|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1-436 |
0e+00 |
|
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: 834.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 1 MIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRPGWINFRELLRVASPEHNCLRTRS 80
Cdd:cd05928 94 FIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLNEASTEHHCVETGS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 81 GDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKAAW-TLFSAWANGACVFVHELPQV 159
Cdd:cd05928 174 QEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVFVHHLPRF 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 160 DAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICG 239
Cdd:cd05928 254 DPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 240 NFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRPFCLFNCYLDNPEKTAASEQGDFYITGDRAHMD 319
Cdd:cd05928 334 NFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRGDFYLTGDRGIMD 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 320 EDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALTRELQEHV 399
Cdd:cd05928 414 EDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQLTKELQQHV 493
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958647527 400 KTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 436
Cdd:cd05928 494 KSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1-432 |
5.06e-179 |
|
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: 506.49 E-value: 5.06e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 1 MIPGISQLTQKDLKYRLQAARVKSIITSDalaphvdaisadcpslqsrllvSDTSrpgwinfrellrvaspehnclrtrs 80
Cdd:cd05972 52 YVPLTTLLGPKDIEYRLEAAGAKAIVTDA----------------------EDPA------------------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 81 gdsmAIYFTSGTTGTPKMVEHSQcSYGLGFVASGRRLMALTESDIFWNTTDTGWVKAAW-TLFSAWANGACVFVHELPQV 159
Cdd:cd05972 85 ----LIYFTSGTTGLPKGVLHTH-SYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 160 DAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICG 239
Cdd:cd05972 160 DAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 240 NFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMD 319
Cdd:cd05972 240 NFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPG---LFLGYVGDPEKTEASIRGDYYLTGDRAYRD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 320 EDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvsHDPEALTRELQEHV 399
Cdd:cd05972 317 EDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGY--EPSEELAEELQGHV 394
|
410 420 430
....*....|....*....|....*....|...
gi 1958647527 400 KTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05972 395 KKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
6-438 |
2.13e-172 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 494.63 E-value: 2.13e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 6 SQLTQKDLKYRLQAARVKSIITSDA---------LAPHVDAISADCPSLQSRLLV----SDTSRPGWINFRELLRVASPE 72
Cdd:COG0365 96 PGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVgrtgADVPMEGDLDWDELLAAASAE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 73 HNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKAAW-TLFSAWANGACV 151
Cdd:COG0365 176 FEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSyIVYGPLLNGATV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 152 FVHELPQV--DAQTILNTLCRFPITTICCVPTLFRLLVQED---LTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIH 226
Cdd:COG0365 256 VLYEGRPDfpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIV 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 227 EGYGQSETV-LICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptRPF-CLFNCYLDNPEKTAAS 304
Cdd:COG0365 336 DGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK----GPWpGMFRGYWNDPERYRET 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 305 EQGDF---YITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP 381
Cdd:COG0365 412 YFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKP 491
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958647527 382 AYVshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 438
Cdd:COG0365 492 GVE--PSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
2-435 |
7.93e-168 |
|
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: 482.38 E-value: 7.93e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 2 IPGISQLTQKDLKYRLQAARVKSIIT--SDALAPHVDAISADCPSLQSRLLVSDTSRPGWINFRELLRVASPE----HNC 75
Cdd:cd05970 100 IPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDferpTAN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 76 LRTRSGDSMAIYFTSGTTGTPKMVEHSQcSYGLGFVASGRRLMALTESDIFWNTTDTGWVKAAW-TLFSAWANGACVFVH 154
Cdd:cd05970 180 SYPCGEDILLVYFSSGTTGMPKMVEHDF-TYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 155 ELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSET 234
Cdd:cd05970 259 DYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTET 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 235 VLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRPFCLFNCYLDNPEKTAASEQGDFYITGD 314
Cdd:cd05970 339 TLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEKTAEVWHDGYYHTGD 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 315 RAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVShdPEALTRE 394
Cdd:cd05970 419 AAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEP--SEELKKE 496
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958647527 395 LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 435
Cdd:cd05970 497 LQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
16-437 |
1.19e-116 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 352.66 E-value: 1.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 16 RLQAARVKSIITSDALAPHVdaISADCPSLQSRLLVSDTSR--PGWINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTT 93
Cdd:PRK04319 140 RLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEegPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGST 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 94 GTPK--------MVEHSQcsyglgfvaSGRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVHElPQVDAQTI 164
Cdd:PRK04319 218 GKPKgvlhvhnaMLQHYQ---------TGKYVLDLHEDDVYWCTADPGWVTGtSYGIFAPWLNGATNVIDG-GRFSPERW 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 165 LNTLCRFPITTICCVPTLFRLLV---QEDLTRYKFQCLRHCLAGGEALNSDVRdKW-KNQTGLEIHEGYGQSET--VLIC 238
Cdd:PRK04319 288 YRILEDYKVTVWYTAPTAIRMLMgagDDLVKKYDLSSLRHILSVGEPLNPEVV-RWgMKVFGLPIHDNWWMTETggIMIA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 239 gNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIriKPTRPfCLFNCYLDNPEKTAASEQGDFYITGDRAHM 318
Cdd:PRK04319 367 -NYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYM 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 319 DEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshDP-EALTRELQE 397
Cdd:PRK04319 443 DEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGY---EPsEELKEEIRG 519
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1958647527 398 HVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWG 437
Cdd:PRK04319 520 FVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWELG 559
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
78-435 |
8.84e-112 |
|
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: 335.69 E-value: 8.84e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 78 TRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASgRRLMALTESDIFWNTTDTGWVKAAWT-LFSAWANGACVFVHEL 156
Cdd:cd05974 82 THADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLST-MYWIGLKPGDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNY 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 157 PQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQcLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVL 236
Cdd:cd05974 161 ARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 237 ICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNvlpPGKEGNIAIRIKPTRPFCLFNCYLDNPEKTAASEQGDFYITGDRA 316
Cdd:cd05974 240 LVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 317 HMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALtrELQ 396
Cdd:cd05974 317 MRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETAL--EIF 394
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958647527 397 EHVKTVTAPYKYPRKVAFiSELPKTVSGKILRSKLRNQE 435
Cdd:cd05974 395 RFSRERLAPYKRIRRLEF-AELPKTISGKIRRVELRRRE 432
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
85-438 |
3.64e-109 |
|
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: 329.46 E-value: 3.64e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 85 AIYFTSGTTGTPKMVEHSQ---CSYGLGFVASgrrlMALTESDIFWNTT----DTGWVkaaWTLFSAWANGACVFVheLP 157
Cdd:COG0318 104 LILYTSGTTGRPKGVMLTHrnlLANAAAIAAA----LGLTPGDVVLVALplfhVFGLT---VGLLAPLLAGATLVL--LP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 158 QVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSET-V 235
Cdd:COG0318 175 RFDPERVLELIERERVTVLFGVPTMLaRLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETsP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 236 LICGNFRGS-TIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptrPFCLFNCYLDNPEKTAASEQGDFYITGD 314
Cdd:COG0318 255 VVTVNPEDPgERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDGWLRTGD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 315 RAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTRE 394
Cdd:COG0318 330 LGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDAEELRAF 408
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958647527 395 LQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 438
Cdd:COG0318 409 LRERL----ARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1-435 |
1.34e-107 |
|
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: 325.23 E-value: 1.34e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 1 MIPGISQLTQKDLKYRLQAARVKSIITSDalaphvdaisadcpslqsrllvsdtsrpgwinfrELLRVASPEhnclrtrs 80
Cdd:cd05969 52 ICPLFSAFGPEAIRDRLENSEAKVLITTE----------------------------------ELYERTDPE-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 81 gDSMAIYFTSGTTGTPKMVEHSQcSYGLGFVASGRRLMALTESDIFWNTTDTGWVK-AAWTLFSAWANGACVFVHElPQV 159
Cdd:cd05969 90 -DPTLLHYTSGTTGTPKGVLHVH-DAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTgTVYGIWAPWLNGVTNVVYE-GRF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 160 DAQTILNTLCRFPITTICCVPTLFRLLVQED---LTRYKFQCLRHCLAGGEALNSDVRdKW-KNQTGLEIHEGYGQSET- 234
Cdd:cd05969 167 DAESWYGIIERVKVTVWYTAPTAIRMLMKEGdelARKYDLSSLRFIHSVGEPLNPEAI-RWgMEVFGVPIHDTWWQTETg 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 235 -VLICgNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIriKPTRPfCLFNCYLDNPEKTAASEQGDFYITG 313
Cdd:cd05969 246 sIMIA-NYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 314 DRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshDP-EALT 392
Cdd:cd05969 322 DLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF---EPsDELK 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958647527 393 RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 435
Cdd:cd05969 399 EEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
82-427 |
3.99e-105 |
|
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: 314.99 E-value: 3.99e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHelPQVDA 161
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL--PKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 162 QTILNTLCRFPITTICCVPTLFRLLVQEDL-TRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSET--VLIC 238
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPEsAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 239 GNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAASEQGDFYITGDRAHM 318
Cdd:cd04433 158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGP-----SVMKGYWNNPEATAAVDEDGWYRTGDLGRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 319 DEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvsHDPEAltRELQEH 398
Cdd:cd04433 233 DEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG---ADLDA--EELRAH 307
|
330 340
....*....|....*....|....*....
gi 1958647527 399 VKTVTAPYKYPRKVAFISELPKTVSGKIL 427
Cdd:cd04433 308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
67-432 |
1.43e-100 |
|
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: 307.05 E-value: 1.43e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 67 RVASPEHNCLRTRSGDSMA-IYFTSGTTGTPKMVEHSQcSYGLGFvASGRRL---MALTESDIFWNTTDTGWVKAAW-TL 141
Cdd:cd05971 73 RLSNSGASALVTDGSDDPAlIIYTSGTTGPPKGALHAH-RVLLGH-LPGVQFpfnLFPRDGDLYWTPADWAWIGGLLdVL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 142 FSAWANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQC-LRHCLAGGEALNSDVRDKWKNQ 220
Cdd:cd05971 151 LPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVkLRAIATGGESLGEELLGWAREQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 221 TGLEIHEGYGQSETVLICGNFRG-STIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptRP-FCLFNCYLDNP 298
Cdd:cd05971 231 FGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVE----LPdPVAFLGYWNNP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 299 EKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 378
Cdd:cd05971 307 SATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVV 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958647527 379 LSPAYVshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05971 387 LNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
82-433 |
9.20e-93 |
|
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: 287.11 E-value: 9.20e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPKMVEHSqCSYGLGFVASGRRLMALTESDIFWNTTDTGWvkaAWTLFSA----WANGACVFVHELP 157
Cdd:cd05973 89 DPFVMMFTSGTTGLPKGVPVP-LRALAAFGAYLRDAVDLRPEDSFWNAADPGW---AYGLYYAitgpLALGHPTILLEGG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 158 qVDAQTILNTLCRFPITTICCVPTLFRLLVQ---EDLTRYKFQcLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSET 234
Cdd:cd05973 165 -FSVESTWRVIERLGVTNLAGSPTAYRLLMAagaEVPARPKGR-LRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTEL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 235 VLICGNFRG--STIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTrPFCLFNCYLDNPEKTAAseqGDFYIT 312
Cdd:cd05973 243 GMVLANHHAleHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANS-PLMWFRGYQLPDTPAID---GGYYLT 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 313 GDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvsHDP-EAL 391
Cdd:cd05973 319 GDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGG---HEGtPAL 395
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958647527 392 TRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:cd05973 396 ADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
2-432 |
9.91e-93 |
|
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: 288.88 E-value: 9.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 2 IPGISQLTQKDLKYRLQAARVKSIITSDALAPHV-DAISADCPSLQsRLLVSDTSRP--GWINFRELLRVASPEHNCLRT 78
Cdd:cd05959 82 VPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLaAALTKSEHTLV-VLIVSGGAGPeaGALLLAELVAAEAEQLKPAAT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 79 RSgDSMAIY-FTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWvkaAWTL-----FSAWANGACVF 152
Cdd:cd05959 161 HA-DDPAFWlYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFF---AYGLgnsltFPLSVGATTVL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 153 VHELPQVDAqtILNTLCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQ 231
Cdd:cd05959 237 MPERPTPAA--VFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 232 SETVLI-CGNFRGStIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRPFclfncYLDNPEKTAASEQGDFY 310
Cdd:cd05959 315 TEMLHIfLSNRPGR-VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM-----YWNNRDKTRDTFQGEWT 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 311 ITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvsHDPEA 390
Cdd:cd05959 389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY--EDSEA 466
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958647527 391 LTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05959 467 LEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
78-432 |
3.35e-89 |
|
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: 277.82 E-value: 3.35e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 78 TRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFwnttdTGWVKAAWT------LFSAWANGACV 151
Cdd:cd05958 94 TASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRF-----VGSPPLAFTfglggvLLFPFGVGASG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 152 FVheLPQVDAQTILNTLCRFPITTICCVPTLFRLLV------QEDLTrykfqCLRHCLAGGEALNSDVRDKWKNQTGLEI 225
Cdd:cd05958 169 VL--LEEATPDLLLSAIARYKPTVLFTAPTAYRAMLahpdaaGPDLS-----SLRKCVSAGEALPAALHRAWKEATGIPI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 226 HEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfclfNCYLDNPEKTAASE 305
Cdd:cd05958 242 IDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVR-GPT------GCRYLADKRQRTYV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 306 QGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvs 385
Cdd:cd05958 315 QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPG--- 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958647527 386 HDP-EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05958 392 VIPgPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
46-432 |
6.31e-83 |
|
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: 262.50 E-value: 6.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 46 QSRLLVSDTSrpgwinFRELLRV-ASPEHNCLRTRsGDSMAIYFTSGTTGTPK--MVEH-------SQCSYGLGFVASGR 115
Cdd:cd05936 96 GAKALIVAVS------FTDLLAAgAPLGERVALTP-EDVAVLQYTSGTTGVPKgaMLTHrnlvanaLQIKAWLEDLLEGD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 116 R--LMALTESDIFwnttdtgwvkaAWT--LFSAWANGACVFVheLPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQED 190
Cdd:cd05936 169 DvvLAALPLFHVF-----------GLTvaLLLPLALGATIVL--IPRFRPIGVLKEIRKHRVTIFPGVPTMYiALLNAPE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 191 LTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNV 269
Cdd:cd05936 236 FKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 270 LPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESA 349
Cdd:cd05936 316 LPPGEVGELWVR-GPQ----VMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEV 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 350 LAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayvsHDPEALT-RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 428
Cdd:cd05936 391 LYEHPAVAEAAVVGVPDPYSGEAVKAFVVL------KEGASLTeEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILR 464
|
....
gi 1958647527 429 SKLR 432
Cdd:cd05936 465 RELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
8-436 |
4.61e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 251.26 E-value: 4.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 8 LTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRPG----WINFRELLRVASPEHNCLRTRSGDS 83
Cdd:PRK06187 90 LKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 84 MAIYFTSGTTGTPK--------MVEHSqcsyglgfvASGRRLMALTESDIFWNTTDTGWVkAAWTL-FSAWANGA-CVFV 153
Cdd:PRK06187 170 AAMLYTSGTTGHPKgvvlshrnLFLHS---------LAVCAWLKLSRDDVYLVIVPMFHV-HAWGLpYLALMAGAkQVIP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 154 HElpqVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTR-YKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQS 232
Cdd:PRK06187 240 RR---FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 233 ETV-LICGNF-----RGSTIKSGSMGKASPPYDVQIVDEEGNVLPP-GKE-GNIAIRiKPtrpfCLFNCYLDNPEKTAAS 304
Cdd:PRK06187 317 ETSpVVSVLPpedqlPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdGGEvGEIIVR-GP----WLMQGYWNRPEATAET 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 305 EQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyV 384
Cdd:PRK06187 392 IDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG-A 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 385 SHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 436
Cdd:PRK06187 471 TLDAK----ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYA 518
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
63-432 |
6.79e-78 |
|
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: 248.53 E-value: 6.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 63 RELLRVASPEHNCLRTRSGDSMAIY-FTSGTTGTPKMVEHSQCSYgLGFV-ASGRRLMALTESDIFWNTTDTGWvkaAW- 139
Cdd:cd05919 72 DDYAYIARDCEARLVVTSADDIAYLlYSSGTTGPPKGVMHAHRDP-LLFAdAMAREALGLTPGDRVFSSAKMFF---GYg 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 140 ---TLFSAWANGACVFVHELPqVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRD 215
Cdd:cd05919 148 lgnSLWFPLAVGASAVLNPGW-PTAERVLATLARFRPTVLYGVPTFYaNLLDSCAGSPDALRSLRLCVSAGEALPRGLGE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 216 KWKNQTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYL 295
Cdd:cd05919 227 RWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVR-GPS----AAVGYW 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 296 DNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKA 375
Cdd:cd05919 302 NNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTA 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958647527 376 FIVLSPAYVSHdpEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05919 382 FVVLKSPAAPQ--ESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
11-433 |
1.37e-72 |
|
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: 239.52 E-value: 1.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 11 KDLKYRLQAARVKSIITSDA---------LAPHVD-AIS------ADCPSLQSRLLVSDTSRPG-WINFRELLRVASPeH 73
Cdd:cd05967 144 KELASRIDDAKPKLIVTASCgiepgkvvpYKPLLDkALElsghkpHHVLVLNRPQVPADLTKPGrDLDWSELLAKAEP-V 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 74 NCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVF 152
Cdd:cd05967 223 DCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGhSYIVYGPLLHGATTV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 153 VHELPQV---DAQTILNTLCRFPITTICCVPTLFRLLVQED-----LTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLE 224
Cdd:cd05967 303 LYEGKPVgtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVP 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 225 IHEGYGQSET-VLICGNFRG---STIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIkPTRPFCLFNCYLDNP-- 298
Cdd:cd05967 383 VIDHWWQTETgWPITANPVGlepLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPGCLLTLWKNDErf 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 299 EKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 378
Cdd:cd05967 462 KKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVV 541
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1958647527 379 LSPAyVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:cd05967 542 LKEG-VKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
8-432 |
2.34e-71 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 233.58 E-value: 2.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 8 LTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDtSRPGWINFRELLRVASPEHNCLRTRSGDSMAIY 87
Cdd:TIGR02262 89 LTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGR-PEAGEVQLAELLATESEQFKPAATQADDPAFWL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 88 FTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIfwnttdtgwVKAAWTLFSAWANG-----------ACVFVHEL 156
Cdd:TIGR02262 168 YSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDV---------CFSAAKLFFAYGLGnaltfpmsvgaTTVLMGER 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 157 PQVDAqtILNTLCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV 235
Cdd:TIGR02262 239 PTPDA--VFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEML 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 236 LICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTRPfclfNCYLDNPEKTAASEQGDFYITGDR 315
Cdd:TIGR02262 317 HIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS-GPSSA----TMYWNNRAKSRDTFQGEWTRSGDK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 316 AHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshdpEALTREL 395
Cdd:TIGR02262 392 YVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ-----TALETEL 466
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958647527 396 QEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:TIGR02262 467 KEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
82-428 |
2.50e-69 |
|
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: 226.34 E-value: 2.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPKMVEHSQcsYGLGFVASGrrlmALTESDIfwNTTDTGWVKA---------AWTLFSAWANGACVF 152
Cdd:cd17631 99 DLALLMYTSGTTGRPKGAMLTH--RNLLWNAVN----ALAALDL--GPDDVLLVVAplfhigglgVFTLPTLLRGGTVVI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 153 vheLPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKnQTGLEIHEGYGQ 231
Cdd:cd17631 171 ---LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQhPRFATTDLSSLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGM 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 232 SETV-LICGNFRGSTI-KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDF 309
Cdd:cd17631 247 TETSpGVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GPH----VMAGYWNRPEATAAAFRDGW 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 310 YITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvSHDPE 389
Cdd:cd17631 322 FHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP---GAELD 398
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958647527 390 ALtrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 428
Cdd:cd17631 399 ED--ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
13-432 |
7.78e-69 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 229.83 E-value: 7.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 13 LKYRLQAARVKSIITSD---------ALAPHVDAISADCPSLQSRLLV---SDTSRPGWIN-----FRELLRVASPEHNC 75
Cdd:TIGR02188 152 LADRINDAGAKLVITADeglrggkviPLKAIVDEALEKCPVSVEHVLVvrrTGNPVVPWVEgrdvwWHDLMAKASAYCEP 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 76 LRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVH 154
Cdd:TIGR02188 232 EPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGhSYIVYGPLANGATTVMF 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 155 E----LPQVD--AQTILntlcRFPITTICCVPTLFRLLVQ---EDLTRYKFQCLRhcLAG--GEALNSDVRDKWKNQTGL 223
Cdd:TIGR02188 312 EgvptYPDPGrfWEIIE----KHKVTIFYTAPTAIRALMRlgdEWVKKHDLSSLR--LLGsvGEPINPEAWMWYYKVVGK 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 224 E---IHEGYGQSETVLIC-GNFRGST-IKSGSMGKASPPYDVQIVDEEGNVLP-PGKEGNIAIRiKPtRPFCLFNCYLDn 297
Cdd:TIGR02188 386 ErcpIVDTWWQTETGGIMiTPLPGATpTKPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVIK-QP-WPGMLRTIYGD- 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 298 PE---KTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVK 374
Cdd:TIGR02188 463 HErfvDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIY 542
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647527 375 AFIVLSPAYvSHDPEaLTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:TIGR02188 543 AFVTLKDGY-EPDDE-LRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLR 598
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
16-433 |
1.07e-68 |
|
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: 228.98 E-value: 1.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 16 RLQAARVKSIITSDA---------LAPHVDAISADCPSLQSRLLVSDTSRPGWIN------FRELLRVASPEHNCLRTRS 80
Cdd:cd05966 151 RINDAQCKLVITADGgyrggkvipLKEIVDEALEKCPSVEKVLVVKRTGGEVPMTegrdlwWHDLMAKQSPECEPEWMDS 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 81 GDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVHE---- 155
Cdd:cd05966 231 EDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGhSYIVYGPLANGATTVMFEgtpt 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 LPQVDaqTILNTLCRFPITTICCVPTLFRLLVQ---EDLTRYKFQCLRHCLAGGEALNSDVrdkWK---NQTGLE---IH 226
Cdd:cd05966 311 YPDPG--RYWDIVEKHKVTIFYTAPTAIRALMKfgdEWVKKHDLSSLRVLGSVGEPINPEA---WMwyyEVIGKErcpIV 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 227 EGYGQSETVLIC-GNFRGST-IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrPFCLFNCYLDNP--EKTA 302
Cdd:cd05966 386 DTWWQTETGGIMiTPLPGATpLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIK-RPW-PGMARTIYGDHEryEDTY 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 303 ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPA 382
Cdd:cd05966 464 FSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDG 543
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958647527 383 YvsHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:cd05966 544 E--EPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
11-427 |
5.31e-68 |
|
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: 226.69 E-value: 5.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 11 KDLKYRLQAARVKSIITSDA---------LAPHVD-AISADCPSLQSRLLVSDTSRP------GWINFRELLRVASPEHN 74
Cdd:cd17634 146 EAVAGRIIDSSSRLLITADGgvragrsvpLKKNVDdALNPNVTSVEHVIVLKRTGSDidwqegRDLWWRDLIAKASPEHQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 75 CLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFV 153
Cdd:cd17634 226 PEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 154 HELPQV--DAQTILNTLCRFPITTICCVPTLFRLLVQED---LTRYKFQCLRHCLAGGEALNSDV-RDKWK--NQTGLEI 225
Cdd:cd17634 306 YEGVPNwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPINPEAyEWYWKkiGKEKCPV 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 226 HEGYGQSETV-LICGNFRGST-IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIK-P--TRPFclfncYLDNPE- 299
Cdd:cd17634 386 VDTWWQTETGgFMITPLPGAIeLKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwPgqTRTL-----FGDHERf 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 300 -KTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 378
Cdd:cd17634 461 eQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVV 540
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1958647527 379 LSPAYVshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 427
Cdd:cd17634 541 LNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
82-432 |
1.09e-66 |
|
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: 219.09 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPK--MVEHSQ-CSYGLGFvasgRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVheLP 157
Cdd:cd05934 82 DPASILYTSGTTGPPKgvVITHANlTFAGYYS----ARRFGLGEDDVYLTVLPLFHINAqAVSVLAALSVGATLVL--LP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 158 QVDAQTILNTLCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRhcLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVL 236
Cdd:cd05934 156 RFSASRFWSDVRRYGATVTNYLGAMLSyLLAQPPSPDDRAHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 237 ICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikPTRPFCLFNCYLDNPEKTAASEQGDFYITGDRA 316
Cdd:cd05934 234 GVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 317 HMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTRELQ 396
Cdd:cd05934 312 YRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG-ETLDPEELFAFCE 390
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958647527 397 EHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05934 391 GQL----AYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
13-432 |
2.39e-63 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 215.39 E-value: 2.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 13 LKYRLQAARVKSIITSD---------ALAPHVDAISADCPSLQSRLLVSDTSRP-GWINFR-----ELLRVASPEHNCLR 77
Cdd:PRK00174 162 LADRIIDAGAKLVITADegvrggkpiPLKANVDEALANCPSVEKVIVVRRTGGDvDWVEGRdlwwhELVAGASDECEPEP 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 78 TRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVHE- 155
Cdd:PRK00174 242 MDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGhSYIVYGPLANGATTLMFEg 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 ---LPQVDaqtilntlcRF-------PITTICCVPTLFRLLVQ---EDLTRYKFQCLRhcLAG--GEALNSDVrdkWK-- 218
Cdd:PRK00174 322 vpnYPDPG---------RFwevidkhKVTIFYTAPTAIRALMKegdEHPKKYDLSSLR--LLGsvGEPINPEA---WEwy 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 219 -NQTGLE---IHEGYGQSET--VLICGnFRGST-IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIrikpTRPF--C 289
Cdd:PRK00174 388 yKVVGGErcpIVDTWWQTETggIMITP-LPGATpLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVI----KDPWpgM 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 290 LFNCYLDnPE---KTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPD 366
Cdd:PRK00174 463 MRTIYGD-HErfvKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPD 541
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647527 367 PIRGEVVKAFIVLSPAYVSHDpeALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:PRK00174 542 DIKGQGIYAFVTLKGGEEPSD--ELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
8-427 |
3.47e-62 |
|
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: 208.99 E-value: 3.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 8 LTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSlQSRLLVSDTSRPGWINFRELLRVAS--PEHN---CLRTRSGD 82
Cdd:cd05911 69 YTADELAHQLKISKPKVIFTDPDGLEKVKEAAKELGP-KDKIIVLDDKPDGVLSIEDLLSPTLgeEDEDlppPLKDGKDD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 83 SMAIYFTSGTTGTPK-----------MVEHSQCSYGLGFVASGRRLMALTesdIFWNTTDTgwvkaaWTLFSAWaNGACV 151
Cdd:cd05911 148 TAAILYSSGTTGLPKgvclshrnliaNLSQVQTFLYGNDGSNDVILGFLP---LYHIYGLF------TTLASLL-NGATV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 152 FVHelPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGL-EIHEGY 229
Cdd:cd05911 218 IIM--PKFDSELFLDLIEKYKITFLYLVPPIAAALAKsPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 230 GQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAIRIkptrPFClFNCYLDNPEKTAAS--EQ 306
Cdd:cd05911 296 GMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVRG----PQV-MKGYYNNPEATKETfdED 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 307 GdFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvsh 386
Cdd:cd05911 371 G-WLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKP----- 444
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958647527 387 DPEALTRELQEHVKTVTAPYKYPRK-VAFISELPKTVSGKIL 427
Cdd:cd05911 445 GEKLTEKEVKDYVAKKVASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
7-337 |
1.11e-61 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 205.62 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 7 QLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDtsRPGWINFRELLRVASPEHNCLRT---RSGDS 83
Cdd:pfam00501 79 RLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLD--RDPVLKEEPLPEEAKPADVPPPPpppPDPDD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 84 MA-IYFTSGTTGTPKMVEHSQ---CSYGLGFVASGRRLMALTESDIFWNTT----DTGWVkaaWTLFSAWANGA-CVFVH 154
Cdd:pfam00501 157 LAyIIYTSGTTGKPKGVMLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLplfhDFGLS---LGLLGPLLAGAtVVLPP 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 155 ELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSE 233
Cdd:pfam00501 234 GFPALDPAALLELIERYKVTVLYGVPTLLNMLLEaGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 234 T---VLICGNFRGSTIKSGSMGKASPPYDVQIVDEE-GNVLPPGKEGNIAIRikptRPfCLFNCYLDNPEKTAAS-EQGD 308
Cdd:pfam00501 314 TtgvVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAfDEDG 388
|
330 340
....*....|....*....|....*....
