd:PRK08279 119 ----TQQRGAVLahslNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDlaaaaagapttnpasrs 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 176 --TPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVL-----------------------------Q 224
Cdd:PRK08279 195 gvTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYcclplyhntggtvawssvlaagatlalrrK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 225 FTSYTF-DFCMAEIITTLLYGGCIC------VPSDRDRHSDLAKAIntmGANwalLTPSV-AQLLNPSDVPtlkilvigg 296
Cdd:PRK08279 275 FSASRFwDDVRRYRATAFQYIGELCryllnqPPKPTDRDHRLRLMI---GNG---LRPDIwDEFQQRFGIP--------- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 297 eqvtskdwnrwptsvQLINGYGPTECCIvctgyTTTQAF-KTGTIG-------TAIASVSWVVDPED--------YHKLA 360
Cdd:PRK08279 340 ---------------RILEFYAASEGNV-----GFINVFnFDGTVGrvplwlaHPYAIVKYDVDTGEpvrdadgrCIKVK 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 361 PlGSVGELLveGPILAR----GYlNDAEKTAA-----AFIEDPAWlvdgcqgyagrrgrlYKTGDLVRYDDEG 424
Cdd:PRK08279 400 P-GEVGLLI--GRITDRgpfdGY-TDPEASEKkilrdVFKKGDAW---------------FNTGDLMRDDGFG 453
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1261-1540 |
8.29e-12 |
|
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: 68.48 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1261 VIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLseeeRRTDlASA 1340
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFV----RRVD-AEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1341 MCRM----KVNWAFLTSTVV------------DLLTPKSVPSLSilcvGGEPIRASQIVRWGSqvHLRQtYGSSEVSGIV 1404
Cdd:cd17636 80 VLELieaeRCTHAFLLPPTIdqivelnadglyDLSSLRSSPAAP----EWNDMATVDTSPWGR--KPGG-YGQTEVMGLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1405 SSAALTTCSTTRdVGRASTGV-FWIVDPNNhnRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFieAPAWraslglsag 1483
Cdd:cd17636 153 TFAALGGGAIGG-AGRPSPLVqVRILDEDG--REVPDGEVGEIVARGPTVMAGYWNRPEVNARRT--RGGW--------- 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 1484 qqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhqARLAEAD-VAEIAV 1540
Cdd:cd17636 219 ----HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVE--RCLRQHPaVADAAV 270
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1141-1525 |
1.24e-11 |
|
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: 69.01 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLASEa 1220
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1221 saplakdlvgtvvivnadsalqlahhaspitsvrPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRT 1300
Cdd:cd05914 88 ----------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1301 LQFASYAFA-GSLVELLMNLCHGGCICVLSEEERRTDLASAMCRMKVN------WAFLTSTVVDLLtPKSVPS------- 1366
Cdd:cd05914 134 LSILPLHHIyPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAFAQVTPTlgvpvpLVIEKIFKMDII-PKLTLKkfkfkla 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1367 -----------------------LSILCVGGEPIrASQIVRWGSQVHLRQT--YGSSEVSGIVSSAALTTCSTTrDVGRA 1421
Cdd:cd05914 213 kkinnrkirklafkkvheafggnIKEFVIGGAKI-NPDVEEFLRTIGFPYTigYGMTETAPIISYSPPNRIRLG-SAGKV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1422 STGV-FWIVDPNnhnrlaPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEApAWraslglsagqqrlYKTGDLARYKDDG 1500
Cdd:cd05914 291 IDGVeVRIDSPD------PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKD-GW-------------FHTGDLGKIDAEG 350
|
410 420
....*....|....*....|....*.
gi 1779949166 1501 SIELIGRKDNQVKL-RGQRIEVEEIE 1525
Cdd:cd05914 351 YLYIRGRKKEMIVLsSGKNIYPEEIE 376
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1117-1577 |
1.32e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 68.87 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1117 HDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDP 1196
Cdd:PRK13383 38 YTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1197 SLPHERLRLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSALQLAHHASPitSVRPThTAYVIFTSGSTGEPKGCRI 1276
Cdd:PRK13383 118 EFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRP--AVAAP-GRIVLLTSGTTGKPKGVPR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1277 EHRAASsavtAHGRYLGMQASTR-----TLQFASYAFAG-SLVELLMNLCHGGCICVlseeERRTDLASAMCRMKVNWAF 1350
Cdd:PRK13383 195 APQLRS----AVGVWVTILDRTRlrtgsRISVAMPMFHGlGLGMLMLTIALGGTVLT----HRHFDAEAALAQASLHRAD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1351 LTSTVVDLLT-----PKSV------PSLSILCVGGEPIRASQIVRWGSQVH--LRQTYGSSEVsGIvssAALTTCSTTRD 1417
Cdd:PRK13383 267 AFTAVPVVLArilelPPRVrarnplPQLRVVMSSGDRLDPTLGQRFMDTYGdiLYNGYGSTEV-GI---GALATPADLRD 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1418 ----VGRASTGV-FWIVDPNNHnrlaPVG--AVGEVLVEGPVLGREYIDEPDKTASTfieapawraslGLSAgqqrlykT 1490
Cdd:PRK13383 343 apetVGKPVAGCpVRILDRNNR----PVGprVTGRIFVGGELAGTRYTDGGGKAVVD-----------GMTS-------T 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1491 GDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHqARLAEADVAEIAVelIQPKDGEDGM-LACFIVVE-----DSAS 1564
Cdd:PRK13383 401 GDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVEN-ALAAHPAVADNAV--IGVPDERFGHrLAAFVVLHpgsgvDAAQ 477
|
490
....*....|...
gi 1779949166 1565 NEDELSGKRTRLD 1577
Cdd:PRK13383 478 LRDYLKDRVSRFE 490
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1105-1569 |
2.13e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 68.42 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1105 NHDVPPAIERCIHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAV 1184
Cdd:PRK08316 2 MERSTRARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1185 LKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLASEASAPLAKDLVGTVVIV------------------NADSALQLAHH 1246
Cdd:PRK08316 82 ARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDtlilslvlggreapggwlDFADWAEAGSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1247 ASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAA----SSAVTAhgryLGMQASTRTLQ-FASYAFAGSLVELLMNLCH 1321
Cdd:PRK08316 162 AEPDVELADDDLAQILYTSGTESLPKGAMLTHRALiaeyVSCIVA----GDMSADDIPLHaLPLYHCAQLDVFLGPYLYV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1322 GGCICVLS-----------EEERRTDLasamcrmkvnwaFLTSTV-VDLL-----TPKSVPSL-------SILCVggEPI 1377
Cdd:PRK08316 238 GATNVILDapdpelilrtiEAERITSF------------FAPPTVwISLLrhpdfDTRDLSSLrkgyygaSIMPV--EVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1378 RasQIVRWGSQVHLRQTYGSSEVsgivssAALTTCSTTRD-------VGRASTGV-FWIVDPnNHNRLAPvGAVGEVLVE 1449
Cdd:PRK08316 304 K--ELRERLPGLRFYNCYGQTEI------APLATVLGPEEhlrrpgsAGRPVLNVeTRVVDD-DGNDVAP-GEVGEIVHR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1450 GPVLGREYIDEPDKTASTFieAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI---EVEEIEH 1526
Cdd:PRK08316 374 SPQLMLGYWDDPEKTAEAF--RGGW-------------FHSGDLGVMDEEGYITVVDRKKDMIKTGGENVasrEVEEALY 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1779949166 1527 QarlaEADVAEIAV-ELIQPKDGEdGMLACFIVVEDSASNEDEL 1569
Cdd:PRK08316 439 T----HPAVAEVAViGLPDPKWIE-AVTAVVVPKAGATVTEDEL 477
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1119-1579 |
2.44e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 68.52 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1119 LFADQAKAR--PDAPAICAWDGdMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDP 1196
Cdd:PRK06060 9 LLAEQASEAgwYDRPAFYAADV-VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1197 SLPHERLRLMCRKVSAKLSLaseASAPLaKDLVGTVVIVNADSALQLAHHASP--ITSVRPTHTAYVIFTSGSTGEPKGC 1274
Cdd:PRK06060 88 ELHRDDHALAARNTEPALVV---TSDAL-RDRFQPSRVAEAAELMSEAARVAPggYEPMGGDALAYATYTSGTTGPPKAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1275 RIEHRAASSAVTAHGR-YLGMQASTRTLQFASYAFAGSL-VELLMNLCHGGCICVLSEEERRTDLASAMCRMKVNWAF-- 1350
Cdd:PRK06060 164 IHRHADPLTFVDAMCRkALRLTPEDTGLCSARMYFAYGLgNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYgv 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1351 --LTSTVVDLLTPKSVPSLSILCVGG---EPIRASQIVRWGSQVHLRQTYGSSEVsgivssaALTTCSTTRDVGRASTgV 1425
Cdd:PRK06060 244 pnFFARVIDSCSPDSFRSLRCVVSAGealELGLAERLMEFFGGIPILDGIGSTEV-------GQTFVSNRVDEWRLGT-L 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1426 FWIVDPNNHNRLAPVGAV------GEVLVEGPVLGREYIDEPDktasTFIEAPAWraslglsagqqrlYKTGDLARYKDD 1499
Cdd:PRK06060 316 GRVLPPYEIRVVAPDGTTagpgveGDLWVRGPAIAKGYWNRPD----SPVANEGW-------------LDTRDRVCIDSD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1500 GSIELIGRKDNQVKLRGQRIEVEEIEHqaRLAEAD-VAEIAVELIQPKDGEDGMLACFIVVEDSASNEDELSGKRTRLDT 1578
Cdd:PRK06060 379 GWVTYRCRADDTEVIGGVNVDPREVER--LIIEDEaVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLN 456
|
.
gi 1779949166 1579 R 1579
Cdd:PRK06060 457 R 457
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1260-1540 |
2.47e-11 |
|
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: 67.41 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1260 YVIFTSGSTGEPKGCRIEH---RAASSAVTAHGRylGMQASTRTLQFASYAFAGSLVELLMNLCHG-------------G 1323
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQediFRMLMGGADFGT--GEFTPSEDAHKAAAAAAGTVMFPAPPLMHGtgswtafggllggQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1324 CICVLSEEERRTDLASAMCRMKVNWAFLTSTV-----VDLLT---PKSVPSLSILCVGGEPIRAS---QIVRWGSQVHLR 1392
Cdd:cd05924 85 TVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAmarplIDALRdagPYDLSSLFAISSGGALLSPEvkqGLLELVPNITLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1393 QTYGSSEVSGIVSSAAlttcsttrDVGRASTGVF-------WIVDPNNHNRLAPVGAVGEVLVEGPV-LGreYIDEPDKT 1464
Cdd:cd05924 165 DAFGSSETGFTGSGHS--------AGSGPETGPFtranpdtVVLDDDGRVVPPGSGGVGWIARRGHIpLG--YYGDEAKT 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1779949166 1465 ASTFIEAPAWRASLglsagqqrlykTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAV 1540
Cdd:cd05924 235 AETFPEVDGVRYAV-----------PGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVE-EALKSHPAVYDVLV 298
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
182-545 |
2.64e-11 |
|
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: 66.66 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 182 YVLFTSGSTGIPKGVVLEHR--AVSTSCLGHGraFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSDRDRHSDL 259
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERswIESFVCNEDL--FNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 260 AKaINTMGANWALLTPSVAQLLNPSDVPTLKILVI-GGEQVTSKDW-----NRWPTSVqLINGYGPTECCIVcTGYTTTQ 333
Cdd:cd17633 82 RK-INQYNATVIYLVPTMLQALARTLEPESKIKSIfSSGQKLFESTkkklkNIFPKAN-LIEFYGTSELSFI-TYNFNQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 334 AFKTGTIGTAIASVSWVVDPEDYhklaplGSVGELLVEGPILARGYLNdaektaAAFIEDPAWlvdgcqgyagrrgrlYK 413
Cdd:cd17633 159 SRPPNSVGRPFPNVEIEIRNADG------GEIGKIFVKSEMVFSGYVR------GGFSNPDGW---------------MS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 414 TGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGCmPEANQIAveVILLEGEKSNTILAAFL---QLDVKTGR 490
Cdd:cd17633 212 VGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAI-PGIEEAI--VVGIPDARFGEIAVALYsgdKLTYKQLK 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1779949166 491 AFptnkaaetgslaqvifpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDR 545
Cdd:cd17633 289 RF-----------------------LKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1096-1594 |
3.04e-11 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 67.98 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1096 EDRQQLWEWNHDVPPAIE----RCIHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLV-ELGVGPEDIVPLC 1170
Cdd:PRK08751 3 QARPWLQSYPAGVAAEIDleqfRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1171 FEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLR--LMCRKVSAKLSLAS--------EASAPL---------------- 1224
Cdd:PRK08751 83 MPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKhqLIDSGASVLVVIDNfgttvqqvIADTPVkqvittglgdmlgfpk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1225 ----------AKDLVGTVVIVNA---DSALQLAH-HASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGR 1290
Cdd:PRK08751 163 aalvnfvvkyVKKLVPEYRINGAirfREALALGRkHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1291 YLGMQAS---------TRTLQFASYAF-AGSLVelLMNLchGGCICVLSEEERRTDLASAMCRMKvnwaFLTSTVVDLL- 1359
Cdd:PRK08751 243 WLAGTGKleegcevviTALPLYHIFALtANGLV--FMKI--GGCNHLISNPRDMPGFVKELKKTR----FTAFTGVNTLf 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1360 -----TPK----SVPSLSILCVGGEPIRASQIVRWGSQVHLR--QTYGSSEVSGIVSSAALTTCSTTRDVGRA--STGVf 1426
Cdd:PRK08751 315 ngllnTPGfdqiDFSSLKMTLGGGMAVQRSVAERWKQVTGLTlvEAYGLTETSPAACINPLTLKEYNGSIGLPipSTDA- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1427 WIVDpnNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTAsTFIEAPAWraslglsagqqrlYKTGDLARYKDDGSIELIG 1506
Cdd:PRK08751 394 CIKD--DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETA-KVMDADGW-------------LHTGDIARMDEQGFVYIVD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1507 RKDNQVKLRGQRIEVEEIEHQARLAEAdVAEI-AVELIQPKDGEdgMLACFIVVEDSASNEDELSGK-RTRLDTRTQRTI 1584
Cdd:PRK08751 458 RKKDMILVSGFNVYPNEIEDVIAMMPG-VLEVaAVGVPDEKSGE--IVKVVIVKKDPALTAEDVKAHaRANLTGYKQPRI 534
|
570 580
....*....|....*....|..
gi 1779949166 1585 ------------GKIQDRLERD 1594
Cdd:PRK08751 535 iefrkelpktnvGKILRRELRD 556
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1118-1540 |
3.24e-11 |
|
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: 67.88 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1118 DLFADQAKA--RPDAPAICAWDGD-----MTYGELDVLSGRLAGHLVEL-GVGPEDIVPLCFEK-SMWTVVAmLAVLKAG 1188
Cdd:cd05928 13 DQWADKEKAgkRPPNPALWWVNGKgdevkWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRvPEWWLVN-VACIRTG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1189 GAFLLLDPSLPHERLRLMCRKVSAKLSLASEASAPLakdlVGTVVI--VNADSALQLAHHASP--------ITSVRPTHT 1258
Cdd:cd05928 92 LVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPE----VDSVASecPSLKTKLLVSEKSRDgwlnfkelLNEASTEHH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1259 AY---------VIFTSGSTGEPKGCRIEHRAASSAVTAHGRY-LGMQASTRTLQFASYAFAGSLVELLMNLCHGGCiCVL 1328
Cdd:cd05928 168 CVetgsqepmaIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYwLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGA-CVF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1329 SEEERRTD-------LAS----AMCRMKVNWAFLtstVVDLLTPKSVPSLSILCVGGEPIRASQIVRWGSQ--VHLRQTY 1395
Cdd:cd05928 247 VHHLPRFDplvilktLSSypitTFCGAPTVYRML---VQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQtgLDIYEGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1396 GSSEVSGIvssaalttCSTTR-------DVGRASTGV-FWIVDPNNHnrLAPVGAVGEVLVE-GPV----LGREYIDEPD 1462
Cdd:cd05928 324 GQTETGLI--------CANFKgmkikpgSMGKASPPYdVQIIDDNGN--VLPPGTEGDIGIRvKPIrpfgLFSGYVDNPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1463 KTASTFieapawraslglsagQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI---EVEE--IEHQArlaeadVAE 1537
Cdd:cd05928 394 KTAATI---------------RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIgpfEVESalIEHPA------VVE 452
|
...