gi 1958647527 309 FYITGDRAHMDEDGYFWFVGRNDDVINSS 337
Cdd:pfam00501 389 WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
15-434 |
1.51e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 207.83 E-value: 1.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 15 YRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDT----SRPGWINFRELLRVASPEHNCLRTRSGDSMAIYFTS 90
Cdd:PRK07656 96 YILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEeddpHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 91 GTTGTPK--MVEHSQ--------CSYgLGFVASGRRLMALTESDIFwnttdtGWvKAAWTlfSAWANGACVFVHelPQVD 160
Cdd:PRK07656 176 GTTGRPKgaMLTHRQllsnaadwAEY-LGLTEGDRYLAANPFFHVF------GY-KAGVN--APLMRGATILPL--PVFD 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 161 AQTILNTLCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRHCLAGGE----ALNSDVRDKWKNQTgleIHEGYGQSE-- 233
Cdd:PRK07656 244 PDEVFRLIETERITVLPGPPTMYNsLLQHPDRSAEDLSSLRLAVTGAAsmpvALLERFESELGVDI---VLTGYGLSEas 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 234 -TVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptrpfcLFNC---YLDNPEKTAASEQGDF 309
Cdd:PRK07656 321 gVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR--------GPNVmkgYYDDPEATAAAIDADG 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 310 YI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdp 388
Cdd:PRK07656 393 WLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG------ 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958647527 389 EALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK07656 467 AELTEEeLIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
85-433 |
3.97e-59 |
|
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: 199.82 E-value: 3.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 85 AIYFTSGTTGTPKMVEHSQCSyglgfVASGRRlmALTESdifWNTTDT-------------GWVKAawTLFSAWANGACV 151
Cdd:cd05941 93 LILYTSGTTGRPKGVVLTHAN-----LAANVR--ALVDA---WRWTEDdvllhvlplhhvhGLVNA--LLCPLFAGASVE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 152 FvheLPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ---------EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTG 222
Cdd:cd05941 161 F---LPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 223 LEIHEGYGQSETVLICGN-FRGSTIkSGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEK 300
Cdd:cd05941 238 HTLLERYGMTEIGMALSNpLDGERR-PGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GPS----VFKEYWNKPEA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 301 TAASEQGD-FYITGDRAHMDEDGYFWFVGR-NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 378
Cdd:cd05941 312 TKEEFTDDgWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVV 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1958647527 379 LSPAYVSHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:cd05941 392 LRAGAAALSLE----ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
8-438 |
1.52e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 200.57 E-value: 1.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 8 LTQKDLKYRLQAARVKSIITSDALAP------------HV------DAISADCP-----SLQSRLLVSDTSRPGWINFRE 64
Cdd:PRK08314 95 NREEELAHYVTDSGARVAIVGSELAPkvapavgnlrlrHVivaqysDYLPAEPEiavpaWLRAEPPLQALAPGGVVAWKE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 65 LLR--VASPEHNclrTRSGDSMAIYFTSGTTGTPKMVEHSQcsyglgfvasgRRLMALTESDIFWNT-TDTGWVKAAWTL 141
Cdd:PRK08314 175 ALAagLAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTH-----------RTVMANAVGSVLWSNsTPESVVLAVLPL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 142 F----------SAWANGACVFVheLPQVDAQTILNTLCRFPITTICCVPT-LFRLLVQEDLTRYKFQCLRHCLAGGEALN 210
Cdd:PRK08314 241 FhvtgmvhsmnAPIYAGATVVL--MPRWDREAAARLIERYRVTHWTNIPTmVVDFLASPGLAERDLSSLRYIGGGGAAMP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 211 SDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTiKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPTrpf 288
Cdd:PRK08314 319 EAVAERLKELTGLDYVEGYGLTETMaQTHSNPPDRP-KLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH-GPQ--- 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 289 cLFNCYLDNPEKTAAS----EQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSS 364
Cdd:PRK08314 394 -VFKGYWNRPEATAEAfieiDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIAT 472
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958647527 365 PDPIRGEVVKAFIVLSPAYVSHDPEAltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 438
Cdd:PRK08314 473 PDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKAR 543
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
78-431 |
1.77e-58 |
|
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: 198.14 E-value: 1.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 78 TRSGDSMAIYFTSGTTGTPK--MVEHSqcsyGLG-FVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGAC-VFV 153
Cdd:cd05930 90 TDPDDLAYVIYTSGSTGKPKgvMVEHR----GLVnLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATlVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 154 HELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEdLTRYKFQCLRHCLAGGEALNSDVRDKW-KNQTGLEIHEGYGQS 232
Cdd:cd05930 166 PEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQE-LELAALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 233 ETVLICGNFRgstIKSGSMGKASPP-------YDVQIVDEEGNVLPPGKEGNIAIrikpTRPfCLFNCYLDNPEKTAAS- 304
Cdd:cd05930 245 EATVDATYYR---VPPDDEEDGRVPigrpipnTRVYVLDENLRPVPPGVPGELYI----GGA-GLARGYLNRPELTAERf 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 305 -----EQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 378
Cdd:cd05930 317 vpnpfGPGErMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958647527 379 LSPayvshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd05930 397 PDE-----GGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
82-431 |
3.72e-56 |
|
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: 191.54 E-value: 3.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFWNTTD----TGWVKaawTLFSAWANGACVFVheLP 157
Cdd:cd05935 85 DLALIPYTSGTTGLPKGCMHTHFSA-AANALQSAVWTGLTPSDVILACLPlfhvTGFVG---SLNTAVYVGGTYVL--MA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 158 QVDAQTILNTLCRFPITTICCVPT-LFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVL 236
Cdd:cd05935 159 RWDRETALELIEKYKVTFWTNIPTmLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 237 ICGNFRGSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD----FYI 311
Cdd:cd05935 239 QTHTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVR-GPQ----IFKGYWNRPEETEESFIEIkgrrFFR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 312 TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVShdpEAL 391
Cdd:cd05935 314 TGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRG---KVT 390
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958647527 392 TRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd05935 391 EEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1-432 |
4.54e-56 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 193.36 E-value: 4.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 1 MIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRP---GWINFRELLRVASPEHNCLR 77
Cdd:PRK08008 89 MVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPaddGVSSFTQLKAQQPATLCYAP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 78 TRSGDSMA-IYFTSGTTGTPKMVEHSQCSYGL-GFVASGRrlMALTESDIFWNTTDTGWV----KAAWTLFSAwanGACV 151
Cdd:PRK08008 169 PLSTDDTAeILFTSGTTSRPKGVVITHYNLRFaGYYSAWQ--CALRDDDVYLTVMPAFHIdcqcTAAMAAFSA---GATF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 152 FVHElpQVDAQTILNTLCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRHCLAggeALN-SDV-RDKWKNQTGLEIHEG 228
Cdd:PRK08008 244 VLLE--KYSARAFWGQVCKYRATITECIPMMIRtLMVQPPSANDRQHCLREVMF---YLNlSDQeKDAFEERFGVRLLTS 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 229 YGQSETVL-ICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRpfCLFNCYLDNPEKTAASEQG 307
Cdd:PRK08008 319 YGMTETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGK--TIFKEYYLDPKATAKVLEA 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 308 DFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSH 386
Cdd:PRK08008 397 DGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG-ETL 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958647527 387 DPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:PRK08008 476 SEEEFFAFCEQNM----AKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
16-432 |
2.13e-55 |
|
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: 193.48 E-value: 2.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 16 RLQAARVKSIITSDA---------LAPHVDAISADCPSLQSRLLVSDTSRP-GWINFREL---LRVASPEHNCLRTRSGD 82
Cdd:cd05968 158 RLQDAEAKALITADGftrrgrevnLKEEADKACAQCPTVEKVVVVRHLGNDfTPAKGRDLsydEEKETAGDGAERTESED 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 83 SMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESD-IFWnTTDTGWVKAAWTLFSAWANGACVFVHE-LPQVD 160
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTW-FTDLGWMMGPWLIFGGLILGATMVLYDgAPDHP 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 161 -AQTILNTLCRFPITTICCVPTLFRLLV---QEDLTRYKFQCLRHCLAGGEALNSD-------VRDKWKN-----QTGLE 224
Cdd:cd05968 317 kADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNPEpwnwlfeTVGKGRNpiinySGGTE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 225 IHEGygqsetvlICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPgKEGNIAIRiKP----TRPFCLFNC-YLDnpe 299
Cdd:cd05968 397 ISGG--------ILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLL-APwpgmTRGFWRDEDrYLE--- 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 300 kTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 379
Cdd:cd05968 464 -TYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVL 542
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958647527 380 SPAYVshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05968 543 KPGVT--PTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
8-433 |
6.71e-55 |
|
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: 189.83 E-value: 6.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 8 LTQKDLKYRLQAARVKSIIT-SDALAPHVDAISADCPSLQ--------SRLLVSDTSRPGWINfreLLRVASPEhncLRT 78
Cdd:cd05926 73 YKKAEFEFYLADLGSKLVLTpKGELGPASRAASKLGLAILelaldvgvLIRAPSAESLSNLLA---DKKNAKSE---GVP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 79 RSGDSMAIYFTSGTTGTPKMVEHSQcsygLGFVASGR---RLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVH 154
Cdd:cd05926 147 LPDDLALILHTSGTTGRPKGVPLTH----RNLAASATnitNTYKLTPDDRTLVVMPLFHVHGlVASLLSTLAAGGSVVLP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 155 elPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ--EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQS 232
Cdd:cd05926 223 --PRFSASTFWPDVRDYNATWYTAVPTIHQILLNrpEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMT 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 233 ETV--LICGNFRGSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAAS-EQGDF 309
Cdd:cd05926 301 EAAhqMTSNPLPPGPRKPGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRGPN-----VTRGYLNNPEANAEAaFKDGW 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 310 YITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshdpE 389
Cdd:cd05926 375 FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA-----S 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958647527 390 ALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:cd05926 450 VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
8-434 |
8.09e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 190.14 E-value: 8.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 8 LTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRP---GWINFRELLRVASPEHNCLRTRSGDSM 84
Cdd:PRK08316 95 LTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREapgGWLDFADWAEAGSVAEPDVELADDDLA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 85 AIYFTSGTTGTPK---------MVEHSQCSYGLGFVASGRRLMAL-----TESDIFWNTTDtgWVKAAWTLfsawangac 150
Cdd:PRK08316 175 QILYTSGTESLPKgamlthralIAEYVSCIVAGDMSADDIPLHALplyhcAQLDVFLGPYL--YVGATNVI--------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 151 vfvheLPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAG-----GEALNsDVRDKWknqTGLE 224
Cdd:PRK08316 244 -----LDAPDPELILRTIEAERITSFFAPPTVWiSLLRHPDFDTRDLSSLRKGYYGasimpVEVLK-ELRERL---PGLR 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 225 IHEGYGQSE-----TVLicgNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPE 299
Cdd:PRK08316 315 FYNCYGQTEiaplaTVL---GPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR-SPQ----LMLGYWDDPE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 300 KTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 379
Cdd:PRK08316 387 KTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVP 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647527 380 SpayvshDPEALTR-ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK08316 467 K------AGATVTEdELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
168-433 |
5.38e-53 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 185.99 E-value: 5.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 168 LCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSET--VLICgNFRGS 244
Cdd:PRK07059 297 LKKYQVHIFPAVNTLYNaLLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETspVATC-NPVDA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 245 TIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGY 323
Cdd:PRK07059 376 TEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR-GPQ----VMAGYWNRPDETAKVMTADgFFRTGDVGVMDERGY 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 324 FWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIvlspayVSHDPeALTRE-LQEHVKTV 402
Cdd:PRK07059 451 TKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV------VKKDP-ALTEEdVKAFCKER 523
|
250 260 270
....*....|....*....|....*....|.
gi 1958647527 403 TAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:PRK07059 524 LTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
57-435 |
3.59e-52 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 183.72 E-value: 3.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 57 PGWINFRELLRVASPEHNCLRTRSGDSMA-IYFTSGTTGTPK--MVEHS-------QCSYGLG-FVASGRRLM--ALTES 123
Cdd:PRK08974 181 PDAISFRSALHKGRRMQYVKPELVPEDLAfLQYTGGTTGVAKgaMLTHRnmlanleQAKAAYGpLLHPGKELVvtALPLY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 124 DIFWNTTDtgwvkaawtlfsawangaCVFVHEL---------PQvDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTR 193
Cdd:PRK08974 261 HIFALTVN------------------CLLFIELggqnllitnPR-DIPGFVKELKKYPFTAITGVNTLFNALLNnEEFQE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 194 YKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSE-TVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPP 272
Cdd:PRK08974 322 LDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPP 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 273 GKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAE 352
Cdd:PRK08974 402 GEPGELWVK-GPQ----VMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVML 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 353 HPAVLESAVVSSPDPIRGEVVKAFIvlspayVSHDPeALTR-ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK08974 477 HPKVLEVAAVGVPSEVSGEAVKIFV------VKKDP-SLTEeELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
....
gi 1958647527 432 RNQE 435
Cdd:PRK08974 550 RDEA 553
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
82-432 |
6.83e-52 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 177.86 E-value: 6.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPK--MVEHsqcsYGL---GFVAsGRRlMALTESDI----------FwnttdtGWVKAawTLFSAWA 146
Cdd:cd05917 3 DVINIQFTSGTTGSPKgaTLTH----HNIvnnGYFI-GER-LGLTEQDRlcipvplfhcF------GSVLG--VLACLTH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 147 NGACVFVHelPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGL-E 224
Cdd:cd05917 69 GATMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 225 IHEGYGQSETVLICGN-FRGSTI--KSGSMGKASPPYDVQIVDEEGNVLPP-GKEGNIAIRikptrPFCLFNCYLDNPEK 300
Cdd:cd05917 147 VTIAYGMTETSPVSTQtRTDDSIekRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 301 TAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 379
Cdd:cd05917 222 TAEAIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958647527 380 SPayvshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05917 302 KE-----GAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
8-437 |
3.67e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 180.10 E-value: 3.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 8 LTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRPGWINFRELLRVASPEHNCLRTRsGDSMAiy 87
Cdd:PRK08276 70 LTAAEIAYIVDDSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETA-GADML-- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 88 FTSGTTGTPKMVEHSQcSYGLGFVASGRRLMALTesdiFWNTTDTGWV--------KAAWTLFSAWAN--GACVFVheLP 157
Cdd:PRK08276 147 YSSGTTGRPKGIKRPL-PGLDPDEAPGMMLALLG----FGMYGGPDSVylspaplyHTAPLRFGMSALalGGTVVV--ME 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 158 QVDAQTILNTLCRFPITTICCVPTLF-RLLV--QEDLTRYKFQCLRHCLAGGEALNSDVR----DKWknqtGLEIHEGYG 230
Cdd:PRK08276 220 KFDAEEALALIERYRVTHSQLVPTMFvRMLKlpEEVRARYDVSSLRVAIHAAAPCPVEVKramiDWW----GPIIHEYYA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 231 QSEtvlicGNfrGSTI--------KSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAIRiKPTRPFClfncYLDNPEKTA 302
Cdd:PRK08276 296 SSE-----GG--GVTVitsedwlaHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPFE----YHNDPEKTA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 303 ASEQG-DFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLSP 381
Cdd:PRK08276 363 AARNPhGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQP 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647527 382 AYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWG 437
Cdd:PRK08276 441 ADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWE 496
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
13-434 |
1.88e-50 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 178.80 E-value: 1.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 13 LKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLV----SDTSRPGWiNFRELLRVASPEhNCLRTRSGDSMAIYF 88
Cdd:PRK06155 110 LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLdapaSVSVPAGW-STAPLPPLDAPA-PAAAVQPGDTAAILY 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 89 TSGTTGTPKMV--EHSQcSYGLGFVASgrRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVheLPQVDAQTILN 166
Cdd:PRK06155 188 TSGTTGPSKGVccPHAQ-FYWWGRNSA--EDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL--EPRFSASGFWP 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 167 TLCRFPITTI----CCVPTLfrlLVQEDLTRYKFQCLRHCLAGGEAlnSDVRDKWKNQTGLEIHEGYGQSETVLICGNFR 242
Cdd:PRK06155 263 AVRRHGATVTyllgAMVSIL---LSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTH 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 243 GSTiKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPtrPFCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDG 322
Cdd:PRK06155 338 GSQ-RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADG 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 323 YFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTRelqeHVKTV 402
Cdd:PRK06155 415 WFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG-TALEPVALVR----HCEPR 489
|
410 420 430
....*....|....*....|....*....|..
gi 1958647527 403 TAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK06155 490 LAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
9-431 |
5.71e-50 |
|
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: 176.66 E-value: 5.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 9 TQKDLKYRLQAARVKSIITSDALAPHVdaisadcPSLQSRLLVSDTSRPGWINFRELLrVASPEHNCLRTRSG--DSMAI 86
Cdd:cd05904 92 TPAEIAKQVKDSGAKLAFTTAELAEKL-------ASLALPVVLLDSAEFDSLSFSDLL-FEADEAEPPVVVIKqdDVAAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 87 YFTSGTTGTPK--MVEHSqcsyglGFVASgrrlMALTESDIFWNTTDTGWVKAAWTLF----------SAWANGACVFVh 154
Cdd:cd05904 164 LYSSGTTGRSKgvMLTHR------NLIAM----VAQFVAGEGSNSDSEDVFLCVLPMFhiyglssfalGLLRLGATVVV- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 155 eLPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLT-RYKFQCLRHCLAGGEALNSDVRDKWK-NQTGLEIHEGYGQS 232
Cdd:cd05904 233 -MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdKYDLSSLRQIMSGAAPLGKELIEAFRaKFPNVDLGQGYGMT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 233 ET---VLICGNFRGSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPtrpfCLFNCYLDNPEKTAAS--EQ 306
Cdd:cd05904 312 EStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP----SIMKGYLNNPEATAATidKE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 307 GdFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvSH 386
Cdd:cd05904 387 G-WLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG--SS 463
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958647527 387 DPEAltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd05904 464 LTED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
7-434 |
6.34e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 177.66 E-value: 6.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 7 QLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMAI 86
Cdd:PRK07786 100 RLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 87 YFTSGTTGTPK--MVEHSQCSyglGFVASGRRLMAL-TESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHELPQVDAQT 163
Cdd:PRK07786 180 MYTSGTTGRPKgaVLTHANLT---GQAMTCLRTNGAdINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQ 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 164 ILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLRhCLAGGEALNSD--VRDKWKNQTGLEIHEGYGQSE----TVLI 237
Cdd:PRK07786 257 LLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALR-VLSWGAAPASDtlLRQMAATFPEAQILAAFGQTEmspvTCML 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 238 CGNfrGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAH 317
Cdd:PRK07786 336 LGE--DAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR-APT----LMSGYWNNPEATAEAFAGGWFHSGDLVR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 318 MDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALTRELQE 397
Cdd:PRK07786 409 QDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTD 488
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958647527 398 HVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK07786 489 RL----ARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
64-434 |
1.03e-49 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 176.22 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 64 ELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPK--MVEHsqcsyglGFVASGrrlmALTESDiFWnttdtgwvkaAWT- 140
Cdd:PRK07514 139 EAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMLSH-------GNLLSN----ALTLVD-YW----------RFTp 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 141 ---------------LFSA----WANGACVFVheLPQVDAQTILNTLCRfpITTICCVPTLF-RLLVQEDLTRYKFQCLR 200
Cdd:PRK07514 197 ddvlihalpifhthgLFVAtnvaLLAGASMIF--LPKFDPDAVLALMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMR 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 201 HCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGN-FRGSTIkSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNI 278
Cdd:PRK07514 273 LFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNpYDGERR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMI 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 279 AIRiKPTrpfcLFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVL 357
Cdd:PRK07514 352 EVK-GPN----VFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVV 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958647527 358 ESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK07514 427 ESAVIGVPHPDFGEGVTAVVVPKPG-AALDEAAILAALKGRL----ARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
9-433 |
1.10e-49 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 177.38 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 9 TQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQS------------------------RLLVSDTSRPGWINFRE 64
Cdd:PRK08751 111 TPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVittglgdmlgfpkaalvnfvvkyvKKLVPEYRINGAIRFRE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 65 LLRVASpEHNC--LRTRSGDSMAIYFTSGTTGTPKmvehsqcsyglGFVASGRRLMALTESDIFWNTTdTGWVKAA---- 138
Cdd:PRK08751 191 ALALGR-KHSMptLQIEPDDIAFLQYTGGTTGVAK-----------GAMLTHRNLVANMQQAHQWLAG-TGKLEEGcevv 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 139 ------WTLFSAWAN-------GACVFVHELPQvDAQTILNTLCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRHCLA 204
Cdd:PRK08751 258 italplYHIFALTANglvfmkiGGCNHLISNPR-DMPGFVKELKKTRFTAFTGVNTLFNgLLNTPGFDQIDFSSLKMTLG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 205 GGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiK 283
Cdd:PRK08751 337 GGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK-G 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 284 PTrpfcLFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 362
Cdd:PRK08751 416 PQ----VMKGYWKRPEETAKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAV 491
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958647527 363 SSPDPIRGEVVKAFIvlspayVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:PRK08751 492 GVPDEKSGEIVKVVI------VKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
19-436 |
2.23e-49 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 175.27 E-value: 2.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 19 AARVkSIITSDALAPHVDAISADC--------PSLQSRLLVSD---TSRPGWINFRELLrVASPEHNCLRTRSGDSMaIY 87
Cdd:PRK12406 83 GARV-LIAHADLLHGLASALPAGVtvlsvptpPEIAAAYRISPallTPPAGAIDWEGWL-AQQEPYDGPPVPQPQSM-IY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 88 fTSGTTGTPKMV-------EHSQcSYGL------GFVASGRRLMA--LTESdifwnttdtgwVKAAWTLFSAWANGACVF 152
Cdd:PRK12406 160 -TSGTTGHPKGVrraaptpEQAA-AAEQmraliyGLKPGIRALLTgpLYHS-----------APNAYGLRAGRLGGVLVL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 153 vheLPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKF--QCLRHCLAGGEALNSDVR----DKWknqtGLEI 225
Cdd:PRK12406 227 ---QPRFDPEELLQLIERHRITHMHMVPTMFiRLLKLPEEVRAKYdvSSLRHVIHAAAPCPADVKramiEWW----GPVI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 226 HEGYGQSETVLIcgNFRGST---IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRPFClfncYLDNPEKTA 302
Cdd:PRK12406 300 YEYYGSTESGAV--TFATSEdalSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFT----YHNKPEKRA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 303 ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPA 382
Cdd:PRK12406 374 EIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958647527 383 yVSHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 436
Cdd:PRK12406 454 -ATLDEADIRAQLKARL----AGYKVPKHIEIMAELPREDSGKIFKRRLRDPYW 502
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
7-432 |
3.70e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 174.81 E-value: 3.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 7 QLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPslqsrLLVSDTSR-PGWINFRELLRVASP---EHNClrtrsgd 82
Cdd:PRK13390 82 HLTAPEADYIVGDSGARVLVASAALDGLAAKVGADLP-----LRLSFGGEiDGFGSFEAALAGAGPrltEQPC------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 83 SMAIYFTSGTTGTPKMV-----EHSQCSYGLGFVASGRRLMALTESDIFWNTTdtgwvkaawTLFSAWANGACVFVHEL- 156
Cdd:PRK13390 150 GAVMLYSSGTTGFPKGIqpdlpGRDVDAPGDPIVAIARAFYDISESDIYYSSA---------PIYHAAPLRWCSMVHALg 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 157 ------PQVDAQTILNTLCRFPITTICCVPTLF-RLLVQED--LTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHE 227
Cdd:PRK13390 221 gtvvlaKRFDAQATLGHVERYRITVTQMVPTMFvRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 228 GYGQSE----TVLICGNFRGstiKSGSMGKaSPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTRPFClfncYLDNPEKTAA 303
Cdd:PRK13390 301 YYSSTEahgmTFIDSPDWLA---HPGSVGR-SVLGDLHICDDDGNELPAGRIGTVYFE-RDRLPFR----YLNDPEKTAA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 304 SEQ--GDFYIT-GDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLS 380
Cdd:PRK13390 372 AQHpaHPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLV 451
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958647527 381 PAYvshDP-EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:PRK13390 452 EGI---RGsDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
82-432 |
5.91e-49 |
|
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: 171.76 E-value: 5.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPKMVEHS---------QCSYGLGFVASGRRLMALTesdIFWnttdtgwVKAAWTLFSAWANGACVF 152
Cdd:cd05912 78 DIATIMYTSGTTGKPKGVQQTfgnhwwsaiGSALNLGLTEDDNWLCALP---LFH-------ISGLSILMRSVIYGMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 153 VHElpQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRY--KFQCLrhcLAGGEALNSDVRDKWKnQTGLEIHEGYG 230
Cdd:cd05912 148 LVD--KFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYpnNLRCI---LLGGGPAPKPLLEQCK-EKGIPVYQSYG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 231 QSETV--LICGNFRGSTIKSGSMGKASPPYDVQIVDEEGnvlPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD 308
Cdd:cd05912 222 MTETCsqIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLK-GPN----VTKGYLNRPDATEESFENG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 309 FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDp 388
Cdd:cd05912 294 WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEE- 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958647527 389 ealtrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05912 372 -----ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELK 410
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
5-431 |
2.22e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 173.69 E-value: 2.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 5 ISQLTQK-DLKYRLQAARVKSIITSDALAPHVDAISADC-----------------PSLQSRLLVSDTSR--PGWINFRE 64
Cdd:PRK06178 113 VSPLFREhELSYELNDAGAEVLLALDQLAPVVEQVRAETslrhvivtsladvlpaePTLPLPDSLRAPRLaaAGAIDLLP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 65 LLRvASPEHNCLRTRSGDSMA-IYFTSGTTGTPKMVEHSQ-------CSYGLGFVASGRRLMALTESDIFW-NTTDTGwv 135
Cdd:PRK06178 193 ALR-ACTAPVPLPPPALDALAaLNYTGGTTGMPKGCEHTQrdmvytaAAAYAVAVVGGEDSVFLSFLPEFWiAGENFG-- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 136 kaawTLFSAWANGACVFvheLPQVDAQTILNTLCRFPIT-TICCVPTLFRLLVQEDLTRYKFQCLRH--CLAGGEALNSD 212
Cdd:PRK06178 270 ----LLFPLFSGATLVL---LARWDAVAFMAAVERYRVTrTVMLVDNAVELMDHPRFAEYDLSSLRQvrVVSFVKKLNPD 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 213 VRDKWKNQTGLEIHEG-YGQSETvLICGNF-RGstIKSGSM---------GKASPPYDVQIVDEE-GNVLPPGKEGNIAI 280
Cdd:PRK06178 343 YRQRWRALTGSVLAEAaWGMTET-HTCDTFtAG--FQDDDFdllsqpvfvGLPVPGTEFKICDFEtGELLPLGAEGEIVV 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 281 RiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESA 360
Cdd:PRK06178 420 R-TPS----LLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSA 494
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958647527 361 VVSSPDPIRGEVVKAFIVLSPAYvSHDPEALTRELQEHVktvtAPYKYPrKVAFISELPKTVSGKILRSKL 431
Cdd:PRK06178 495 VVGRPDPDKGQVPVAFVQLKPGA-DLTAAALQAWCRENM----AVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
57-432 |
2.35e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 173.65 E-value: 2.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 57 PGWINFRELLRVASPEH----NCLRTRSGDSMAIYFTSGTTGTPKMVEhsqcsyglgfvasgrrlmaLTESDIFWNTTD- 131
Cdd:PRK05605 191 PGTVPWETLVDAAIGGDgsdvSHPRPTPDDVALILYTSGTTGKPKGAQ-------------------LTHRNLFANAAQg 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 132 TGWVK----------AAWTLFSAWANGAC----VFVHE----LPQVDAQTILNTLCRFPITTICCVPTLFRLLVQE---- 189
Cdd:PRK05605 252 KAWVPglgdgpervlAALPMFHAYGLTLCltlaVSIGGelvlLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeer 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 190 --DLTRykfqcLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTIKSGSMGKASPPYDVQIVDEE 266
Cdd:PRK05605 332 gvDLSG-----VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 267 --GNVLPPGKEGNIAIRiKPTRpfclFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPV 344
Cdd:PRK05605 407 dpDETMPDGEEGELLVR-GPQV----FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPA 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 345 EVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEAltreLQEHVKTVTAPYKYPRKVAFISELPKTVSG 424
Cdd:PRK05605 482 EVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEG----LRAYCREHLTRYKVPRRFYHVDELPRDQLG 556
|
....*...