gi 1779949166 1538 IAV 1540
Cdd:cd05928 453 SAV 455
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
574-642 |
5.24e-11 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 60.25 E-value: 5.24e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 574 PSTENEKALQQLWAGVLAIDADSIGLDDSFFR-LGGDSIAAMKLVGEARRA-GIHLTVADLFRNPKLEAVA 642
Cdd:COG0236 2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLA 72
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
46-427 |
5.32e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 67.38 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 46 LAQPNAPAiCAWDGeMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDP-------D 118
Cdd:PRK12582 68 LAQREPGH-GQWRK-VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPayslmshD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 119 H---------------------PVSRHKEILRQTGARMVVVSAQHSARWASSSCHVVTLS-----EASIGQLTveddlpg 172
Cdd:PRK12582 146 HaklkhlfdlvkprvvfaqsgaPFARALAALDLLDVTVVHVTGPGEGIASIAFADLAATPptaavAAAIAAIT------- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 173 fsatPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHG--RAFGITDQ-SRVLQFTSYTFDFCMAEIITTLLY-GGCIC 248
Cdd:PRK12582 219 ----PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEqlRPREPDPPpPVSLDWMPWNHTMGGNANFNGLLWgGGTLY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 249 VPSDRDRHSDLAKAIN--------TMG---ANWALLTPSVAQ--LLNPSDVPTLKILVIGGEQVTSKDWNRWPT------ 309
Cdd:PRK12582 295 IDDGKPLPGMFEETIRnlreisptVYGnvpAGYAMLAEAMEKddALRRSFFKNLRLMAYGGATLSDDLYERMQAlavrtt 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 310 --SVQLINGYGPTEccivcTGYTTTQAF----KTGTIGTAIASVSWvvdpedyhKLAPLGSVGELLVEGPILARGYLNDA 383
Cdd:PRK12582 375 ghRIPFYTGYGATE-----TAPTTTGTHwdteRVGLIGLPLPGVEL--------KLAPVGDKYEVRVKGPNVTPGYHKDP 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1779949166 384 EKTAAAFIEdpawlvdgcQGYagrrgrlYKTGDLVRYDDEGNLV 427
Cdd:PRK12582 442 ELTAAAFDE---------EGF-------YRLGDAARFVDPDDPE 469
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1254-1525 |
5.76e-11 |
|
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: 67.24 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1254 RPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTA----HGRYLGMQASTRTLQFASYA--FAgSLVELLMnLCHGGCICV 1327
Cdd:cd05927 112 KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGvfkiLEILNKINPTDVYISYLPLAhiFE-RVVEALF-LYHGAKIGF 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1328 LSEEER--RTDLA----------------------------SAMCRMKVNWAF------------LTSTVVDLLTPKSVP 1365
Cdd:cd05927 190 YSGDIRllLDDIKalkptvfpgvprvlnriydkifnkvqakGPLKRKLFNFALnyklaelrsgvvRASPFWDKLVFNKIK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1366 SL-----SILCVGGEPIRASQIVR----WGSQVhlRQTYGSSEVSGIvssaalTTCSTTRDVgraSTGVFWIVDPNNHNR 1436
Cdd:cd05927 270 QAlggnvRLMLTGSAPLSPEVLEFlrvaLGCPV--LEGYGQTECTAG------ATLTLPGDT---SVGHVGGPLPCAEVK 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1437 L-----------APVGAvGEVLVEGPVLGREYIDEPDKTASTFIEApAWraslglsagqqrlYKTGDLARYKDDGSIELI 1505
Cdd:cd05927 339 LvdvpemnydakDPNPR-GEVCIRGPNVFSGYYKDPEKTAEALDED-GW-------------LHTGDIGEWLPNGTLKII 403
|
330 340
....*....|....*....|.
gi 1779949166 1506 GRKDNQVKL-RGQRIEVEEIE 1525
Cdd:cd05927 404 DRKKNIFKLsQGEYVAPEKIE 424
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1263-1568 |
7.28e-11 |
|
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: 65.76 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1263 FTSGSTGEPKGCRIEHRAassaVTAHGRYLGMQASTRT-----LQFASYAFAGSLVELLMNLCHGgCICVLSEE--ERRT 1335
Cdd:cd05917 9 FTSGTTGSPKGATLTHHN----IVNNGYFIGERLGLTEqdrlcIPVPLFHCFGSVLGVLACLTHG-ATMVFPSPsfDPLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1336 DLAsAMCRMKVNWAFLTSTV-VDLLTPKSVP--SLSILCVG---GEPIRASQIVRWGSQVHLRQ---TYGSSEVSgivss 1406
Cdd:cd05917 84 VLE-AIEKEKCTALHGVPTMfIAELEHPDFDkfDLSSLRTGimaGAPCPPELMKRVIEVMNMKDvtiAYGMTETS----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1407 aALTTCSTTRD--------VGRASTGVFW-IVDPNNhNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTfieapawras 1477
Cdd:cd05917 158 -PVSTQTRTDDsiekrvntVGRIMPHTEAkIVDPEG-GIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA---------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1478 lglsAGQQRLYKTGDLARYKDDGSIELIGR-KDNQVKlRGQRIEVEEIEhQARLAEADVAEIAVELI-QPKDGEDgmLAC 1555
Cdd:cd05917 226 ----IDGDGWLHTGDLAVMDEDGYCRIVGRiKDMIIR-GGENIYPREIE-EFLHTHPKVSDVQVVGVpDERYGEE--VCA 297
|
330
....*....|...
gi 1779949166 1556 FIVVEDSASNEDE 1568
Cdd:cd05917 298 WIRLKEGAELTEE 310
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
38-433 |
7.92e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 66.90 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 38 HDLFAEQVLAQPNAPAIC------AWDG--EMSYSVLDGLSTKLAGYLVKIGVKPGDVV----PLCFEksmwTVVAMLAV 105
Cdd:PRK07529 28 YELLSRAAARHPDAPALSflldadPLDRpeTWTYAELLADVTRTANLLHSLGVGPGDVVafllPNLPE----THFALWGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 106 LKAGGAFA--P-LDPDHPVsrhkEILRQTGARMVVVSA-------------------------------------QHSAR 145
Cdd:PRK07529 104 EAAGIANPinPlLEPEQIA----ELLRAAGAKVLVTLGpfpgtdiwqkvaevlaalpelrtvvevdlarylpgpkRLAVP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 146 WASSSCHVVTLS-EASIGQLTVEDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQ 224
Cdd:PRK07529 180 LIRRKAHARILDfDAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 225 FTS-YTFDFCMAEIITTLLYGGCICVPS----------DR-----DRHSdlakaINTMGAnwallTPSV-AQLL----NP 283
Cdd:PRK07529 260 GLPlFHVNALLVTGLAPLARGAHVVLATpqgyrgpgviANfwkivERYR-----INFLSG-----VPTVyAALLqvpvDG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 284 SDVPTLKILVIGGEQVTSKDWNRWP--TSVQLINGYGPTEC-CIVCTGYTTTQAfKTGTIG-----TAIASVswVVDPE- 354
Cdd:PRK07529 330 HDISSLRYALCGAAPLPVEVFRRFEaaTGVRIVEGYGLTEAtCVSSVNPPDGER-RIGSVGlrlpyQRVRVV--ILDDAg 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 355 DYHKLAPLGSVGELLVEGPILARGYLNdAEKTAAAFIEDpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGR-KD 433
Cdd:PRK07529 407 RYLRDCAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLED-GWL---------------NTGDLGRIDADGYFWLTGRaKD 469
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1146-1525 |
9.30e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 66.36 E-value: 9.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1146 DVLSgrLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGG----------------AFLLLDPSL----------- 1198
Cdd:PLN02860 41 GVLS--LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGivaplnyrwsfeeaksAMLLVRPVMlvtdetcsswy 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1199 -PHERLRLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSALQLAHHASPitsvrPTHTAYVIFTSGSTGEPKGCRIE 1277
Cdd:PLN02860 119 eELQNDRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLKQRALGTTELDYAWA-----PDDAVLICFTSGTTGRPKGVTIS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1278 HRAASSAVTAHGRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTDLaSAMCRMKVNwAFLT--STV 1355
Cdd:PLN02860 194 HSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAAL-QAIKQHNVT-SMITvpAMM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1356 VDLLTP-------KSVPSLSILCVGGEPIRASQI---VRWGSQVHLRQTYGSSEVSGIVSSAALTTCSTTRDVGRASTGV 1425
Cdd:PLN02860 272 ADLISLtrksmtwKVFPSVRKILNGGGSLSSRLLpdaKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTVN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1426 FWIVDPNNHNRLAPVGA----------------VGEVLVEGPVLGREYIDEPDKTASTfIEAPAWRAslglsagqqrlyk 1489
Cdd:PLN02860 352 QTKSSSVHQPQGVCVGKpaphvelkigldessrVGRILTRGPHVMLGYWGQNSETASV-LSNDGWLD------------- 417
|
410 420 430
....*....|....*....|....*....|....*.
gi 1779949166 1490 TGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIE 1525
Cdd:PLN02860 418 TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVE 453
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
31-551 |
1.09e-10 |
|
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: 66.18 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 31 GVTNKCIH--DLFAEQvlAQPNAPAIcAWDGEM-------SYS-VLDGLStKLAGYLVKIGVKPGDVV----PLCFEksm 96
Cdd:cd05967 47 GRLNTCYNalDRHVEA--GRGDQIAL-IYDSPVtgtertyTYAeLLDEVS-RLAGVLRKLGVVKGDRViiymPMIPE--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 97 wTVVAMLAVLKAG-------GAFAP---------------------LDPDHPV------------SRHKE----ILRQTG 132
Cdd:cd05967 120 -AAIAMLACARIGaihsvvfGGFAAkelasriddakpklivtascgIEPGKVVpykplldkalelSGHKPhhvlVLNRPQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 133 ARMVVVSAQHSARWASsschvVTLSEASIGQLTVEDDLPgfsatpgnaAYVLFTSGSTGIPKGVVlehR-------AVST 205
Cdd:cd05967 199 VPADLTKPGRDLDWSE-----LLAKAEPVDCVPVAATDP---------LYILYTSGTTGKPKGVV---RdngghavALNW 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 206 SC-----LGHGRAF-GITDQSRVLQFtSYtfdFCMAEII---TTLLYGGcicVPsdrDRHSDlakaintMGANW------ 270
Cdd:cd05967 262 SMrniygIKPGDVWwAASDVGWVVGH-SY---IVYGPLLhgaTTVLYEG---KP---VGTPD-------PGAFWrvieky 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 271 ---ALLT-----------PSVAQLLNPSDVPTLKILVIGGEQ--VTSKDWNRWPTSVQLINGYGPTEC--CIV--CTGYT 330
Cdd:cd05967 325 qvnALFTaptairairkeDPDGKYIKKYDLSSLRTLFLAGERldPPTLEWAENTLGVPVIDHWWQTETgwPITanPVGLE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 331 TtQAFKTGTIGTAIASVSWVVDPEDYHKLAPlGSVGELLVEGPI----LARGYLNDAEKTAAAFIEDPawlvdgcqGYag 406
Cdd:cd05967 405 P-LPIKAGSPGKPVPGYQVQVLDEDGEPVGP-NELGNIVIKLPLppgcLLTLWKNDERFKKLYLSKFP--------GY-- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 407 rrgrlYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHI--QGCMPEANQIAVEVILlegeKSNTILA-AFLQ 483
Cdd:cd05967 473 -----YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVlsHPAVAECAVVGVRDEL----KGQVPLGlVVLK 543
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 484 LDVKtgrafPTNKAAETGSLAQV---IFPVEAGKKLaerlpsymvpdvyFVVTQLPITVSGKTDRKRLREI 551
Cdd:cd05967 544 EGVK-----ITAEELEKELVALVreqIGPVAAFRLV-------------IFVKRLPKTRSGKILRRTLRKI 596
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1124-1272 |
1.17e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 65.66 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERL 1203
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 1204 RLMCRKVSAKLSLASEASAPLAkdlvgtvvivNADSALQLAHHASPITSVRPTHTAYVIFTSGSTGEPK 1272
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENTFS----------ALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPK 151
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
40-550 |
1.25e-10 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 65.94 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 40 LFAEQVLAQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDH 119
Cdd:PRK13382 48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 120 PVSRHKEILRQTGARMVVVSAQHSARW--ASSSCHVVTLSEA---SIGQLTVEddlpGFSATPGN---------AAYVLF 185
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSATVdrALADCPQATRIVAwtdEDHDLTVE----VLIAAHAGqrpeptgrkGRVILL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 186 TSGSTGIPKGvvlehrAVSTSCLGHGRAFGITDQS--RVLQ-------------FTSYTFDFCMAEIITT---------- 240
Cdd:PRK13382 204 TSGTTGTPKG------ARRSGPGGIGTLKAILDRTpwRAEEptvivapmfhawgFSQLVLAASLACTIVTrrrfdpeatl 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 241 -LL-----YGGCIcVPSDRDRHSDLakaintmganwalltpsVAQLLNPSDVPTLKILVIGGE----QVTSKDWNRWPTS 310
Cdd:PRK13382 278 dLIdrhraTGLAV-VPVMFDRIMDL-----------------PAEVRNRYSGRSLRFAAASGSrmrpDVVIAFMDQFGDV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 311 vqLINGYGPTECCIVCTGYTTTQAFKTGTIGT-AIASVSWVVDPEdyHKLAPLGSVGELLVEGPILARGYLNDAEKtaaA 389
Cdd:PRK13382 340 --IYNNYNATEAGMIATATPADLRAAPDTAGRpAEGTEIRILDQD--FREVPTGEVGTIFVRNDTQFDGYTSGSTK---D 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 390 FIEdpawlvdgcqGYAGrrgrlykTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIqGCMPEANQIAveVILL 469
Cdd:PRK13382 413 FHD----------GFMA-------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTL-ATHPDVAEAA--VIGV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 470 EGEKSNTILAAFLqldvktgraFPTNKAAETgslaqvifPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:PRK13382 473 DDEQYGQRLAAFV---------VLKPGASAT--------PETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
.
gi 1779949166 550 E 550
Cdd:PRK13382 536 A 536
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1124-1594 |
1.25e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 65.87 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPA-ICAWDGD-MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHE 1201
Cdd:PRK13391 7 AQTTPDKPAvIMASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1202 RLRLMCRKVSAKLSLASEASAPLAKDLVGTV------VIVNADSALQ---------LAHHASPITSvRPTHTAyVIFTSG 1266
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLDVARALLKQCpgvrhrLVLDGDGELEgfvgyaeavAGLPATPIAD-ESLGTD-MLYSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1267 STGEPKGCRIE--HRAASSAVTAHG---RYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTDLAsAM 1341
Cdd:PRK13391 165 TTGRPKGIKRPlpEQPPDTPLPLTAflqRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLA-LI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1342 CRMKVNWAFLTSTVVD--LLTPKS------VPSLSILCVGGEP----IRASQIVRWGSQVHlrQTYGSSE---VSGIVSS 1406
Cdd:PRK13391 244 EEYGVTHTQLVPTMFSrmLKLPEEvrdkydLSSLEVAIHAAAPcppqVKEQMIDWWGPIIH--EYYAATEglgFTACDSE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1407 AALTTCSTtrdVGRASTGVFWIVDPNnhNRLAPVGAVGEVLVEGpvlGR--EYIDEPDKTASTFIEAPAWRaslglsagq 1484
Cdd:PRK13391 322 EWLAHPGT---VGRAMFGDLHILDDD--GAELPPGEPGTIWFEG---GRpfEYLNDPAKTAEARHPDGTWS--------- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1485 qrlyKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEH----QARLAEA--------DVAEIAVELIQPKDGEDG- 1551
Cdd:PRK13391 385 ----TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENllitHPKVADAavfgvpneDLGEEVKAVVQPVDGVDPg 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1779949166 1552 -----MLACF-------IVVEDSASNEDELSgkrtRLDTrtqrtiGKIQDRLERD 1594
Cdd:PRK13391 461 palaaELIAFcrqrlsrQKCPRSIDFEDELP----RLPT------GKLYKRLLRD 505
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
53-414 |
1.50e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 65.70 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 53 AICAWDGE-MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPldpdhpVSRH---KE-- 126
Cdd:PRK08276 3 VIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTP------INWHltaAEia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 127 -ILRQTGARMVVVSAqhsaRWASSSCHVVTLSEASIGQLTVED-DLPGF----------SATPGNA----AYVLFTSGST 190
Cdd:PRK08276 77 yIVDDSGAKVLIVSA----ALADTAAELAAELPAGVPLLLVVAgPVPGFrsyeealaaqPDTPIADetagADMLYSSGTT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 191 GIPKGVV--LEHRAVSTSCLGH----GRAFGITDQSRVLQ----FTSYTFDFCMaeiiTTLLYGGCICVPSDRDRHSDLA 260
Cdd:PRK08276 153 GRPKGIKrpLPGLDPDEAPGMMlallGFGMYGGPDSVYLSpaplYHTAPLRFGM----SALALGGTVVVMEKFDAEEALA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 261 kAIN-----------TMGANWALLTPSVAqllNPSDVPTLKILVIGGEqvtskdwnrwPTSV----QLINGYGP------ 319
Cdd:PRK08276 229 -LIEryrvthsqlvpTMFVRMLKLPEEVR---ARYDVSSLRVAIHAAA----------PCPVevkrAMIDWWGPiiheyy 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 320 --TECCIVCTGYTTTQAFKTGTIGTAIASVSWVVDpEDYHKLAPlGSVGELLVEGPILARGYLNDAEKTAAAFIeDPAWL 397
Cdd:PRK08276 295 asSEGGGVTVITSEDWLAHPGSVGKAVLGEVRILD-EDGNELPP-GEIGTVYFEMDGYPFEYHNDPEKTAAARN-PHGWV 371
|
410
....*....|....*..
gi 1779949166 398 VDGCQGYAGRRGRLYKT 414
Cdd:PRK08276 372 TVGDVGYLDEDGYLYLT 388
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
41-202 |
1.92e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 65.28 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 41 FAEQvlaQPNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHP 120
Cdd:PRK09029 12 WAQV---RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 121 VSRHKEILRQTGARMVVVSAQHsaRWASSSCHVVTLSEASIGQLTVEDDLPgfsatpgnaAYVLFTSGSTGIPKGVVLEH 200
Cdd:PRK09029 89 QPLLEELLPSLTLDFALVLEGE--NTFSALTSLHLQLVEGAHAVAWQPQRL---------ATMTLTSGSTGLPKAAVHTA 157
|
..