gi 1958647527 425 KILRSKLR 432
Cdd:PRK05605 557 KVRRREVR 564
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
86-428 |
8.99e-48 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 173.21 E-value: 8.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 86 IYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVHE-LP-QVDAq 162
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGhSYIVYAPLLAGMATIMYEgLPtRPDA- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 163 TILNTLC-RFPITTICCVPTLFRLLVQED---LTRYKFQCLRHC-LAG-----------GEALNSDVRDK-WKNQTG--- 222
Cdd:PRK10524 317 GIWWRIVeKYKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLRALfLAGepldeptaswiSEALGVPVIDNyWQTETGwpi 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 223 LEIHEGYGQSETvlicgnfrgstiKSGSMGKASPPYDVQIVDEE-GNVLPPGKEGNIAIRiKPTRPFCLFNCYLDNPE-- 299
Cdd:PRK10524 397 LAIARGVEDRPT------------RLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIE-GPLPPGCMQTVWGDDDRfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 300 KTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 378
Cdd:PRK10524 464 KTYWSLFGRqVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVV 543
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958647527 379 LSPAYVSHDPE---ALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 428
Cdd:PRK10524 544 PKDSDSLADREarlALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
8-433 |
1.42e-47 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 169.76 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 8 LTQKDLKYRLQAARVKSIITSDALAphvDAISADCPSLQSRLLVSDTSRPGWINFRELLRVASpehnclrtrsgdsmaIY 87
Cdd:PRK03640 86 LSREELLWQLDDAEVKCLITDDDFE---AKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVAT---------------IM 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 88 FTSGTTGTPKMVehsQCSYGLGFV-ASGRRL-MALTESDifwnttdtGWVkAAWTLF-----SAWAN----GACVFVHEl 156
Cdd:PRK03640 148 YTSGTTGKPKGV---IQTYGNHWWsAVGSALnLGLTEDD--------CWL-AAVPIFhisglSILMRsviyGMRVVLVE- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 157 pQVDAQTILNTLCRFPITTICCVPT-LFRLLVQEDLTRY--KFQCLrhcLAGGEALNSDVRDKWKnQTGLEIHEGYGQSE 233
Cdd:PRK03640 215 -KFDAEKINKLLQTGGVTIISVVSTmLQRLLERLGEGTYpsSFRCM---LLGGGPAPKPLLEQCK-EKGIPVYQSYGMTE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 234 TV-LICG-NFRGSTIKSGSMGKASPPYDVQIVDEeGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYI 311
Cdd:PRK03640 290 TAsQIVTlSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVK-GPN----VTKGYLNREDATRETFQDGWFK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 312 TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayvSHDPEAl 391
Cdd:PRK03640 364 TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS----GEVTEE- 438
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958647527 392 trELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:PRK03640 439 --ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQ 478
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
82-432 |
5.12e-47 |
|
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: 168.00 E-value: 5.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPK--MVEHSQCSYGLGFVASgrrLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHELPQV 159
Cdd:cd05922 118 DLALLLYTSGSTGSPKlvRLSHQNLLANARSIAE---YLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 160 DAQTIlnTLCR-FPITTICCVPTLFRLLVQEDLTRYKFQCLRHCL-AGG---EALNSDVRDKWKnqtGLEIHEGYGQSET 234
Cdd:cd05922 195 DDAFW--EDLReHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTqAGGrlpQETIARLRELLP---GAQVYVMYGQTEA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 235 vlicgnFRGSTI--------KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAirikPTRPFCLFNCYLDNPEKTAASEQ 306
Cdd:cd05922 270 ------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIV----HRGPNVMKGYWNDPPYRRKEGRG 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 307 GDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIrGEVVKAFIVLSPAYvsh 386
Cdd:cd05922 340 GGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKI--- 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958647527 387 DPEALTRELQEhvktVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05922 416 DPKDVLRSLAE----RLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
156-435 |
5.26e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 169.83 E-value: 5.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 LPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTR-YKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSET 234
Cdd:PRK06710 281 IPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKeYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTES 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 235 VLIC-GNFRGSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYIT 312
Cdd:PRK06710 361 SPVThSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK-GPQ----IMKGYWNKPEETAAVLQDGWLHT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 313 GDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayvSHDPEALT 392
Cdd:PRK06710 436 GDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVL-----KEGTECSE 510
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958647527 393 RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 435
Cdd:PRK06710 511 EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
17-432 |
8.37e-47 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 170.52 E-value: 8.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 17 LQAARVKSIIT------SDaLAPHVDAISADCPSLQSRLLVsDTSR--PGW----------------INF-RELLRVASP 71
Cdd:PRK07529 125 LRAAGAKVLVTlgpfpgTD-IWQKVAEVLAALPELRTVVEV-DLARylPGPkrlavplirrkahariLDFdAELARQPGD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 72 EHNCLRTRSGDSMAIYF-TSGTTGTPKMVEHSqcsYGlGFVA---SGRRLMALTESDIFWNTTDTGWVKAAW-TLFSAWA 146
Cdd:PRK07529 203 RLFSGRPIGPDDVAAYFhTGGTTGMPKLAQHT---HG-NEVAnawLGALLLGLGPGDTVFCGLPLFHVNALLvTGLAPLA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 147 NGACVfVHELPQ--------------VDaqtilntlcRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSD 212
Cdd:PRK07529 279 RGAHV-VLATPQgyrgpgvianfwkiVE---------RYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 213 VRDKWKNQTGLEIHEGYGQSE-TVLICGNFRGSTIKSGSMGKASPPYDVQIV--DEEGNVL---PPGKEGNIAIRiKPTr 286
Cdd:PRK07529 349 VFRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIA-GPN- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 287 pfcLFNCYLdNPEKTAASE-QGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSP 365
Cdd:PRK07529 427 ---VFSGYL-EAAHNKGLWlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRP 502
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958647527 366 DPIRGEVVKAFIVLSP-AYVSHDpealtrELQEHVKTVTA-PYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:PRK07529 503 DAHAGELPVAYVQLKPgASATEA------ELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
15-433 |
7.44e-46 |
|
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: 165.88 E-value: 7.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 15 YRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSD------TSRPGWINFRELLRVASPEHNCLRTRSGDSMAIYF 88
Cdd:cd12119 91 YIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDdaampePAGVGVLAYEELLAAESPEYDWPDFDENTAAAICY 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 89 TSGTTGTPKMVEHSQCS---YGLGFVASGrrLMALTESDIFWNTTDTGWVkAAWTL-FSAWANGACvFVHELPQVDAQTI 164
Cdd:cd12119 171 TSGTTGNPKGVVYSHRSlvlHAMAALLTD--GLGLSESDVVLPVVPMFHV-NAWGLpYAAAMVGAK-LVLPGPYLDPASL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 165 LNTLCRFPITTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGGEALNSDVRDKWKnQTGLEIHEGYGQSET--VLICGNF 241
Cdd:cd12119 247 AELIEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIEAFE-ERGVRVIHAWGMTETspLGTVARP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 242 RGSTIKSGSMGKAS-------PPYDVQ--IVDEEGNVLP-PGKE-GNIAIRikptRPFcLFNCYLDNPEKTAASEQGDFY 310
Cdd:cd12119 326 PSEHSNLSEDEQLAlrakqgrPVPGVElrIVDDDGRELPwDGKAvGELQVR----GPW-VTKSYYKNDEESEALTEDGWL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 311 ITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP-AYVSHDpe 389
Cdd:cd12119 401 RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEgATVTAE-- 478
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958647527 390 altrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:cd12119 479 ----ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
17-432 |
2.61e-45 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 164.93 E-value: 2.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 17 LQAARVKSIITSDALAPHVDAISADCPslQSRLLVSDTSRPGWINFRELlrVASPEHNCLRTRSGDSMAIYFTSGTTGTP 96
Cdd:PRK13382 136 VTREGVDTVIYDEEFSATVDRALADCP--QATRIVAWTDEDHDLTVEVL--IAAHAGQRPEPTGRKGRVILLTSGTTGTP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 97 KMVEHSqcsyGLGFVASGRRLMalteSDIFWNTTDTGWVKAAwtLFSAWANGACVFVHELP-------QVDAQTILNTLC 169
Cdd:PRK13382 212 KGARRS----GPGGIGTLKAIL----DRTPWRAEEPTVIVAP--MFHAWGFSQLVLAASLActivtrrRFDPEATLDLID 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 170 RFPITTICCVPTLFRL---LVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLIC-GNFRGST 245
Cdd:PRK13382 282 RHRATGLAVVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIAtATPADLR 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 246 IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYldNPEKTAASEQGdFYITGDRAHMDEDGYFW 325
Cdd:PRK13382 362 AAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRND-----TQFDGY--TSGSTKDFHDG-FMASGDVGYLDENGRLF 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 326 FVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvshDPEALTRELQEHVKTVTAP 405
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-----GASATPETLKQHVRDNLAN 508
|
410 420
....*....|....*....|....*..
gi 1958647527 406 YKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:PRK13382 509 YKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
6-438 |
3.08e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 164.09 E-value: 3.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 6 SQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLV-SDTSRPGWINFRELLRvASPEHNCLRTRSGDSM 84
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVA-GLPATPIADESLGTDM 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 85 aiYFTSGTTGTPKMVE----HSQCSYGLGFVASGRRLMALTESDIF------WNTTDTGWVKAAWTLfsawanGACVFVH 154
Cdd:PRK13391 160 --LYSSGTTGRPKGIKrplpEQPPDTPLPLTAFLQRLWGFRSDMVYlspaplYHSAPQRAVMLVIRL------GGTVIVM 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 155 ElpQVDAQTILNTLCRFPITTICCVPTLF-RLLV--QEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQ 231
Cdd:PRK13391 232 E--HFDAEQYLALIEEYGVTHTQLVPTMFsRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 232 SETVLICG-NFRGSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAIriKPTRPFClfncYLDNPEKTAAS--EQGD 308
Cdd:PRK13391 310 TEGLGFTAcDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWF--EGGRPFE----YLNDPAKTAEArhPDGT 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 309 FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDP 388
Cdd:PRK13391 383 WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDG-VDPGP 461
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958647527 389 EaLTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 438
Cdd:PRK13391 462 A-LAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGN 510
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
7-434 |
2.74e-44 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 161.18 E-value: 2.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 7 QLTQKDLKYRLQAARVKSIITSDALAPHVDAISAdcpslqsrllVSDTSRPGWINFRELLRVASPEhNCLRTRSGDSMAI 86
Cdd:PRK06839 86 RLTENELIFQLKDSGTTVLFVEKTFQNMALSMQK----------VSYVQRVISITSLKEIEDRKID-NFVEKNESASFII 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 87 YFTSGTTGTPKmvehsqcsyglGFVasgrrlmaLTESDIFWN------TTDTGWVKAAWTL-------------FSAWAN 147
Cdd:PRK06839 155 CYTSGTTGKPK-----------GAV--------LTQENMFWNalnntfAIDLTMHDRSIVLlplfhiggiglfaFPTLFA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 148 GACVFVHElpQVDAQTILNTLCRFPITTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQtGLEIH 226
Cdd:PRK06839 216 GGVIIVPR--KFEPTKALSMIEKHKVTVVMGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 227 EGYGQSET-----VLICGNFRGstiKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKT 301
Cdd:PRK06839 293 QGFGMTETsptvfMLSEEDARR---KVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIR-GPN----VMKEYWNRPDAT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 302 AASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP 381
Cdd:PRK06839 365 EETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958647527 382 AYVshdpeALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK06839 445 SSV-----LIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
181-435 |
5.05e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 161.85 E-value: 5.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 181 TLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGStIKSGSMGKASPPY 258
Cdd:PRK05677 309 TLFVALCNnEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQA-IQVGTIGIPVPST 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 259 DVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSS 337
Cdd:PRK05677 388 LCKVIDDDGNELPLGEVGELCVK-GPQ----VMKGYWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVS 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 338 SYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpEALTRE-LQEHVKTVTAPYKYPRKVAFIS 416
Cdd:PRK05677 463 GFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG------ETLTKEqVMEHMRANLTGYKVPKAVEFRD 536
|
250
....*....|....*....
gi 1958647527 417 ELPKTVSGKILRSKLRNQE 435
Cdd:PRK05677 537 ELPTTNVGKILRRELRDEE 555
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
13-438 |
9.02e-44 |
|
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: 164.26 E-value: 9.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 13 LKYRLQAARVKSIITSDALAPHVdaisadcPSLQSRLLVSDTSRPGwinfrellrvASPEHNCLRTRSGDSMA-IYFTSG 91
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARL-------PELGVPVLALDALALA----------AEPATNPPVPVTPDDLAyVIYTSG 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 92 TTGTPK--MVEHSqcsyGLG-FVASGRRLMALTESDIF-WNTT---DTgwvkAAWTLFSAWANGAC-VFVHELPQVDAQT 163
Cdd:COG1020 628 STGRPKgvMVEHR----ALVnLLAWMQRRYGLGPGDRVlQFASlsfDA----SVWEIFGALLSGATlVLAPPEARRDPAA 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 164 ILNTLCRFPITTICCVPTLFRLLVQEDLTRykFQCLRHCLAGGEALNSDVRDKWKNQT-GLEIHEGYGQSETVlICGNFR 242
Cdd:COG1020 700 LAELLARHRVTVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETT-VDSTYY 776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 243 gsTIKSGSMGKASPPY-------DVQIVDEEGNVLPPGKEGNIAI------RikptrpfclfnCYLDNPEKTAA------ 303
Cdd:COG1020 777 --EVTPPDADGGSVPIgrpiantRVYVLDAHLQPVPVGVPGELYIggaglaR-----------GYLNRPELTAErfvadp 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 304 -SEQGD-FYITGDRAHMDEDGYFWFVGRNDD-V-INSssYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 379
Cdd:COG1020 844 fGFPGArLYRTGDLARWLPDGNLEFLGRADDqVkIRG--FRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVP 921
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958647527 380 SPayvshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 438
Cdd:COG1020 922 EA-----GAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAA 975
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
23-432 |
9.29e-44 |
|
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: 159.47 E-value: 9.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 23 KSIITSDALAPHVDAISAdCPSLQSRLLVSDTSrPGWINFrELLRVASPEHNCLRTRSGDSMaiYFTSGTTGTPKMVEHS 102
Cdd:cd05929 72 KSSRAPRAEACAIIEIKA-AALVCGLFTGGGAL-DGLEDY-EAAEGGSPETPIEDEAAGWKM--LYSGGTTGRPKGIKRG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 103 ------------QCSYGLGFVASGRRLMalteSDIFWNTTDTGWVkaawtlFSAWANGACVFVheLPQVDAQTILNTLCR 170
Cdd:cd05929 147 lpggppdndtlmAAALGFGPGADSVYLS----PAPLYHAAPFRWS------MTALFMGGTLVL--MEKFDPEEFLRLIER 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 171 FPITTICCVPTLF-RLLVQEDLTRYKFQ--CLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVlicgnfrGSTIK 247
Cdd:cd05929 215 YRVTFAQFVPTMFvRLLKLPEAVRNAYDlsSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-------GLTII 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 248 S--------GSMGKASPPyDVQIVDEEGNVLPPGKEGNIAIRIKPTrpfclFNcYLDNPEKTAASEQGDFYIT-GDRAHM 318
Cdd:cd05929 288 NgeewlthpGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG-----FE-YTNDPEKTAAARNEGGWSTlGDVGYL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 319 DEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLSPAYVSHDPEALTRELQEH 398
Cdd:cd05929 361 DEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGADAGTALAEELIAF 438
|
410 420 430
....*....|....*....|....*....|....
gi 1958647527 399 VKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05929 439 LRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
19-435 |
1.88e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 160.09 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 19 AAR--VKSIITSDALAPHVDAISADCPSLQSRLLVSD---TSRPGWINFRELlrVASPEHNCLRTRSGDSMAIYFTSGTT 93
Cdd:PRK07788 142 AARegVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDddePSGSTDETLDDL--IAGSSTAPLPKPPKPGGIVILTSGTT 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 94 GTPKMVEHSQCSyGLGFVAS-------GRRLMALTESDIFWNTtdtGWvkAAWTLfsAWANGACVFVHElpQVDAQTILN 166
Cdd:PRK07788 220 GTPKGAPRPEPS-PLAPLAGllsrvpfRAGETTLLPAPMFHAT---GW--AHLTL--AMALGSTVVLRR--RFDPEATLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 167 TLCRFPITTICCVPTLFRLLV---QEDLTRYKFQCLRHCLAGGEALNSDVrdkwknqtGLEIHEGYGQsetvLICgNFRG 243
Cdd:PRK07788 290 DIAKHKATALVVVPVMLSRILdlgPEVLAKYDTSSLKIIFVSGSALSPEL--------ATRALEAFGP----VLY-NLYG 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 244 ST--------------IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIairikptrpFC----LFNCYLDNPEKTAAse 305
Cdd:PRK07788 357 STevafatiatpedlaEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRI---------FVgngfPFEGYTDGRDKQII-- 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 306 qGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvs 385
Cdd:PRK07788 426 -DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG--- 501
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958647527 386 hdpEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 435
Cdd:PRK07788 502 ---AALDEDaIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
8-432 |
1.99e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 159.44 E-value: 1.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 8 LTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLqsRLLVSDTSRPGWINFRELLR--------VASPEHNclrtr 79
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDL--THVVAIGGARAGLDYEALVArhlgarvaNAAVDHD----- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 80 sgDSMAIYFTSGTTGTPK--MVEHSQcsygLGFVASGRRlmalteSDIFWNTT--DTGWVKAAWTlfsawaNGACVfvHE 155
Cdd:PRK07470 164 --DPCWFFFTSGTTGRPKaaVLTHGQ----MAFVITNHL------ADLMPGTTeqDASLVVAPLS------HGAGI--HQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 LPQV--DAQTILNTLCRFPI------------TTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQ 220
Cdd:PRK07470 224 LCQVarGAATVLLPSERFDPaevwalverhrvTNLFTVPTILKMLVEhPAVDRYDHSSLRYVIYAGAPMYRADQKRALAK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 221 TGLEIHEGYGQSE-----TVL-ICGNFR--GSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFN 292
Cdd:PRK07470 304 LGKVLVQYFGLGEvtgniTVLpPALHDAedGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPA-----VFA 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 293 CYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 372
Cdd:PRK07470 379 GYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEV 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958647527 373 VKAFIVLS-PAYVSHDpealtrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:PRK07470 459 GVAVCVARdGAPVDEA------ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
35-362 |
2.03e-43 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 157.04 E-value: 2.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 35 VDAISADCpslQSRLLVSDT---SRPGWINFRELLRV----------ASPEHNCLRTRSGDSMAIYFTSGTTGTPK--MV 99
Cdd:TIGR01733 64 LAFILEDA---GARLLLTDSalaSRLAGLVLPVILLDplelaalddaPAPPPPDAPSGPDDLAYVIYTSGSTGRPKgvVV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 100 EHSQCSYglgFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVheLPQVDAQTILNTLCRF----PITT 175
Cdd:TIGR01733 141 THRSLVN---LLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVV--PPEDEERDDAALLAALiaehPVTV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 176 ICCVPTLFRLLVQEDLTRykFQCLRHCLAGGEALNSDVRDKWKNQTG-LEIHEGYGQSETVLICGNFRGSTIKSGSM--- 251
Cdd:TIGR01733 216 LNLTPSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLVDPDDAPREspv 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 252 --GKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAA---------SEQGDFYITGDRAHMDE 320
Cdd:TIGR01733 294 piGRPLANTRLYVLDDDLRPVPVGVVGELYIGGP-----GVARGYLNRPELTAErfvpdpfagGDGARLYRTGDLVRYLP 368
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958647527 321 DGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVlESAVV 362
Cdd:TIGR01733 369 DGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGV-REAVV 409
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
180-428 |
2.98e-43 |
|
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: 154.74 E-value: 2.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 180 PTLFRLLVQEDLTRYKFQCLRHcLAGGEAlnSDVRDKWKNQTGLEIHEGYGQSETV-LICgnFRGSTIKSGSMGKASPPY 258
Cdd:cd17637 97 PILSNLLDAAEKSGVDLSSLRH-VLGLDA--PETIQRFEETTGATFWSLYGQTETSgLVT--LSPYRERPGSAGRPGPLV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 259 DVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRN--DDVINS 336
Cdd:cd17637 172 RVRIVDDNDRPVPAGETGEIVVR-GPL----VFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKP 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 337 SSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpEALT-RELQEHVKTVTAPYKYPRKVAFI 415
Cdd:cd17637 247 GGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG------ATLTaDELIEFVGSRIARYKKPRYVVFV 320
|
250
....*....|...