gi 1779949166 201 RA 202
Cdd:PRK09029 158 QA 159
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1124-1550 |
2.11e-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: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPherl 1203
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1204 RLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSALQlahHASPITSVRPTHtaYVIFTSGSTGEPKGCRIEHrAASS 1283
Cdd:cd05929 78 RAEACAIIEIKAAALVCGLFTGGGALDGLEDYEAAEGGS---PETPIEDEAAGW--KMLYSGGTTGRPKGIKRGL-PGGP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1284 AVTAHGR----YLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEERRTDLAsAMCRMKVNWAFLTSTV-VDL 1358
Cdd:cd05929 152 PDNDTLMaaalGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLR-LIERYRVTFAQFVPTMfVRL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1359 LT-PKSVP------SLSILCVGGEPIRA---SQIVRWGSQVhLRQTYGSSEVSGivssaaLTTCSTTR------DVGRAS 1422
Cdd:cd05929 231 LKlPEAVRnaydlsSLKRVIHAAAPCPPwvkEQWIDWGGPI-IWEYYGGTEGQG------LTIINGEEwlthpgSVGRAV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1423 TGVFWIVDPNNhNRLAPvGAVGEVLVEGPVlGREYIDEPDKTASTfIEAPAWRaSLglsagqqrlyktGDLARYKDDGSI 1502
Cdd:cd05929 304 LGKVHILDEDG-NEVPP-GEIGEVYFANGP-GFEYTNDPEKTAAA-RNEGGWS-TL------------GDVGYLDEDGYL 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 1503 ELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAV------EL-------IQPKDGED 1550
Cdd:cd05929 367 YLTDRRSDMIISGGVNIYPQEIE-NALIAHPKVLDAAVvgvpdeELgqrvhavVQPAPGAD 426
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
768-982 |
2.14e-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: 64.70 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 768 NELEQYLEKDKSVSMGL-GDSLARYALVRdVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPG---FNAF 843
Cdd:cd19533 91 GAAQQWMQEDLRKPLPLdNDPLFRHALFT-LGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPAPpapFGSF 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 844 IKYL-GEQDH------EAAAAYWQGTLADcqaisfpaLPPAVQ------QPVADAT--TAFQCPALAR------RPSDIT 902
Cdd:cd19533 170 LDLVeEEQAYrqserfERDRAFWTEQFED--------LPEPVSlarrapGRSLAFLrrTAELPPELTRtlleaaEAHGAS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 903 MSTLIRAAWALLASSYTSSDDVVFGATVTGRnAPVAGIEaMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATEMI---- 978
Cdd:cd19533 242 WPSFFIALVAAYLHRLTGANDVVLGVPVMGR-LGAAARQ-TPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLrhqr 319
|
....*
gi 1779949166 979 -PYEQ 982
Cdd:cd19533 320 yRYED 324
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
33-554 |
2.18e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 65.22 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 33 TNKCIHDLFAEQVLAQPNAPAICAWDGEM--SYSVLDGLSTKLAGYLVKIGVKPGDVV----PLCFEksmWTVVaMLAVL 106
Cdd:PRK08315 14 LEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVgiwaPNVPE---WVLT-QFATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 107 KAGGAFAPLDPDHPVSRHKEILRQTGARMVVVSAQ------------------HSARWASSSC------HVVTL-SEASI 161
Cdd:PRK08315 90 KIGAILVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamlyelapelaTCEPGQLQSArlpelrRVIFLgDEKHP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 162 GQLTVED-----------DLPGFSAT--PGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVlqftsy 228
Cdd:PRK08315 170 GMLNFDEllalgravddaELAARQATldPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRL------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 229 tfdfCmaeiITTLLY---------------GGCICVPSDR-DRHSDLAkAIN-----------TMganwalltpSVAQLL 281
Cdd:PRK08315 244 ----C----IPVPLYhcfgmvlgnlacvthGATMVYPGEGfDPLATLA-AVEeerctalygvpTM---------FIAELD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 282 NPS----DVPTLKILVIGG--------EQVTSKDWNRWPTSVqlingYGPTECCIVCTGYTTTQAF--KTGTIGTAIASV 347
Cdd:PRK08315 306 HPDfarfDLSSLRTGIMAGspcpievmKRVIDKMHMSEVTIA-----YGMTETSPVSTQTRTDDPLekRVTTVGRALPHL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 348 -SWVVDPEDyHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAfIEDPAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNL 426
Cdd:PRK08315 381 eVKIVDPET-GETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDADGWM---------------HTGDLAVMDEEGYV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 427 VCLGR-KDsqVKVRGqrvelG------EIE----HH--IQgcmpeanqiAVEVILLEGEKSNTILAAFLQLdvktgrafp 493
Cdd:PRK08315 444 NIVGRiKD--MIIRG-----GeniyprEIEeflyTHpkIQ---------DVQVVGVPDEKYGEEVCAWIIL--------- 498
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 494 tnKAAETGSLAQVI-FpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLREIGAS 554
Cdd:PRK08315 499 --RPGATLTEEDVRdF-------CRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIE 551
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
58-552 |
2.34e-10 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 64.68 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 58 DGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDpdhpvsrhkeiLRQTGARMVv 137
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN-----------YNLRGESLA- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 138 vsaqhsarwassscHVVTLSEAsiGQLTVEddlpgfsatpgnAAYVLFTSGSTGIPKGVVLEH-RAVSTSCLGHGraFGI 216
Cdd:cd05940 69 --------------HCLNVSSA--KHLVVD------------AALYIYTSGTTGLPKAAIISHrRAWRGGAFFAG--SGG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 217 TDQSRVLqftsYTfdfCM------AEII---TTLLYGGCICVP---SDRDRHSDLAKaintmgaNWALLTPSVAQ----L 280
Cdd:cd05940 119 ALPSDVL----YT---CLplyhstALIVgwsACLASGATLVIRkkfSASNFWDDIRK-------YQATIFQYIGElcryL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 281 LNPSDVPT---LKILVIGGEQVTSKDWNRWPTSVQLIN---GYGPTECCIVCTGYTTtqafKTGTIG---------TAIA 345
Cdd:cd05940 185 LNQPPKPTerkHKVRMIFGNGLRPDIWEEFKERFGVPRiaeFYAATEGNSGFINFFG----KPGAIGrnpsllrkvAPLA 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 346 SVSW-------VVDPEDYHKLAPLGSVGELLVEGPILAR--GYLnDAEKTAAAFIEDpawlvdgcqgyAGRRG-RLYKTG 415
Cdd:cd05940 261 LVKYdlesgepIRDAEGRCIKVPRGEPGLLISRINPLEPfdGYT-DPAATEKKILRD-----------VFKKGdAWFNTG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 416 DLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGC--MPEANQIAVEVILLEGEksntilAAFLQLDVKTGRAFP 493
Cdd:cd05940 329 DLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFpgVEEANVYGVQVPGTDGR------AGMAAIVLQPNEEFD 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 494 TNKAAETgslaqvifpveagkkLAERLPSYMVPdvYFV--VTQLPITVSGKTDRKRLREIG 552
Cdd:cd05940 403 LSALAAH---------------LEKNLPGYARP--LFLrlQPEMEITGTFKQQKVDLRNEG 446
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
60-549 |
2.38e-10 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 65.09 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 60 EMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMVVVS 139
Cdd:PRK08008 37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 140 AQ-----HSARWASSSC--HVVTLSEAS------------IGQLTVE-DDLPGFSATpgNAAYVLFTSGSTGIPKGVVLE 199
Cdd:PRK08008 117 AQfypmyRQIQQEDATPlrHICLTRVALpaddgvssftqlKAQQPATlCYAPPLSTD--DTAEILFTSGTTSRPKGVVIT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 200 HRAVSTSclGHGRAF--GITDQSRVLQ-FTSYTFDFCMAEIITTLLYGGCICVPSD----------RDRHSDLAKAINTM 266
Cdd:PRK08008 195 HYNLRFA--GYYSAWqcALRDDDVYLTvMPAFHIDCQCTAAMAAFSAGATFVLLEKysarafwgqvCKYRATITECIPMM 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 267 GANWALLTPS----------VAQLLNPSDvptlkilviggeqvTSKDWNRWPTSVQLINGYGPTECCIVCTGYTTTQAFK 336
Cdd:PRK08008 273 IRTLMVQPPSandrqhclreVMFYLNLSD--------------QEKDAFEERFGVRLLTSYGMTETIVGIIGDRPGDKRR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 337 TGTIGTAIASVSWVVDPEDYHKLAPlGSVGELLVEG---PILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrgrlyK 413
Cdd:PRK08008 339 WPSIGRPGFCYEAEIRDDHNRPLPA-GEIGEICIKGvpgKTIFKEYYLDPKATAKVLEAD-GWL---------------H 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 414 TGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEhHIQGCMPEANQIAV----EVILLEGEKSNTILAAFLQLDVKTG 489
Cdd:PRK08008 402 TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELE-NIIATHPKIQDIVVvgikDSIRDEAIKAFVVLNEGETLSEEEF 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 490 RAFptnkaaetgslaqvifpveagkkLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLR 549
Cdd:PRK08008 481 FAF-----------------------CEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1260-1576 |
2.51e-10 |
|
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: 63.58 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1260 YVIFTSGSTGEPKGCRIEHR--AASSAVTAHGRYlgMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLseeeRRTDL 1337
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERswIESFVCNEDLFN--ISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQ----RKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1338 ASAM---CRMKVNWAFLTSTVVDLLTPKSVPSL---SILCVGG--EPIRASQIVRWGSQVHLRQTYGSSEVSgIVSSAAL 1409
Cdd:cd17633 78 KSWIrkiNQYNATVIYLVPTMLQALARTLEPESkikSIFSSGQklFESTKKKLKNIFPKANLIEFYGTSELS-FITYNFN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1410 TTCSTTRDVGRASTGVfwivdpNNHNRLAPVGAVGEVLVEGPVLGREYIDEpdktasTFIEAPAWraslglsagqqrlYK 1489
Cdd:cd17633 157 QESRPPNSVGRPFPNV------EIEIRNADGGEIGKIFVKSEMVFSGYVRG------GFSNPDGW-------------MS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1490 TGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVelIQPKDGEDGMLACFIVVEDSASNEDEL 1569
Cdd:cd17633 212 VGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIE-SVLKAIPGIEEAIV--VGIPDARFGEIAVALYSGDKLTYKQLK 288
|
....*..
gi 1779949166 1570 SGKRTRL 1576
Cdd:cd17633 289 RFLKQKL 295
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1259-1577 |
2.93e-10 |
|
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: 63.50 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1259 AYVIFTSGSTGEPKGcrIEHRAA---SSAVTAHGRyLGMQASTRTL-QFASYAFAGsLVELLMNLCHGGcicVLSEEERR 1334
Cdd:cd17630 3 ATVILTSGSTGTPKA--VVHTAAnllASAAGLHSR-LGFGGGDSWLlSLPLYHVGG-LAILVRSLLAGA---ELVLLERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1335 TDLASAMCRMKVNWAFLTST-----VVDLLTPKSVPSLSILCVGGEPIrASQIVRWGSQVHLR--QTYGSSEVSGIVssa 1407
Cdd:cd17630 76 QALAEDLAPPGVTHVSLVPTqlqrlLDSGQGPAALKSLRAVLLGGAPI-PPELLERAADRGIPlyTTYGMTETASQV--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1408 altTCSTTRDVGRASTGVfwivdPNNHNRLAPVGAvGEVLVEGPVLGREYIDEPDKTASTfieAPAWraslglsagqqrl 1487
Cdd:cd17630 152 ---ATKRPDGFGRGGVGV-----LLPGRELRIVED-GEIWVGGASLAMGYLRGQLVPEFN---EDGW------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1488 YKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVelIQPKDGEDG-MLACFIVVEDSASNE 1566
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIE-AALAAHPAVRDAFV--VGVPDEELGqRPVAVIVGRGPADPA 283
|
330
....*....|.
gi 1779949166 1567 DELSGKRTRLD 1577
Cdd:cd17630 284 ELRAWLKDKLA 294
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1133-1582 |
4.23e-10 |
|
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: 64.19 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1133 ICAWDGDM-----TYGELDVLSGRLAGHLVELGVGPEDIVPLCfeksMWT----VVAMLAVLKAGGAFLLLDPSLPHERL 1203
Cdd:cd12119 14 IVSRTHEGevhryTYAEVAERARRLANALRRLGVKPGDRVATL----AWNthrhLELYYAVPGMGAVLHTINPRLFPEQI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1204 RLMCRKVSAKLSLASEASAPLAKDLVGT-----VVIVNADSA-------LQLAHHASPITSVRPT--------HTAYVI- 1262
Cdd:cd12119 90 AYIINHAEDRVVFVDRDFLPLLEAIAPRlptveHVVVMTDDAampepagVGVLAYEELLAAESPEydwpdfdeNTAAAIc 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1263 FTSGSTGEPKGCRIEHRA----ASSAVTAHGRYLGmqastrtlQFASY--------------AFAGSLVellmnlchgGC 1324
Cdd:cd12119 170 YTSGTTGNPKGVVYSHRSlvlhAMAALLTDGLGLS--------ESDVVlpvvpmfhvnawglPYAAAMV---------GA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1325 ICVLSEeeRRTD---LASAMCRMKVNWAFLTSTVVDLL------TPKSVPSLSILCVGGEPIRASQIVRWGSQ-VHLRQT 1394
Cdd:cd12119 233 KLVLPG--PYLDpasLAELIEREGVTFAAGVPTVWQGLldhleaNGRDLSSLRRVVIGGSAVPRSLIEAFEERgVRVIHA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1395 YGSSEVSGIVSSAALTTCSTTRDVG-----RASTGVF------WIVDPNNhNRLAPVG-AVGEVLVEGPVLGREYIDEPD 1462
Cdd:cd12119 311 WGMTETSPLGTVARPPSEHSNLSEDeqlalRAKQGRPvpgvelRIVDDDG-RELPWDGkAVGELQVRGPWVTKSYYKNDE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1463 KTASTFieAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQArLAEADVAEIAVEL 1542
Cdd:cd12119 390 ESEALT--EDGW-------------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAI-MAHPAVAEAAVIG 453
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1779949166 1543 I-QPKDGEDGMLacFIVV-EDSASNEDELsgkRTRLDTRTQR 1582
Cdd:cd12119 454 VpHPKWGERPLA--VVVLkEGATVTAEEL---LEFLADKVAK 490
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1109-1498 |
6.09e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 63.91 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1109 PPAIERCIHDLFADQAKARPDAPAIC-------AWDGdMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAM 1181
Cdd:PRK12582 44 LGPYPRSIPHLLAKWAAEAPDRPWLAqrepghgQWRK-VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1182 LAVLKAG-------GAFLLLdpSLPHERLRLMCRKVSAKLSLASEAsAPLAK-----DLVG-TVVIVNAD----SALQLA 1244
Cdd:PRK12582 123 LAAMQAGvpaapvsPAYSLM--SHDHAKLKHLFDLVKPRVVFAQSG-APFARalaalDLLDvTVVHVTGPgegiASIAFA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1245 HHAS-PITS--------VRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAvtahgryLGMQASTRT----------LQFA- 1304
Cdd:PRK12582 200 DLAAtPPTAavaaaiaaITPDTVAKYLFTSGSTGMPKAVINTQRMMCAN-------IAMQEQLRPrepdppppvsLDWMp 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1305 -SYAFAGSlVELLMNLCHGGCICV--------LSEEERR-----------------TDLASAMCRMKVnwafltstvvdl 1358
Cdd:PRK12582 273 wNHTMGGN-ANFNGLLWGGGTLYIddgkplpgMFEETIRnlreisptvygnvpagyAMLAEAMEKDDA------------ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1359 LTPKSVPSLSILCVGG--------EPIRASQIVRWGSQVHLRQTYGSSEVSGIvssaalttcsttrdvgraSTGVFWIVD 1430
Cdd:PRK12582 340 LRRSFFKNLRLMAYGGatlsddlyERMQALAVRTTGHRIPFYTGYGATETAPT------------------TTGTHWDTE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 1431 ---------PNNHNRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapawraslglsagqQRLYKTGDLARYKD 1498
Cdd:PRK12582 402 rvgliglplPGVELKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDE--------------EGFYRLGDAARFVD 464
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
41-200 |
6.27e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 64.05 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 41 FAEQVL--AQPNAPAICAW--DG---EMSYSVLDGLSTKLAGYLVKIGVKPGDVV----PLCFEksmwTVVAMLAVLKAG 109
Cdd:PRK03584 88 YAENLLrhRRDDRPAIIFRgeDGprrELSWAELRRQVAALAAALRALGVGPGDRVaaylPNIPE----TVVAMLATASLG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 110 ----------GA------FAPLDP--------------DHPVS-RHKEILRQ--TGARMVVVSAQHSARWASSSCHVVTL 156
Cdd:PRK03584 164 aiwsscspdfGVqgvldrFGQIEPkvliavdgyryggkAFDRRaKVAELRAAlpSLEHVVVVPYLGPAAAAAALPGALLW 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 157 SEASIgqlTVEDDLPGFSATPGNA-AYVLFTSGSTGIPK-------GVVLEH 200
Cdd:PRK03584 244 EDFLA---PAEAAELEFEPVPFDHpLWILYSSGTTGLPKcivhghgGILLEH 292
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1109-1569 |
1.26e-09 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 62.85 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1109 PPAiERCIHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPL-CFEK----SMWTVVAMLA 1183
Cdd:PRK06155 17 PPS-ERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALmCGNRieflDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1184 VLKAGGAFLLLDPSLPH----ERLRLMCrkVSAKLSLASEASAPLAKDLVgTVVIVNADSALQLAH-----------HAS 1248
Cdd:PRK06155 96 AIAVPINTALRGPQLEHilrnSGARLLV--VEAALLAALEAADPGDLPLP-AVWLLDAPASVSVPAgwstaplppldAPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1249 PITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQAS----TRTLQFASYAFAgSLVELLMNlchgGC 1324
Cdd:PRK06155 173 PAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADdvlyTTLPLFHTNALN-AFFQALLA----GA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1325 ICVLSEEERRTDLASAMCRMKVNWAFLTSTVVDLL--TPKSVPS----LSILCVGGEPIRASQIVRWGSQVHLRQTYGSS 1398
Cdd:PRK06155 248 TYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILlsQPARESDrahrVRVALGPGVPAALHAAFRERFGVDLLDGYGST 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1399 EVSGIVSsaalTTCSTTR--DVGRASTGV-FWIVDpnNHNRLAPVGAVGEVLVEGpvlgreyiDEPDKTASTFIEAP--- 1472
Cdd:PRK06155 328 ETNFVIA----VTHGSQRpgSMGRLAPGFeARVVD--EHDQELPDGEPGELLLRA--------DEPFAFATGYFGMPekt 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1473 --AWRaslglsagqQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVELIQPKDGED 1550
Cdd:PRK06155 394 veAWR---------NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVE-QVLLSHPAVAAAAVFPVPSELGED 463
|
490
....*....|....*....
gi 1779949166 1551 GMLACFIVVEDSASNEDEL 1569
Cdd:PRK06155 464 EVMAAVVLRDGTALEPVAL 482
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1140-1525 |
1.27e-09 |
|
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: 62.62 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1140 MTYGELDVLSGRLAGHLVELGVGPEDIVPLcFEKSMWT-VVAMLAVLKAGgaFLLldpslpherlrlmcrkVSAKLSLAS 1218
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAI-FAETRAEwLITALGCWSQN--IPI----------------VTVYATLGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1219 EAsapLAKDLVGTVVivnadSALqlahhaspITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHG--------- 1289
Cdd:cd17639 67 DA---LIHSLNETEC-----SAI--------FTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGdrvpellgp 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1290 --RYLG-------MQ----------------ASTRTLQFASYAFA-GSLVEL---LMnlchggcICV--LSEEERRTDLA 1338
Cdd:cd17639 131 ddRYLAylplahiFElaaenvclyrggtigyGSPRTLTDKSKRGCkGDLTEFkptLM-------VGVpaIWDTIRKGVLA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1339 -----SAMCR--------MKVNW--AFLTSTVVDLLTPKSVPS-----LSILCVGGEPIRAS-QivRWGSQVHLR--QTY 1395
Cdd:cd17639 204 klnpmGGLKRtlfwtayqSKLKAlkEGPGTPLLDELVFKKVRAalggrLRYMLSGGAPLSADtQ--EFLNIVLCPviQGY 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1396 GSSEVSG---IVSSAALTTCSttrdVGRASTGV-FWIVD--------PNNHNRlapvgavGEVLVEGPVLGREYIDEPDK 1463
Cdd:cd17639 282 GLTETCAggtVQDPGDLETGR----VGPPLPCCeIKLVDweeggystDKPPPR-------GEILIRGPNVFKGYYKNPEK 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 1464 TASTFIEapawraslglsagqQRLYKTGDLARYKDDGSIELIGRKDNQVKLR-GQRIEVEEIE 1525
Cdd:cd17639 351 TKEAFDG--------------DGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLE 399
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
183-467 |
1.37e-09 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 61.55 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 183 VLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQ----FTSYTFDFCMAeiitTLLYGG-CICVPsdRDRHS 257
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNsgplFHIGTLMFTLA----TFHAGGtNVFVR--RVDAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 258 DLAKAINTMGANWALLT-PSVAQL--LNPSDVPTLKILViggEQVTSKDWN--------RWPTSVqliNGYGPTECcivc 326
Cdd:cd17636 79 EVLELIEAERCTHAFLLpPTIDQIveLNADGLYDLSSLR---SSPAAPEWNdmatvdtsPWGRKP---GGYGQTEV---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 327 TGYTTTQAFKTGTIGTAIASVSWV----VDPEDyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFiedpawlvdgcq 402
Cdd:cd17636 149 MGLATFAALGGGAIGGAGRPSPLVqvriLDEDG--REVPDGEVGEIVARGPTVMAGYWNRPEVNARRT------------ 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1779949166 403 gyagrRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEhhiqGCMPEANQIA-VEVI 467
Cdd:cd17636 215 -----RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVE----RCLRQHPAVAdAAVI 271
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
183-545 |
2.75e-09 |
|
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: 60.75 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 183 VLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQ----FtsYTFDFCMAeiITTLLYGGCICVPS--DRDRH 256
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNmlplF--HIAGLNLA--LATFHAGGANVVMEkfDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 257 SDL--AKAINTMGAnwalLTPSVAQLL-----NPSDVPTLKIlVIGGEqvTSKDWNRWP--TSVQLINGYGPTECcivcT 327
Cdd:cd17637 81 LELieEEKVTLMGS----FPPILSNLLdaaekSGVDLSSLRH-VLGLD--APETIQRFEetTGATFWSLYGQTET----S 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 328 GYTTTQAF--KTGTIGTAIASVSW-VVDpeDYHKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFiedpawlvdgcqgy 404
Cdd:cd17637 150 GLVTLSPYreRPGSAGRPGPLVRVrIVD--DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 405 agrRGRLYKTGDLVRYDDEGNLVCLGRKDSQ--VKVRGQRVELGEIEHHI--QGCMPEANQIAVEvillegeksntilaa 480
Cdd:cd17637 214 ---RNGWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVIleHPAIAEVCVIGVP--------------- 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1779949166 481 flqlDVKTGRAFptnKAAETGSLAQVIFPVEAGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDR 545
Cdd:cd17637 276 ----DPKWGEGI---KAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1163-1531 |
2.87e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 61.67 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1163 PEDIVPLCFEKSMWTVVAMLAVLKAGG-AFLLLDPSLP-H-ERLRLMCRKVSAKLSLASEASAPLAKDLVGT-------- 1231
Cdd:PRK07769 78 PGDRVAILAPQNLDYLIAFFGALYAGRiAVPLFDPAEPgHvGRLHAVLDDCTPSAILTTTDSAEGVRKFFRArpakerpr 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1232 VVIVNA--DSALQlahhaspiTSVRPTHT----AYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFAS 1305
Cdd:PRK07769 158 VIAVDAvpDEVGA--------TWVPPEANedtiAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1306 -YAFAGSLVELLMNLChGGCICVLS-------------EEERRTDLASAMCRMKVNWAFLTSTVVDLltPKS-VPSLSIL 1370
Cdd:PRK07769 230 fFHDMGLITVLLPALL-GHYITFMSpaafvrrpgrwirELARKPGGTGGTFSAAPNFAFEHAAARGL--PKDgEPPLDLS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1371 CV-----GGEPIRASQIVRWG---SQVHLRQT-----YGSSE----VSGIVSSAALTTCSTTRD---------------- 1417
Cdd:PRK07769 307 NVkgllnGSEPVSPASMRKFNeafAPYGLPPTaikpsYGMAEatlfVSTTPMDEEPTVIYVDRDelnagrfvevpadapn 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1418 -VGRASTGVF----W--IVDPNNHNRLaPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEAPAWRASLGLSAG---QQRL 1487
Cdd:PRK07769 387 aVAQVSAGKVgvseWavIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILKSRLSESHAEGapdDALW 465
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1779949166 1488 YKTGDLARYKdDGSIELIGRKDNQVKLRGQRIEVEEIEHQARLA 1531
Cdd:PRK07769 466 VRTGDYGVYF-DGELYITGRVKDLVIIDGRNHYPQDLEYTAQEA 508
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1109-1273 |
3.74e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 61.43 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1109 PPAIERCIHDLFADQAKARPDAPAICAWDGD-----MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLA 1183
Cdd:PRK08180 34 LGDYPRRLTDRLVHWAQEAPDRVFLAERGADggwrrLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1184 VLKAGGAFLLLDP-----SLPHERLRLMCRKVSAKLSLASE----ASAPLAKDLVGTVVIVNADS--------------- 1239
Cdd:PRK08180 114 AMYAGVPYAPVSPayslvSQDFGKLRHVLELLTPGLVFADDgaafARALAAVVPADVEVVAVRGAvpgraatpfaallat 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 1779949166 1240 ----ALQLAHHAspitsVRPTHTAYVIFTSGSTGEPKG 1273
Cdd:PRK08180 194 pptaAVDAAHAA-----VGPDTIAKFLFTSGSTGLPKA 226
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1124-1540 |
4.62e-09 |
|
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: 60.97 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPAIcAWDGD------MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPS 1197
Cdd:cd05970 27 AKEYPDKLAL-VWCDDageeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1198 LPHERLRLMCRKVSAKLSLA--------------SEASAPLAKDLVGTVVIVNADSALQLAHHASPITSvRPTHTAY--- 1260
Cdd:cd05970 106 LTAKDIVYRIESADIKMIVAiaednipeeiekaaPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDFE-RPTANSYpcg 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1261 -----VIFTSGSTGEPKgcRIEHRAA---SSAVTAHgRYLGMQASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEE 1332
Cdd:cd05970 185 edillVYFSSGTTGMPK--MVEHDFTyplGHIVTAK-YWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1333 RRTDLA----------SAMCRMKVNWAFLtstVVDLLTPKSVPSLSILCVGGEPIRASQIVRW--GSQVHLRQTYGSSEV 1400
Cdd:cd05970 262 KFDPKAlleklskygvTTFCAPPTIYRFL---IREDLSRYDLSSLRYCTTAGEALNPEVFNTFkeKTGIKLMEGFGQTET 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1401 sgiVSSAALTTCSTTR--DVGRASTGvfWIVDPNNHN-RLAPVGAVGEVLV---EGPVLG--REYIDEPDKTASTFIEAp 1472
Cdd:cd05970 339 ---TLTIATFPWMEPKpgSMGKPAPG--YEIDLIDREgRSCEAGEEGEIVIrtsKGKPVGlfGGYYKDAEKTAEVWHDG- 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 1473 awraslglsagqqrLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAV 1540
Cdd:cd05970 413 --------------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVE-SALIQHPAVLECAV 465
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1172-1540 |
9.29e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 60.08 E-value: 9.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1172 EKSMWTVVAMLAvlkaGGAFLLLDPSLPHERLRLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSAL---QLAHHAS 1248
Cdd:PRK07867 66 EFSLLLGAAALS----GIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAwadELAAHRD 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1249 ---PITSVRPTHTAYVIFTSGSTGEPKGCRIEH-RAASSAVTAHGR---------YLGMQAstrtlqFASYA-FAGSLVE 1314
Cdd:PRK07867 142 aepPFRVADPDDLFMLIFTSGTSGDPKAVRCTHrKVASAGVMLAQRfglgpddvcYVSMPL------FHSNAvMAGWAVA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1315 llmnLCHGGCICVlseeeRRTDLASAMC----RMKVNWA-FLTSTVVDLLTPKSVP-----SLSIlcVGGEPIRASQIVR 1384
Cdd:PRK07867 216 ----LAAGASIAL-----RRKFSASGFLpdvrRYGATYAnYVGKPLSYVLATPERPddadnPLRI--VYGNEGAPGDIAR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1385 WGSQ--VHLRQTYGSSEvSGIVSSAALTTCSTTrdVGRASTGVFwIVDP-----------NNHNRLAPVGAVGE-VLVEG 1450
Cdd:PRK07867 285 FARRfgCVVVDGFGSTE-GGVAITRTPDTPPGA--LGPLPPGVA-IVDPdtgtecppaedADGRLLNADEAIGElVNTAG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1451 PVLGREYIDEPdktastfiEAPAWRASLGlsagqqrLYKTGDLArYKD-DGSIELIGRKDNQVKLRGQRIEVEEIEHqAR 1529
Cdd:PRK07867 361 PGGFEGYYNDP--------EADAERMRGG-------VYWSGDLA-YRDaDGYAYFAGRLGDWMRVDGENLGTAPIER-IL 423
|
410
....*....|.
gi 1779949166 1530 LAEADVAEIAV 1540
Cdd:PRK07867 424 LRYPDATEVAV 434
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
710-1008 |
1.07e-08 |
|
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: 59.59 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 710 YIMQSVLALHDDTDEDRFRAAWERVVQSTAVLRTriVHSSKMGM-LQVVLADG---IEWEQ----ANELEQYLEKDKSVS 781
Cdd:cd19538 24 YNIPLVIKLKGKLDVQALQQALYDVVERHESLRT--VFPEEDGVpYQLILEEDeatPKLEIkevdEEELESEINEAVRYP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 782 MGLGDSLARYALVRDVGTGKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPGFNAF-IKY----------LGEQ 850
Cdd:cd19538 102 FDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLpVQYadyalwqqelLGDE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 851 DHEAAA-----AYWQGTLADcqaisFPA---LPPAVQQPVADATTA----FQCPA--------LARRpSDITMSTLIRAA 910
Cdd:cd19538 182 SDPDSLiarqlAYWKKQLAG-----LPDeieLPTDYPRPAESSYEGgtltFEIDSelhqqllqLAKD-NNVTLFMVLQAG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 911 WALLASSYTSSDDVVFGATVTGRNApvAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATEM-----IPYEQtgL 985
Cdd:cd19538 256 FAALLTRLGAGTDIPIGSPVAGRND--DSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAyehqdIPFER--L 331
|
330 340
....*....|....*....|....
gi 1779949166 986 HETAK-VSADARHACsFQTLLIVQ 1008
Cdd:cd19538 332 VEALNpTRSRSRHPL-FQIMLALQ 354
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1140-1325 |
1.10e-08 |
|
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: 59.29 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1140 MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKlslase 1219
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAK------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1220 asaplakdlvgtVVIVNadsalqlahhaspitsvrpthTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTR 1299
Cdd:cd05940 78 ------------HLVVD---------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDV 124
|
170 180
....*....|....*....|....*....
gi 1779949166 1300 ---TLQFasYAFAGSLVELLMNLCHGGCI 1325
Cdd:cd05940 125 lytCLPL--YHSTALIVGWSACLASGATL 151
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
73-422 |
1.32e-08 |
|
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: 59.37 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 73 LAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDP-------DHPVSRHKEILRQTGARMVVVSAQHSAR 145
Cdd:cd05921 38 IAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPayslmsqDLAKLKHLFELLKPGLVFAQDAAPFARA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 146 WAS-----SSCHVVTLSEASIGQLTVEDDL---------PGFSA-TPGNAAYVLFTSGSTGIPKGVVLEHR--AVSTSCL 208
Cdd:cd05921 118 LAAifplgTPLVVSRNAVAGRGAISFAELAatpptaavdAAFAAvGPDTVAKFLFTSGSTGLPKAVINTQRmlCANQAML 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 209 GHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGCICVPSD------------RDRHSDLAKAINTMGANWALLTPS 276
Cdd:cd05921 198 EQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDDgkpmpggfeetlRNLREISPTVYFNVPAGWEMLVAA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 277 VA--QLLNPSDVPTLKILVIGGEQVTSKDWNRWPT-SVQ-------LINGYGPTECCIVCTGyTTTQAFKTGTIGTAIAS 346
Cdd:cd05921 278 LEkdEALRRRFFKRLKLMFYAGAGLSQDVWDRLQAlAVAtvgeripMMAGLGATETAPTATF-THWPTERSGLIGLPAPG 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1779949166 347 VSWvvdpedyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpawlvdgcqGYagrrgrlYKTGDLVRYDD 422
Cdd:cd05921 357 TEL--------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEE---------GF-------YCLGDAAKLAD 408
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1140-1546 |
1.84e-08 |
|
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: 58.73 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1140 MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGG----AFLLLDPSLPHERLRlMCRKVSAKLS 1215
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAvvipATTLLTPDDLRDRVD-RGGAVYAAVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1216 LASEASAPLakdlvgtvvivnadsalqlahhaspitsvrpthtaYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQ 1295
Cdd:cd05974 80 ENTHADDPM-----------------------------------LLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1296 ASTRTLQFASYAFAGSLVELLMNLCHGGCICVLSEEER--RTDLASAMCRMKVNWAFLTSTVVDLLTPKSVPSLSI---- 1369
Cdd:cd05974 125 PGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARfdAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVklre 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1370 LCVGGEPIRASQIVR----WGsqVHLRQTYGSSEVSGIVSSAALTTCSTTrDVGRASTGVfwivdpnnhnRLAPVGAVGE 1445
Cdd:cd05974 205 VVGAGEPLNPEVIEQvrraWG--LTIRDGYGQTETTALVGNSPGQPVKAG-SMGRPLPGY----------RVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1446 VLVEGPV-----------LGREYIDEPDKTASTFIEApawraslglsagqqrLYKTGDLARYKDDGSIELIGRKDNQVKL 1514
Cdd:cd05974 272 PATEGEValdlgdtrpvgLMKGYAGDPDKTAHAMRGG---------------YYRTGDIAMRDEDGYLTYVGRADDVFKS 336
|
410 420 430
....*....|....*....|....*....|....*....
gi 1779949166 1515 RGQRI---EVEE--IEHQArLAEADV--AEIAVELIQPK 1546
Cdd:cd05974 337 SDYRIspfELESvlIEHPA-VAEAAVvpSPDPVRLSVPK 374
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
63-212 |
2.99e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 58.48 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 63 YSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPdhPVSR-HKEILRQTGARMVVvSAQ 141
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPL--PMGFgGRESYIAQLRGMLA-SAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 142 HSA--------RWASSSCH----VVTLSEASIGQLTVED-DLPgfSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCL 208
Cdd:PRK09192 129 PAAiitpdellPWVNEATHgnplLHVLSHAWFKALPEADvALP--RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLR 206
|
....