gi 1958647527 416 SELPKTVSGKILR 428
Cdd:cd17637 321 EALPKTADGSIDR 333
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
12-432 |
3.48e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 159.55 E-value: 3.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 12 DLKYRLQAARVKSIITSDA------------LAPHV------DAISADCPSLQSRLLVSDTSRPGWINFRELLRVA---S 70
Cdd:PRK12583 108 ELEYALGQSGVRWVICADAfktsdyhamlqeLLPGLaegqpgALACERLPELRGVVSLAPAPPPGFLAWHELQARGetvS 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 71 PEHNCLRT---RSGDSMAIYFTSGTTGTPK--MVEHSQCSYGLGFVAsgrRLMALTESDI------FWNTTdtGWVKAAw 139
Cdd:PRK12583 188 REALAERQaslDRDDPINIQYTSGTTGFPKgaTLSHHNILNNGYFVA---ESLGLTEHDRlcvpvpLYHCF--GMVLAN- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 140 tlFSAWANGACVfVHELPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWK 218
Cdd:PRK12583 262 --LGCMTVGACL-VYPNEAFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVM 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 219 NQTGL-EIHEGYGQSET---VLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAirikpTRPFCLFNCY 294
Cdd:PRK12583 339 DEMHMaEVQIAYGMTETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC-----TRGYSVMKGY 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 295 LDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVV 373
Cdd:PRK12583 414 WNNPEATAESIDEDGWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEI 493
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958647527 374 KAFIVLSPayvshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:PRK12583 494 VAWVRLHP-----GHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
12-437 |
6.96e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 157.84 E-value: 6.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 12 DLKYRLQAARVKSIITSDAlaPHVD---AISADCPSLQSRLLVSDTsrPGWINFRELLRVASPEHNCLRTRSGDSMAIYF 88
Cdd:PRK06188 100 DHAYVLEDAGISTLIVDPA--PFVEralALLARVPSLKHVLTLGPV--PDGVDLLAAAAKFGPAPLVAAALPPDIAGLAY 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 89 TSGTTGTPKMVEHSQcsyglgfvasgRRLMALTEsdifWNTTDTGWVKAAWTLFSA---WANGACV--------FVHELP 157
Cdd:PRK06188 176 TGGTTGKPKGVMGTH-----------RSIATMAQ----IQLAEWEWPADPRFLMCTplsHAGGAFFlptllrggTVIVLA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 158 QVDAQTILNTLCRFPITTICCVPT-LFRLLVQEDLTRYKFQCLRHCLAGGEALNSDvrdkwKNQTGLEI-----HEGYGQ 231
Cdd:PRK06188 241 KFDPAEVLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYYGASPMSPV-----RLAEAIERfgpifAQYYGQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 232 SE-----TVLICGNFRGSTIK-SGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptRPFcLFNCYLDNPEKTAASE 305
Cdd:PRK06188 316 TEapmviTYLRKRDHDPDDPKrLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVR----GPL-VMDGYWNRPEETAEAF 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 306 QGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVS 385
Cdd:PRK06188 391 RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG-AA 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 386 HDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWG 437
Cdd:PRK06188 470 VDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWE 517
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
32-431 |
1.26e-42 |
|
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: 156.67 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 32 APHVDAISADCPSlqsRLLVSDTSRPGWinFRELLRVASPEHNCLRTRSG---------DSMA-IYFTSGTTGTPK--MV 99
Cdd:cd17646 84 ADRLAYMLADAGP---AVVLTTADLAAR--LPAGGDVALLGDEALAAPPAtpplvpprpDNLAyVIYTSGSTGRPKgvMV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 100 EHS---------QCSYGLGfvASGRRLMAltesdifwntTDTGWVKAAWTLFSAWANGACVFVHElP--QVDAQTILNTL 168
Cdd:cd17646 159 THAgivnrllwmQDEYPLG--PGDRVLQK----------TPLSFDVSVWELFWPLVAGARLVVAR-PggHRDPAYLAALI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 169 CRFPITTICCVPTLFRLLVQEdLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVL------ICGNFR 242
Cdd:cd17646 226 REHGVTTCHFVPSMLRVFLAE-PAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIdvthwpVRGPAE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 243 GSTIksgSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIR-IKPTRPfclfncYLDNPEKTAAS------EQGD-FYITGD 314
Cdd:cd17646 305 TPSV---PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGgVQLARG------YLGRPALTAERfvpdpfGPGSrMYRTGD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 315 RAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALTRE 394
Cdd:cd17646 376 LARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAALRAH 455
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958647527 395 LQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd17646 456 LAERL----PEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
46-433 |
1.31e-42 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 156.69 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 46 QSRLLVSDTSrpgwINFRELLRVASPEHNCLRTRSG-DSMAIYFTSGTTGTPKMVEHSQcsyglgfvaSGRRLMALtESD 124
Cdd:cd12118 101 EAKVLFVDRE----FEYEDLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHH---------RGAYLNAL-ANI 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 125 IFWNT-TDTGWVkaaWTL--FSA------WANGACVFVHE-LPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTR 193
Cdd:cd12118 167 LEWEMkQHPVYL---WTLpmFHCngwcfpWTVAAVGGTNVcLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANaPPSDA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 194 YKFQCLRHCLAGGEALNSDVRDKwKNQTGLEIHEGYGQSET---VLICG-----NFRGSTIKSGSMGKASPPY----DVQ 261
Cdd:cd12118 244 RPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTETygpATVCAwkpewDELPTEERARLKARQGVRYvgleEVD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 262 IVDEEGNVLPP--GKE-GNIAIRIKptrpfCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSS 338
Cdd:cd12118 323 VLDPETMKPVPrdGKTiGEIVFRGN-----IVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGG 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 339 YRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshdpEALTRELQEHVKTVTAPYKYPRKVAFiSEL 418
Cdd:cd12118 398 ENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGA-----KVTEEEIIAFCREHLAGFMVPKTVVF-GEL 471
|
410
....*....|....*
gi 1958647527 419 PKTVSGKILRSKLRN 433
Cdd:cd12118 472 PKTSTGKIQKFVLRD 486
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
81-432 |
2.06e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 153.02 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 81 GDSMAIYF-TSGTTGTPKMVEHSQCsyglGFVAS---GRRLMALTESDIFWNTTDTGWVKAAW-TLFSAWANGACVFV-- 153
Cdd:cd05944 1 SDDVAAYFhTGGTTGTPKLAQHTHS----NEVYNawmLALNSLFDPDDVLLCGLPLFHVNGSVvTLLTPLASGAHVVLag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 154 ---HELPQVdAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRyKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYG 230
Cdd:cd05944 77 pagYRNPGL-FDNFWKLVERYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 231 QSE-TVLICGNFRGSTIKSGSMGKASPPYDVQIV--DEEGNVL---PPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAAS 304
Cdd:cd05944 155 LTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLrdcAPDEVGEICVA-GPG----VFGGYLYTEGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 305 EQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP-AY 383
Cdd:cd05944 230 VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPgAV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958647527 384 VShdPEALTRELQEHVKTVTApykYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05944 310 VE--EEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
86-435 |
8.67e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 153.99 E-value: 8.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 86 IYFTSGTTGTPKmvehsqcsyglGFVASgRRLMAltesdifwntTDTGWVKAAWtlfsAWaNGACVFVHELP--QVDAqT 163
Cdd:PRK07787 133 IVYTSGTTGPPK-----------GVVLS-RRAIA----------ADLDALAEAW----QW-TADDVLVHGLPlfHVHG-L 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 164 ILNTL-----------------------CRFPITTICCVPTLF-RLLVQEDLTRyKFQCLRHCLAGGEALNSDVRDKWKN 219
Cdd:PRK07787 185 VLGVLgplrignrfvhtgrptpeayaqaLSEGGTLYFGVPTVWsRIAADPEAAR-ALRGARLLVSGSAALPVPVFDRLAA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 220 QTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKE--GNIAIRiKPTrpfcLFNCYLDN 297
Cdd:PRK07787 264 LTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVR-GPT----LFDGYLNR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 298 PEKTAASEQGD-FYITGDRAHMDEDGYFWFVGRND-DVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKA 375
Cdd:PRK07787 339 PDATAAAFTADgWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVA 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 376 FIvlspayVSHDPEALTrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 435
Cdd:PRK07787 419 YV------VGADDVAAD-ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
88-433 |
1.07e-41 |
|
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: 150.17 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 88 FTSGTTGTPKMVEHSQ----------CSYgLGFVASGRRLMALTESDIfwnttdTG---WVKAAWTlfsawanGACVFVH 154
Cdd:cd17630 7 LTSGSTGTPKAVVHTAanllasaaglHSR-LGFGGGDSWLLSLPLYHV------GGlaiLVRSLLA-------GAELVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 155 ELPQVDAQTILntlcRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQtGLEIHEGYGQSET 234
Cdd:cd17630 73 ERNQALAEDLA----PPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 235 V-LICGNFRGSTiKSGSMGKASPPYDVQIVDEegnvlppgkeGNIAIRikptrPFCLFNCYLDNPEKTAASEQGDFYiTG 313
Cdd:cd17630 148 AsQVATKRPDGF-GRGGVGVLLPGRELRIVED----------GEIWVG-----GASLAMGYLRGQLVPEFNEDGWFT-TK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 314 DRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayvshDPEALTR 393
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-------RGPADPA 283
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958647527 394 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:cd17630 284 ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
48-431 |
1.26e-41 |
|
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: 153.90 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 48 RLLVSDTSRPGWINFRELLRV------ASPEHNCLRTRSGDSMA-IYFTSGTTGTPK--MVEHsqcsYGLGFVASGRRLM 118
Cdd:cd12117 96 KVLLTDRSLAGRAGGLEVAVVidealdAGPAGNPAVPVSPDDLAyVMYTSGSTGRPKgvAVTH----RGVVRLVKNTNYV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 119 ALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHElPQV--DAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRykF 196
Cdd:cd12117 172 TLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAP-KGTllDPDALGALIAEEGVTVLWLTAALFNQLADEDPEC--F 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 197 QCLRHCLAGGEALNSDVRDKWKNQT-GLEIHEGYGQSE-TVLIC------GNFRGSTIksgSMGKASPPYDVQIVDEEGN 268
Cdd:cd12117 249 AGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEnTTFTTshvvteLDEVAGSI---PIGRPIANTRVYVLDEDGR 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 269 VLPPGKEGNIairikptrpfCLFNC-----YLDNPEKTAAS-------EQGDFYITGDRAHMDEDGYFWFVGRNDDVINS 336
Cdd:cd12117 326 PVPPGVPGEL----------YVGGDglalgYLNRPALTAERfvadpfgPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 337 SSYRIGPVEVESALAEHPAVLESAVVsspdPIRGEVVKAFIVlspAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFIS 416
Cdd:cd12117 396 RGFRIELGEIEAALRAHPGVREAVVV----VREDAGGDKRLV---AYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLD 468
|
410
....*....|....*
gi 1958647527 417 ELPKTVSGKILRSKL 431
Cdd:cd12117 469 ELPLTANGKVDRRAL 483
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
79-434 |
3.26e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 153.12 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 79 RSGDSMAIYFTSGTTGTPKMVEHSqcsYG------------LGFVASGRRLMALTESDIfwNTTDTGWVKAAWtlfsawa 146
Cdd:PRK06145 147 APTDLVRLMYTSGTTDRPKGVMHS---YGnlhwksidhviaLGLTASERLLVVGPLYHV--GAFDLPGIAVLW------- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 147 NGACVFVHElpQVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEAL-NSDVRDKWKNQTGLE 224
Cdd:PRK06145 215 VGGTLRIHR--EFDPEAVLAAIERHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEKTpESRIRDFTRVFTRAR 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 225 IHEGYGQSETvliCGnfrGSTI--------KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIR-IKPTRPfclfncYL 295
Cdd:PRK06145 293 YIDAYGLTET---CS---GDTLmeagreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRgPKVTKG------YW 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 296 DNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKA 375
Cdd:PRK06145 361 KDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITA 440
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 376 FIVLSPAyvshdpEALT-RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK06145 441 VVVLNPG------ATLTlEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
63-431 |
3.93e-41 |
|
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: 151.63 E-value: 3.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 63 RELLRVASPEhnCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLF 142
Cdd:cd05945 81 REILDAAKPA--LLIADGDDNAYIIFTSGSTGRPKGVQISHDNL-VSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 143 SAWANGACVF-VHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQ 220
Cdd:cd05945 158 PALASGATLVpVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEVLPHKTARALQQR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 221 T-GLEIHEGYGQSETVLICGNFR-----GSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCY 294
Cdd:cd05945 238 FpDARIYNTYGPTEATVAVTYIEvtpevLDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGP-----SVSKGY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 295 LDNPEKTAAS----EQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRG 370
Cdd:cd05945 313 LNNPEKTAAAffpdEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKV 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958647527 371 EVVKAFIVLSPayvsHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd05945 393 TELIAFVVPKP----GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
81-432 |
1.99e-40 |
|
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: 149.45 E-value: 1.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 81 GDSMAIYFTSGTTGTPKMVEHSQCSyglgFVASGRRL---MALTESDIFWNTTD----TGWVKAAWTLFSAwanGACVFV 153
Cdd:cd05903 93 DAVALLLFTSGTTGEPKGVMHSHNT----LSASIRQYaerLGLGPGDVFLVASPmahqTGFVYGFTLPLLL---GAPVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 154 HEL--PQVDAQTILNTLCRFpitTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQ 231
Cdd:cd05903 166 QDIwdPDKALALMREHGVTF---MMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 232 SETVLICGNFRG--STIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDF 309
Cdd:cd05903 243 TECPGAVTSITPapEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSR-GPS----VFLGYLDRPDLTADAAPEGW 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 310 YITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPE 389
Cdd:cd05903 318 FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSG-ALLTFD 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958647527 390 ALTRELQEHvktVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd05903 397 ELVAYLDRQ---GVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
13-425 |
5.17e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 150.04 E-value: 5.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 13 LKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTS----RPGWINFRELLRVASPEHNcLRTRSGDSMAIYF 88
Cdd:PRK07798 92 LRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSgndlLPGAVDYEDALAAGSPERD-FGERSPDDLYLLY 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 89 TSGTTGTPK--MVEHSQCsyglgFVAS--GRRLM----ALTESDIFWNTTDTG---WVKAA--------WTLFSAWANGA 149
Cdd:PRK07798 171 TGGTTGMPKgvMWRQEDI-----FRVLlgGRDFAtgepIEDEEELAKRAAAGPgmrRFPAPplmhgagqWAAFAALFSGQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 150 CVFVHELPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQE--DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQ-TGLEI 225
Cdd:PRK07798 246 TVVLLPDVRFDADEVWRTIEREKVNVITIVGDAMaRPLLDAleARGPYDLSSLFAIASGGALFSPSVKEALLELlPNVVL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 226 HEGYGQSETvlicGNFRGSTIKSGSMGKASPPY----DVQIVDEEGNVLPPG--------KEGNIAIRikptrpfclfnc 293
Cdd:PRK07798 326 TDSIGSSET----GFGGSGTVAKGAVHTGGPRFtigpRTVVLDEDGNPVEPGsgeigwiaRRGHIPLG------------ 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 294 YLDNPEKTAAS---EQGDFY-ITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIR 369
Cdd:PRK07798 390 YYKDPEKTAETfptIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERW 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647527 370 GEVVKAFIVLSPAyVSHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 425
Cdd:PRK07798 470 GQEVVAVVQLREG-ARPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
29-434 |
8.00e-40 |
|
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: 149.53 E-value: 8.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 29 DALAphvDAISADCPSLQSRLLVSDTSrpGWINFRELLrvASPEHNCLRTRSGDSMAIYFTS-GTTGTPKMVEHSQCSYG 107
Cdd:COG1021 138 RALA---RELQAEVPSLRHVLVVGDAG--EFTSLDALL--AAPADLSEPRPDPDDVAFFQLSgGTTGLPKLIPRTHDDYL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 108 LGFVASGRrLMALTESDIFWnttdtgwvkAA-----------WTLFSAWANGACVFVHELPqvDAQTILNTLCRFPITTI 176
Cdd:COG1021 211 YSVRASAE-ICGLDADTVYL---------AAlpaahnfplssPGVLGVLYAGGTVVLAPDP--SPDTAFPLIERERVTVT 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 177 CCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETvLICGnfrgsT-------IKS 248
Cdd:COG1021 279 ALVPPLALLWLDaAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEG-LVNY-----TrlddpeeVIL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 249 GSMGKASPPYD-VQIVDEEGNVLPPGKEGNIAIRIKPTrpfclFNCYLDNPEKTAAS--EQGdFYITGDRAHMDEDGYFW 325
Cdd:COG1021 353 TTQGRPISPDDeVRIVDEDGNPVPPGEVGELLTRGPYT-----IRGYYRAPEHNARAftPDG-FYRTGDLVRRTPDGYLV 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 326 FVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayvshDPEALT-RELQEHVKTV-T 403
Cdd:COG1021 427 VEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-------RGEPLTlAELRRFLRERgL 499
|
410 420 430
....*....|....*....|....*....|.
gi 1958647527 404 APYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:COG1021 500 AAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
79-432 |
1.75e-39 |
|
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: 147.88 E-value: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 79 RSGDSMA-IYFTSGTTGTPK--MVEHSQCsygLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGAC-VFVH 154
Cdd:cd17651 133 LDADDLAyVIYTSGSTGRPKgvVMPHRSL---ANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATlVLPP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 155 ELPQVDAQTILNTLCRFPITtICCVPTLFRLLVQEDLTRYKFQ--CLRHCLAGGEAL--NSDVRDKWKNQTGLEIHEGYG 230
Cdd:cd17651 210 EEVRTDPPALAAWLDEQRIS-RVFLPTVALRALAEHGRPLGVRlaALRYLLTGGEQLvlTEDLREFCAGLPGLRLHNHYG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 231 QSET-VLICGNFRGSTIKSG---SMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAA--- 303
Cdd:cd17651 289 PTEThVVTALSLPGDPAAWPappPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGA-----GLARGYLNRPELTAErfv 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 304 ----SEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 379
Cdd:cd17651 364 pdpfVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVG 443
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958647527 380 SPAyVSHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd17651 444 DPE-APVDAAELRAALATHL----PEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
82-432 |
2.53e-39 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 150.05 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVHE-LPQV 159
Cdd:PLN02654 276 DPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGhSYVTYGPMLNGATVLVFEgAPNY 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 160 -DAQTILNTLCRFPITTICCVPTLFRLLVQED---LTRYKFQCLRHCLAGGEALNSDVRDKWKNQTG---LEIHEGYGQS 232
Cdd:PLN02654 356 pDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 233 ETvlicGNFRGSTI------KSGSmgKASPPYDVQ--IVDEEGNVLPPGKEGNIAIriKPTRPFCLFNCYLDNP--EKTA 302
Cdd:PLN02654 436 ET----GGFMITPLpgawpqKPGS--ATFPFFGVQpvIVDEKGKEIEGECSGYLCV--KKSWPGAFRTLYGDHEryETTY 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 303 ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPA 382
Cdd:PLN02654 508 FKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEG 587
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958647527 383 yVSHDPEaLTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:PLN02654 588 -VPYSEE-LRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
82-428 |
2.82e-39 |
|
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: 144.33 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPKMV-----------EHSQcSYGLGFVASGRRLMALTESDIFwnttdtgwvKAAWTLFSAWANGAC 150
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVllanktffavpDILQ-KEGLNWVVGDVTYLPLPATHIG---------GLWWILTCLIHGGLC 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 151 VFVHELPQVdaQTILNTLCRFPITTICCVPTLFRLLVQE--DLTRYKFQcLRHCLAGGE-ALNSDVRD-KWKNQTGLEIH 226
Cdd:cd17635 72 VTGGENTTY--KSLFKILTTNAVTTTCLVPTLLSKLVSElkSANATVPS-LRLIGYGGSrAIAADVRFiEATGLTNTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 227 egYGQSET-VLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIriKPTRpfcLFNCYLDNPEKTAASE 305
Cdd:cd17635 149 --YGLSETgTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWI--KSPA---NMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 306 QGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayvS 385
Cdd:cd17635 222 IDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS----A 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958647527 386 HDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 428
Cdd:cd17635 298 ELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
82-428 |
1.53e-38 |
|
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: 141.87 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPK--MVEHSQCsygLGFVASGRRLMALTESD------IFWNTTdtGWvKAAWtlFSAWANGACVfv 153
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQT---LRAAAAWADCADLTEDDryliinPFFHTF--GY-KAGI--VACLLTGATV-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 154 heLPQV--DAQTILNTLCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLE-IHEGY 229
Cdd:cd17638 71 --VPVAvfDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 230 GQSE--TVLICGNFRGSTIKSGSMGKASPPYDVQIVDEeGNVLppgkegniairikpTRPFCLFNCYLDNPEKTAASEQG 307
Cdd:cd17638 149 GLTEagVATMCRPGDDAETVATTCGRACPGFEVRIADD-GEVL--------------VRGYNVMQGYLDDPEATAEAIDA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 308 DFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSH 386
Cdd:cd17638 214 DGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG-VTL 292
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958647527 387 DPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILR 428
Cdd:cd17638 293 TEEDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
44-434 |
1.92e-38 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 147.87 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 44 SLQSRLLVSDTSRPGWInFRELLRVASPEHNCLrtrSGDSMAI-YFTSGTTGTPKMVEHSQCSYgLGFV-ASGRRLMALT 121
Cdd:PRK06060 111 ALRDRFQPSRVAEAAEL-MSEAARVAPGGYEPM---GGDALAYaTYTSGTTGPPKAAIHRHADP-LTFVdAMCRKALRLT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 122 ESDIFWNTTDTGWvkaAWTL-FSAW---ANGACVFVHELPqVDAQTILNTLCRFPITTICCVPTLFRLLVqEDLTRYKFQ 197
Cdd:PRK06060 186 PEDTGLCSARMYF---AYGLgNSVWfplATGGSAVINSAP-VTPEAAAILSARFGPSVLYGVPNFFARVI-DSCSPDSFR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 198 CLRHCLAGGEALNSDVRDKWKNQ-TGLEIHEGYGQSEtvlICGNFRGSTI---KSGSMGKASPPYDVQIVDEEGNVLPPG 273
Cdd:PRK06060 261 SLRCVVSAGEALELGLAERLMEFfGGIPILDGIGSTE---VGQTFVSNRVdewRLGTLGRVLPPYEIRVVAPDGTTAGPG 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 274 KEGNIAIRiKPTrpfcLFNCYLDNPEKTAasEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEH 353
Cdd:PRK06060 338 VEGDLWVR-GPA----IAKGYWNRPDSPV--ANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIED 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 354 PAVLESAVVSSPDPIRGEVVKAFIVlsPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:PRK06060 411 EAVAEAAVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRK 488
|
.
gi 1958647527 434 Q 434
Cdd:PRK06060 489 Q 489
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
32-434 |
2.51e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 144.95 E-value: 2.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 32 APHVDAISADCpslQSRLLVSDTS----RPGWINFrELLRVASPEHNCLRTRSGDSMA---IYFTSGTTGTPKMV---EH 101
Cdd:PRK09088 83 ASELDALLQDA---EPRLLLGDDAvaagRTDVEDL-AAFIASADALEPADTPSIPPERvslILFTSGTSGQPKGVmlsER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 102 SQCSYGLGFVASGR---RLMALTESDIFwnttdtGWVKAAWTLFSAWANGACVFVHelPQVDAQTILNTLC--RFPITTI 176
Cdd:PRK09088 159 NLQQTAHNFGVLGRvdaHSSFLCDAPMF------HIIGLITSVRPVLAVGGSILVS--NGFEPKRTLGRLGdpALGITHY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 177 CCVPTLFRLLvqEDLTRYKFQCLRHCLA----GGEALNSDVRdKWKNQtGLEIHEGYGQSE--TVL----ICGNFRGsti 246
Cdd:PRK09088 231 FCVPQMAQAF--RAQPGFDAAALRHLTAlftgGAPHAAEDIL-GWLDD-GIPMVDGFGMSEagTVFgmsvDCDVIRA--- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 247 KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFW 325
Cdd:PRK09088 304 KAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR-GPN----LSPGYWRRPQATARAFTGDgWFRTGDIARRDADGFFW 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 326 FVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVShDPEaltrELQEHVKTVTAP 405
Cdd:PRK09088 379 VVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPL-DLE----RIRSHLSTRLAK 453
|
410 420
....*....|....*....|....*....
gi 1958647527 406 YKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK09088 454 YKVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
11-426 |
1.30e-37 |
|
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: 142.86 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 11 KDLKYRLQAARVKSIITSDAL-----APHVDAISADC-----PSLQSRLLVSD--------TSRPGWINFRELLRVASPE 72
Cdd:cd05909 68 RELRACIKLAGIKTVLTSKQFieklkLHHLFDVEYDArivylEDLRAKISKADkckaflagKFPPKWLLRIFGVAPVQPD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 73 hnclrtrsgDSMAIYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFWNTTDT----GWVKAAWTLFSAwanG 148
Cdd:cd05909 148 ---------DPAVILFTSGSEGLPKGVVLSHKNL-LANVEQITAIFDPNPEDVVFGALPFfhsfGLTGCLWLPLLS---G 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 149 ACVFVHELPqVDAQTILNTLCRFPITTICCVPTLFRLLVQEdLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEG 228
Cdd:cd05909 215 IKVVFHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 229 YGQSETV-LICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNV-LPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQ 306
Cdd:cd05909 293 YGTTECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVR-GPN----VMLGYLNEPELTSFAFG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 307 GDFYITGDRAHMDEDGYFWFVGRnddviNSSSYRIG----PVE-VESALAEH-PAVLESAVVSSPDPIRGEVVKAFivls 380
Cdd:cd05909 368 DGWYDTGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL---- 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958647527 381 payvsHDPEALTR-ELQEHVKTVTAPYKY-PRKVAFISELPKTVSGKI 426
Cdd:cd05909 439 -----TTTTDTDPsSLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKP 481
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
89-431 |
2.82e-37 |
|
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: 141.70 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 89 TSGTTGTPKMVEHSQCSYGLGFVASGRrLMALTESDIFW--NTTDTGWVKAAWTLFSAWANGACVFVHelPQVDAQTILN 166
Cdd:cd05920 147 SGGTTGTPKLIPRTHNDYAYNVRASAE-VCGLDQDTVYLavLPAAHNFPLACPGVLGTLLAGGRVVLA--PDPSPDAAFP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 167 TLCRFPITTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRGS- 244
Cdd:cd05920 224 LIEREGVTVTALVPALVSLWLDAaASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLDDPd 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 245 TIKSGSMGKASPPYD-VQIVDEEGNVLPPGKEGNIAIRIKPTrpfclFNCYLDNPEKTAAS--EQGdFYITGDRAHMDED 321
Cdd:cd05920 304 EVIIHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTRGPYT-----IRGYYRAPEHNARAftPDG-FYRTGDLVRRTPD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 322 GYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVShdpealTRELQEHVKT 401
Cdd:cd05920 378 GYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPS------AAQLRRFLRE 451
|
330 340 350
....*....|....*....|....*....|.
gi 1958647527 402 V-TAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd05920 452 RgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
86-428 |
4.14e-37 |
|
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: 137.92 E-value: 4.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 86 IYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALT-ESDIFWNTT--DTGWVKAAwtLFSAWANGAcvfVHELPQVDAQ 162
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSW-IESFVCNEDLFNISgEDAILAPGPlsHSLFLYGA--ISALYLGGT---FIGQRKFNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 163 TILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLrhcLAGGEALNSDVRDKWKNQT-GLEIHEGYGQSETVLICGNF 241
Cdd:cd17633 79 SWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 242 RGSTIKSGSMGKASPPYDVQIVDEEGnvlppGKEGNIAIRiKPTRpfclFNCYLDNPEktaaSEQGDFYITGDRAHMDED 321
Cdd:cd17633 156 NQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVK-SEMV----FSGYVRGGF----SNPDGWMSVGDIGYVDEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 322 GYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayvshdpEALTRELQEHVKT 401
Cdd:cd17633 222 GYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD--------KLTYKQLKRFLKQ 293
|
330 340
....*....|....*....|....*..
gi 1958647527 402 VTAPYKYPRKVAFISELPKTVSGKILR 428
Cdd:cd17633 294 KLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
81-431 |
4.38e-37 |
|
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: 140.52 E-value: 4.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 81 GDSMA--IYfTSGTTGTPK--MVEHSQCsygLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGA-CVFVHE 155
Cdd:cd17643 92 PDDLAyvIY-TSGSTGRPKgvVVSHANV---LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGrLVVVPY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 LPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQ-CLRHCLAGGEALNSDVRDKWKNQTGL---EIHEGYGQ 231
Cdd:cd17643 168 EVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPlALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 232 SET-VLIcgNFR-----------GSTIksgsmGKASPPYDVQIVDEEGNVLPPGKEGNIAI-RIKPTRPfclfncYLDNP 298
Cdd:cd17643 248 TETtVHV--TFRpldaadlpaaaASPI-----GRPLPGLRVYVLDADGRPVPPGVVGELYVsGAGVARG------YLGRP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 299 EKTA-------ASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRG 370
Cdd:cd17643 315 ELTAerfvanpFGGPGSrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGD 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958647527 371 EVVKAFIVLSPAyvshdPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd17643 395 TRLVAYVVADDG-----AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
79-425 |
1.55e-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.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 137.51 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 79 RSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGfVASGRRLMALTESDIFW------NTTDTGWVKAA--------WTLFSA 144
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVMWRQEDIFRM-LMGGADFGTGEFTPSEDahkaaaAAAGTVMFPAPplmhgtgsWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 145 WANGACVFVHElPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQE--DLTRYKFQCLRHCLAGGEALNSDVRDKW-KNQ 220
Cdd:cd05924 80 LLGGQTVVLPD-DRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDAlrDAGPYDLSSLFAISSGGALLSPEVKQGLlELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 221 TGLEIHEGYGQSET-VLICGNFRGSTIKSGSMGKASPpyDVQIVDEEGNVLPPGKE--GNIAIR-IKPtrpfclfNCYLD 296
Cdd:cd05924 159 PNITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGgvGWIARRgHIP-------LGYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 297 NPEKTAAS--EQGD--FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 372
Cdd:cd05924 230 DEAKTAETfpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958647527 373 VKAFIVLSPAyvsHDPEAltRELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 425
Cdd:cd05924 310 VVAVVQLREG---AGVDL--EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
79-431 |
1.81e-36 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 139.95 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 79 RSGDSMAIYFTSGTTGTPK---------------MVEHSQCSYGLGFVASGrrLMALTESDIFWnttdtgwvkaAWTLFS 143
Cdd:cd05923 148 EPEQPAFVFYTSGTTGLPKgavipqraaesrvlfMSTQAGLRHGRHNVVLG--LMPLYHVIGFF----------AVLVAA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 144 AWANGACVFVHELpqvDAQTILNTLCRFPITTICCVPTLFRLLV-QEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTG 222
Cdd:cd05923 216 LALDGTYVVVEEF---DPADALKLIEQERVTSLFATPTHLDALAaAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 223 LEIHEGYGQSETVlicgnfrGSTI----KSGSMGKASPPYDVQIVDEEGNV---LPPGKEGNIAIRIKPTRPFclfNCYL 295
Cdd:cd05923 293 GEKVNIYGTTEAM-------NSLYmrdaRTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAAAADAAF---TGYL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 296 DNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKA 375
Cdd:cd05923 363 NQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTA 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958647527 376 FIVLSPAYVSHDpealtrELQEHVKTVT-APYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd05923 443 CVVPREGTLSAD------ELDQFCRASElADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
72-432 |
1.84e-36 |
|
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: 139.04 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 72 EHNCLRTRSGDSMA-IYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLmALTESDIFWNTTDTGWVKAAWTLFSAWANGAC 150
Cdd:cd17649 84 GAGLLLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAERY-GLTPGDRELQFASFNFDGAHEQLLPPLICGAC 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 151 VFVHELPQ-VDAQTILNTLCRFPITTICCVPTLFRLLVQE--DLTRYKFQCLRHCLAGGEALNSDVRDKWKnQTGLEIHE 227
Cdd:cd17649 163 VVLRPDELwASADELAEMVRELGVTVLDLPPAYLQQLAEEadRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVRLFN 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 228 GYGQSETV---LICGNFRGSTIKSGSM--GKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTA 302
Cdd:cd17649 242 AYGPTEATvtpLVWKCEAGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGELYIGGE-----GLARGYLGRPELTA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 303 --------ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVk 374
Cdd:cd17649 317 erfvpdpfGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV- 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 375 AFIVLSpayvshDPEALTrELQEHVKTVTA----PYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:cd17649 396 AYVVLR------AAAAQP-ELRAQLRTALRaslpDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
148-424 |
2.43e-36 |
|
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: 135.89 E-value: 2.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 148 GACVFVhelPQVDAQTILNTLCRFPIT-TICCVPTLFRLLVQEDLTRYKFQCLRHCLA--GGEALNSDVRDKWKNQTGle 224
Cdd:cd17636 67 GTNVFV---RRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGLYDLSSLRSSPAapEWNDMATVDTSPWGRKPG-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 225 iheGYGQSETV-LICGNFRGSTIKsGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAA 303
Cdd:cd17636 142 ---GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVAR-GPT----VMAGYWNRPEVNAR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 304 SEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP-A 382
Cdd:cd17636 213 RTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPgA 292
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958647527 383 YVSHDpealtrELQEHVKTVTAPYKYPRKVAFISELPKTVSG 424
Cdd:cd17636 293 SVTEA------ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
88-433 |
1.39e-35 |
|
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: 136.90 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 88 FTSGTTGTPK--MVEHSqcSYGLGFVASGRRLMALTESDIFWnttdtgwvKAAWT-------LFSAWANGACVFV---HE 155
Cdd:cd05918 113 FTSGSTGKPKgvVIEHR--ALSTSALAHGRALGLTSESRVLQ--------FASYTfdvsileIFTTLAAGGCLCIpseED 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 LPQvdaqTILNTLCRFPITTICCVPTLFRLLVQEDLTrykfqCLRHCLAGGEALNSDVRDKWKNQTGLeiHEGYGQSE-T 234
Cdd:cd05918 183 RLN----DLAGFINRLRVTWAFLTPSVARLLDPEDVP-----SLRTLVLGGEALTQSDVDTWADRVRL--INAYGPAEcT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 235 VLICGNFRGSTIKSGSMGkasPPYDVQ--IVDEEGN--VLPPGKEGNIAIrikpTRPfCLFNCYLDNPEKTAAS------ 304
Cdd:cd05918 252 IAATVSPVVPSTDPRNIG---RPLGATcwVVDPDNHdrLVPIGAVGELLI----EGP-ILARGYLNDPEKTAAAfiedpa 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 305 --------EQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVK-- 374
Cdd:cd05918 324 wlkqegsgRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPql 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 375 -AFIVLSP------------AYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:cd05918 404 vAFVVLDGsssgsgdgdslfLEPSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
39-434 |
2.30e-35 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 137.63 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 39 SADCPSLQSRLLVSDTSRPGWINFRELL-RVASPEHNCLRTRSG-----DSMAIYFTSGTTGTPK--MVEHsqcsYGLG- 109
Cdd:PRK08315 151 SARLPELRRVIFLGDEKHPGMLNFDELLaLGRAVDDAELAARQAtldpdDPINIQYTSGTTGFPKgaTLTH----RNILn 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 110 ---FVAsgrRLMALTESD---I-------FwnttdtGWVKAawTLfSAWANGACVfVHELPQVDAQTILNTLCRFPITTI 176
Cdd:PRK08315 227 ngyFIG---EAMKLTEEDrlcIpvplyhcF------GMVLG--NL-ACVTHGATM-VYPGEGFDPLATLAAVEEERCTAL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 177 CCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGL-EIHEGYGQSETVlicgnfRGSTIKS------ 248
Cdd:PRK08315 294 YGVPTMFiAELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMsEVTIAYGMTETS------PVSTQTRtddple 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 249 ---GSMGKASPPYDVQIVDEE-GNVLPPGKEGNIAirikpTRPFCLFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGY 323
Cdd:PRK08315 368 krvTTVGRALPHLEVKIVDPEtGETVPRGEQGELC-----TRGYSVMKGYWNDPEKTAEAIDADGWMhTGDLAVMDEEGY 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 324 FWFVGRNDDVI-----NsssyrIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayvsHDPEALTRE-LQE 397
Cdd:PRK08315 443 VNIVGRIKDMIirggeN-----IYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIL------RPGATLTEEdVRD 511
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958647527 398 HVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK08315 512 FCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
79-432 |
6.49e-35 |
|
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: 136.12 E-value: 6.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 79 RSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVAS-----GRRLMALTE--SDIFWNttdtgwvkAAWTLFSAWANGACV 151
Cdd:cd17642 182 RDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHArdpifGNQIIPDTAilTVIPFH--------HGFGMFTTLGYLICG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 152 F-VHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLT-RYKFQCLRHCLAGGEALNSDVRDKWKNQTGLE-IHEG 228
Cdd:cd17642 254 FrVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVdKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 229 YGQSET---VLICGNfrgSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAAS 304
Cdd:cd17642 334 YGLTETtsaILITPE---GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVK-GPM----IMKGYVNNPEATKAL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 305 EQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspay 383
Cdd:cd17642 406 IDKDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL---- 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958647527 384 vSHDPEALTRELQEHVKTVTAPYKYPR-KVAFISELPKTVSGKILRSKLR 432
Cdd:cd17642 482 -EAGKTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
50-433 |
1.23e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 135.72 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 50 LVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMAIY-FTSGTTGTPK--MVEHSQCSYGLGFVasgRRLMALTESDIF 126
Cdd:PRK12492 175 MVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLDDIAVLqYTGGTTGLAKgaMLTHGNLVANMLQV---RACLSQLGPDGQ 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 127 WNTTDTGWVKAA----WTLFSAWANGACVFV---HELPQVDAQTI---LNTLCRFPITTICCVPTLF-RLLVQEDLTRYK 195
Cdd:PRK12492 252 PLMKEGQEVMIAplplYHIYAFTANCMCMMVsgnHNVLITNPRDIpgfIKELGKWRFSALLGLNTLFvALMDHPGFKDLD 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 196 FQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGK 274
Cdd:PRK12492 332 FSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 275 EGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEH 353
Cdd:PRK12492 412 RGELCIK-GPQ----VMKGYWQQPEATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAH 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 354 PAVLESAVVSSPDPIRGEVVKAFIvlspayVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:PRK12492 487 PKVANCAAIGVPDERSGEAVKLFV------VARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
76-434 |
1.26e-34 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 135.18 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 76 LRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLmALTESD-IFWNTT---DTGW---------VKAAWTLF 142
Cdd:PRK13295 192 LRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERL-GLGADDvILMASPmahQTGFmyglmmpvmLGATAVLQ 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 143 SAWANGACVfvhELPQVDAQTIlntlcrfpitTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTG 222
Cdd:PRK13295 271 DIWDPARAA---ELIRTEGVTF----------TMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 223 LEIHEGYGQSETVLICGNFRGSTIK--SGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptRPFcLFNCYLDNPEK 300
Cdd:PRK13295 338 AKIVSAWGMTENGAVTLTKLDDPDEraSTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVR----GCS-NFGGYLKRPQL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 301 TAASEQGdFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLS 380
Cdd:PRK13295 413 NGTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958647527 381 PAYvSHDPEALTRELQEHvkTVTAPYkYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK13295 492 PGQ-SLDFEEMVEFLKAQ--KVAKQY-IPERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
71-431 |
1.82e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 137.01 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 71 PEHNCLRTRSGDSMA-IYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGA 149
Cdd:PRK12316 4683 PAHDPAVRLHPDNLAyVIYTSGSTGRPKGVAVSHGSL-VNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGA 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 150 CVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDK-WKNQTGLEIHEG 228
Cdd:PRK12316 4762 SVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNG 4841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 229 YGQSETVL--ICGNFRGSTIKSGS---MGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAA 303
Cdd:PRK12316 4842 YGPTETTVtvLLWKARDGDACGAAympIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGE-----GVARGYLERPALTAE 4916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 304 -------SEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVkA 375
Cdd:PRK12316 4917 rfvpdpfGAPGGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLV-G 4995
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958647527 376 FIVLSPAYVSHDPEA---LTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK12316 4996 YVVPQDPALADADEAqaeLRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
37-438 |
2.94e-34 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 134.10 E-value: 2.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 37 AISADCPSLQSRLLVsDTSRPGW--INFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPK--MVEHSQcsyglgFVA 112
Cdd:PRK06087 142 PLQNQLPQLQQIVGV-DKLAPATssLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKgvMLTHNN------ILA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 113 SGRRLMA---LTESDIFWnttdtgwvkaawtlFSAWANGACVFVHELPQ---VDAQTILntLCRF-PITTI-------C- 177
Cdd:PRK06087 215 SERAYCArlnLTWQDVFM--------------MPAPLGHATGFLHGVTApflIGARSVL--LDIFtPDACLalleqqrCt 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 178 CV----PTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSD-VRDKWknQTGLEIHEGYGQSETV-LICGNFRGSTIKSGSM 251
Cdd:PRK06087 279 CMlgatPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKvARECQ--QRGIKLLSVYGSTESSpHAVVNLDDPLSRFMHT 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 252 -GKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAAS--EQGDFYiTGDRAHMDEDGYFWFVG 328
Cdd:PRK06087 357 dGYAAAGVEIKVVDEARKTLPPGCEGEEASR-GPN----VFMGYLDEPELTARAldEEGWYY-SGDLCRMDEAGYIKITG 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 329 RNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALTRELQEhvKTVtAPYKY 408
Cdd:PRK06087 431 RKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFSR--KRV-AKYKY 507
|
410 420 430
....*....|....*....|....*....|
gi 1958647527 409 PRKVAFISELPKTVSGKILRSKLRnQEWGR 438
Cdd:PRK06087 508 PEHIVVIDKLPRTASGKIQKFLLR-KDIMR 536
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
79-431 |
5.63e-33 |
|
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: 129.76 E-value: 5.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 79 RSGDSMAIYFTSGTTGTPK--MVEHSQCSYglgFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHEL 156
Cdd:cd17655 135 KSDDLAYVIYTSGSTGKPKgvMIEHRGVVN---LVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 157 PQV-DAQTILNTLCRFPITTICCVPTLFRLLVQEDLTryKFQCLRHCLAGGEALNSDVRDKWKNQTGL--EIHEGYGQSE 233
Cdd:cd17655 212 ETVlDGQALTQYIRQNRITIIDLTPAHLKLLDAADDS--EGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 234 TVLIC--GNFRGSTIKSGS--MGKASPPYDVQIVDEEGNVLPPGKEGNIAI------RikptrpfclfnCYLDNPEKTAA 303
Cdd:cd17655 290 TTVDAsiYQYEPETDQQVSvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIggegvaR-----------GYLNRPELTAE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 304 S------EQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAf 376
Cdd:cd17655 359 KfvddpfVPGErMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDE-QGQNYLC- 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1958647527 377 ivlspAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd17655 437 -----AYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
13-431 |
7.01e-33 |
|
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: 129.33 E-value: 7.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 13 LKYRLQAARVKSIITSDALAphvDAISADCPSLQsrllvsdtsrpgwinfRELLRVASPEHNCLRTRSGDSMA-IYFTSG 91
Cdd:cd12116 76 LRYILEDAEPALVLTDDALP---DRLPAGLPVLL----------------LALAAAAAAPAAPRTPVSPDDLAyVIYTSG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 92 TTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLF-SAWANGACVFVHELPQVDAQTILNTLCR 170
Cdd:cd12116 137 STGRPKGVVVSHRNL-VNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLlPLLAGARVVIAPRETQRDPEALARLIEA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 171 FPITTICCVPTLFRLLVQEDltrykFQCLR--HCLAGGEALNSDVRDKWKNQTGlEIHEGYGQSETVL------ICGNFR 242
Cdd:cd12116 216 HSITVMQATPATWRMLLDAG-----WQGRAglTALCGGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 243 GSTIksgsmGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAAS--------EQGDFYITGD 314
Cdd:cd12116 290 PIPI-----GRPLANTQVYVLDAALRPVPPGVPGELYIGGD-----GVAQGYLGRPALTAERfvpdpfagPGSRLYRTGD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 315 RAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVkAFIVLspayvsHDPEAL-TR 393
Cdd:cd12116 360 LVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL------KAGAAPdAA 432
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958647527 394 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd12116 433 ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
53-432 |
8.94e-33 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 130.35 E-value: 8.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 53 DTSRPGWINFRELLRvASPEHnCLR--TRSGDSMAIYFTSGTTGTPKmvehsqcsyglGFVASGRRLMALTE-------S 123
Cdd:PLN02574 170 DSKRIEFPKFYELIK-EDFDF-VPKpvIKQDDVAAIMYSSGTTGASK-----------GVVLTHRNLIAMVElfvrfeaS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 124 DIFWNTTDTGWVkAAWTLFSAWanGACVFVHEL----------PQVDAQTILNTLCRFPITTICCVPTLFRLLVQ--EDL 191
Cdd:PLN02574 237 QYEYPGSDNVYL-AALPMFHIY--GLSLFVVGLlslgstivvmRRFDASDMVKVIDRFKVTHFPVVPPILMALTKkaKGV 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 192 TRYKFQCLRHCLAGGEALNSD-VRDKWKNQTGLEIHEGYGQSETVLIcgNFRGSTIKS----GSMGKASPPYDVQIVD-E 265
Cdd:PLN02574 314 CGEVLKSLKQVSCGAAPLSGKfIQDFVQTLPHVDFIQGYGMTESTAV--GTRGFNTEKlskySSVGLLAPNMQAKVVDwS 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 266 EGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPV 344
Cdd:PLN02574 392 TGCLLPPGNCGELWIQ-GPG----VMKGYLNNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPA 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 345 EVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVS 423
Cdd:PLN02574 467 DLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG------STLSQEaVINYVAKQVAPYKKVRKVVFVQSIPKSPA 540
|
....*....
gi 1958647527 424 GKILRSKLR 432
Cdd:PLN02574 541 GKILRRELK 549
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
63-431 |
3.73e-32 |
|
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: 127.05 E-value: 3.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 63 RELLRVASPEHncLRTRSGDSMAIYFTSGTTGTPKMV--EHSQCSYGLGFVA---SGRRLMALTESdifwntTDTGWVKA 137
Cdd:cd12115 89 RFILEDAQARL--VLTDPDDLAYVIYTSGSTGRPKGVaiEHRNAAAFLQWAAaafSAEELAGVLAS------TSICFDLS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 138 AWTLFSAWANGACVFVHE-------LPQVDAQTILNTlcrfpitticcVPTLFRLLVQEDLTRYKFQCLrhCLAGgEALN 210
Cdd:cd12115 161 VFELFGPLATGGKVVLADnvlalpdLPAAAEVTLINT-----------VPSAAAELLRHDALPASVRVV--NLAG-EPLP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 211 SD-VRDKWKNQTGLEIHEGYGQSE-----TVLIcgnFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKP 284
Cdd:cd12115 227 RDlVQRLYARLQVERVVNLYGPSEdttysTVAP---VPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 285 trpfcLFNCYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVL 357
Cdd:cd12115 304 -----VARGYLGRPGLTAERflpdpfGPGArLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVR 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958647527 358 ESAVVSSPDPIRGEVVKAFIVLSPAYVShdpeaLTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd12115 379 EAVVVAIGDAAGERRLVAYIVAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
10-434 |
6.77e-32 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 127.40 E-value: 6.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 10 QKDLKYRLQAARVKSIITSDALAPHVDAISADCpslqsrLLVSDTSRPGWINFRELLRVASpehnclrtRSGDSM----- 84
Cdd:PLN02330 116 ESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPV------IVLGEEKIEGAVNWKELLEAAD--------RAGDTSdneei 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 85 ------AIYFTSGTTGTPK--MVEHSQ-----CS--YGLGFVASGRrLMALTESDIFWNTTDTGwvkaawTLFSAWANGA 149
Cdd:PLN02330 182 lqtdlcALPFSSGTTGISKgvMLTHRNlvanlCSslFSVGPEMIGQ-VVTLGLIPFFHIYGITG------ICCATLRNKG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 150 CVFVheLPQVDAQTILNTLCRFPITTICCVPTLFRLLVQE------DLTRYKfqcLRHCLAGGEALNSDVRDKWKNQ-TG 222
Cdd:PLN02330 255 KVVV--MSRFELRTFLNALITQEVSFAPIVPPIILNLVKNpiveefDLSKLK---LQAIMTAAAPLAPELLTAFEAKfPG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 223 LEIHEGYGQSETVLICGNF----RGSTI-KSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRIKptrpfCLFNCYLD 296
Cdd:PLN02330 330 VQVQEAYGLTEHSCITLTHgdpeKGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ-----CVMQGYYN 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 297 NPEKTAASEQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKA 375
Cdd:PLN02330 405 NKEETDRTIDEDGWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAA 484
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958647527 376 FIVLSPAYVSHDPEALtrelqEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PLN02330 485 CVVINPKAKESEEDIL-----NFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
82-434 |
1.19e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 126.78 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFT-SGTTGTPKMVEHSQ---------CSYGLGFVASGRRLMALTESDIFWNTTdtgwvkaawtLFSAWANGACV 151
Cdd:PRK06164 181 DAGALLFTtSGTTSGPKLVLHRQatllrharaIARAYGYDPGAVLLAALPFCGVFGFST----------LLGALAGGAPL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 152 fvHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHC-----LAGGEALNSDVRDKWKNQTGLeih 226
Cdd:PRK06164 251 --VCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFgfasfAPALGELAALARARGVPLTGL--- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 227 egYGQSETVLICGNFRGSTIKS----GSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKT 301
Cdd:PRK06164 326 --YGSSEVQALVALQPATDPVSvrieGGGRPASPEARVRARDpQDGALLPDGESGEIEIR-APS----LMRGYLDNPDAT 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 302 AASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSpdPIRGE-VVKAFIVL 379
Cdd:PRK06164 399 ARALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIP 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647527 380 SPAyVSHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSG---KILRSKLRNQ 434
Cdd:PRK06164 477 TDG-ASPDEAGLMAACREAL----AGFKVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-434 |
1.66e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 126.25 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 9 TQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLqsrLLVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMAIYF 88
Cdd:PLN02246 110 TPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVT---VVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVALPY 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 89 TSGTTGTPK--MVEHSqcsyglGFVASGRRLMALTESDIFWNTTDTgwVKAAWTLFSAWA----------NGACVFVheL 156
Cdd:PLN02246 187 SSGTTGLPKgvMLTHK------GLVTSVAQQVDGENPNLYFHSDDV--ILCVLPMFHIYSlnsvllcglrVGAAILI--M 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 157 PQVDAQTILNTLCRFPITTICCVPTLFRLLVQED-LTRYKFQCLRHCLAG----GEALNSDVRDKWKNQTgleIHEGYGQ 231
Cdd:PLN02246 257 PKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGaaplGKELEDAFRAKLPNAV---LGQGYGM 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 232 SE--TVL-ICGNFRGS--TIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAASE 305
Cdd:PLN02246 334 TEagPVLaMCLAFAKEpfPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQ-----IMKGYLNDPEATANTI 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 306 QGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAY- 383
Cdd:PLN02246 409 DKDGWLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSe 488
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958647527 384 VSHDpealtrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PLN02246 489 ITED------EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
82-434 |
2.26e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 125.83 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPK-MVEHSQCSYglgfvasgrrLMALTesdifwNTTDTGWVKAA---WTL--FS------AWANGA 149
Cdd:PRK08162 183 DAIALNYTSGTTGNPKgVVYHHRGAY----------LNALS------NILAWGMPKHPvylWTLpmFHcngwcfPWTVAA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 150 CVFVHE-LPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNqTGLEIHE 227
Cdd:PRK08162 247 RAGTNVcLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEE-IGFDLTH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 228 GYGQSET---VLICGNFRG-----STIKSGSMGKASPPYDVQivdEEGNVLPP---------GKE-GNIAIR----IKPt 285
Cdd:PRK08162 326 VYGLTETygpATVCAWQPEwdalpLDERAQLKARQGVRYPLQ---EGVTVLDPdtmqpvpadGETiGEIMFRgnivMKG- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 286 rpfclfncYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSP 365
Cdd:PRK08162 402 --------YLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKP 473
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958647527 366 DPIRGEVVKAFIVLSPayvshDPEALTRELQEHVKTVTAPYKYPRKVAFiSELPKTVSGKILRSKLRNQ 434
Cdd:PRK08162 474 DPKWGEVPCAFVELKD-----GASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
39-434 |
2.69e-31 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 126.07 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 39 SADCPSLQSRLLVSDTSRPGWINFRELLRvasPEHncLRTRSG------------DSMAIYFTSGTTGTPKMVEHSQCSY 106
Cdd:PLN02860 123 NDRLPSLMWQVFLESPSSSVFIFLNSFLT---TEM--LKQRALgtteldyawapdDAVLICFTSGTTGRPKGVTISHSAL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 107 ---GLGFVAsgrrLMALTESDIFWNTT---DTGWVKAAWTLFSAwanGAC-VFvheLPQVDAQTILNTLCRFPITTICCV 179
Cdd:PLN02860 198 ivqSLAKIA----IVGYGEDDVYLHTAplcHIGGLSSALAMLMV---GAChVL---LPKFDAKAALQAIKQHNVTSMITV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 180 PTLFRLLV---QEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQ-TGLEIHEGYGQSETvliCGNFRGSTIKSGSMgkAS 255
Cdd:PLN02860 268 PAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLfPNAKLFSAYGMTEA---CSSLTFMTLHDPTL--ES 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 256 PPYDVQIVDEEGNVLPPGKEG--------NIAIRIKP----------TRPFCLFNCYLDNPEKTAASEQGDFYI-TGDRA 316
Cdd:PLN02860 343 PKQTLQTVNQTKSSSVHQPQGvcvgkpapHVELKIGLdessrvgrilTRGPHVMLGYWGQNSETASVLSNDGWLdTGDIG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 317 HMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALTR--- 393
Cdd:PLN02860 423 WIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKENAkkn 502
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1958647527 394 ------ELQEHVKTVT-APYKYPRK-VAFISELPKTVSGKILRSKLRNQ 434
Cdd:PLN02860 503 ltlsseTLRHHCREKNlSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRRE 551
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
25-436 |
2.77e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 125.52 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 25 IITSDALAPHVDAIsaDCPSLqsRLLVSDTsrPGWinfRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKMVehsQC 104
Cdd:PRK13388 103 LVTDAEHRPLLDGL--DLPGV--RVLDVDT--PAY---AELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAV---RC 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 105 SYG----LGFVASGRRlmALTESDIFWNTT---DTGWVKAAWTlfSAWANGACVFVHelPQVDAQTILNTLCRFPITTIC 177
Cdd:PRK13388 171 SHGrlafAGRALTERF--GLTRDDVCYVSMplfHSNAVMAGWA--PAVASGAAVALP--AKFSASGFLDDVRRYGATYFN 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 178 CV-PTLFRLLVQEDLTRYKFQCLRHCLaGGEALNSDvRDKWKNQTGLEIHEGYGQSETVLICgnFRGSTIKSGSMGKASP 256
Cdd:PRK13388 245 YVgKPLAYILATPERPDDADNPLRVAF-GNEASPRD-IAEFSRRFGCQVEDGYGSSEGAVIV--VREPGTPPGSIGRGAP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 257 pyDVQIV-------------DEEGNVLPPGKegniAI-RIKPTRPFCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDG 322
Cdd:PRK13388 321 --GVAIYnpetltecavarfDAHGALLNADE----AIgELVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 323 YFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTREL--QEHVK 400
Cdd:PRK13388 395 WIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDG-ATFDPDAFAAFLaaQPDLG 473
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958647527 401 TVTApykyPRKVAFISELPKTVSGKILRSKLRNQEW 436
Cdd:PRK13388 474 TKAW----PRYVRIAADLPSTATNKVLKRELIAQGW 505
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
65-431 |
5.44e-30 |
|
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: 120.82 E-value: 5.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 65 LLRVASPEhnCLRTRSGDSMAIYFTSGTTGTPK--MVEHSqcsyGL-GFVASGRRLMALTESDIFWNTTDTGWVKAAWTL 141
Cdd:cd17652 79 MLADARPA--LLLTTPDNLAYVIYTSGSTGRPKgvVVTHR----GLaNLAAAQIAAFDVGPGSRVLQFASPSFDASVWEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 142 FSAWANGAC-VFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRykfqcLRHCLAGGEALNSDVRDKWKNq 220
Cdd:cd17652 153 LMALLAGATlVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPD-----LRTLVVAGEACPAELVDRWAP- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 221 tGLEIHEGYGQSETVLicgnfrGSTIKSGSMGKASPP-------YDVQIVDEEGNVLPPGKEGNIAIR-IKPTRPfclfn 292
Cdd:cd17652 227 -GRRMINAYGPTETTV------CATMAGPLPGGGVPPigrpvpgTRVYVLDARLRPVPPGVPGELYIAgAGLARG----- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 293 cYLDNPEKTAASEQGD--------FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSS 364
Cdd:cd17652 295 -YLNRPGLTAERFVADpfgapgsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVR 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958647527 365 PDPIRGEVVKAFIVLSPayvshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd17652 374 DDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
75-426 |
2.53e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 121.18 E-value: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 75 CLRTRSGDSMA-IYFTSGTTGTPKmvehsqcsyglGFVASGRRLMALTE--SDIFwNTTDTGWVKAAWTLFSA------- 144
Cdd:PRK08633 775 YGPTFKPDDTAtIIFSSGSEGEPK-----------GVMLSHHNILSNIEqiSDVF-NLRNDDVILSSLPFFHSfgltvtl 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 145 W---ANGACVFVHELPqVDAQTILNTLCRFPITTICCVPTLFRLLvqedlTRYK------FQCLRHCLAGGEALNSDVRD 215
Cdd:PRK08633 843 WlplLEGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLY-----LRNKklhplmFASLRLVVAGAEKLKPEVAD 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 216 KWKNQTGLEIHEGYGQSET----------VLICGNFRGSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKP 284
Cdd:PRK08633 917 AFEEKFGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG-GP 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 285 TrpfcLFNCYLDNPEKTAA----SEQGDFYITGDRAHMDEDGYFWFVGRnddviNSSSYRIG----PV-EVESALAE--H 353
Cdd:PRK08633 996 Q----VMKGYLGDPEKTAEvikdIDGIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemvPLgAVEEELAKalG 1066
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647527 354 PAVLESAVVSSPDPIRGEVVkafIVLspayvsHDPEAL-TRELQEHVKTVTAP--YKyPRKVAFISELPKTVSGKI 426
Cdd:PRK08633 1067 GEEVVFAVTAVPDEKKGEKL---VVL------HTCGAEdVEELKRAIKESGLPnlWK-PSRYFKVEALPLLGSGKL 1132
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
25-436 |
3.29e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 119.79 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 25 IITSDALAPHVDAISADCPslqsrllVSDTSRPGWINFRELLRVASPEHNclRTRSGDSMAIYFTSGTTGTPKMVehsQC 104
Cdd:PRK07867 105 VLTESAHAELLDGLDPGVR-------VINVDSPAWADELAAHRDAEPPFR--VADPDDLFMLIFTSGTSGDPKAV---RC 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 105 SYGLgFVASGRRLMA---LTESDIFWNTT---DTGWVKAAWTLfsAWANGACVFVHelPQVDAQTILNTLCRFPITTICC 178
Cdd:PRK07867 173 THRK-VASAGVMLAQrfgLGPDDVCYVSMplfHSNAVMAGWAV--ALAAGASIALR--RKFSASGFLPDVRRYGATYANY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 179 V--PtLFRLLVQEDLTRYKFQCLRhCLAGGEALNSDVrDKWKNQTGLEIHEGYGQSETVLICGnfRGSTIKSGSMGKASP 256
Cdd:PRK07867 248 VgkP-LSYVLATPERPDDADNPLR-IVYGNEGAPGDI-ARFARRFGCVVVDGFGSTEGGVAIT--RTPDTPPGALGPLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 257 pyDVQIVD-EEGNVLPPGK-------EGNIAI--RIKPTRPfCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWF 326
Cdd:PRK07867 323 --GVAIVDpDTGTECPPAEdadgrllNADEAIgeLVNTAGP-GGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 327 VGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTRELqeHVKTVTAPY 406
Cdd:PRK07867 400 AGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPG-AKFDPDAFAEFL--AAQPDLGPK 476
|
410 420 430
....*....|....*....|....*....|
gi 1958647527 407 KYPRKVAFISELPKTVSGKILRSKLRNQEW 436
Cdd:PRK07867 477 QWPSYVRVCAELPRTATFKVLKRQLSAEGV 506
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
80-433 |
2.21e-28 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 117.92 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 80 SGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHE---- 155
Cdd:PTZ00237 253 SSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEggii 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 LPQVDAQTILNTLCRFPITTICCVPTLFRLLVQED------LTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGY 229
Cdd:PTZ00237 333 KNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 230 GQSE---TVLICgnFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIkPTRPfCLFNCYLDNPE--KTAAS 304
Cdd:PTZ00237 413 GQTEigiTYLYC--YGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PMPP-SFATTFYKNDEkfKQLFS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 305 EQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYV 384
Cdd:PTZ00237 489 KFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQS 568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958647527 385 SH--DPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:PTZ00237 569 NQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
82-433 |
5.39e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 116.66 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPKmvehsqcsyglGFVASGRRLMALTESDIFwnttdtGWVKAA-----WTL-----------FSAW 145
Cdd:PLN03102 187 DPISLNYTSGTTADPK-----------GVVISHRGAYLSTLSAII------GWEMGTcpvylWTLpmfhcngwtftWGTA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 146 ANGACVFVheLPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLR-HCLAGGEALNSDVRDKWKnQTGLE 224
Cdd:PLN03102 250 ARGGTSVC--MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPvHVLTGGSPPPAALVKKVQ-RLGFQ 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 225 IHEGYGQSET---VLIC-----------GNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKE-GNIAIRIKptrpfC 289
Cdd:PLN03102 327 VMHAYGLTEAtgpVLFCewqdewnrlpeNQQMELKARQGVSILGLADVDVKNKETQESVPRDGKTmGEIVIKGS-----S 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 290 LFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIR 369
Cdd:PLN03102 402 IMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTW 481
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958647527 370 GEVVKAFIVL--SPAYVSHDPEALT---RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:PLN03102 482 GETPCAFVVLekGETTKEDRVDKLVtreRDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
39-432 |
7.32e-28 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 116.10 E-value: 7.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 39 SADCPSLQSRLlvsdtsRPGWINFRELLRVASPEHNCLRTRSG-DSMAIYFTSGTTGTPK-MVEHSQCSYglgfvasgrr 116
Cdd:PLN02479 158 TCDPKSLQYAL------GKGAIEYEKFLETGDPEFAWKPPADEwQSIALGYTSGTTASPKgVVLHHRGAY---------- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 117 LMALTESdIFWNTTD-------------TGWVkAAWTLFSAWANGACvfvheLPQVDAQTILNTLCRFPITTICCVPTLF 183
Cdd:PLN02479 222 LMALSNA-LIWGMNEgavylwtlpmfhcNGWC-FTWTLAALCGTNIC-----LRQVTAKAIYSAIANYGVTHFCAAPVVL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 184 RLLVQ--EDLTRYKFQCLRHCLAGGEALNSDVRDKWkNQTGLEIHEGYGQSETvlicgnFRGSTIKSGSMGKASPPYDVQ 261
Cdd:PLN02479 295 NTIVNapKSETILPLPRVVHVMTAGAAPPPSVLFAM-SEKGFRVTHTYGLSET------YGPSTVCAWKPEWDSLPPEEQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 262 ------------------IVDEEGNVLPP--GKE-GNIAIRIKptrpfCLFNCYLDNPEKTAASEQGDFYITGDRAHMDE 320
Cdd:PLN02479 368 arlnarqgvryiglegldVVDTKTMKPVPadGKTmGEIVMRGN-----MVMKGYLKNPKANEEAFANGWFHSGDLGVKHP 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 321 DGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALTRELQEHVK 400
Cdd:PLN02479 443 DGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAEDIMKFCR 522
|
410 420 430
....*....|....*....|....*....|..