gi 1779949166 209 GHGR 212
Cdd:PRK09192 207 AISH 210
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1141-1569 |
3.14e-08 |
|
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: 58.13 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVE-LGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLASE 1219
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTVE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1220 ASAPLAKDLVGTVV--------------IVNADSALQLAHHASPITS---VRPTHTAYVIFTSGSTGEPKGCRIEHRAAS 1282
Cdd:cd05905 96 ACLKGLPKKLLKSKtaaeiakkkgwpkiLDFVKIPKSKRSKLKKWGPhppTRDGDTAYIEYSFSSDGSLSGVAVSHSSLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1283 SAVTAHGRYLGMQAStRTL--QFASYAFAGSLVELLMNLCHGGCICVLSEEERRTDLAS---AMCRMKVNWAFLTSTVVD 1357
Cdd:cd05905 176 AHCRALKEACELYES-RPLvtVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLwlqTLSQYKVRDAYVKLRTLH 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1358 LLT----------PKSVPSLS----ILCVGGEPIRASQIVRWGS--QVH-LRQTYGSSEVSGIVSSA-----ALTTCSTT 1415
Cdd:cd05905 255 WCLkdlsstlaslKNRDVNLSslrmCMVPCENRPRISSCDSFLKlfQTLgLSPRAVSTEFGTRVNPFicwqgTSGPEPSR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1416 -----------------RDVGRA-----STGVF-----WIVDPNNHNrLAPVGAVGEVLVEGPVLGREYIDEPDKTASTF 1468
Cdd:cd05905 335 vyldmralrhgvvrldeRDKPNSlplqdSGKVLpgaqvAIVNPETKG-LCKDGEIGEIWVNSPANASGYFLLDGETNDTF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1469 IEAPAWRASLGlsAGQQRLYKTGDL----------ARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQARLAEADVAEI 1538
Cdd:cd05905 414 KVFPSTRLSTG--ITNNSYARTGLLgflrptkctdLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHPYRGRC 491
|
490 500 510
....*....|....*....|....*....|....*
gi 1779949166 1539 AV----ELIqpkdgedgmlacFIVVEDSASNEDEL 1569
Cdd:cd05905 492 AVfsitGLV------------VVVAEQPPGSEEEA 514
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
61-550 |
4.05e-08 |
|
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: 57.58 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 61 MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAP----LDPDHPVSRhkeILRQTGARMV 136
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDR---VDRGGAVYAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 137 VVSAQHSarwassschvvtlseasigqltvEDDLpgfsatpgnaaYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGI 216
Cdd:cd05974 78 VDENTHA-----------------------DDPM-----------LLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 217 TDQSRVLQFTSYTF-DFCMAEIITTLLYGGCICVPSD-RDRHSDLAKAINTMGANWALLTPSVAQLLNPSDVPTLKI--- 291
Cdd:cd05974 124 KPGDVHWNISSPGWaKHAWSCFFAPWNAGATVFLFNYaRFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVklr 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 292 -LVIGGE-------QVTSKDWNRwptsvQLINGYGPTECCiVCTGYTTTQAFKTGTIGTaiasvswvvdPEDYHKLAPLG 363
Cdd:cd05974 204 eVVGAGEplnpeviEQVRRAWGL-----TIRDGYGQTETT-ALVGNSPGQPVKAGSMGR----------PLPGYRVALLD 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 364 SVGELLVEGPI-----------LARGYLNDAEKTAAAFiedpawlvdgcqgyagrRGRLYKTGDLVRYDDEGNLVCLGRK 432
Cdd:cd05974 268 PDGAPATEGEValdlgdtrpvgLMKGYAGDPDKTAHAM-----------------RGGYYRTGDIAMRDEDGYLTYVGRA 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 433 DSQVKVRGQRVELGEIEhhiqGCMPEANQIAVEVILLEGEKsntilaafLQLDVKTGRAFPTNKAAETGSLAQVIFpvea 512
Cdd:cd05974 331 DDVFKSSDYRISPFELE----SVLIEHPAVAEAAVVPSPDP--------VRLSVPKAFIVLRAGYEPSPETALEIF---- 394
|
490 500 510
....*....|....*....|....*....|....*....
gi 1779949166 513 gKKLAERLPSYM-VPDVYFVvtQLPITVSGKTDRKRLRE 550
Cdd:cd05974 395 -RFSRERLAPYKrIRRLEFA--ELPKTISGKIRRVELRR 430
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
168-464 |
4.71e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 57.77 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 168 DDLPGFS-ATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGIT-DQSRVLQFTSYTFDFCMAEIITTLLYGG 245
Cdd:PRK07867 141 DAEPPFRvADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGpDDVCYVSMPLFHSNAVMAGWAVALAAGA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 246 CICVPSdRDRHSDLAKAINTMGANWA----------LLTPSVaqllnPSDVP-TLKILVigGEQVTSKDWNRWPT--SVQ 312
Cdd:PRK07867 221 SIALRR-KFSASGFLPDVRRYGATYAnyvgkplsyvLATPER-----PDDADnPLRIVY--GNEGAPGDIARFARrfGCV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 313 LINGYGPTECCIvctGYTTTQAFKTGTIGTAIASVSwVVDPE-----------DYHKLAPLGSVGELL-VEGPILARGYL 380
Cdd:PRK07867 293 VVDGFGSTEGGV---AITRTPDTPPGALGPLPPGVA-IVDPDtgtecppaedaDGRLLNADEAIGELVnTAGPGGFEGYY 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 381 NDAEKTAAAfiedpawlvdgcqgyagRRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEAN 460
Cdd:PRK07867 369 NDPEADAER-----------------MRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLR-YPDAT 430
|
....
gi 1779949166 461 QIAV 464
Cdd:PRK07867 431 EVAV 434
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
61-550 |
4.95e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 57.40 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 61 MSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAgGAFAPldpdhPVSRHKE------ILRQTGAR 134
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRL-GAYAV-----PVNWHFKpeeiayILEDSGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 135 MVVVSAQ--HSARWA-SSSCHVVT------------LSEASI----GQLTVEDDLPGFSATPG----NAAYVLFTSGSTG 191
Cdd:PRK12406 86 VLIAHADllHGLASAlPAGVTVLSvptppeiaaayrISPALLtppaGAIDWEGWLAQQEPYDGppvpQPQSMIYTSGTTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 192 IPKGV-----VLEHRAVSTSCLghGRAFGITDQSRVLqftsytfdfcmaeiITTLLY--------------GGCICVPSD 252
Cdd:PRK12406 166 HPKGVrraapTPEQAAAAEQMR--ALIYGLKPGIRAL--------------LTGPLYhsapnayglragrlGGVLVLQPR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 253 RD---------RHS-DLAKAINTMGANWALLTPSVAqllNPSDVPTLKILVIGGEQVtskdwnrwPTSV--QLINGYGP- 319
Cdd:PRK12406 230 FDpeellqlieRHRiTHMHMVPTMFIRLLKLPEEVR---AKYDVSSLRHVIHAAAPC--------PADVkrAMIEWWGPv 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 320 -------TECCIVcTGYTTTQAF-KTGTIGTAIASVSWVVDPEDYHKLaPLGSVGELLVEGPILAR-GYLNDAEKTAAAf 390
Cdd:PRK12406 299 iyeyygsTESGAV-TFATSEDALsHPGTVGKAAPGAELRFVDEDGRPL-PQGEIGEIYSRIAGNPDfTYHNKPEKRAEI- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 391 iedpawlvdgcqgyagRRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcMPEANQIAVEVILLE 470
Cdd:PRK12406 376 ----------------DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHA-VPGVHDCAVFGIPDA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 471 --GEksntILAAFLQLDvktgrafptnkAAETGSLAQVifpveaGKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRL 548
Cdd:PRK12406 439 efGE----ALMAVVEPQ-----------PGATLDEADI------RAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
..
gi 1779949166 549 RE 550
Cdd:PRK12406 498 RD 499
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1125-1559 |
5.10e-08 |
|
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: 57.71 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1125 KARPDAPAIcAWDGDM-------TYGELDVLSGRLAGHLVELGVGPEDIV----PLCFEksmwTVVAMLAVLKAG----- 1188
Cdd:cd05967 62 AGRGDQIAL-IYDSPVtgtertyTYAELLDEVSRLAGVLRKLGVVKGDRViiymPMIPE----AAIAMLACARIGaihsv 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1189 --GAF---------------LLLDPSLPHERLRLMCRK--VSAKLSLASEASA-------PLAKdLVGTVVIVNADSALQ 1242
Cdd:cd05967 137 vfGGFaakelasriddakpkLIVTASCGIEPGKVVPYKplLDKALELSGHKPHhvlvlnrPQVP-ADLTKPGRDLDWSEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1243 LAHHAS-PITSVRPTHTAYVIFTSGSTGEPKGcriehraassAVTAHGRYLGM-QASTRTL---QFASYAFAGSLVELLM 1317
Cdd:cd05967 216 LAKAEPvDCVPVAATDPLYILYTSGTTGKPKG----------VVRDNGGHAVAlNWSMRNIygiKPGDVWWAASDVGWVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1318 N--------LCHGgCICVLSE-EERRTDLASAMCRM----KVNWAFLTSTVV----------DLLTPKSVPSLSILCVGG 1374
Cdd:cd05967 286 GhsyivygpLLHG-ATTVLYEgKPVGTPDPGAFWRViekyQVNALFTAPTAIrairkedpdgKYIKKYDLSSLRTLFLAG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1375 EPIRASQiVRWGSQV-------HLRQTYGSSEVSGIVssaaltTCSTTRDVGRASTGV------FWIVDPNNHNrlAPVG 1441
Cdd:cd05967 365 ERLDPPT-LEWAENTlgvpvidHWWQTETGWPITANP------VGLEPLPIKAGSPGKpvpgyqVQVLDEDGEP--VGPN 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1442 AVGEVLVEGPVlgreyidePDKTASTFieapaWR-------ASLGLSAGqqrLYKTGDLARYKDDGSIELIGRKDNQVKL 1514
Cdd:cd05967 436 ELGNIVIKLPL--------PPGCLLTL-----WKnderfkkLYLSKFPG---YYDTGDAGYKDEDGYLFIMGRTDDVINV 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1779949166 1515 RGQRIEVEEIEhQARLAEADVAEIAVelIQPKDGEDGMLACFIVV 1559
Cdd:cd05967 500 AGHRLSTGEME-ESVLSHPAVAECAV--VGVRDELKGQVPLGLVV 541
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-549 |
1.23e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 55.56 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 177 PGNAAYVLFTSGSTGIPKgvVLEHR----AVSTSCLGHGRAFGITDqsrVLQFTSYTFDF--CMAEIITTLLYGGCICVP 250
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPK--LAQHThsneVYNAWMLALNSLFDPDD---VLLCGLPLFHVngSVVTLLTPLASGAHVVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 251 S-----DRDRHSDLAKAINTMGANWALLTPSV----AQLLNPSDVPTLKILVIGGEQVTSKDWNRWP--TSVQLINGYGP 319
Cdd:cd05944 76 GpagyrNPGLFDNFWKLVERYRITSLSTVPTVyaalLQVPVNADISSLRFAMSGAAPLPVELRARFEdaTGLPVVEGYGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 320 TEC-CIVCTGYTTTqAFKTGTIGTAI--ASVSWVVDPEDYHKLAPLG--SVGELLVEGPILARGYLNDaEKTAAAFIEDp 394
Cdd:cd05944 156 TEAtCLVAVNPPDG-PKRPGSVGLRLpyARVRIKVLDGVGRLLRDCApdEVGEICVAGPGVFGGYLYT-EGNKNAFVAD- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 395 AWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGR-KDsqVKVRGQrvelgeieHHIQGCMPEAnqiaveviLLEGEK 473
Cdd:cd05944 233 GWL---------------NTGDLGRLDADGYLFITGRaKD--LIIRGG--------HNIDPALIEE--------ALLRHP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 474 SNTILAAFLQLDVKTGR---AF----PTNKAAETGSLAQvifpveAGKKLAERLPsymVPDVYFVVTQLPITVSGKTDRK 546
Cdd:cd05944 280 AVAFAGAVGQPDAHAGElpvAYvqlkPGAVVEEEELLAW------ARDHVPERAA---VPKHIEVLEELPVTAVGKVFKP 350
|
...
gi 1779949166 547 RLR 549
Cdd:cd05944 351 ALR 353
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1258-1559 |
1.35e-07 |
|
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: 55.20 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1258 TAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQ----FASYAF-AGSLVELL-------MNLCHGGCI 1325
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIinpfFHTFGYkAGIVACLLtgatvvpVAVFDVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1326 CVLSEEERRTDLASAMCrmkvnwAFLTSTVVDLLTPKSVPSLSILCVGGEPIRASQIVRWGSQVHLRQT---YGSSEvSG 1402
Cdd:cd17638 82 LEAIERERITVLPGPPT------LFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVltaYGLTE-AG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1403 IVS----SAALTTCSTTrdVGRASTGV-FWIVDPnnhnrlapvgavGEVLVEGPVLGREYIDEPDKTASTfIEAPAWras 1477
Cdd:cd17638 155 VATmcrpGDDAETVATT--CGRACPGFeVRIADD------------GEVLVRGYNVMQGYLDDPEATAEA-IDADGW--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1478 lglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQarLAEAD-VAEIAVelIQPKDGEDGMLACF 1556
Cdd:cd17638 217 ----------LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGA--LAEHPgVAQVAV--IGVPDERMGEVGKA 282
|
...
gi 1779949166 1557 IVV 1559
Cdd:cd17638 283 FVV 285
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-556 |
1.84e-07 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 56.03 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 31 GVTNKCiHDLFAEQVLAQPNAPAIcAWDGEM-------SYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAML 103
Cdd:cd05966 50 GKLNIS-YNCLDRHLKERGDKVAI-IWEGDEpdqsrtiTYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAML 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 104 AVLKAG-------GAFAPldpdhpvsrhkEILRQ----TGARmVVVSAQHSARW------------ASSSC----HVVTL 156
Cdd:cd05966 128 ACARIGavhsvvfAGFSA-----------ESLADrindAQCK-LVITADGGYRGgkviplkeivdeALEKCpsveKVLVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 157 SEASIGQLTVED-DLPGFSATPGNAAY-------------VLFTSGSTGIPKGVVleHravSTSclghGRAFGitdqsrV 222
Cdd:cd05966 196 KRTGGEVPMTEGrDLWWHDLMAKQSPEcepewmdsedplfILYTSGSTGKPKGVV--H---TTG----GYLLY------A 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 223 LQFTSYTFD-------FCMAEI-----------------ITTLLYGGcicVPS--DRDRHSDLAK------------AIN 264
Cdd:cd05966 261 ATTFKYVFDyhpddiyWCTADIgwitghsyivygplangATTVMFEG---TPTypDPGRYWDIVEkhkvtifytaptAIR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 265 T---MGANWalltpsvaqlLNPSDVPTLKILVIGGEQVTSKDWnRWPTSVqlingYGPTECCIVCTGYTTtqafKTGTI- 340
Cdd:cd05966 338 AlmkFGDEW----------VKKHDLSSLRVLGSVGEPINPEAW-MWYYEV-----IGKERCPIVDTWWQT----ETGGIm 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 341 ------------GTA------IASVswVVDPEDYHklAPLGSVGELLVEG--PILARGYLNDAEKtaaaFIedpawlvdg 400
Cdd:cd05966 398 itplpgatplkpGSAtrpffgIEPA--ILDEEGNE--VEGEVEGYLVIKRpwPGMARTIYGDHER----YE--------- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 401 cQGYAGRRGRLYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIE------------------HHIQGcmpeaNQI 462
Cdd:cd05966 461 -DTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVEsalvahpavaeaavvgrpHDIKG-----EAI 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 463 AVEVILLEGEKSNTILAAFLQLDVktgrafptnkAAETGSLAqvifpveagkklaerlpsymVPDVYFVVTQLPITVSGK 542
Cdd:cd05966 535 YAFVTLKDGEEPSDELRKELRKHV----------RKEIGPIA--------------------TPDKIQFVPGLPKTRSGK 584
|
650
....*....|....
gi 1779949166 543 TDRKRLREIGASFS 556
Cdd:cd05966 585 IMRRILRKIAAGEE 598
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1395-1540 |
2.00e-07 |
|
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: 54.97 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1395 YGSSEVSGIVSSAALTTCSTTrdVGRASTGV-FWIVDPNNhnRLAPVGAVGEVLVEGPVLGREYIDEPDKTASTFIEapA 1473
Cdd:cd17637 143 YGQTETSGLVTLSPYRERPGS--AGRPGPLVrVRIVDDND--RPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRN--G 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 1474 WraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQ--VKLRGQRIEVEEIEhQARLAEADVAEIAV 1540
Cdd:cd17637 217 W-------------HHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVE-KVILEHPAIAEVCV 271
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1140-1579 |
2.86e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 55.09 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1140 MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSLA-S 1218
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1219 EASAPLAKDLVGTVVIVNADSALQL-------AHHAS----------------PITSVRPTHTAYVIFTSGSTGEPKGCR 1275
Cdd:PRK12406 92 DLLHGLASALPAGVTVLSVPTPPEIaaayrisPALLTppagaidwegwlaqqePYDGPPVPQPQSMIYTSGTTGHPKGVR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1276 iehRA------ASSAVTAHGRYLGMQASTRTL------QFASYAFAgslvelLMNLCHGGCIcVLSEEERRTDLASAMCR 1343
Cdd:PRK12406 172 ---RAaptpeqAAAAEQMRALIYGLKPGIRALltgplyHSAPNAYG------LRAGRLGGVL-VLQPRFDPEELLQLIER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1344 MKVNWAFLTSTV-VDLLT-PKSV------PSLSILCVGGEP----IRASQIVRWGSQVHlrQTYGSSEVSGIV---SSAA 1408
Cdd:PRK12406 242 HRITHMHMVPTMfIRLLKlPEEVrakydvSSLRHVIHAAAPcpadVKRAMIEWWGPVIY--EYYGSTESGAVTfatSEDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1409 LTTCSTtrdVGRASTGV-FWIVDPNNHNrlAPVGAVGEVLVEGPVLgreyidePDktaSTFIEAPAWRASLglsaGQQRL 1487
Cdd:PRK12406 320 LSHPGT---VGKAAPGAeLRFVDEDGRP--LPQGEIGEIYSRIAGN-------PD---FTYHNKPEKRAEI----DRGGF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1488 YKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVELIqpKDGEDGMLACfIVVEDSASNED 1567
Cdd:PRK12406 381 ITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIE-AVLHAVPGVHDCAVFGI--PDAEFGEALM-AVVEPQPGATL 456
|
490
....*....|..