gi 1958647527 401 TVTAPYKYPRKVAFiSELPKTVSGKILRSKLR 432
Cdd:PLN02479 523 ERLPAYWVPKSVVF-GPLPKTATGKIQKHVLR 553
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
79-434 |
7.82e-28 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 115.75 E-value: 7.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 79 RSGDSMaIYFTSGTTGTPKMVE----------HSQCS-YGLGFVASGRRLMALTESDifwnttdtGWVKAawtLFSAWAN 147
Cdd:PRK05852 175 RPDDAM-IMFTGGTTGLPKMVPwthaniassvRAIITgYRLSPRDATVAVMPLYHGH--------GLIAA---LLATLAS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 148 GACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLT------RYKFQCLRHCLAggeALNSDVRDKWKNQT 221
Cdd:PRK05852 243 GGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATepsgrkPAALRFIRSCSA---PLTAETAQALQTEF 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 222 GLEIHEGYGQSET--------VLICGNFRGSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNC 293
Cdd:PRK05852 320 AAPVVCAFGMTEAthqvtttqIEGIGQTENPVVSTGLVGRSTGA-QIRIVGSDGLPLPAGAVGEVWLR-GTT----VVRG 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 294 YLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVV 373
Cdd:PRK05852 394 YLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAV 473
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 374 KAFIV-LSPAYVSHDpealtrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK05852 474 AAVIVpRESAPPTAE------ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
75-433 |
1.14e-27 |
|
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: 113.94 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 75 CLRTRSGDSMA-IYFTSGTTGTPK--MVEHSQCSYGLGFVAS------GRRlMALTESDIFWnttdtgwvKAAWTLFSAW 145
Cdd:cd17653 98 LLTTDSPDDLAyIIFTSGSTGIPKgvMVPHRGVLNYVSQPPArldvgpGSR-VAQVLSIAFD--------ACIGEIFSTL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 146 ANGACVFVHElPQVDAQTILNTLCRFPITticcvPTLFRLLVQEDltrykFQCLRHCLAGGEALNSDVRDKWKNqtGLEI 225
Cdd:cd17653 169 CNGGTLVLAD-PSDPFAHVARTVDALMST-----PSILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 226 HEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIR-IKPTRPfclfncYLDNPEKTAAS 304
Cdd:cd17653 236 YNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISgVQVARG------YLGNPALTASK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 305 EQGD-------FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSpdpIRGEVVkAFI 377
Cdd:cd17653 310 FVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFV 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647527 378 VlsPAYVshDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:cd17653 386 T--PETV--DVDGLRSELAKHL----PSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
76-431 |
1.22e-27 |
|
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: 114.19 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 76 LRTRSGDSMAIYFTSGTTGTPK--MVEHSQCsygLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVfv 153
Cdd:cd17645 99 LLTNPDDLAYVIYTSGSTGLPKgvMIEHHNL---VNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAAL-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 154 HELPQVDAQTI--LNTLCRFPITTICCVPTLfrllVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKnqtgleIHEGYGQ 231
Cdd:cd17645 174 HVVPSERRLDLdaLNDYFNQEGITISFLPTG----AAEQFMQLDNQSLRVLLTGGDKLKKIERKGYK------LVNNYGP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 232 SETVLICGNFR-GSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAASEQGD-- 308
Cdd:cd17645 244 TENTVVATSFEiDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEG-----LARGYLNRPELTAEKFIVHpf 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 309 -----FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDpirGEVVKAFIvlspAY 383
Cdd:cd17645 319 vpgerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKED---ADGRKYLV----AY 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958647527 384 VSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd17645 392 VTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
9-434 |
1.30e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 114.49 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 9 TQKDLKYRLQAARVKSIITSDALAPHVDaiSADCPSLQSRLLVSDTSRpgwiNFRELLRVASPEHnclrtrsgDSMAIYF 88
Cdd:PRK07638 85 KQDELKERLAISNADMIVTERYKLNDLP--DEEGRVIEIDEWKRMIEK----YLPTYAPIENVQN--------APFYMGF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 89 TSGTTGTPKMVEHSQCSYGLGFvasgrrlmALTESDIFWNTTDTgwVKAAWTLFSA---WANGACVF----VHELPQVDA 161
Cdd:PRK07638 151 TSGSTGKPKAFLRAQQSWLHSF--------DCNVHDFHMKREDS--VLIAGTLVHSlflYGAISTLYvgqtVHLMRKFIP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 162 QTILNTLCRFPITTICCVPTLFRLLVQEDltRYKFQCLRhCLAGGEALNSDVRDKWKNQ-TGLEIHEGYGQSETVLICG- 239
Cdd:PRK07638 221 NQVLDKLETENISVMYTVPTMLESLYKEN--RVIENKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASELSFVTAl 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 240 NFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTRpfclFNCYLDNPEKTAASEQGDFYITGDRAHMD 319
Cdd:PRK07638 298 VDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVK-SPQF----FMGYIIGGVLARELNADGWMTVRDVGYED 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 320 EDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIvlspayvshDPEALTRELQEHV 399
Cdd:PRK07638 373 EEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFC 443
|
410 420 430
....*....|....*....|....*....|....*
gi 1958647527 400 KTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK07638 444 LQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSW 478
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
8-398 |
1.44e-27 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 115.20 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 8 LTQKDLKYRLQAARVKSIITSD-ALAPHVDAISADCPSLQsRLLVSD----TSRPGWINFRELLR----VASPE--HNCL 76
Cdd:COG1022 99 SSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLR-HIVVLDprglRDDPRLLSLDELLAlgreVADPAelEARR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 77 RTRSGDSMA-IYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIF------WnttdtgWVKA-AWTLFsAWANG 148
Cdd:COG1022 178 AAVKPDDLAtIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRTlsflplA------HVFErTVSYY-ALAAG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 149 ACVFVHElpqvDAQTILNTLCRFPITTICCVPTLF-----RLLVQ-EDLTRYK---FQ---------------------- 197
Cdd:COG1022 250 ATVAFAE----SPDTLAEDLREVKPTFMLAVPRVWekvyaGIQAKaEEAGGLKrklFRwalavgrryararlagkspsll 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 198 ----------------------CLRHCLAGGEALNSDVrDKWKNQTGLEIHEGYGQSET-VLICGNfRGSTIKSGSMGKA 254
Cdd:COG1022 326 lrlkhaladklvfsklrealggRLRFAVSGGAALGPEL-ARFFRALGIPVLEGYGLTETsPVITVN-RPGDNRIGTVGPP 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 255 SPPYDVQIvDEEGNVLppgkegniairIK-PtrpfCLFNCYLDNPEKTAAS--EQGDFYiTGDRAHMDEDGYFWFVGRND 331
Cdd:COG1022 404 LPGVEVKI-AEDGEIL-----------VRgP----NVMKGYYKNPEATAEAfdADGWLH-TGDIGELDEDGFLRITGRKK 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 332 DVI-NSSSYRIGPVEVESALAEHPAVLESAVVsspdpirGE----VVkAFIVLspayvshDPEALTRELQEH 398
Cdd:COG1022 467 DLIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALIVP-------DFEALGEWAEEN 523
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
345-425 |
1.57e-27 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 104.55 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 345 EVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSG 424
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 1958647527 425 K 425
Cdd:pfam13193 76 K 76
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
86-398 |
2.86e-27 |
|
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: 113.07 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 86 IYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESD----------IFWNTTDtgwvkaawtLFSAWANGACVFVHE 155
Cdd:cd05907 92 IIYTSGTTGRPKGVMLSHRNI-LSNALALAERLPATEGDrhlsflplahVFERRAG---------LYVPLLAGARIYFAS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 lpqvDAQTILNTLCRFPITTICCVPTLFR----LLVQEDLTRYK--------FQCLRHCLAGGEALNSDVrDKWKNQTGL 223
Cdd:cd05907 162 ----SAETLLDDLSEVRPTVFLAVPRVWEkvyaAIKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAEL-LHFFRALGI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 224 EIHEGYGQSETV-LICGNfRGSTIKSGSMGKASPPYDVQIvDEEGNVLppgkegniairikpTRPFCLFNCYLDNPEKTA 302
Cdd:cd05907 237 PVYEGYGLTETSaVVTLN-PPGDNRIGTVGKPLPGVEVRI-ADDGEIL--------------VRGPNVMLGYYKNPEATA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 303 ASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVI-NSSSYRIGPVEVESALAEHPAVLESAVVSSPDPirgeVVKAFIVLs 380
Cdd:cd05907 301 EALDADgWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVP- 375
|
330
....*....|....*...
gi 1958647527 381 payvshDPEALTRELQEH 398
Cdd:cd05907 376 ------DPEALEAWAEEH 387
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
255-432 |
3.08e-27 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 113.93 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 255 SPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTrpfclFNCYLDNPEKTAAS--EQGdFYITGDRAHMDEDGYFWFVGRNDD 332
Cdd:PRK10946 360 SPDDEVWVADADGNPLPQGEVGRLMTRGPYT-----FRGYYKSPQHNASAfdANG-FYCSGDLVSIDPDGYITVVGREKD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 333 VINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshDPEALTRELQEHvktVTAPYKYPRKV 412
Cdd:PRK10946 434 QINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPL---KAVQLRRFLREQ---GIAEFKLPDRV 507
|
170 180
....*....|....*....|
gi 1958647527 413 AFISELPKTVSGKILRSKLR 432
Cdd:PRK10946 508 ECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
43-431 |
3.46e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 115.26 E-value: 3.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 43 PSLQSRLLVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMA-IYFTSGTTGTPK--MVEHSQCSyglGFVASGRRLMA 119
Cdd:PRK12467 617 SHLLAQLPVPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAyVIYTSGSTGQPKgvAISHGALA---NYVCVIAERLQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 120 LTESDIFWNTTDTGWVKAAWTLFSAWANGACVfvHELPQ---VDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRykf 196
Cdd:PRK12467 694 LAADDSMLMVSTFAFDLGVTELFGALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVA--- 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 197 QCLR-HCLA-GGEALNSDVRDKWKN-QTGLEIHEGYGQSETVLICGNFR----GSTIKSGSMGKASPPYDVQIVDEEGNV 269
Cdd:PRK12467 769 LPRPqRALVcGGEALQVDLLARVRAlGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILDHYLNP 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 270 LPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRI 341
Cdd:PRK12467 849 VPVGVVGELYIGGAG-----LARGYHRRPALTAerfvpdpfGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRI 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 342 GPVEVESALAEHPAVLESAVVSSPDPIRGEVVkAFIVLSPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKT 421
Cdd:PRK12467 924 ELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLT 1002
|
410
....*....|
gi 1958647527 422 VSGKILRSKL 431
Cdd:PRK12467 1003 PNGKLDRKAL 1012
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
15-434 |
9.89e-26 |
|
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: 109.68 E-value: 9.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 15 YRLQAARVKS------------IITSDALAPHVDAISADCPSLQSRLLVSDtsrpgwinfrELLRVASPEHncLRTRSGD 82
Cdd:cd05906 100 YDEPNARLRKlrhiwqllgspvVLTDAELVAEFAGLETLSGLPGIRVLSIE----------ELLDTAADHD--LPQSRPD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 83 SMA-IYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFWNttdtgWVKaawtLFSAwanGACVFVHELP---- 157
Cdd:cd05906 168 DLAlLMLTSGSTGFPKAVPLTHRNI-LARSAGKIQHNGLTPQDVFLN-----WVP----LDHV---GGLVELHLRAvylg 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 158 --QVDAQT---------ILNTLCRFPITtICCVPTLFRLLVQEDLTR-----YKFQCLRHCLAGGEALNSDVRDKWKN-- 219
Cdd:cd05906 235 cqQVHVPTeeiladplrWLDLIDRYRVT-ITWAPNFAFALLNDLLEEiedgtWDLSSLRYLVNAGEAVVAKTIRRLLRll 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 220 -QTGLE---IHEGYGQSET---VLICGNFRGSTIKSG----SMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpf 288
Cdd:cd05906 314 ePYGLPpdaIRPAFGMTETcsgVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP----- 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 289 CLFNCYLDNPEKTAASEQGD-FYITGDRAHMDeDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLES--AVVSSP 365
Cdd:cd05906 389 VVTKGYYNNPEANAEAFTEDgWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVR 467
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958647527 366 DPIRGEVVKAfIVLSPAYVSHDP-EALTRELQEHVK---TVTAPYKYP-RKvafiSELPKTVSGKILRSKLRNQ 434
Cdd:cd05906 468 DPGAETEELA-IFFVPEYDLQDAlSETLRAIRSVVSrevGVSPAYLIPlPK----EEIPKTSLGKIQRSKLKAA 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-431 |
1.46e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.43 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 72 EHNCLRTRSGDSMA-IYFTSGTTGTPKMVEHSQCSYGLGFVASGRrLMALTESDIFWNTTDTGWVKAAWTLFSAWANGAC 150
Cdd:PRK12316 3186 EANPAIRTMPENLAyVIYTSGSTGKPKGVGIRHSALSNHLCWMQQ-AYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGAR 3264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 151 VFVHELPQVDAQTILNTLCRFP-ITTICCVPTLFRLLVQEDLTRyKFQCLRHCLAGGEALNSDVRDKWknQTGLEIHEGY 229
Cdd:PRK12316 3265 VVLAGPEDWRDPALLVELINSEgVDVLHAYPSMLQAFLEEEDAH-RCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLY 3341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 230 GQSETVLICGNFRGSTIKSGS--MGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAA---- 303
Cdd:PRK12316 3342 GPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGELYLGGEG-----LARGYHNRPGLTAErfvp 3416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 304 ---SEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSspdpIRGEVVKAFIVLS 380
Cdd:PRK12316 3417 dpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPE 3492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 381 payvshDPE-ALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK12316 3493 ------DEAgDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
19-431 |
2.86e-25 |
|
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: 107.74 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 19 AARVKSIItSDAlapHVDAISADCPSLQSRLLVSDTSRPgwinfRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPK- 97
Cdd:cd12114 73 AARREAIL-ADA---GARLVLTDGPDAQLDVAVFDVLIL-----DLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKg 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 98 -MVEHSQCsygLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGAC-VFVHELPQVDAQTILNTLCRFPITT 175
Cdd:cd12114 144 vMISHRAA---LNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATlVLPDEARRRDPAHWAELIERHGVTL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 176 ICCVPTLFRLLVQEDLTRYKFQC-LRHCLAGGEALNSDVRDKWKNQT-GLEIHEGYGQSETVlICGNFRgsTIKSGSMGK 253
Cdd:cd12114 221 WNSVPALLEMLLDVLEAAQALLPsLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEAS-IWSIYH--PIDEVPPDW 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 254 ASPPYDV-------QIVDEEGNVLPPGKEGNIAI--RikptrpfCLFNCYLDNPEKTAAS-----EQGDFYITGDRAHMD 319
Cdd:cd12114 298 RSIPYGRplanqryRVLDPRGRDCPDWVPGELWIggR-------GVALGYLGDPELTAARfvthpDGERLYRTGDLGRYR 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 320 EDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAFIVLSPAYVSHDPEALTRELQEHV 399
Cdd:cd12114 371 PDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQTL 449
|
410 420 430
....*....|....*....|....*....|..
gi 1958647527 400 ktvtAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd12114 450 ----PAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
13-431 |
4.54e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 108.89 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 13 LKYRLQAARVKSIITSDALaphvdaiSADCPSLQSrLLVSDTSRPGWINfrellrvASPEHNCLRTRSGDSMA-IYFTSG 91
Cdd:PRK12316 2092 LAYMLEDSGAALLLTQRHL-------LERLPLPAG-VARLPLDRDAEWA-------DYPDTAPAVQLAGENLAyVIYTSG 2156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 92 TTGTPKMVEHSQCSYGLGFVASGRRlMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHELPQVDAQTILNTLCRF 171
Cdd:PRK12316 2157 STGLPKGVAVSHGALVAHCQAAGER-YELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERH 2235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 172 PITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLE-IHEGYGQSETVLI-----CGNFRGST 245
Cdd:PRK12316 2236 GVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTpllwkCRPQDPCG 2315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 246 IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTA--------ASEQGDFYITGDRAH 317
Cdd:PRK12316 2316 AAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLAR 2390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 318 MDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSpDPIRGEVVKAFIvlspayVSHDP-EALTRELQ 396
Cdd:PRK12316 2391 YRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYV------VPDDAaEDLLAELR 2463
|
410 420 430
....*....|....*....|....*....|....*
gi 1958647527 397 EHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK12316 2464 AWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
82-431 |
1.54e-24 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 105.86 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPKMVehsqcsyglgfVASGRRLMA----LTESDIFWNTtdtgWVKAA---------------WTLF 142
Cdd:PRK05857 170 DPLAMIFTSGTTGEPKAV-----------LLANRTFFAvpdiLQKEGLNWVT----WVVGEttysplpathigglwWILT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 143 SAWANGACVFVHElpqvDAQTILNTLCRFPITTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGG-EALNSDVRdkWKNQ 220
Cdd:PRK05857 235 CLMHGGLCVTGGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSElKSANATVPSLRLVGYGGsRAIAADVR--FIEA 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 221 TGLEIHEGYGQSET-----VLICGNFRGSTIKSGSMGKASPPYDVQIVDEEG------NVLPPGKEGNIAIRikptRPFC 289
Cdd:PRK05857 309 TGVRTAQVYGLSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIK----SPAN 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 290 LFNcYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIR 369
Cdd:PRK05857 385 MLG-YWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEF 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 370 GEVVKAFIVLSPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK05857 464 GALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
32-434 |
1.47e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 102.86 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 32 APHVDAISADCPSLQSRLLVSDTSR-PG----WINFRELLRVASPEHN--CLRTRSGDSMAiyFTSGTTGTPKMVEHSQC 104
Cdd:PRK07008 122 LPLVDALAPQCPNVKGWVAMTDAAHlPAgstpLLCYETLVGAQDGDYDwpRFDENQASSLC--YTSGTTGNPKGALYSHR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 105 SYGL-GFVASGRRLMALTESDIFWNTTDTGWVKAaWTL-FSAWANGaCVFVHELPQVDAQTILNTLCRFPITTICCVPTL 182
Cdd:PRK07008 200 STVLhAYGAALPDAMGLSARDAVLPVVPMFHVNA-WGLpYSAPLTG-AKLVLPGPDLDGKSLYELIEAERVTFSAGVPTV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 183 FRLLVQE-DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSE-----TVLICGNFRGSTIKSGSM----- 251
Cdd:PRK07008 278 WLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEmsplgTLCKLKWKHSQLPLDEQRkllek 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 252 -GKASPPYDVQIVDEEGNVLP-PGKE-GNIAIRikptRPFCLfncylDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFV 327
Cdd:PRK07008 358 qGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVR----GPWVI-----DRYFRGDASPLVDgWFPTGDVATIDADGFMQIT 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 328 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshdpeALTR-ELQEHVKTVTAPY 406
Cdd:PRK07008 429 DRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA------EVTReELLAFYEGKVAKW 502
|
410 420
....*....|....*....|....*...
gi 1958647527 407 KYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK07008 503 WIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
11-434 |
1.92e-23 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 102.59 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 11 KDLKYRLQAARVKSIITSDALA------PHVDAISADCPSLQSRLLVSDTS-----RPGWINFRELLRVASPEH----NC 75
Cdd:PLN03051 31 KEIATRLDISGAKGVFTQDVVLrggralPLYSKVVEAAPAKAIVLPAAGEPvavplREQDLSWCDFLGVAAAQGsvggNE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 76 LRTRSGDS---MAIYFTSGTTGTPKMVEHSQCSyGLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVF 152
Cdd:PLN03051 111 YSPVYAPVesvTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 153 VHElpqvdAQTILNTLCRF----PITTICCVPTLFR--------LLVQEDLTRYKFQCLRhclagGEALNSD-------V 213
Cdd:PLN03051 190 LYG-----GAPLGRGFGKFvqdaGVTVLGLVPSIVKawrhtgafAMEGLDWSKLRVFAST-----GEASAVDdvlwlssV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 214 RDKWKNQT----GLEIHEGYGQSETVLICGNfrgSTIKSGSMGKAsppydVQIVDEEGNVLPPGKE--GNIAIRIkptrP 287
Cdd:PLN03051 260 RGYYKPVIeycgGTELASGYISSTLLQPQAP---GAFSTASLGTR-----FVLLNDNGVPYPDDQPcvGEVALAP----P 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 288 FCLFNCYLDNPEKTAASEQG--DFYITGD--RAHMDE-----DGYFWFVGRNDDVINSSSYRIGPVEVESALAE-HPAVL 357
Cdd:PLN03051 328 MLGASDRLLNADHDKVYYKGmpMYGSKGMplRRHGDImkrtpGGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 358 ESAVVSSPDPIRGE----VVKAFIVLSPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 433
Cdd:PLN03051 408 ETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRD 487
|
.
gi 1958647527 434 Q 434
Cdd:PLN03051 488 Q 488
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
13-431 |
2.15e-23 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 103.59 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 13 LKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRPgwinfrelLRVASPEHnclrtrsgdSMAIYFTSGT 92
Cdd:PRK10252 547 LKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAP--------LQLSQPHH---------TAYIIFTSGS 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 93 TGTPK--MVEHSqcsyglgfvASGRRLM------ALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHElPQV--DAQ 162
Cdd:PRK10252 610 TGRPKgvMVGQT---------AIVNRLLwmqnhyPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAE-PEAhrDPL 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 163 TILNTLCRFPITTICCVPTLFRLLVQE---DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVL--- 236
Cdd:PRK10252 680 AMQQFFAEYGVTTTHFVPSMLAAFVASltpEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVdvs 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 237 ---ICG----NFRGSTIKSGsmgkaSPPYDVQ--IVDEEGNVLPPGKEGNIAIR-IKptrpfcLFNCYLDNPEKTA---- 302
Cdd:PRK10252 760 wypAFGeelaAVRGSSVPIG-----YPVWNTGlrILDARMRPVPPGVAGDLYLTgIQ------LAQGYLGRPDLTAsrfi 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 303 ---ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHP----AVLESAVVSSPDPIRGEVVKa 375
Cdd:PRK10252 829 adpFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQAAATGGDARQ- 907
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647527 376 fIVlspAY-VSHDPEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK10252 908 -LV---GYlVSQSGLPLDTSaLQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
67-431 |
3.87e-23 |
|
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: 101.01 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 67 RVASPEHNCLRTRSGDSMA-IYFTSGTTGTPKMVE-HSQCSygLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSA 144
Cdd:cd17654 103 LSFTPEHRHFNIRTDECLAyVIHTSGTTGTPKIVAvPHKCI--LPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 145 WANGAC---------VFVHELPQVDAQtilntlcRFPITTICCVPTLFRLLVQEDLTRY---KFQCLRHCLAGGEALNSD 212
Cdd:cd17654 181 LSSGATllivptsvkVLPSKLADILFK-------RHRITVLQATPTLFRRFGSQSIKSTvlsATSSLRVLALGGEPFPSL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 213 VRDKWKNQTGLEIH--EGYGQSETVLICGNFRGSTIKSG-SMGKASPPYDVQIVDEEGNvlppGKEGNIAIRIKPTRpfC 289
Cdd:cd17654 254 VILSSWRGKGNRTRifNIYGITEVSCWALAYKVPEEDSPvQLGSPLLGTVIEVRDQNGS----EGTGQVFLGGLNRV--C 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 290 LFNCYLDNPEktaaseqGDFYITGDRAHMdEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDpir 369
Cdd:cd17654 328 ILDDEVTVPK-------GTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ--- 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 370 gEVVKAFIVlspayvshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd17654 397 -QRLIAFIV--------GESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
86-431 |
7.47e-23 |
|
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: 100.59 E-value: 7.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 86 IYFTSGTTGTPK--MVEH-SQCSYGLGFVasgrRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGAC-VFVHELPQVDA 161
Cdd:cd17644 111 VIYTSGSTGKPKgvMIEHqSLVNLSHGLI----KEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATlVLRPEEMRSSL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 162 QTILNTLCRFPITTICCVPTLFRLLVQEDL--TRYKFQCLRHCLAGGEALNSDVRDKWKNQTG--LEIHEGYGQSE---T 234
Cdd:cd17644 187 EDFVQYIQQWQLTVLSLPPAYWHLLVLELLlsTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEatiA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 235 VLIC--GNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptrPFCLFNCYLDNPEKTA---------A 303
Cdd:cd17644 267 ATVCrlTQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIG-----GVGLARGYLNRPELTAekfishpfnS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 304 SEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlsPAY 383
Cdd:cd17644 342 SESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV--PHY 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958647527 384 vshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd17644 420 ---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
20-434 |
7.53e-23 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 100.98 E-value: 7.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 20 ARVKSIITSDALAPHVDAISADCPSLQSRLLVSD------TSRPGWINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTT 93
Cdd:PRK06018 110 AEDRVVITDLTFVPILEKIADKLPSVERYVVLTDaahmpqTTLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 94 GTPKMVEHSQCSYGL-GFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVfVHELPQVDAQTILNTLCRFP 172
Cdd:PRK06018 190 GDPKGVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKL-VMPGAKLDGASVYELLDTEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 173 ITTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQtGLEIHEGYGQSETVLIcGNFrgSTIK---S 248
Cdd:PRK06018 269 VTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMTEMSPL-GTL--AALKppfS 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 249 GSMGKAS---------PPYDVQ--IVDEEGNVLPpgKEGNIAIRIKPTRPfCLFNCYLdNPEKTAASEQGdFYITGDRAH 317
Cdd:PRK06018 345 KLPGDARldvlqkqgyPPFGVEmkITDDAGKELP--WDGKTFGRLKVRGP-AVAAAYY-RVDGEILDDDG-FFDTGDVAT 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 318 MDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvshDPEALTRELQE 397
Cdd:PRK06018 420 IDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKP-----GETATREEILK 494
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958647527 398 HVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:PRK06018 495 YMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
82-428 |
9.89e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 100.21 E-value: 9.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPK--MVEHSQCsygLGFVASGRRLMALTESDIFWNTTDTGWV-KAAWTLFSAWANGA-CVFVHELP 157
Cdd:cd05914 90 DVALINYTSGTTGNSKgvMLTYRNI---VSNVDGVKEVVLLGKGDKILSILPLHHIyPLTFTLLLPLLNGAhVVFLDKIP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 158 QvdAQTILNTLCRFPITTICCVPTLFR------LLVQEDLTRYKFQC------------------------LRHCLAGGE 207
Cdd:cd05914 167 S--AKIIALAFAQVTPTLGVPVPLVIEkifkmdIIPKLTLKKFKFKLakkinnrkirklafkkvheafggnIKEFVIGGA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 208 ALNSDVRDKWKnQTGLEIHEGYGQSETV-LICGNfRGSTIKSGSMGKASPPYDVQIVDEEgnvlPPGKEGNIAIRIKPtr 286
Cdd:cd05914 245 KINPDVEEFLR-TIGFPYTIGYGMTETApIISYS-PPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPN-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 287 pfcLFNCYLDNPEKTAA--SEQGDFYiTGDRAHMDEDGYFWFVGRNDDVINSSSYR-IGPVEVESALAEHPAVLESAVVs 363
Cdd:cd05914 317 ---VMKGYYKNPEATAEafDKDGWFH-TGDLGKIDAEGYLYIRGRKKEMIVLSSGKnIYPEEIEAKINNMPFVLESLVV- 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958647527 364 spdpIRGEVVKAFIVLSPAY-------VSHDPEALTRELQEHVKTVTAPYKYPRKVAFI-SELPKTVSGKILR 428
Cdd:cd05914 392 ----VQEKKLVALAYIDPDFldvkalkQRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
71-431 |
1.05e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.78 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 71 PEHNCLRTRSGDSMA--IYfTSGTTGTPKMVEHSQCSYGLGFVASGRRLmALTESDIFWNTTDTGWVKAAWTLFSAWANG 148
Cdd:PRK12467 1707 SDSNPAVNLAPQNLAyvIY-TSGSTGRPKGAGNRHGALVNRLCATQEAY-QLSAADVVLQFTSFAFDVSVWELFWPLING 1784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 149 ACVFV-----HELPqvdAQTIlNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTG- 222
Cdd:PRK12467 1785 ARLVIappgaHRDP---EQLI-QLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPd 1860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 223 LEIHEGYGQSETVlICGNFRGSTIKSGSMGKASP---PYD---VQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLD 296
Cdd:PRK12467 1861 TGLFNLYGPTETA-VDVTHWTCRRKDLEGRDSVPigqPIAnlsTYILDASLNPVPIGVAGELYLGGVG-----LARGYLN 1934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 297 NPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSpDPI 368
Cdd:PRK12467 1935 RPALTAerfvadpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGA 2013
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647527 369 RGEVVKAFIV-LSPAYVSHD--PEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK12467 2014 NGKQLVAYVVpTDPGLVDDDeaQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
86-431 |
1.11e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 100.46 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 86 IYFTSGTTGTPKMVEHS-QCSYGLGF---------VASGRRLMALTEsdiFWNTTDTGWVKAAWTLfsawanGACVFVHE 155
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRApQLRSAVGVwvtildrtrLRTGSRISVAMP---MFHGLGLGMLMLTIAL------GGTVLTHR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 lpQVDAQTILNTLCRFPITTICCVP-TLFRLLVQEDLTRYK--FQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQS 232
Cdd:PRK13383 250 --HFDAEAALAQASLHRADAFTAVPvVLARILELPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGST 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 233 EtVLICGNFRGSTIKSG--SMGKASPPYDVQIVDEEGNVLPPGKEGNIAI--RIKPTRpfclfncYLDNPEKTAASEQGD 308
Cdd:PRK13383 328 E-VGIGALATPADLRDApeTVGKPVAGCPVRILDRNNRPVGPRVTGRIFVggELAGTR-------YTDGGGKAVVDGMTS 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 309 fyiTGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvsHDP 388
Cdd:PRK13383 400 ---TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG---SGV 473
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958647527 389 EAltRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK13383 474 DA--AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
80-436 |
2.50e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 100.63 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 80 SGDSMA-IYFTSGTTGTPKMVehsqcsyGLGFVASGRRLM------ALTESDIFWNTTDTGWVKAAWTLFSAWANGaCVF 152
Cdd:PRK05691 1271 HGDNLAyVIYTSGSTGQPKGV-------GNTHAALAERLQwmqatyALDDSDVLMQKAPISFDVSVWECFWPLITG-CRL 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 153 VHELP--QVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRykfQC--LRHCLAGGEALNSDVRDKWKNQ-TGLEIHE 227
Cdd:PRK05691 1343 VLAGPgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA---ACtsLRRLFSGGEALPAELRNRVLQRlPQVQLHN 1419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 228 GYGQSETVLICGNFRGStiksGSMGKASP---PYD---VQIVDEEGNVLPPGKEGNIAIRikptrPFCLFNCYLDNPEKT 301
Cdd:PRK05691 1420 RYGPTETAINVTHWQCQ----AEDGERSPigrPLGnvlCRVLDAELNLLPPGVAGELCIG-----GAGLARGYLGRPALT 1490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 302 AA-------SEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVsspdpIRGEVV 373
Cdd:PRK05691 1491 AErfvpdplGEDGArLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAA 1565
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958647527 374 KAFIVlspAYVSHD--PEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 436
Cdd:PRK05691 1566 GAQLV---GYYTGEagQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVW 1627
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
37-432 |
9.39e-22 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 97.50 E-value: 9.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 37 AISADCPSLQSRLLVSDTSRPGWINFRELLRVASPEHNCLR-TRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASG- 114
Cdd:cd05915 108 PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVrVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASl 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 115 RRLMALTESDIFWNTTD----TGWVkAAWTLFSAwaNGACVFVHELPqvDAQTILNTLCRFPITTICCVPTLFRLLVQ-E 189
Cdd:cd05915 188 VDGTALSEKDVVLPVVPmfhvNAWC-LPYAATLV--GAKQVLPGPRL--DPASLVELFDGEGVTFTAGVPTVWLALADyL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 190 DLTRYKFQCLRHCLAGGEAlNSDVRDKWKNQTGLEIHEGYGQSEtVLICGNF-----RGSTIKSGSMGKASPPYDVQIVD 264
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTE-TSPVVVQnfvksHLESLSEEEKLTLKAKTGLPIPL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 265 EEGNVLPPGK----EGNIAIRIKPTRPFCLFNCYLDNPEKTAASE-QGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSY 339
Cdd:cd05915 341 VRLRVADEEGrpvpKDGKALGEVQLKGPWITGGYYGNEEATRSALtPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 340 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpEALTRELQEHVKTVTAPYKY-PRKVAFISEL 418
Cdd:cd05915 421 WISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGE------KPTPEELNEHLLKAGFAKWQlPDAYVFAEEI 494
|
410
....*....|....
gi 1958647527 419 PKTVSGKILRSKLR 432
Cdd:cd05915 495 PRTSAGKFLKRALR 508
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
62-415 |
2.44e-21 |
|
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: 96.38 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 62 FRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGfVASGRRLMALTESDIFWNTTDTGWVKAAWTL 141
Cdd:cd05932 118 WDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWA-AQAGIEHIGTEENDRMLSYLPLAHVTERVFV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 142 FSAWANGACV--FVHELpqvdaQTILNTLCRFPITTICCVP---TLFRLLVQEDLTRYKFQCL----------------- 199
Cdd:cd05932 197 EGGSLYGGVLvaFAESL-----DTFVEDVQRARPTLFFSVPrlwTKFQQGVQDKIPQQKLNLLlkipvvnslvkrkvlkg 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 200 ---RHC--LAGGEALNSDVRDKWKNQTGLEIHEGYGQSEtvlicgNFRGSTI------KSGSMGKASPPYDVQIvDEEGN 268
Cdd:cd05932 272 lglDQCrlAGCGSAPVPPALLEWYRSLGLNILEAYGMTE------NFAYSHLnypgrdKIGTVGNAGPGVEVRI-SEDGE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 269 VLppgkegniairikpTRPFCLFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYR-IGPVEV 346
Cdd:cd05932 345 IL--------------VRSPALMMGYYKDPEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFKTSKGKyVAPAPI 410
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958647527 347 ESALAEHPAVLESAVVSS--PDPIRGEVVKAFIVlsPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFI 415
Cdd:cd05932 411 ENKLAEHDRVEMVCVIGSglPAPLALVVLSEEAR--LRADAFARAELEASLRAHLARVNSTLDSHEQLAGI 479
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
71-431 |
3.53e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 96.77 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 71 PEHNCLRTRSGDSMA-IYFTSGTTGTPK--MVEHS---------QCSYGLGfvASGRRLMALTES-DIfwnttdtgwvkA 137
Cdd:PRK12467 3226 SENNPSTRVMGENLAyVIYTSGSTGKPKgvGVRHGalanhlcwiAEAYELD--ANDRVLLFMSFSfDG-----------A 3292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 138 AWTLFSAWANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQeDLTRYKFQCLRHCLAGGEALNSD----V 213
Cdd:PRK12467 3293 QERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAE-DAGGADCASLDIYVFGGEAVPPAafeqV 3371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 214 RDKWKNQTgleIHEGYGQSETVLI-----CGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpf 288
Cdd:PRK12467 3372 KRKLKPRG---LTNGYGPTEAVVTvtlwkCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV----- 3443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 289 CLFNCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESA 360
Cdd:PRK12467 3444 GLARGYHQRPSLTAerfvadpfSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAV 3523
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 361 VVSSpDPIRGEVVKAFIVLspayvsHDP-EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK12467 3524 VLAR-DGAGGKQLVAYVVP------ADPqGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
86-431 |
1.87e-20 |
|
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: 93.31 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 86 IYFTSGTTGTPK--MVEHSQCsygLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVF-VHELPQVDAQ 162
Cdd:cd17656 133 IIYTSGTTGKPKgvQLEHKNM---VNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYiIREETKRDVE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 163 TILNTLCRFPITTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGGEAL--NSDVRDKWKNQtGLEIHEGYGQSETVLICg 239
Cdd:cd17656 210 QLFDLVKRHNIEVVFLPVAFLKFIFSErEFINRFPTCVKHIITAGEQLviTNEFKEMLHEH-NVHLHNHYGPSETHVVT- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 240 nfrGSTIKSGSMGKASPPY-------DVQIVDEEGNVLPPGKEGNIAIrikptRPFCLFNCYLDNPEKTAASEQGD---- 308
Cdd:cd17656 288 ---TYTINPEAEIPELPPIgkpisntWIYILDQEQQLQPQGIVGELYI-----SGASVARGYLNRQELTAEKFFPDpfdp 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 309 ---FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayvs 385
Cdd:cd17656 360 nerMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM------ 433
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958647527 386 hDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd17656 434 -EQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
78-426 |
2.39e-20 |
|
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: 92.85 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 78 TRSGDSMAIYFTSGTTGTPK--MVEHSqcsyglGFVASGRRLMALtesdIFWNTTDTgwvkAAWTLFSAWangacVFVHE 155
Cdd:cd17648 91 TNSTDLAYAIYTSGTTGKPKgvLVEHG------SVVNLRTSLSER----YFGRDNGD----EAVLFFSNY-----VFDFF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 LPQ-VDAQTILNTLCRFPITTICCVPTLFRLLVQEDLT----------RYKFQCLRH---CLAGGEALNSDVRDKWKNQT 221
Cdd:cd17648 152 VEQmTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTylsgtpsvlqQYDLARLPHlkrVDAAGEEFTAPVFEKLRSRF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 222 GLEIHEGYGQSETVL--ICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptrPFCLFNCYLDNPE 299
Cdd:cd17648 232 AGLIINAYGPTETTVtnHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLG-----GDGVARGYLNRPE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 300 KTA--------ASEQ-------GDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSS 364
Cdd:cd17648 307 LTAerflpnpfQTEQerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAK 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958647527 365 PDP-IRGEVVKAFIVlspAYVSHDPEALTR-ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKI 426
Cdd:cd17648 387 EDAsQAQSRIQKYLV---GYYLPEPGHVPEsDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-431 |
1.57e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 91.94 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 2 IPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDaisadcpsLQSRLLVSDTSRPG-WINfrellrvASPEHNCLRTRS 80
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLP--------LAAGVQVLDLDRPAaWLE-------GYSEENPGTELN 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 81 GDSMA-IYFTSGTTGTPKMV--EHS---------QCSYGLGfvASGRRLMALTES-DIfwnttdtgwvkAAWTLFSAWAN 147
Cdd:PRK12316 654 PENLAyVIYTSGSTGKPKGAgnRHRalsnrlcwmQQAYGLG--VGDTVLQKTPFSfDV-----------SVWEFFWPLMS 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 148 GACVfvHELPQ---VDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRykfQC--LRHCLAGGEALNSDVRDKW---KN 219
Cdd:PRK12316 721 GARL--VVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA---SCtsLRRIVCSGEALPADAQEQVfakLP 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 220 QTGLEIHegYGQSETV--LICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDN 297
Cdd:PRK12316 796 QAGLYNL--YGPTEAAidVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRG-----LARGYHGR 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 298 PEKTA----ASEQGD---FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSspdpIRG 370
Cdd:PRK12316 869 PGLTAerfvPSPFVAgerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDG 944
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 371 EVVKAFIVLSpayvshDPEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK12316 945 KQLVGYVVLE------SEGGDWREaLKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
17-431 |
3.43e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 91.00 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 17 LQAARVKSIITSDAlAPhVDAISADCPSLQSRLL--VSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMA-IYFTSGTT 93
Cdd:PRK05691 3804 LPAQRLQRIIELSR-TP-VLVCSAACREQARALLdeLGCANRPRLLVWEEVQAGEVASHNPGIYSGPDNLAyVIYTSGST 3881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 94 GTPK--MVEH--------SQCSYglgfvasgrrlMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVheLPQV---D 160
Cdd:PRK05691 3882 GLPKgvMVEQrgmlnnqlSKVPY-----------LALSEADVIAQTASQSFDISVWQFLAAPLFGARVEI--VPNAiahD 3948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 161 AQTILNTLCRFPITTICCVPTLFRLLVQEDltRYKFQCLRHCLAGGEALNSDVRDKWKN---QTGLEihEGYGQSETVLI 237
Cdd:PRK05691 3949 PQGLLAHVQAQGITVLESVPSLIQGMLAED--RQALDGLRWMLPTGEAMPPELARQWLQrypQIGLV--NAYGPAECSDD 4024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 238 CGNFR-------GSTIKSGSmgkaspPYD---VQIVDEEGNVLPPGKEGNIairikptrpfCLFNC-----YLDNPEKTA 302
Cdd:PRK05691 4025 VAFFRvdlastrGSYLPIGS------PTDnnrLYLLDEALELVPLGAVGEL----------CVAGTgvgrgYVGDPLRTA 4088
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 303 AS-------EQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVK 374
Cdd:PRK05691 4089 LAfvphpfgAPGErLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLV 4167
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958647527 375 AFIVlsPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK05691 4168 GYLV--PHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
76-431 |
4.71e-19 |
|
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: 89.06 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 76 LRTRSGDSMAIYFTSGTTGTPK--MVEHSQCS---------YGLGFVASGRRLMALTESDIFwnttdtgwvkAAWTLFSA 144
Cdd:cd17650 88 LLTQPEDLAYVIYTSGTTGKPKgvMVEHRNVAhaahawrreYELDSFPVRLLQMASFSFDVF----------AGDFARSL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 145 WANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGGEAlnsdVRDKWKNQ--- 220
Cdd:cd17650 158 LNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIVGSDG----CKAQDFKTlaa 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 221 ---TGLEIHEGYGQSETVLICGNFRGS-----TIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAI------Rikptr 286
Cdd:cd17650 234 rfgQGMRIINSYGVTEATIDSTYYEEGrdplgDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIggagvaR----- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 287 pfclfnCYLDNPEKTAA-------SEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLES 359
Cdd:cd17650 309 ------GYLNRPELTAErfvenpfAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEA 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647527 360 AVVSSPDPiRGEvvkAFIVlspAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd17650 383 VVAVREDK-GGE---ARLC---AYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
267-432 |
6.64e-19 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 88.51 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 267 GNVLP-------PGKEGNIAIRIKPtrpfcLFNCYLdnPEKTAASEqgdFYITGDRAHMDEDGYFWFVGRNDDVINSSSY 339
Cdd:PRK07445 286 GQVLPhaqitipANQTGNITIQAQS-----LALGYY--PQILDSQG---IFETDDLGYLDAQGYLHILGRNSQKIITGGE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 340 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFivlspaYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELP 419
Cdd:PRK07445 356 NVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAI------YVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLP 429
|
170
....*....|...
gi 1958647527 420 KTVSGKILRSKLR 432
Cdd:PRK07445 430 RNPQGKINRQQLQ 442
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
42-398 |
3.05e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 86.88 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 42 CPSLQSRLLVSDTSRPGWINFRELLRVASP-EHNCLRTRSGDSMAIYFTSGTTGTPKMV--EHSQcsyglgFVAsgrRLM 118
Cdd:PRK09274 134 KPSVRRLVTVGGRLLWGGTTLATLLRDGAAaPFPMADLAPDDMAAILFTSGSTGTPKGVvyTHGM------FEA---QIE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 119 ALTES-DIFWNTTDTgwvkAAWTLFS--AWANGACVFVHEL----P-QVDAQTILNTLCRFPITTICCVPTLFRLLVQED 190
Cdd:PRK09274 205 ALREDyGIEPGEIDL----PTFPLFAlfGPALGMTSVIPDMdptrPaTVDPAKLFAAIERYGVTNLFGSPALLERLGRYG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 191 LTR-YKFQCLRHCLAGG------------EALNSDVrdkwknqtglEIHEGYGQSETVLICG-----NFRGSTIKSGSM- 251
Cdd:PRK09274 281 EANgIKLPSLRRVISAGapvpiavierfrAMLPPDA----------EILTPYGATEALPISSiesreILFATRAATDNGa 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 252 ----GKASPPYDVQIVD---------EEGNVLPPGKEGNIAIRiKP--TRpfclfnCYLDNPEKTAAS----EQGDFY-I 311
Cdd:PRK09274 351 gicvGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVA-GPmvTR------SYYNRPEATRLAkipdGQGDVWhR 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 312 TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPirGEVVKAFIVLSPAYVSHDPEAL 391
Cdd:PRK09274 424 MGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPVLCVELEPGVACSKSAL 501
|
....*..
gi 1958647527 392 TRELQEH 398
Cdd:PRK09274 502 YQELRAL 508
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
80-433 |
6.11e-18 |
|
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: 85.87 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 80 SGDSMA-IYFTSGTTGTPK--MVEHSQCSYGLGFVAS------GRRLMALTESdifWNTTDtgwvKAAWTLFSAWAnGAC 150
Cdd:cd17640 86 DSDDLAtIIYTSGTTGNPKgvMLTHANLLHQIRSLSDivppqpGDRFLSILPI---WHSYE----RSAEYFIFACG-CSQ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 151 VFVhelpqvDAQTILNTLCRFPITTICCVPTLFRLL---VQEDLTRYKF------------QCLRHCLAGGEALNSDVrD 215
Cdd:cd17640 158 AYT------SIRTLKDDLKRVKPHYIVSVPRLWESLysgIQKQVSKSSPikqflflfflsgGIFKFGISGGGALPPHV-D 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 216 KWKNQTGLEIHEGYGQSET--VLICGNFRGSTIksGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAIRIKPtrpfcLFN 292
Cdd:cd17640 231 TFFEAIGIEVLNGYGLTETspVVSARRLKCNVR--GSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQ-----VMK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 293 CYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVIN-SSSYRIGPVEVESALAEHPaVLESAVVSSPDPIRg 370
Cdd:cd17640 304 GYYKNPEATSKVLDSDgWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSP-FIEQIMVVGQDQKR- 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958647527 371 evVKAFIVlsPayvshDPEALTRELQEhvktvtapykypRKVAFISELPKTVSGKILRSKLRN 433
Cdd:cd17640 382 --LGALIV--P-----NFEELEKWAKE------------SGVKLANDRSQLLASKKVLKLYKN 423
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
252-431 |
7.80e-18 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 85.33 E-value: 7.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 252 GKASPPYDVQIVDEEGNVLPPGKEGNIAIrIKPtrpfCLFNCYLDNPEKTAA---SEQGD-FYITGDRAHMDeDGYFWFV 327
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVI-SGP----SVSKGYLNNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 328 GRNDDVINSSSYRIGPVEVESALAEHPAVlESAVVSspdPI-RGEVVK---AFIVLSPAYVSHDpEALTRELQEHVKTVT 403
Cdd:PRK04813 395 GRIDFQIKLNGYRIELEEIEQNLRQSSYV-ESAVVV---PYnKDHKVQyliAYVVPKEEDFERE-FELTKAIKKELKERL 469
|
170 180
....*....|....*....|....*...
gi 1958647527 404 APYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK04813 470 MEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
66-434 |
1.32e-17 |
|
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: 84.71 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 66 LRVASPEHnCLRTRSgdsMAIYfTSGTTGTPK--MVEHSQCSYGLGFVASGRRLMAlteSDIFWNTTD--------TGWV 135
Cdd:cd05940 71 LNVSSAKH-LVVDAA---LYIY-TSGTTGLPKaaIISHRRAWRGGAFFAGSGGALP---SDVLYTCLPlyhstaliVGWS 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 136 K---AAWTL-----FSA---W----ANGACVFVHelpqvdaqtiLNTLCRFpittICCVPTlfrllvQEDLTRYKFQClr 200
Cdd:cd05940 143 AclaSGATLvirkkFSAsnfWddirKYQATIFQY----------IGELCRY----LLNQPP------KPTERKHKVRM-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 201 hclAGGEALNSDVRDKWKNQTGL-EIHEGYGQSETVLICGNFRGstiKSGSMGKASPP-----------YDVQ----IVD 264
Cdd:cd05940 201 ---IFGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFINFFG---KPGAIGRNPSLlrkvaplalvkYDLEsgepIRD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 265 EEGNV--LPPGKEGNIAIRIKPTRPFclfNCYLDNPEKTA-----ASEQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINS 336
Cdd:cd05940 275 AEGRCikVPRGEPGLLISRINPLEPF---DGYTDPAATEKkilrdVFKKGDAWFnTGDLMRLDGEGFWYFVDRLGDTFRW 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 337 SSYRIGPVEVESALAEHPAVLESAV--VSSPDpIRGEVVKAFIVLSPAYvSHDPEALTRELQEHVktvtAPYKYPRKVAF 414
Cdd:cd05940 352 KGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAAIVLQPNE-EFDLSALAAHLEKNL----PGYARPLFLRL 425
|
410 420
....*....|....*....|
gi 1958647527 415 ISELPKTVSGKILRSKLRNQ 434
Cdd:cd05940 426 QPEMEITGTFKQQKVDLRNE 445
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
6-366 |
4.74e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 83.39 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 6 SQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADcPSLQSRLLVSD----TSRPGWINFRELLRvASPEHNcLRTRSG 81
Cdd:PRK08279 119 TQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARAD-LARPPRLWVAGgdtlDDPEGYEDLAAAAA-GAPTTN-PASRSG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSM---AIY-FTSGTTGTPK--MVEHS--QCSYGlGFVAsgrrLMALTESDIFWNTT----DTGWVkAAWTlfSAWANGA 149
Cdd:PRK08279 196 VTAkdtAFYiYTSGTTGLPKaaVMSHMrwLKAMG-GFGG----LLRLTPDDVLYCCLplyhNTGGT-VAWS--SVLAAGA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 150 CVFVHELPQV-----DAQtilntlcRFPITTICCVPTLFRLLVQ----EDLTRYKfqcLRhcLAGGEALNSDVRDKWKNQ 220
Cdd:PRK08279 268 TLALRRKFSAsrfwdDVR-------RYRATAFQYIGELCRYLLNqppkPTDRDHR---LR--LMIGNGLRPDIWDEFQQR 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 221 TGLE-IHEGYGQSE--TVLIcgNFRGstiKSGSMGKaSPP----------YDVQ----IVDEEGNVLP--PGKEGNIAIR 281
Cdd:PRK08279 336 FGIPrILEFYAASEgnVGFI--NVFN---FDGTVGR-VPLwlahpyaivkYDVDtgepVRDADGRCIKvkPGEVGLLIGR 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 282 IKPTRPFclfNCYLDnPEKTAAS------EQGDFYI-TGDRAHMDEDGYFWFVGRNDDvinssSYR-----IGPVEVESA 349
Cdd:PRK08279 410 ITDRGPF---DGYTD-PEASEKKilrdvfKKGDAWFnTGDLMRDDGFGHAQFVDRLGD-----TFRwkgenVATTEVENA 480
|
410
....*....|....*....
gi 1958647527 350 LAEHPAVLESAV--VSSPD 366
Cdd:PRK08279 481 LSGFPGVEEAVVygVEVPG 499
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
312-428 |
6.49e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 82.39 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 312 TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfivlspAYVSH---DP 388
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA------KVISHeeiDP 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958647527 389 EALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILR 428
Cdd:PRK08308 369 VQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSR 404
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
6-436 |
1.71e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 81.75 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 6 SQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLV--SDTSRPGwINFRELLRVASPEhNCLRTRSG-- 81
Cdd:PRK05620 96 KQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECPCVRAVVFIgpSDADSAA-AHMPEGIKVYSYE-ALLDGRSTvy 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 --------DSMAIYFTSGTTGTPKMVEHSQCSYGLgfvasgrRLMALTESDIFWNTTDTGWVKA-------AWTL-FSAW 145
Cdd:PRK05620 174 dwpeldetTAAAICYSTGTTGAPKGVVYSHRSLYL-------QSLSLRTTDSLAVTHGESFLCCvpiyhvlSWGVpLAAF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 146 ANGA-CVFV-HEL-PQVDAQTILNTLCRfpitTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQT 221
Cdd:PRK05620 247 MSGTpLVFPgPDLsAPTLAKIIATAMPR----VAHGVPTLWiQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERY 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 222 GLEIHEGYGQSETVLIcgnfrGSTIK--SGSMGKASPPYDV-----------QIVDEeGNVLPPG--KEGNIAIRiKPTr 286
Cdd:PRK05620 323 GVDVVHVWGMTETSPV-----GTVARppSGVSGEARWAYRVsqgrfpasleyRIVND-GQVMESTdrNEGEIQVR-GNW- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 287 pfcLFNCYLDNPEKT---AASEQGDFYI--------------TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESA 349
Cdd:PRK05620 395 ---VTASYYHSPTEEgggAASTFRGEDVedandrftadgwlrTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENY 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 350 LAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshDPEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKI-- 426
Cdd:PRK05620 472 IMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGI---EPTRETAErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFdk 548
|
490
....*....|..