gi 1779949166 1568 ELSGKRTRLDTR 1579
Cdd:PRK12406 457 DEADIRAQLKAR 468
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
181-550 |
2.87e-07 |
|
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: 55.19 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 181 AYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGITDQSRVLQFTSYTFDFCMAEIITTLLYGGC----------ICVP 250
Cdd:cd05908 109 AFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMnqylmptrlfIRRP 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 251 SDRDRHSDLAKAINTMGANWA------LLTPSVAqllNPSDVPTLKILVIGGEQVTSKDWNRWPTSVQ--------LING 316
Cdd:cd05908 189 ILWLKKASEHKATIVSSPNFGykyflkTLKPEKA---NDWDLSSIRMILNGAEPIDYELCHEFLDHMSkyglkrnaILPV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 317 YGPTECCIVCTGYTTTQAFKTGTI---------------------------GTAIASVSWVVDPEDYHKLaPLGSVGELL 369
Cdd:cd05908 266 YGLAEASVGASLPKAQSPFKTITLgrrhvthgepepevdkkdsecltfvevGKPIDETDIRICDEDNKIL-PDGYIGHIQ 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 370 VEGPILARGYLNDAEKTAAAFIEDpAWLVDGCQGYAgRRGRLYKTgdlvryddegnlvclGRKDSQVKVRGQRVELGEIE 449
Cdd:cd05908 345 IRGKNVTPGYYNNPEATAKVFTDD-GWLKTGDLGFI-RNGRLVIT---------------GREKDIIFVNGQNVYPHDIE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 450 hhiqgcmpeanQIAVEVILLE-----------GEKSNTILAAFLQLDVKTGRAFPTNKAAETgslaqvIFPVEAGKKLAE 518
Cdd:cd05908 408 -----------RIAEELEGVElgrvvacgvnnSNTRNEEIFCFIEHRKSEDDFYPLGKKIKK------HLNKRGGWQINE 470
|
410 420 430
....*....|....*....|....*....|..
gi 1779949166 519 RLPsymvpdvyfvVTQLPITVSGKTDRKRLRE 550
Cdd:cd05908 471 VLP----------IRRIPKTTSGKVKRYELAQ 492
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1104-1569 |
4.40e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 54.44 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1104 WNHDVPPAIE--------RCIHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVE-LGVGPEDIVPLCFEKS 1174
Cdd:PRK12492 6 WNDKRPAGVPstidlaayKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1175 MWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKL--------SLASEASA----------------PLAKD-LV 1229
Cdd:PRK12492 86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARAlvylnmfgKLVQEVLPdtgieylieakmgdllPAAKGwLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1230 GTVV--------------IVNADSALQLAHhASPITSVRPTH--TAYVIFTSGSTGEPKGCRIEH----------RAASS 1283
Cdd:PRK12492 166 NTVVdkvkkmvpayhlpqAVPFKQALRQGR-GLSLKPVPVGLddIAVLQYTGGTTGLAKGAMLTHgnlvanmlqvRACLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1284 AVTAHGRYLGMQASTRTLQ----FASYAFAGSLVELLMNLCHGgcicVLSEEERrtDLASAMCRMKvNWAF-----LTST 1354
Cdd:PRK12492 245 QLGPDGQPLMKEGQEVMIAplplYHIYAFTANCMCMMVSGNHN----VLITNPR--DIPGFIKELG-KWRFsallgLNTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1355 VVDLLTPKSVPSL--SILCV---GGEPIRASQIVRWGSQVHLR--QTYGSSEVSGIVSSAALTTCSTTRDVGRASTGVFW 1427
Cdd:PRK12492 318 FVALMDHPGFKDLdfSALKLtnsGGTALVKATAERWEQLTGCTivEGYGLTETSPVASTNPYGELARLGTVGIPVPGTAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1428 IVDPNNHNRLaPVGAVGEVLVEGPVLGREYIDEPDKTASTfIEAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGR 1507
Cdd:PRK12492 398 KVIDDDGNEL-PLGERGELCIKGPQVMKGYWQQPEATAEA-LDAEGW-------------FKTGDIAVIDPDGFVRIVDR 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 1508 KDNQVKLRGQRIEVEEIEhQARLAEADVAEIA-VELIQPKDGEDGMLacFIVVEDSASNEDEL 1569
Cdd:PRK12492 463 KKDLIIVSGFNVYPNEIE-DVVMAHPKVANCAaIGVPDERSGEAVKL--FVVARDPGLSVEEL 522
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
49-431 |
4.49e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 54.66 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 49 PNAPAICAWDGEMSYSVLDGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAP----LDPDhpvsrh 124
Cdd:PRK07470 21 PDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPtnfrQTPD------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 125 kEIL---RQTGARMVVVSA---QHSARWASSSC---HVVTLSEASIGqLTVEDDLPGFSATPGNAAYV--------LFTS 187
Cdd:PRK07470 95 -EVAylaEASGARAMICHAdfpEHAAAVRAASPdltHVVAIGGARAG-LDYEALVARHLGARVANAAVdhddpcwfFFTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 188 GSTGIPKGVVLEHravstsclgHGRAFGIT-------------DQSRVLQFTSY---TFDFC-MAEIITTLLyggcicVP 250
Cdd:PRK07470 173 GTTGRPKAAVLTH---------GQMAFVITnhladlmpgtteqDASLVVAPLSHgagIHQLCqVARGAATVL------LP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 251 SDRdrhSDLAKAintmganWALL----------TPSVAQLL--NPS----DVPTLKILVIGGEQVTSKDWNR-----WPT 309
Cdd:PRK07470 238 SER---FDPAEV-------WALVerhrvtnlftVPTILKMLveHPAvdryDHSSLRYVIYAGAPMYRADQKRalaklGKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 310 SVQLingYGPTEccivCTGYTTT-----------QAFKTGTIGTAIASVSWVVDPEDYHKLAPlGSVGELLVEGPILARG 378
Cdd:PRK07470 308 LVQY---FGLGE----VTGNITVlppalhdaedgPDARIGTCGFERTGMEVQIQDDEGRELPP-GETGEICVIGPAVFAG 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 379 YLNDAEKTAAAFiedpawlvdgcqgyagrRGRLYKTGDLVRYDDEGNLVCLGR 431
Cdd:PRK07470 380 YYNNPEANAKAF-----------------RDGWFRTGDLGHLDARGFLYITGR 415
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1097-1570 |
5.35e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 54.27 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1097 DRQQLWEWNHDVPPAIERCIHDL--FADQAKAR-PDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEK 1173
Cdd:PRK06710 4 EKPWLKSYPEEIPSTISYDIQPLhkYVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1174 SMWTVVAMLAVLKAGGAFLLLDPSLPHERLRLMCRKVSAKLSL---------ASEASA---------------PLAKDLV 1229
Cdd:PRK06710 84 CPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvTNVQSAtkiehvivtriadflPFPKNLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1230 -------GTVVIVNADSAlQLAHHASPITSVRPTHT----------AYVIFTSGSTGEPKGCRIEHR--AASSAVTAHGR 1290
Cdd:PRK06710 164 ypfvqkkQSNLVVKVSES-ETIHLWNSVEKEVNTGVevpcdpendlALLQYTGGTTGFPKGVMLTHKnlVSNTLMGVQWL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1291 YLGMQASTRTLQFASYaFAGSLVELLMNLC-HGGCICVLSEEERRTDLASAMCRMKVNW---------AFLTSTvvdLLT 1360
Cdd:PRK06710 243 YNCKEGEEVVLGVLPF-FHVYGMTAVMNLSiMQGYKMVLIPKFDMKMVFEAIKKHKVTLfpgaptiyiALLNSP---LLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1361 PKSVPSLSIlCVGGE---PIRASQIVRWGSQVHLRQTYGSSEVSGIVSSAALTTcstTRDVGraSTGVFWivdPNNHNRL 1437
Cdd:PRK06710 319 EYDISSIRA-CISGSaplPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWE---KRVPG--SIGVPW---PDTEAMI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1438 A--------PVGAVGEVLVEGPVLGREYIDEPDKTASTFieapawraslglsagQQRLYKTGDLARYKDDGSIELIGRKD 1509
Cdd:PRK06710 390 MsletgealPPGEIGEIVVKGPQIMKGYWNKPEETAAVL---------------QDGWLHTGDVGYMDEDGFFYVKDRKK 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1779949166 1510 NQVKLRGQRI---EVEEI--EHQaRLAEAdvaeIAVELIQPKDGEdgMLACFIVV-EDSASNEDELS 1570
Cdd:PRK06710 455 DMIVASGFNVyprEVEEVlyEHE-KVQEV----VTIGVPDPYRGE--TVKAFVVLkEGTECSEEELN 514
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
570-642 |
6.84e-07 |
|
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: 48.79 E-value: 6.84e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 570 LKRQPSTENEKALQQL----WAGVLAI-DADSIGLDDSFFRLGGDSIAAMKLVGEARRA-GIHLTVADLFRNPKLEAVA 642
Cdd:smart00823 1 LAALPPAERRRLLLDLvreqVAAVLGHaAAEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALA 79
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1116-1569 |
7.28e-07 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 53.83 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1116 IHDLFADQAKARPDAPaiCAWDGD----MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAF 1191
Cdd:PLN02246 25 LHDYCFERLSEFSDRP--CLIDGAtgrvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1192 LLLDP-SLPHErLRLMCRKVSAKL----SLASEASAPLAKDLVGTVVIVNAD-------SALQLAHHAS-PITSVRPTHT 1258
Cdd:PLN02246 103 TTANPfYTPAE-IAKQAKASGAKLiitqSCYVDKLKGLAEDDGVTVVTIDDPpegclhfSELTQADENElPEVEISPDDV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1259 AYVIFTSGSTGEPKGCRIEHRAASSAVT----AHGRYLGMQASTRTL----QFASYAFaGSLveLLMNLCHGGCICVLse 1330
Cdd:PLN02246 182 VALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFHSDDVILcvlpMFHIYSL-NSV--LLCGLRVGAAILIM-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1331 eeRRTDLASAM---CRMKVNWAFLTSTVVdLLTPKS-------VPSLSILCVGGEP--------IRASQivrwgSQVHLR 1392
Cdd:PLN02246 257 --PKFEIGALLeliQRHKVTIAPFVPPIV-LAIAKSpvvekydLSSIRMVLSGAAPlgkeledaFRAKL-----PNAVLG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1393 QTYGSSEvSGIVSSAALTTCSTTRDVGRASTGV------FWIVDPNNHNRLaPVGAVGEVLVEGPVLGREYIDEPDKTAS 1466
Cdd:PLN02246 329 QGYGMTE-AGPVLAMCLAFAKEPFPVKSGSCGTvvrnaeLKIVDPETGASL-PRNQPGEICIRGPQIMKGYLNDPEATAN 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1467 TfIEAPAWraslglsagqqrLYkTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhqARL-AEADVAEIAVelIQP 1545
Cdd:PLN02246 407 T-IDKDGW------------LH-TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELE--ALLiSHPSIADAAV--VPM 468
|
490 500
....*....|....*....|....*.
gi 1779949166 1546 KDGEDGMLACFIVV--EDSASNEDEL 1569
Cdd:PLN02246 469 KDEVAGEVPVAFVVrsNGSEITEDEI 494
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1110-1569 |
7.76e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 53.62 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1110 PAIERCIHDLFADQAKARPDAPAICAWDGD--MTYGELDVLSGRLAGHLVELGVGPEDIV----PLCFEksmWTVVAMlA 1183
Cdd:PRK12583 14 PLLTQTIGDAFDATVARFPDREALVVRHQAlrYTWRQLADAVDRLARGLLALGVQPGDRVgiwaPNCAE---WLLTQF-A 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1184 VLKAGGAFLLLDPSLPHERLRLM-----CRKV--------------------SAKLSLASEASAPLAKDLVGTVVIVNAD 1238
Cdd:PRK12583 90 TARIGAILVNINPAYRASELEYAlgqsgVRWVicadafktsdyhamlqellpGLAEGQPGALACERLPELRGVVSLAPAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1239 SALQLAHH--------------ASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTR-TLQF 1303
Cdd:PRK12583 170 PPGFLAWHelqargetvsrealAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRlCVPV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1304 ASYAFAGSLVELLMNLCHGGCICVLS------------EEERRTDLasamcrmkvnWAFLTSTVVDLLTPK----SVPSL 1367
Cdd:PRK12583 250 PLYHCFGMVLANLGCMTVGACLVYPNeafdplatlqavEEERCTAL----------YGVPTMFIAELDHPQrgnfDLSSL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1368 SILCVGGEPIRASQIVRWGSQVHLRQT---YGSSEVSGIV--SSAALTTCSTTRDVGRASTGV-FWIVDPNNHNrlAPVG 1441
Cdd:PRK12583 320 RTGIMAGAPCPIEVMRRVMDEMHMAEVqiaYGMTETSPVSlqTTAADDLERRVETVGRTQPHLeVKVVDPDGAT--VPRG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1442 AVGEVLVEGPVLGREYIDEPDKTASTfIEAPAWraslglsagqqrLYkTGDLARYKDDGSIELIGRKDNQVKLRGQRIEV 1521
Cdd:PRK12583 398 EIGELCTRGYSVMKGYWNNPEATAES-IDEDGW------------MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYP 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1522 EEIEhQARLAEADVAEIAV-ELIQPKDGEDgmLACFIVVE-DSASNEDEL 1569
Cdd:PRK12583 464 REIE-EFLFTHPAVADVQVfGVPDEKYGEE--IVAWVRLHpGHAASEEEL 510
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1141-1569 |
8.44e-07 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 53.59 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLV-ELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLrLMCRKVSAklslase 1219
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPL-IHCLKLSG------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1220 asaplakdlvGTVVIVNADSAlqlahhaspitsvrpthtAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTR 1299
Cdd:cd05937 79 ----------SRFVIVDPDDP------------------AILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1300 TLQ----FASYAFAGSLVELLMnlcHGGCIC-------------VLSEEERRTDLASAMCRmkvnwaFLtstvvdLLTPK 1362
Cdd:cd05937 131 TYTcmplYHGTAAFLGACNCLM---SGGTLAlsrkfsasqfwkdVRDSGATIIQYVGELCR------YL------LSTPP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1363 SV--PSLSILCVGGEPIRASQivrWGSqvhLRQTYGSSEVSGIVSSAALTTCSTTRDVGRASTGVF----WI-------- 1428
Cdd:cd05937 196 SPydRDHKVRVAWGNGLRPDI---WER---FRERFNVPEIGEFYAATEGVFALTNHNVGDFGAGAIghhgLIrrwkfenq 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1429 -----VDPNNHNRL----------APVGAVGEVLVEGPVLGRE----YIDEPDKTASTFIEAPAWRASLglsagqqrLYK 1489
Cdd:cd05937 270 vvlvkMDPETDDPIrdpktgfcvrAPVGEPGEMLGRVPFKNREafqgYLHNEDATESKLVRDVFRKGDI--------YFR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1490 TGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQ----ARLAEADVAEIAVeliQPKDGEDGMLACFIvvEDSASN 1565
Cdd:cd05937 342 TGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVlgahPDIAEANVYGVKV---PGHDGRAGCAAITL--EESSAV 416
|
....
gi 1779949166 1566 EDEL 1569
Cdd:cd05937 417 PTEF 420
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1106-1595 |
9.87e-07 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 53.49 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1106 HDVPPAIERCIHDLFADQAKARPDAPAICAWDGDMTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVL 1185
Cdd:PRK07059 15 AEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1186 KAGGAFLLLDP-SLPHErLRLMCRKVSAKL-----SLASEASAPLAKDLVGTVV-------------IVN--------AD 1238
Cdd:PRK07059 95 RAGYVVVNVNPlYTPRE-LEHQLKDSGAEAivvleNFATTVQQVLAKTAVKHVVvasmgdllgfkghIVNfvvrrvkkMV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1239 SALQLAHHAS--------------PITsVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYL--GMQASTRTLQ 1302
Cdd:PRK07059 174 PAWSLPGHVRfndalaegarqtfkPVK-LGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLqpAFEKKPRPDQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1303 FAS-------YAFAGSlVELLMNLCHGGCICVLSEEERRTDLASAMCRMKVNW---------AFLTSTVVDLLtpkSVPS 1366
Cdd:PRK07059 253 LNFvcalplyHIFALT-VCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIfpavntlynALLNNPDFDKL---DFSK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1367 LSILCVGGEPIRASQIVRWGSQVH--LRQTYGSSEVSGIVSSAALTTCSTTRDVGR--ASTgvfWIVDPNNHNRLAPVGA 1442
Cdd:PRK07059 329 LIVANGGGMAVQRPVAERWLEMTGcpITEGYGLSETSPVATCNPVDATEFSGTIGLplPST---EVSIRDDDGNDLPLGE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1443 VGEVLVEGPVLGREYIDEPDKTASTFIEapawraslglsagqQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRI--- 1519
Cdd:PRK07059 406 PGEICIRGPQVMAGYWNRPDETAKVMTA--------------DGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVypn 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1520 EVEEI--EHQARLaeaDVAEIAVEliQPKDGEDGMLacFIVVEDSASNEDE--------LSG-KRTR-LDTRTQ---RTI 1584
Cdd:PRK07059 472 EIEEVvaSHPGVL---EVAAVGVP--DEHSGEAVKL--FVVKKDPALTEEDvkafckerLTNyKRPKfVEFRTElpkTNV 544
|
570
....*....|.
gi 1779949166 1585 GKIqdrLERDL 1595
Cdd:PRK07059 545 GKI---LRREL 552
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
316-423 |
1.32e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 52.96 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 316 GYGPTECCIVCTgYTTTQAFKTGTIGTAIASVSWvvdpedyhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpa 395
Cdd:PRK08180 371 GLGMTETAPSAT-FTTGPLSRAGNIGLPAPGCEV--------KLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEE-- 439
|
90 100
....*....|....*....|....*...
gi 1779949166 396 wlvdgcqGYagrrgrlYKTGDLVRYDDE 423
Cdd:PRK08180 440 -------GY-------YRSGDAVRFVDP 453
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
715-974 |
1.44e-06 |
|
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: 52.57 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 715 VLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKmGMLQVVLADGIEWEQANELEQYLEKDKSvsmglgDSLARYALV 794
Cdd:cd19537 29 ACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDG-GLRRSYSSSPPRVQRVDTLDVWKEINRP------FDLEREDPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 795 RDVGTgKRWMVWTLHHALYDGWSLPQIANLVTEVYHGAEVGKQPgfnafIKYLG-----EQDHEAAAAYWQGTLADCQAI 869
Cdd:cd19537 102 RVFIS-PDTLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVR-----REYLDstawsRPASPEDLDFWSEYLSGLPLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 870 SFPA---------------LPPAVQQPVADATTAfqcpalarrpSDITMSTLIRAAWALLASSYTSSDDVVFGATVTGRN 934
Cdd:cd19537 176 NLPRrtssksyrgtsrvfqLPGSLYRSLLQFSTS----------SGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRT 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1779949166 935 APvaGIEAMAG----PtiatVPVRVRVQHS--HKVSEFLHSVQ---QQA 974
Cdd:cd19537 246 SE--EDMETVGlfleP----LPIRIRFPSSsdASAADFLRAVRrssQAA 288
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
723-971 |
1.89e-06 |
|
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: 52.32 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 723 DEDRFRAAWERVVQSTAVLRTRIVHSSKMGMLQVVLADGIEWEQAN-------ELEQYL-EKDKSVSMGLGDSLARYALV 794
Cdd:cd20484 37 DVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEEDisslkesEIIAYLrEKAKEPFVLENGPLMRVHLF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 795 RDVGTgKRWMVWTLHHALYDGWS-LPQIANLVtEVYHGAEVGKQPGFNAFI-----------KYLGEQDHEAAAAYWQ-- 860
Cdd:cd20484 117 SRSEQ-EHFVLITIHHIIFDGSSsLTLIHSLL-DAYQALLQGKQPTLASSPasyydfvaweqDMLAGAEGEEHRAYWKqq 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 861 --GTLADCQaisFPALPP--AVQQPVADATTAFQCPALAR------RPSDITMSTLIRAAWALLASSYTSSDDVVFGATV 930
Cdd:cd20484 195 lsGTLPILE---LPADRPrsSAPSFEGQTYTRRLPSELSNqiksfaRSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPT 271
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1779949166 931 TGRnaPVAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQ 971
Cdd:cd20484 272 MGR--PEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQ 310
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1139-1533 |
3.45e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 51.67 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1139 DMTYGELDVLSGRLAGHLVELgVGPEDIVPLCFEKSMWTVVAMLAVLKAGG-AFLLLDPSLP-H-ERLRLMCRKVSAKLS 1215
Cdd:PRK12476 68 ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTiAVPLFAPELPgHaERLDTALRDAEPTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1216 LASEASAPLAKDLVGT--------VVIVNA--DSAlqlAHHASPItsvrPTHT---AYVIFTSGSTGEPKGCRIEHRAAS 1282
Cdd:PRK12476 147 LTTTAAAEAVEGFLRNlprlrrprVIAIDAipDSA---GESFVPV----ELDTddvSHLQYTSGSTRPPVGVEITHRAVG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1283 SAVTAhgRYLGMQASTRTLQFAS----YAFAGSLVELLMNLCHGGC---------------ICVLSEEER--RTDLASAm 1341
Cdd:PRK12476 220 TNLVQ--MILSIDLLDRNTHGVSwlplYHDMGLSMIGFPAVYGGHStlmsptafvrrpqrwIKALSEGSRtgRVVTAAP- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1342 crmkvNWAFLTSTVVDLLTPKSVPSLS--ILCVGGEPIRASQIVRWGS--------QVHLRQTYGSSE----VSGIVSSA 1407
Cdd:PRK12476 297 -----NFAYEWAAQRGLPAEGDDIDLSnvVLIIGSEPVSIDAVTTFNKafapyglpRTAFKPSYGIAEatlfVATIAPDA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1408 ALTTCSTTRD---VGRA--------------STGVF----W--IVDPNNHNRLaPVGAVGEVLVEGPVLGREYIDEPDKT 1464
Cdd:PRK12476 372 EPSVVYLDREqlgAGRAvrvaadapnavahvSCGQVarsqWavIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEET 450
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 1465 ASTFIEAPAWRASLGLSAG----QQRLYKTGDLARYKdDGSIELIGRKDNQVKLRGQRIEVEEIEhqARLAEA 1533
Cdd:PRK12476 451 ERTFGAKLQSRLAEGSHADgaadDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIE--ATVAEA 520
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
138-449 |
3.51e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 51.66 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 138 VSAQHSARW-ASSSCHVVTLSEASigqlTVEDDLPgfsaTPGNAAYVLFTSGSTGIPKGVVLEHR-------AVST---- 205
Cdd:PLN02387 217 SSLSGSSNWtVSSFSEVEKLGKEN----PVDPDLP----SPNDIAVIMYTSGSTGLPKGVMMTHGnivatvaGVMTvvpk 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 206 -----------------------------SCLGHGRAFGITDQSRVLQFTSYTfDfcMAEIITTLLyggcICVPSDRDRH 256
Cdd:PLN02387 289 lgkndvylaylplahilelaaesvmaavgAAIGYGSPLTLTDTSNKIKKGTKG-D--ASALKPTLM----TAVPAILDRV 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 257 SD-----------LAK------------AINT--MGAnW--------ALLTPSVAQLLNPSdvptLKILVIGGEQVtSKD 303
Cdd:PLN02387 362 RDgvrkkvdakggLAKklfdiaykrrlaAIEGswFGA-WglekllwdALVFKKIRAVLGGR----IRFMLSGGAPL-SGD 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 304 WNRWptsvqlIN---------GYGPTEcciVCTGYTTTQAFKT--GTIG-----TAIASVSWvvdPEDYHKLA--PLGSv 365
Cdd:PLN02387 436 TQRF------INiclgapigqGYGLTE---TCAGATFSEWDDTsvGRVGpplpcCYVKLVSW---EEGGYLISdkPMPR- 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 366 GELLVEGPILARGYLNDAEKTaaafieDPAWLVDgcqgyagRRG-RLYKTGDLVRYDDEGNLVCLGRKDSQVKVR-GQRV 443
Cdd:PLN02387 503 GEIVIGGPSVTLGYFKNQEKT------DEVYKVD-------ERGmRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYV 569
|
....*.
gi 1779949166 444 ELGEIE 449
Cdd:PLN02387 570 SLGKVE 575
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
1141-1308 |
4.29e-06 |
|
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: 51.27 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1141 TYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDPSLPHERLrLMCRKVSAKLSLASEA 1220
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESL-LHCITVSKAKALIFNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1221 SAPL---AKDLVGTVVIVNADSALqlahhaspitsvrpthtaYVIFTSGSTGEPKgcriehraasSAVTAHGRYLGMQAs 1297
Cdd:cd05939 84 LDPLltqSSTEPPSQDDVNFRDKL------------------FYIYTSGTTGLPK----------AAVIVHSRYYRIAA- 134
|
170
....*....|.
gi 1779949166 1298 trtlqFASYAF 1308
Cdd:cd05939 135 -----GAYYAF 140
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
177-489 |
8.58e-06 |
|
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: 50.43 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 177 PGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLGHGRAFGItDQSRVLQ--FTSY-TFDFCMAEII---TTLLYGGCIC-- 248
Cdd:cd05933 149 PNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDL-RPATVGQesVVSYlPLSHIAAQILdiwLPIKVGGQVYfa 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 249 -----------------------VPSDRDRHSDLAKA-------INTMGANWAL---LTPSVAQLLNPSDVPT----LKI 291
Cdd:cd05933 228 qpdalkgtlvktlrevrptafmgVPRVWEKIQEKMKAvgaksgtLKRKIASWAKgvgLETNLKLMGGESPSPLfyrlAKK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 292 LV-------IGGEQVTSKDWNRWPTS-----------VQLINGYGPTECcivcTGYTTT---QAFKTGTIGTAIASVSWV 350
Cdd:cd05933 308 LVfkkvrkaLGLDRCQKFFTGAAPISretlefflslnIPIMELYGMSET----SGPHTIsnpQAYRLLSCGKALPGCKTK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 351 VDPEDYHKlaplgsVGELLVEGPILARGYLNDAEKTAAAfIEDPAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLG 430
Cdd:cd05933 384 IHNPDADG------IGEICFWGRHVFMGYLNMEDKTEEA-IDEDGWL---------------HSGDLGKLDEDGFLYITG 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1779949166 431 R-KDSQVKVRGQRVELGEIEHHIQGCMPeanqiAVEVILLEGEKSNtILAAFL----QLDVKTG 489
Cdd:cd05933 442 RiKELIITAGGENVPPVPIEDAVKKELP-----IISNAMLIGDKRK-FLSMLLtlkcEVNPETG 499
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1120-1183 |
9.83e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 50.18 E-value: 9.83e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1779949166 1120 FADQA--KARPDAPAICAWDGD-----MTYGELDVLSGRLAGHLVELGVGPEDIV----PLCFEksmwTVVAMLA 1183
Cdd:PRK03584 88 YAENLlrHRRDDRPAIIFRGEDgprreLSWAELRRQVAALAAALRALGVGPGDRVaaylPNIPE----TVVAMLA 158
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
848-1013 |
1.17e-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: 49.79 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 848 GEQDHEAAA----AYWQGTLADC-QAISFPALPPAVQQPVADATT---AFQCPALAR-----RPSDITMSTLIRAAWALL 914
Cdd:cd19546 183 GEDDRDSLIgdqiAYWRDALAGApDELELPTDRPRPVLPSRRAGAvplRLDAEVHARlmeaaESAGATMFTVVQAALAML 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 915 ASSYTSSDDVVFGaTVTGRNAPVAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATEM-----IPYEQtgLHETA 989
Cdd:cd19546 263 LTRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREArrhqdVPFER--LAELL 339
|
170 180
....*....|....*....|....*
gi 1779949166 990 KVSAD-ARHACsFQTLLIVQPGSNG 1013
Cdd:cd19546 340 ALPPSaDRHPV-FQVALDVRDDDND 363
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1250-1525 |
1.65e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 49.43 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1250 ITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYLGMQASTRTLQFA----SYAF-AGSLVELLMnlchGGC 1324
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLppfhAYGFnSCTLFPLLS----GVP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1325 ICVLSEEERRTDLASAMCRMKVNwaFLTSTVV----DLLTPK----SVPSLSILCVGGEPIRAS---QIVRWGSQVHLRQ 1393
Cdd:PRK06334 253 VVFAYNPLYPKKIVEMIDEAKVT--FLGSTPVffdyILKTAKkqesCLPSLRFVVIGGDAFKDSlyqEALKTFPHIQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1394 TYGSSEVSGIVSSAALTTCSTTRDVGRASTGV-FWIVDPNNHnrlAPV--GAVGEVLVEGPVLGREYIDEpDKTAStFIE 1470
Cdd:PRK06334 331 GYGTTECSPVITINTVNSPKHESCVGMPIRGMdVLIVSEETK---VPVssGETGLVLTRGTSLFSGYLGE-DFGQG-FVE 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1779949166 1471 ApawraslglsaGQQRLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIE 1525
Cdd:PRK06334 406 L-----------GGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALE 449
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
715-976 |
2.89e-05 |
|
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: 48.41 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 715 VLALHDDTDEDRFRAAWERVVQSTAVLRTRIVHSSKMGmLQVVLADG------IEWEQANELEQYLEKDKSVSMGL---- 784
Cdd:cd20483 29 VCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFG-EQQVLDDPsfhlivIDLSEAADPEAALDQLVRNLRRQeldi 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 785 --GDsLARYALVRDVGTGKRwMVWTLHHALYDGWSLPQIANLVTEVY-----HGAEVG-KQPGFNaFIKY-LGEQDH--- 852
Cdd:cd20483 108 eeGE-VIRGWLVKLPDEEFA-LVLASHHIAWDRGSSKSIFEQFTALYdalraGRDLATvPPPPVQ-YIDFtLWHNALlqs 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 853 ---EAAAAYWQGTLADCQAISfPALP------PAVQQP-VADATTAFQCPALAR-----RPSDITMSTLIRAAWALLASS 917
Cdd:cd20483 185 plvQPLLDFWKEKLEGIPDAS-KLLPfakaerPPVKDYeRSTVEATLDKELLARmkricAQHAVTPFMFLLAAFRAFLYR 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 918 YTSSDDVVFGatVTGRNAPVAGIEAMAGPTIATVPVRVRVQHSHKVSEFLHSVQQQATE 976
Cdd:cd20483 264 YTEDEDLTIG--MVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLE 320
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1373-1569 |
3.60e-05 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 48.51 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1373 GGEPIRASQIVRWGS--QVHLRQTYGSSEVSGIVSSAALTTCSTTRDVG--RASTGVfWIVDPNNHNrlAPVGAVGEVLV 1448
Cdd:PRK08974 333 GGMAVQQAVAERWVKltGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGlpVPSTEI-KLVDDDGNE--VPPGEPGELWV 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1449 EGPVLGREYIDEPDKTAStfIEAPAWRAslglsagqqrlykTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEHQA 1528
Cdd:PRK08974 410 KGPQVMLGYWQRPEATDE--VIKDGWLA-------------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVV 474
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1779949166 1529 RLaEADVAEIAVeLIQPKDGEDGMLACFIVVEDSASNEDEL 1569
Cdd:PRK08974 475 ML-HPKVLEVAA-VGVPSEVSGEAVKIFVVKKDPSLTEEEL 513
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1428-1540 |
3.69e-05 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 48.14 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1428 IVDpnNHNRLAPVGAVGEVLVEGpVLGR----EYIDEPDKTASTFiEAPAWraslglsagqqrlYKTGDLARYKDDGSIE 1503
Cdd:PRK08008 353 IRD--DHNRPLPAGEIGEICIKG-VPGKtifkEYYLDPKATAKVL-EADGW-------------LHTGDTGYVDEEGFFY 415
|
90 100 110
....*....|....*....|....*....|....*..
gi 1779949166 1504 LIGRKDNQVKLRGQRIEVEEIEHqARLAEADVAEIAV 1540
Cdd:PRK08008 416 FVDRRCNMIKRGGENVSCVELEN-IIATHPKIQDIVV 451
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
60-223 |
4.86e-05 |
|
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: 48.11 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 60 EMSYSVLDGLSTKLAGYLV-KIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDHPVSRHKEILRQTGARMV-- 136
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVAlt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 137 --VVSAQH--SARWASSSCH----------VVTLSEASIGQLTVEDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRA 202
Cdd:cd05905 94 veACLKGLpkKLLKSKTAAEiakkkgwpkiLDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173
|
170 180
....*....|....*....|.
gi 1779949166 203 VSTSCLGHgRAFGITDQSRVL 223
Cdd:cd05905 174 LLAHCRAL-KEACELYESRPL 193
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1120-1280 |
4.92e-05 |
|
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: 48.04 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1120 FADQAKAR---PDAPAICAWDG----DMTYGELDVLSGRLAGHLVELGVGPED----IVPLCFEksmwTVVAMLAVLKAG 1188
Cdd:cd05943 72 YAENLLRHadaDDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDrvagYLPNIPE----AVVAMLATASIG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1189 GAFLLLDPSL-PH---ERLrlmcRKVSAKLSLASEAS-------------APLAK---DLVGTVVIVNADSALQ------ 1242
Cdd:cd05943 148 AIWSSCSPDFgVPgvlDRF----GQIEPKVLFAVDAYtyngkrhdvrekvAELVKglpSLLAVVVVPYTVAAGQpdlski 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1243 ---------LAHHASPI---TSVRPTHTAYVIFTSGSTGEPKGcrIEHRA 1280
Cdd:cd05943 224 akaltledfLATGAAGElefEPLPFDHPLYILYSSGTTGLPKC--IVHGA 271
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
37-207 |
7.49e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 47.24 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAIC------AWDG---EMSYSVLDGLSTKLAGYLVKIGVkPGDVVPLCFEKSMWTVVAMLAVLK 107
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTfidyeqDPAGvaeTLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 108 AGGAFAPLDPDHPVSRHKEI---LRQTGARMVVVSAqhsarwaSSSCHVVTLSEASIGQLT---VEDDLPGFSATPG--- 178
Cdd:PRK05850 82 AGLIAVPLSVPQGGAHDERVsavLRDTSPSVVLTTS-------AVVDDVTEYVAPQPGQSAppvIEVDLLDLDSPRGsda 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1779949166 179 ------NAAYVLFTSGSTGIPKGVVLEHRAVSTSC 207
Cdd:PRK05850 155 rprdlpSTAYLQYTSGSTRTPAGVMVSHRNVIANF 189
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1152-1295 |
9.52e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 46.92 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1152 LAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGgaflLLDPSLPH-----------ERLRLMCRKVSAKLSLASEA 1220
Cdd:PRK09192 62 GARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAG----LVPVPLPLpmgfggresyiAQLRGMLASAQPAAIITPDE 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 1221 SAPLAKDLVGTVVIVNADSALQLAHHASP---ITSVRPTHTAYVIFTSGSTGEPKGCRIEHRAASSAVTAHGRYlGMQ 1295
Cdd:PRK09192 138 LLPWVNEATHGNPLLHVLSHAWFKALPEAdvaLPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHD-GLK 214
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1128-1279 |
1.04e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 46.91 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1128 PDAPAICAWdgdmtyGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLL-------DPSLPH 1200
Cdd:PRK07768 24 PDAPVRHTW------GEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLhqptprtDLAVWA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1779949166 1201 ERLRLMCRKVSAKLSLASEASAPLAKDLVGTVVIVNADSALqLAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHR 1279
Cdd:PRK07768 98 EDTLRVIGMIGAKAVVVGEPFLAAAPVLEEKGIRVLTVADL-LAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHG 175
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1227-1564 |
1.13e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 46.56 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1227 DLVGTVVIVNADSA----LQLAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEH----RAASSAVTAHGR------YL 1292
Cdd:PRK13388 117 DLPGVRVLDVDTPAyaelVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHgrlaFAGRALTERFGLtrddvcYV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1293 GMQASTRTLQFASYAFAgslvellmnLCHGGCICVlseeeRRTDLASamcrmkvnwAFLTS---------TVVD------ 1357
Cdd:PRK13388 197 SMPLFHSNAVMAGWAPA---------VASGAAVAL-----PAKFSAS---------GFLDDvrrygatyfNYVGkplayi 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1358 LLTP-KSVPSLSILCVG-----GEPIRASQIVRWGSQVHlrQTYGSSEVSGIVssaalttcstTRD-------VGRASTG 1424
Cdd:PRK13388 254 LATPeRPDDADNPLRVAfgneaSPRDIAEFSRRFGCQVE--DGYGSSEGAVIV----------VREpgtppgsIGRGAPG 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1425 VFwIVDPNN-----------HNRLA-PVGAVGE-VLVEGPVLGREYIDEPDKTASTFieAPAWraslglsagqqrlYKTG 1491
Cdd:PRK13388 322 VA-IYNPETltecavarfdaHGALLnADEAIGElVNTAGAGFFEGYYNNPEATAERM--RHGM-------------YWSG 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1779949166 1492 DLArYKD-DGSIELIGRKDNQVKLRGQRIEVEEIEH-QARLAE-ADVAEIAVEliQPKDGEDGMLAcfIVVEDSAS 1564
Cdd:PRK13388 386 DLA-YRDaDGWIYFAGRTADWMRVDGENLSAAPIERiLLRHPAiNRVAVYAVP--DERVGDQVMAA--LVLRDGAT 456
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1487-1587 |
1.39e-04 |
|
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: 46.40 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1487 LYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVELIqPKD--GEdgMLACFIVVEDSAS 1564
Cdd:cd05966 470 YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVE-SALVAHPAVAEAAVVGR-PHDikGE--AIYAFVTLKDGEE 545
|
90 100
....*....|....*....|...
gi 1779949166 1565 NEDELsgkRTRLDTRTQRTIGKI 1587
Cdd:cd05966 546 PSDEL---RKELRKHVRKEIGPI 565
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1124-1499 |
1.52e-04 |
|
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: 46.27 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1124 AKARPDAPAICAWDGD-----MTYGELDVLSGRLAGHLVELGVGPEDIVPLCFEKSMWTVVAMLAVLKAGGAFLLLDP-- 1196
Cdd:cd05921 5 ARQAPDRTWLAEREGNggwrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPay 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1197 ---SLPHERLRLMCRKVSAKLSLASEASA---------PLAKDLVGTVVIVNADSALQLAH-HASPIT--------SVRP 1255
Cdd:cd05921 85 slmSQDLAKLKHLFELLKPGLVFAQDAAPfaralaaifPLGTPLVVSRNAVAGRGAISFAElAATPPTaavdaafaAVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1256 THTAYVIFTSGSTGEPKGCRIEHR--AASSAvtahgrylgMQASTRTLQFA-----------SYAFAGSLVeLLMNLCHG 1322
Cdd:cd05921 165 DTVAKFLFTSGSTGLPKAVINTQRmlCANQA---------MLEQTYPFFGEeppvlvdwlpwNHTFGGNHN-FNLVLYNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1323 GCICV----------------LSE-----------------EERRTDlaSAMCR--------MKVNWAFLTSTVVDLLTP 1361
Cdd:cd05921 235 GTLYIddgkpmpggfeetlrnLREisptvyfnvpagwemlvAALEKD--EALRRrffkrlklMFYAGAGLSQDVWDRLQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1362 KSVPSLsilcvgGEPIRasqivrwgsqvhLRQTYGSSEVSGivssaalTTCSTTRDVGRAstGVFWIVDPNNHNRLAPVG 1441
Cdd:cd05921 313 LAVATV------GERIP------------MMAGLGATETAP-------TATFTHWPTERS--GLIGLPAPGTELKLVPSG 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 1442 AVGEVLVEGPVLGREYIDEPDKTASTFIEapawraslglsagqQRLYKTGDLARYKDD 1499
Cdd:cd05921 366 GKYEVRVKGPNVTPGYWRQPELTAQAFDE--------------EGFYCLGDAAKLADP 409
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
74-201 |
1.80e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 46.14 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 74 AGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLdpdH-PVSRH---------KEILRQTGARMVVVSAQHS 143
Cdd:PRK07768 43 AGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTML---HqPTPRTdlavwaedtLRVIGMIGAKAVVVGEPFL 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 144 ArwASSschvvTLSEASIGQLTVEDDLPGFSATP-----GNAAYVLFTSGSTGIPKGVVLEHR 201
Cdd:PRK07768 120 A--AAP-----VLEEKGIRVLTVADLLAADPIDPvetgeDDLALMQLTSGSTGSPKAVQITHG 175
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
287-444 |
1.99e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 46.25 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 287 PTLKILVIGGEQVTSKDWNRWPT--SVQLINGYGPTECcivcTGYTTTQ---AFKTGTIGTAIAS------VSWvvdpED 355
Cdd:PTZ00342 461 PNLEVILNGGGKLSPKIAEELSVllNVNYYQGYGLTET----TGPIFVQhadDNNTESIGGPISPntkykvRTW----ET 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 356 YhKLAPLGSVGELLVEGPILARGYLNDAEKTAAAFIEDpawlvdgcqGYagrrgrlYKTGDLVRYDDEGNLVCLGRKDSQ 435
Cdd:PTZ00342 533 Y-KATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTED---------GY-------FKTGDIVQINKNGSLTFLDRSKGL 595
|
170
....*....|
gi 1779949166 436 VKV-RGQRVE 444
Cdd:PTZ00342 596 VKLsQGEYIE 605
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1259-1540 |
2.03e-04 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.42 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1259 AYVIFTSGSTGEPKGCRIEHRA-ASSAVTAH------GRYL---------GMQASTRTLQfasyafAGSlVELLMNLCHG 1322
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAAlTASADATHdrlggpGQWLlalpahhiaGLQVLVRSVI------AGS-EPVELDVSAG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1323 GCIcvlseeerrTDLASAMCRMKVN--WAFLTSTVVD--LLTPKSVPSLSIL---CVGGEPIRAsQIVRWGSQVHLR--Q 1393
Cdd:PRK07824 111 FDP---------TALPRAVAELGGGrrYTSLVPMQLAkaLDDPAATAALAELdavLVGGGPAPA-PVLDAAAAAGINvvR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1394 TYGSSEVSGivssaaltTCSTTrdvGRASTGV-FWIVDpnnhnrlapvgavGEVLVEGPVLGREYIDEPDKTAstFIEaP 1472
Cdd:PRK07824 181 TYGMSETSG--------GCVYD---GVPLDGVrVRVED-------------GRIALGGPTLAKGYRNPVDPDP--FAE-P 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1779949166 1473 AWraslglsagqqrlYKTGDLARYkDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAV 1540
Cdd:PRK07824 234 GW-------------FRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVE-AALATHPAVADCAV 286
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
808-970 |
2.90e-04 |
|
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: 45.11 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 808 LHHALYDGWSLPQIANLVTEVYHGAEVGKQPGFNAF-IKY----------LG-EQDHEAAAA----YWQGTLADcqAISF 871
Cdd:cd19540 128 VHHIAADGWSMAPLARDLATAYAARRAGRAPDWAPLpVQYadyalwqrelLGdEDDPDSLAArqlaYWRETLAG--LPEE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 872 PALP-----PAVQQPVAdATTAFQCPA--------LARRpSDITMSTLIRAAWALLASSYTSSDDVVFGATVTGRNAPVa 938
Cdd:cd19540 206 LELPtdrprPAVASYRG-GTVEFTIDAelharlaaLARE-HGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEA- 282
|
170 180 190
....*....|....*....|....*....|..
gi 1779949166 939 gIEAMAGPTIATVPVRVRVQHSHKVSEFLHSV 970
Cdd:cd19540 283 -LDDLVGMFVNTLVLRTDVSGDPTFAELLARV 313
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
73-442 |
3.28e-04 |
|
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: 45.11 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 73 LAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGAFAPLDPDhpvSRHKEI---LRQTGARMVVVSAQ-------- 141
Cdd:cd17641 24 FALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQD---SMAEEVaylLNYTGARVVIAEDEeqvdklle 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 142 HSARWASSScHVVTLSEA-----------SIGQLTVEDDL-----PGF------SATPGNAAYVLFTSGSTGIPKGVVLE 199
Cdd:cd17641 101 IADRIPSVR-YVIYCDPRgmrkyddprliSFEDVVALGRAldrrdPGLyerevaAGKGEDVAVLCTTSGTTGKPKLAMLS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 200 HRAVstscLGHGRAFGITD-QSRVLQFTSY-TFDFCMAEIIT---TLLYGGCICVPSD---------------------- 252
Cdd:cd17641 180 HGNF----LGHCAAYLAADpLGPGDEYVSVlPLPWIGEQMYSvgqALVCGFIVNFPEEpetmmedlreigptfvllpprv 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 253 --------------------------------------RDRHSDLAKAINTMGANWALLTPSVAQLlnpsDVPTLKILVI 294
Cdd:cd17641 256 wegiaadvrarmmdatpfkrfmfelgmklglraldrgkRGRPVSLWLRLASWLADALLFRPLRDRL----GFSRLRSAAT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 295 GGEQVtSKDWNRWPTS--VQLINGYGPTECCIVCTGYTTTQAfKTGTIGTAIASVSWVVDpedyhklaplgSVGELLVEG 372
Cdd:cd17641 332 GGAAL-GPDTFRFFHAigVPLKQLYGQTELAGAYTVHRDGDV-DPDTVGVPFPGTEVRID-----------EVGEILVRS 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779949166 373 PILARGYLNDAEKTAAAFIEDpAWLvdgcqgyagrrgrlyKTGDLVRYDDEGNLVCLGR-KDSQVKVRGQR 442
Cdd:cd17641 399 PGVFVGYYKNPEATAEDFDED-GWL---------------HTGDAGYFKENGHLVVIDRaKDVGTTSDGTR 453
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1094-1569 |
4.14e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 44.95 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1094 TPEDRQQLWE--WNHDVPPAierCIHDLFADQAKARPDAPAIC------AWDG--DMTYGEL--DVLsgRLAGHLVELGV 1161
Cdd:PRK07529 6 TLADIEAIEAvpLAARDLPA---STYELLSRAAARHPDAPALSflldadPLDRpeTWTYAELlaDVT--RTANLLHSLGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1162 GPEDIV----PLCFEksmwTVVAMLAVLKAGGAFL---LLDPSLPHERLR------LMC----------RKVSAKLSLAS 1218
Cdd:PRK07529 81 GPGDVVafllPNLPE----THFALWGGEAAGIANPinpLLEPEQIAELLRaagakvLVTlgpfpgtdiwQKVAEVLAALP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1219 EASAPLAKDLVG-----------------TVVIVNADSAL--QLAHHASPITSVRPTHTAYVIFTSGSTGEPKGCRIEHR 1279
Cdd:PRK07529 157 ELRTVVEVDLARylpgpkrlavplirrkaHARILDFDAELarQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1280 AASSAVTAHGRYLGMQaSTRTLQFASYAF--AGSLVELLMNLCHGGCICVLSEEERRTD-----LASAMCRMKVNwaFLT 1352
Cdd:PRK07529 237 NEVANAWLGALLLGLG-PGDTVFCGLPLFhvNALLVTGLAPLARGAHVVLATPQGYRGPgvianFWKIVERYRIN--FLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1353 S--TVVDLL--TP---KSVPSLSILCVGGEPIRASQIVRWGSQ--VHLRQTYGSSEvsgivssaalTTCSTTRDVGRAST 1423
Cdd:PRK07529 314 GvpTVYAALlqVPvdgHDISSLRYALCGAAPLPVEVFRRFEAAtgVRIVEGYGLTE----------ATCVSSVNPPDGER 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1424 GVFWI-------------VDPNNHN-RLAPVGAVGEVLVEGPVLGREYIdEPDKTASTFIEapawraslglsagqQRLYK 1489
Cdd:PRK07529 384 RIGSVglrlpyqrvrvviLDDAGRYlRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLE--------------DGWLN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1490 TGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVeLIQPkDGEDGMLACFIV--VEDSASNED 1567
Cdd:PRK07529 449 TGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIE-EALLRHPAVALAAA-VGRP-DAHAGELPVAYVqlKPGASATEA 525
|
..
gi 1779949166 1568 EL 1569
Cdd:PRK07529 526 EL 527
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
313-431 |
5.41e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 44.58 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 313 LINGYGPTE--CC--IVCTGYTTTQAfktgtIGTAIASVSW-VVDPEDY-HKLAPLGSvGELLVEGPILARGYLNDAEKT 386
Cdd:PTZ00216 455 VIQGWGLTEtvCCggIQRTGDLEPNA-----VGQLLKGVEMkLLDTEEYkHTDTPEPR-GEILLRGPFLFKGYYKQEELT 528
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1779949166 387 AAAFIEDpAWlvdgcqgyagrrgrlYKTGDLVRYDDEGNLVCLGR 431
Cdd:PTZ00216 529 REVLDED-GW---------------FHTGDVGSIAANGTLRIIGR 557
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
37-208 |
5.84e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 44.35 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 37 IHDLFAEQVLAQPNAPAICAWdgEMSYSVLdGLSTKLAGYLVKIGVKPGDVVPLCFEKSMWTVVAMLAVLKAGGA----F 112
Cdd:PRK12476 47 VGDTVAYRYLDHSHSAAGCAV--ELTWTQL-GVRLRAVGARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIavplF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 113 APLDPDHpVSRHKEILRQtgARMVVVSAQHSARWASSScHVVTLSEASIGQLTVEDDLP-----GFSATP---GNAAYVL 184
Cdd:PRK12476 124 APELPGH-AERLDTALRD--AEPTVVLTTTAAAEAVEG-FLRNLPRLRRPRVIAIDAIPdsageSFVPVEldtDDVSHLQ 199
|
170 180
....*....|....*....|....
gi 1779949166 185 FTSGSTGIPKGVVLEHRAVSTSCL 208
Cdd:PRK12476 200 YTSGSTRPPVGVEITHRAVGTNLV 223
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
1389-1535 |
6.12e-04 |
|
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: 44.34 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1389 VHLRQTYGSSEVSGIvssaalTTCSTTRDVGRASTGVFWivdPNNHNRLApvgAVGEVLVEGPVLGREYIDEPDKTASTF 1468
Cdd:cd17641 349 VPLKQLYGQTELAGA------YTVHRDGDVDPDTVGVPF---PGTEVRID---EVGEILVRSPGVFVGYYKNPEATAEDF 416
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1779949166 1469 IEApAWraslglsagqqrlYKTGDLARYKDDGSIELIGR-KDNQVKLRGQRIEVEEIEHQAR----LAEADV 1535
Cdd:cd17641 417 DED-GW-------------LHTGDAGYFKENGHLVVIDRaKDVGTTSDGTRFSPQFIENKLKfspyIAEAVV 474
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1428-1552 |
6.34e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.77 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1428 IVDPNNHNRLAPvGAVGEVLVEGPVLGREYIDEPDKTASTFIEapawraslglSAGQQRLyKTGDLArYKDDGSIELIGR 1507
Cdd:PRK05691 383 IVDPQSLEVLGD-NRVGEIWASGPSIAHGYWRNPEASAKTFVE----------HDGRTWL-RTGDLG-FLRDGELFVTGR 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 1508 KDNQVKLRGQRIEVEEIEhqaRLAEADVAEI--------AVEliqpKDGEDGM 1552
Cdd:PRK05691 450 LKDMLIVRGHNLYPQDIE---KTVEREVEVVrkgrvaafAVN----HQGEEGI 495
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1109-1188 |
1.16e-03 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 43.65 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1109 PPAIERCIHDLFADQAKARPDAPAICAWDGDM--TYGELDVLSGRLAGHLVELGVGPEDIV----PLCFEksmWTVVaML 1182
Cdd:PRK08315 11 VPLLEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVgiwaPNVPE---WVLT-QF 86
|
....*.
gi 1779949166 1183 AVLKAG 1188
Cdd:PRK08315 87 ATAKIG 92
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1439-1594 |
1.60e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 43.21 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1439 PVGAVGEVLVEGPVLGREYIDEPDKTASTFiEAPAWraslglsagqqrlYKTGDLARYKDDGSIELIGRKDNQVKLRGQR 1518
Cdd:PRK05677 400 PLGEVGELCVKGPQVMKGYWQRPEATDEIL-DSDGW-------------LKTGDIALIQEDGYMRIVDRKKDMILVSGFN 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1519 IEVEEIEhQARLAEADVAEI-AVELIQPKDGEdgMLACFIVVEDSAS---------NEDELSG-KRTRL----DTRTQRT 1583
Cdd:PRK05677 466 VYPNELE-DVLAALPGVLQCaAIGVPDEKSGE--AIKVFVVVKPGETltkeqvmehMRANLTGyKVPKAvefrDELPTTN 542
|
170
....*....|.
gi 1779949166 1584 IGKIQDRLERD 1594
Cdd:PRK05677 543 VGKILRRELRD 553
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1481-1568 |
3.57e-03 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 41.86 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 1481 SAGQQrLYKTGDLARYKDDGSIELIGRKDNQVKLRGQRIEVEEIEhQARLAEADVAEIAVelIQPKDGEDGMLA-CFIVV 1559
Cdd:PRK10524 469 LFGRQ-VYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIE-ESISSHPAVAEVAV--VGVKDALKGQVAvAFVVP 544
|
....*....
gi 1779949166 1560 EDSASNEDE 1568
Cdd:PRK10524 545 KDSDSLADR 553
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
147-209 |
6.94e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 40.85 E-value: 6.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1779949166 147 ASSSCHVVTLSEasIGQLTVEDDLPGFSATPGNAAYVLFTSGSTGIPKGVVLEHRAVSTSCLG 209
Cdd:PLN02736 192 SGTGVEIVTYSK--LLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAG 252
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
411-585 |
8.02e-03 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 40.70 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 411 LYKTGDLVRYDDEGNLVCLGRKDSQVKVRGQRVELGEIEHHIQGcmpEANQIAVEVILLEGEKSNTILAAFLQLdvKTGR 490
Cdd:PRK10524 474 VYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISS---HPAVAEVAVVGVKDALKGQVAVAFVVP--KDSD 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779949166 491 AFPTnkAAETGSLAQVIFpveagKKLAERLPSYMVPDVYFVVTQLPITVSGKTDRKRLreigasfsaQQLAEIRTSGQgl 570
Cdd:PRK10524 549 SLAD--REARLALEKEIM-----ALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAI---------QAIAEGRDPGD-- 610
|
170
....*....|....*
gi 1779949166 571 krQPSTENEKALQQL 585
Cdd:PRK10524 611 --LTTIEDPAALQQI 623
|
|
| |