gi 1958647527 427 --LRSKLRNQEW 436
Cdd:PRK05620 549 kdLRQHLADGDF 560
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
64-431 |
2.18e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.06 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 64 ELLRVASPEHNclrtrsgdSMAIYfTSGTTGTPKMVEHSQCSYGLGFVASGRRLmALTESDIFWNTTDTGWVKAAWTLFS 143
Cdd:PRK05691 2325 PLPFLSLPQHQ--------AYLIY-TSGSTGKPKGVVVSHGEIAMHCQAVIERF-GMRADDCELHFYSINFDAASERLLV 2394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 144 AWANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSD----VRDKWKN 219
Cdd:PRK05691 2395 PLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEhlqrIRQAFAP 2474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 220 QtglEIHEGYGQSETVLI-CGNFRGSTIKSGS----MGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCY 294
Cdd:PRK05691 2475 Q---LFFNAYGPTETVVMpLACLAPEQLEEGAasvpIGRVVGARVAYILDADLALVPQGATGELYVGGAG-----LAQGY 2546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 295 LDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLEsAVVSSPD 366
Cdd:PRK05691 2547 HDRPGLTAerfvadpfAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE-AVVLALD 2625
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647527 367 PIRGEVVKAFIVLSPAYVSHDPEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:PRK05691 2626 TPSGKQLAGYLVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
203-432 |
6.52e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.85 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 203 LAGGEALNSDVRDKWKnQTGLEIHEGYGQSETvliCGnfrgstiksGSMGKASPPYDVQIVDEEGNVLPPGkegniairi 282
Cdd:PRK07824 157 LVGGGPAPAPVLDAAA-AAGINVVRTYGMSET---SG---------GCVYDGVPLDGVRVRVEDGRIALGG--------- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 283 kPTrpfcLFNCYLDNPEKTAASEQGDFyITGDRAHMDeDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 362
Cdd:PRK07824 215 -PT----LAKGYRNPVDPDPFAEPGWF-RTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 363 SSPDPIRGEVVKAFIVLSPAyvshdPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 432
Cdd:PRK07824 288 GLPDDRLGQRVVAAVVGDGG-----PAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
16-434 |
6.86e-15 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 77.04 E-value: 6.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 16 RLQAARVKSIITSD-----------------ALAPHVDAISADCPSLQSRLLVSDTSrpgWINFRELLR-VASPEHNCLR 77
Cdd:PLN03052 275 RLKISKAKAIFTQDvivrggksiplysrvveAKAPKAIVLPADGKSVRVKLREGDMS---WDDFLARANgLRRPDEYKAV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 78 TRSGDS-MAIYFTSGTTGTPKMVEHSQCSyGLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACV----- 151
Cdd:PLN03052 352 EQPVEAfTNILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDIVCWPTNLGWMMGPWLVYASLLNGATLalyng 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 152 ---------FVHelpqvDAQ-TILNTlcrfpitticcVPTLFRLL----VQEDLTRYKFQCLRhclAGGEALNSD----- 212
Cdd:PLN03052 431 splgrgfakFVQ-----DAKvTMLGT-----------VPSIVKTWkntnCMAGLDWSSIRCFG---STGEASSVDdylwl 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 213 -VRDKWKnqtglEIHEGYGQSEtvlICGNF-RGSTIKSGSMGKASPP---YDVQIVDEEGNVLP---PGKeGNIAirikp 284
Cdd:PLN03052 492 mSRAGYK-----PIIEYCGGTE---LGGGFvTGSLLQPQAFAAFSTPamgCKLFILDDSGNPYPddaPCT-GELA----- 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 285 trpfcLFNCYLDNPEKTAASEQGDFYITGD--------RAHMDE-----DGYFWFVGRNDDVINSSSYRIGPVEVESAL- 350
Cdd:PLN03052 558 -----LFPLMFGASSTLLNADHYKVYFKGMpvfngkilRRHGDIfertsGGYYRAHGRADDTMNLGGIKVSSVEIERVCn 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 351 AEHPAVLESAVVSSPDPIRG--EVVKAFIVLSPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 428
Cdd:PLN03052 633 AADESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMR 712
|
....*.
gi 1958647527 429 SKLRNQ 434
Cdd:PLN03052 713 RVLRQQ 718
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
19-426 |
1.67e-14 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 75.77 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 19 AARVKSIITSDA------LAPHVDAISAdcpslQSRLLVSDTSRPG---WINFRELLRVASPEHNCLRTRSGDSMAIYFT 89
Cdd:PRK06814 727 AAQVKTVLTSRAfiekarLGPLIEALEF-----GIRIIYLEDVRAQiglADKIKGLLAGRFPLVYFCNRDPDDPAVILFT 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 90 SGTTGTPKmvehsqcsyglGFVASGRRLMA----------LTESDIFWNttdtgwvkaAWTLFSAWA----------NGA 149
Cdd:PRK06814 802 SGSEGTPK-----------GVVLSHRNLLAnraqvaaridFSPEDKVFN---------ALPVFHSFGltgglvlpllSGV 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 150 CVFVHELP-----------QVDAqTILntlcrFPITTIccvptlfrllvqedLT-------RYKFQCLRHCLAGGEALNS 211
Cdd:PRK06814 862 KVFLYPSPlhyriipeliyDTNA-TIL-----FGTDTF--------------LNgyaryahPYDFRSLRYVFAGAEKVKE 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 212 DVRDKWKNQTGLEIHEGYGQSET--VLICgnfrgST---IKSGSMGKASPPYD-----VQIVDEEGNVLPPGKegNIAIR 281
Cdd:PRK06814 922 ETRQTWMEKFGIRILEGYGVTETapVIAL-----NTpmhNKAGTVGRLLPGIEyrlepVPGIDEGGRLFVRGP--NVMLG 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 282 ikptrpfclfncYL--DNPEKTAASEQGdFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLES 359
Cdd:PRK06814 995 ------------YLraENPGVLEPPADG-WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALH 1061
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647527 360 AVVSSPDPIRGEVvkafIVLspayVSHDPEALTRELQEHVKTVTAPYKY-PRKVAFISELPKTVSGKI 426
Cdd:PRK06814 1062 AAVSIPDARKGER----IIL----LTTASDATRAAFLAHAKAAGASELMvPAEIITIDEIPLLGTGKI 1121
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
35-427 |
1.66e-13 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 72.30 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 35 VDAISADCPSLQSRLLVSDTSRPGWINFRELLRVASPEhNCLRTRSG-----------DSMAIYFTSGTTGTPKMVEHSq 103
Cdd:cd05943 193 VAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAKALTLE-DFLATGAAgelefeplpfdHPLYILYSSGTTGLPKCIVHG- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 104 csyglgfvASGRRLMALTE---------SD-IFWNTTdTGWVKAAWtLFSAWANGA-CVFVHELPQVDAQTILNTLC-RF 171
Cdd:cd05943 271 --------AGGTLLQHLKEhilhcdlrpGDrLFYYTT-CGWMMWNW-LVSGLAVGAtIVLYDGSPFYPDTNALWDLAdEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 172 PITTICCVPTLFRLLVQEDL---TRYKFQCLRHCLAGGEALNSD----VRDKWKNqtGLEIHEGYGQSEtvlICGNF-RG 243
Cdd:cd05943 341 GITVFGTSAKYLDALEKAGLkpaETHDLSSLRTILSTGSPLKPEsfdyVYDHIKP--DVLLASISGGTD---IISCFvGG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 244 STIKSGSMGKASPPY---DVQIVDEEGNVLPpGKEGNIAIrikpTRPFCLFNCYLDNPEKTAASEQGDF------YITGD 314
Cdd:cd05943 416 NPLLPVYRGEIQCRGlgmAVEAFDEEGKPVW-GEKGELVC----TKPFPSMPVGFWNDPDGSRYRAAYFakypgvWAHGD 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 315 RAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpEALTRE 394
Cdd:cd05943 491 WIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------VELDDE 564
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958647527 395 LQEHVKTVTA----PYKYPRKVAFISELPKTVSGKIL 427
Cdd:cd05943 565 LRKRIRSTIRsalsPRHVPAKIIAVPDIPRTLSGKKV 601
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
82-434 |
1.05e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 69.64 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIY-FTSGTTGTPKMVehsQCSYGlGFVASGRRLMALTESDIfwnttDTGwVKAAW-TLFsawangacvfvHE---- 155
Cdd:PRK07768 152 DDLALMqLTSGSTGSPKAV---QITHG-NLYANAEAMFVAAEFDV-----ETD-VMVSWlPLF-----------HDmgmv 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 ----LP-QVDAQTILNTLCRF---PIT----------TICCVP----TLF--RLLVQEDLTRYKFQCLRHCLAGGEALNS 211
Cdd:PRK07768 211 gfltVPmYFGAELVKVTPMDFlrdPLLwaeliskyrgTMTAAPnfayALLarRLRRQAKPGAFDLSSLRFALNGAEPIDP 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 212 DVRDKWKNQT---GLE---IHEGYGQSETVLI-----CGN---------------------FRGSTIKSGSMGKASPPYD 259
Cdd:PRK07768 291 ADVEDLLDAGarfGLRpeaILPAYGMAEATLAvsfspCGAglvvdevdadllaalrravpaTKGNTRRLATLGPPLPGLE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 260 VQIVDEEGNVLPPGKEGNIAIRIKPTRPFclfncYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSY 339
Cdd:PRK07768 371 VRVVDEDGQVLPPRGVGVIELRGESVTPG-----YLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGR 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 340 RIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAFIVLSPAYVSHDPEALTRELQEHVKTVTAPYKY-PRKVAFIS-- 416
Cdd:PRK07768 446 NIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVrPRNVVVLGpg 524
|
410
....*....|....*...
gi 1958647527 417 ELPKTVSGKILRSKLRNQ 434
Cdd:PRK07768 525 SIPKTPSGKLRRANAAEL 542
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
15-432 |
3.02e-12 |
|
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: 68.42 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 15 YRLQA----ARVKSIITSDALAPHVDAISADCPSLqsrllvsdtsRPGWINFRELLRVASPEHNCLRTRSGDSMA-IYFT 89
Cdd:cd05931 88 ERLAAiladAGPRVVLTTAAALAAVRAFAASRPAA----------GTPRLLVVDLLPDTSAADWPPPSPDPDDIAyLQYT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 90 SGTTGTPK--MVEHsqcsyglgfvasgRRLMA---LTESDIFWNTTDTGwvkAAW-----------TLFSAWANGA-CVF 152
Cdd:cd05931 158 SGSTGTPKgvVVTH-------------RNLLAnvrQIRRAYGLDPGDVV---VSWlplyhdmgligGLLTPLYSGGpSVL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 153 VHELPQVdAQTI--LNTLCRFPITtICCVPTL-FRLLVQ----EDLTRYKFQCLRHCLAGGEALNSDVRDKWKN---QTG 222
Cdd:cd05931 222 MSPAAFL-RRPLrwLRLISRYRAT-ISAAPNFaYDLCVRrvrdEDLEGLDLSSWRVALNGAEPVRPATLRRFAEafaPFG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 223 LE---IHEGYGQSETVLI--------------------CGNFRGSTIKSG------SMGKASPPYDVQIVDEEGN-VLPP 272
Cdd:cd05931 300 FRpeaFRPSYGLAEATLFvsggppgtgpvvlrvdrdalAGRAVAVAADDPaarelvSCGRPLPDQEVRIVDPETGrELPD 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 273 GKEGNIAIRIKPTRPfclfnCYLDNPEKTAASEQ-------GDFYITGDRAHMDeDGYFWFVGRNDDVINSSSYRIGPVE 345
Cdd:cd05931 380 GEVGEIWVRGPSVAS-----GYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQD 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 346 VESALAEHPAVLES---AVVSSPDPIRGEVVkAFIVLSPAYVSHDPEALTRELQEHVKT---VTapykyPRKVAFIS--E 417
Cdd:cd05931 454 IEATAEEAHPALRPgcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAVARehgVA-----PADVVLVRpgS 527
|
490
....*....|....*
gi 1958647527 418 LPKTVSGKILRSKLR 432
Cdd:cd05931 528 IPRTSSGKIQRRACR 542
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
59-425 |
6.60e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 67.43 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 59 WInFRELLrvaSPEHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFwnttdtgwvKAA 138
Cdd:PRK08043 347 WI-FAHLL---MPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRF---------MSA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 139 WTLFSAWA----------NGACVFVHELPQ-----------------VDAQTILNTLCRF--Pitticcvptlfrllvqe 189
Cdd:PRK08043 413 LPLFHSFGltvglftpllTGAEVFLYPSPLhyrivpelvydrnctvlFGTSTFLGNYARFanP----------------- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 190 dltrYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSE---TVLIcgNFRGSTiKSGSMGKASPPYDVQIVdee 266
Cdd:PRK08043 476 ----YDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEcapVVSI--NVPMAA-KPGTVGRILPGMDARLL--- 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 267 gNVlpPGKE--GNIAIRiKPTrpfcLFNCYL--DNPEK----TAASEQGD----FYITGDRAHMDEDGYFWFVGRNDDVI 334
Cdd:PRK08043 546 -SV--PGIEqgGRLQLK-GPN----IMNGYLrvEKPGVlevpTAENARGEmergWYDTGDIVRFDEQGFVQIQGRAKRFA 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 335 NSSSYRIGPVEVES-ALAEHPAVLESAVVSSpDPIRGEVVKAFivlspayvSHDPEaLTRE-LQEHVKTVTAP-YKYPRK 411
Cdd:PRK08043 618 KIAGEMVSLEMVEQlALGVSPDKQHATAIKS-DASKGEALVLF--------TTDSE-LTREkLQQYAREHGVPeLAVPRD 687
|
410
....*....|....
gi 1958647527 412 VAFISELPKTVSGK 425
Cdd:PRK08043 688 IRYLKQLPLLGSGK 701
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
78-362 |
3.82e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 64.79 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 78 TRSGDSMAIYFTSGTTGTPKMVEHSQCSYGlGFVASGRRLMALTESDIFWnttdtgwvkAAWTLFSAW--ANGACVFVHE 155
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFA-AQIDALRQLYGIRPGEVDL---------ATFPLFALFgpALGLTSVIPD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 156 L-----PQVDAQTILNTLCRFPITTICCVPTLFRLLvqedlTRY------KFQCLRHCLAGGEALNSDVRDKWKN--QTG 222
Cdd:cd05910 152 MdptrpARADPQKLVGAIRQYGVSIVFGSPALLERV-----ARYcaqhgiTLPSLRRVLSAGAPVPIALAARLRKmlSDE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 223 LEIHEGYGQSETVLICG----NFRGSTIKSGS------MGKASPPYDVQIV--DEEG-------NVLPPGKEGNIAIRIK 283
Cdd:cd05910 227 AEILTPYGATEALPVSSigsrELLATTTAATSggagtcVGRPIPGVRVRIIeiDDEPiaewddtLELPRGEIGEITVTGP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 284 PTRPfclfnCYLDNPEKTAASE-----QGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLE 358
Cdd:cd05910 307 TVTP-----TYVNRPVATALAKiddnsEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRR 381
|
....
gi 1958647527 359 SAVV 362
Cdd:cd05910 382 SALV 385
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
182-385 |
3.99e-11 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 64.75 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 182 LFRLLVQEDL-TRYKFQCLRHCLAGGEALNSDVRDKWKnQTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDV 260
Cdd:cd17641 308 LADALLFRPLrDRLGFSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEV 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 261 QIvDEEGNVLppgkegniairikpTRPFCLFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSS-S 338
Cdd:cd17641 387 RI-DEVGEIL--------------VRSPGVFVGYYKNPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVGTTSdG 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958647527 339 YRIGPVEVESALAEHPAVLESAVVSSPDPIrgevVKAFIVLSPAYVS 385
Cdd:cd17641 452 TRFSPQFIENKLKFSPYIAEAVVLGAGRPY----LTAFICIDYAIVG 494
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
203-436 |
6.56e-11 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 63.99 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 203 LAGGEALNSDVRDKWKNQTGL-EIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYD---------VQIVDEEGNVL-- 270
Cdd:cd05937 206 VAWGNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRwkfenqvvlVKMDPETDDPIrd 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 271 ---------PPGKEGNIAIRIkPTRPFCLFNCYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYFWFVGRNDDVI 334
Cdd:cd05937 286 pktgfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESKlvrdvfRKGDiYFRTGDLLRQDADGRWYFLDRLGDTF 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 335 NSSSYRIGPVEVESALAEHPAVLESAVVSSPDP-IRGEVVKAFIVLSPAyvSHDPEALTR-ELQEHVKTVTAPYKYPRKV 412
Cdd:cd05937 365 RWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEES--SAVPTEFTKsLLASLARKNLPSYAVPLFL 442
|
250 260
....*....|....*....|....
gi 1958647527 413 AFISELPKTVSGKILRSKLRNQEW 436
Cdd:cd05937 443 RLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
252-433 |
3.30e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 61.94 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 252 GKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMdEDGYFWFVGRND 331
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR-GPS----LMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 332 DVINSSSYRIGPVEVESALAEHPAVL--ESAVVSSPDPIRGEVVkafiVLSPAYVShDPE---ALTRELQEHVKTVTApy 406
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIV----LLVQCRIS-DEErrgQLIHALAALVRSEFG-- 534
|
170 180
....*....|....*....|....*....
gi 1958647527 407 kYPRKVAFIS--ELPKTVSGKILRSKLRN 433
Cdd:PRK09192 535 -VEAAVELVPphSLPRTSSGKLSRAKAKK 562
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
250-434 |
1.22e-09 |
|
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: 60.19 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 250 SMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRPfclfnCYLDNPEKTAA--SEQGdFYITGDRAHMdEDGYFWFV 327
Cdd:cd05908 315 EVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP-----GYYNNPEATAKvfTDDG-WLKTGDLGFI-RNGRLVIT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 328 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVS---SPDPIRGEVVKAFIVLSPAyvSHDPEALTRELQEHVKTVTA 404
Cdd:cd05908 388 GREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRKS--EDDFYPLGKKIKKHLNKRGG 465
|
170 180 190
....*....|....*....|....*....|
gi 1958647527 405 pyKYPRKVAFISELPKTVSGKILRSKLRNQ 434
Cdd:cd05908 466 --WQINEVLPIRRIPKTTSGKVKRYELAQR 493
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
17-434 |
1.38e-09 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 60.00 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 17 LQAARVKSIITSDALaphVDAISADCPSLQSR-----LLVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSM---AIY- 87
Cdd:cd05938 74 FRCCGAKVLVVAPEL---QEAVEEVLPALRADgvsvwYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIkspALYi 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 88 FTSGTTGTPK--MVEHSQCSYGLGFVasgrRLMALTESDIFWNTTD-----------TGWVKAAWTL-----FSA---WA 146
Cdd:cd05938 151 YTSGTTGLPKaaRISHLRVLQCSGFL----SLCGVTADDVIYITLPlyhssgfllgiGGCIELGATCvlkpkFSAsqfWD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 147 NgacvfvhelpqvdaqtilntlCR-FPITTICCVPTLFRLLV----QEDLTRYKFQclrhcLAGGEALNSDVRDKWKNQT 221
Cdd:cd05938 227 D---------------------CRkHNVTVIQYIGELLRYLCnqpqSPNDRDHKVR-----LAIGNGLRADVWREFLRRF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 222 G-LEIHEGYGQSEtvlicGN--FRGSTIKSGSMGKAS-------P----PYDVQ----IVDEEGNVLP--PGKEGNIAIR 281
Cdd:cd05938 281 GpIRIREFYGSTE-----GNigFFNYTGKIGAVGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLLVAK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 282 IKPTRPFclfNCYLDNPEKTAAS------EQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHP 354
Cdd:cd05938 356 ITQQSPF---LGYAGDKEQTEKKllrdvfKKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 355 AVLESAV--VSSPDpIRGEVVKAFIVLSPayvshdPEALT-RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd05938 433 FLQEVNVygVTVPG-HEGRIGMAAVKLKP------GHEFDgKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
...
gi 1958647527 432 RNQ 434
Cdd:cd05938 506 VEE 508
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
65-434 |
1.39e-09 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 59.75 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 65 LLRVASPEHNCLRTRSGDSMAIY-FTSGTTGTPK--MVEHSQcsYgLGFVASGRRLMALTESDIFWNT-----TDTGWVK 136
Cdd:cd05939 87 LLTQSSTEPPSQDDVNFRDKLFYiYTSGTTGLPKaaVIVHSR--Y-YRIAAGAYYAFGMRPEDVVYDClplyhSAGGIMG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 137 AAwtlfSAWANGACVFVHElpQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQ-CLRhcLAGGEALNSDVrd 215
Cdd:cd05939 164 VG----QALLHGSTVVIRK--KFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKhNVR--LAVGNGLRPQI-- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 216 kWKNQTG----LEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPP-YDVQIV-----------DEEGNVLP--PGKEGN 277
Cdd:cd05939 234 -WEQFVRrfgiPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSvYPIRLIkvdedtgelirDSDGLCIPcqPGEPGL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 278 IAIRIKPTRPFCLFNCYLD---NPEKTAAS--EQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALA 351
Cdd:cd05939 313 LVGKIIQNDPLRRFDGYVNegaTNKKIARDvfKKGDsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILS 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 352 EHPAVLESAV--VSSPDpIRGEVVKAFIVLSPAYVshDPEALTRELQEhvktVTAPYKYPRKVAFISELPKTVSGKILRS 429
Cdd:cd05939 393 NVLGLEDVVVygVEVPG-VEGRAGMAAIVDPERKV--DLDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFKLQKT 465
|
....*
gi 1958647527 430 KLRNQ 434
Cdd:cd05939 466 DLQKE 470
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
313-427 |
5.74e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 58.27 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 313 GDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDpeALT 392
Cdd:PRK03584 503 GDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDD--ALR 580
|
90 100 110
....*....|....*....|....*....|....*
gi 1958647527 393 RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 427
Cdd:PRK03584 581 ARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKV 615
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
89-403 |
4.71e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 54.77 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 89 TSGTTGTPKMVEHSQ-------CSYGLGFVASGrrlmaLTESDIFWNTTDTGWVKAAWTLFS-AWANGACVFVHELPQVD 160
Cdd:COG1541 91 SSGTTGKPTVVGYTRkdldrwaELFARSLRAAG-----VRPGDRVQNAFGYGLFTGGLGLHYgAERLGATVIPAGGGNTE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 161 AQtiLNTLCRFPITTICCVPTLFRLLVQE------DLTRYKfqcLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSET 234
Cdd:COG1541 166 RQ--LRLMQDFGPTVLVGTPSYLLYLAEVaeeegiDPRDLS---LKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 235 -VLI---CGNFRGSTIKSGSMgkasppYdVQIVDEE-GNVLPPGKEGNIA-----------IRikptrpfclfncyldnp 298
Cdd:COG1541 241 gPGVayeCEAQDGLHIWEDHF------L-VEIIDPEtGEPVPEGEEGELVvttltkeamplIR----------------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 299 ektaaseqgdfYITGDRAHMDED----G------YFWFvGRNDDVInssSYR---IGPVEVESALAEHPAVLESAVVSSP 365
Cdd:COG1541 297 -----------YRTGDLTRLLPEpcpcGrthpriGRIL-GRADDML---IIRgvnVFPSQIEEVLLRIPEVGPEYQIVVD 361
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958647527 366 DPIRGEVVKAFIVLSPAYvshDPEALTRELQEHVKTVT 403
Cdd:COG1541 362 REGGLDELTVRVELAPGA---SLEALAEAIAAALKAVL 396
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
82-394 |
6.02e-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: 54.75 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIY-FTSGTTGTPKMVEHSQcsyglGFVASGRRLMALTESD-----------IFWNTTDTGWVKAAWTLFsawaNGA 149
Cdd:cd05921 165 DTVAKFlFTSGSTGLPKAVINTQ-----RMLCANQAMLEQTYPFfgeeppvlvdwLPWNHTFGGNHNFNLVLY----NGG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 150 CVFVHE---LPQVDAQTILNtLCRFPITTICCVPTLFRLLVQ-----EDLTRYKFQCLRHCLAGGEALNSDVRDKWKN-- 219
Cdd:cd05921 236 TLYIDDgkpMPGGFEETLRN-LREISPTVYFNVPAGWEMLVAalekdEALRRRFFKRLKLMFYAGAGLSQDVWDRLQAla 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 220 --QTGLEI--HEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVdeegnvlPPGkeGNIAIRIK-PTrpfcLFNCY 294
Cdd:cd05921 315 vaTVGERIpmMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV-------PSG--GKYEVRVKgPN----VTPGY 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 295 LDNPEKTAAS--EQGdFYITGDRAHM----DEDGYFWFVGR--NDDVINSSSY-RIGPVEVESALAEHPAVLEsAVVSSP 365
Cdd:cd05921 382 WRQPELTAQAfdEEG-FYCLGDAAKLadpdDPAKGLVFDGRvaEDFKLASGTWvSVGPLRARAVAACAPLVHD-AVVAGE 459
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958647527 366 DpirGEVVKAFIVLSPAYV--------SHDPEALTRE 394
Cdd:cd05921 460 D---RAEVGALVFPDLLACrrlvglqeASDAEVLRHA 493
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
20-353 |
2.74e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 52.90 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 20 ARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRPGwINFRELLRVA----SPEHNCLR------TRSGDSMAIYFT 89
Cdd:PRK06334 113 VGVTHVLTSKQLMQHLAQTHGEDAEYPFSLIYMEEVRKE-LSFWEKCRIGiymsIPFEWLMRwfgvsdKDPEDVAVILFT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 90 SGTTGTPKMVEHSQCSyglgfvasgrrLMALTESDI-FWNTTDTGWVKAAWTLFSAWANGACVFVHELPQV--------- 159
Cdd:PRK06334 192 SGTEKLPKGVPLTHAN-----------LLANQRACLkFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVpvvfaynpl 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 160 DAQTILNTLCRFPITTICCVPTLFRLLvqedLTRYKFQ-----CLRHCLAGGEALNSDVRDK-WKNQTGLEIHEGYGQSE 233
Cdd:PRK06334 261 YPKKIVEMIDEAKVTFLGSTPVFFDYI----LKTAKKQesclpSLRFVVIGGDAFKDSLYQEaLKTFPHIQLRQGYGTTE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 234 -TVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNV-LPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAASEQG--DF 309
Cdd:PRK06334 337 cSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTS-----LFSGYLGEDFGQGFVELGgeTW 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958647527 310 YITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEH 353
Cdd:PRK06334 412 YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
18-352 |
6.97e-07 |
|
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: 51.59 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 18 QAARVKSIitSDALaPHVDAIsadcpsLQSRLLVSDtSRPGWINFRELLRVA--SPEHNCL----RTRSGDSMAIYFTSG 91
Cdd:cd05933 91 QLQKILQI--QDKL-PHLKAI------IQYKEPLKE-KEPNLYSWDEFMELGrsIPDEQLDaiisSQKPNQCCTLIYTSG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 92 TTGTPK--MVEHSQCSY-GLGFVASGRRLMA----------LTESDIFWNTTDTgWVKAAWtlfsawanGACVFvheLPQ 158
Cdd:cd05933 161 TTGMPKgvMLSHDNITWtAKAASQHMDLRPAtvgqesvvsyLPLSHIAAQILDI-WLPIKV--------GGQVY---FAQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 159 VDA--QTILNTLCRFPITTICCVPTLF----------------------------------RLLVQEDLTRYKFQCLRH- 201
Cdd:cd05933 229 PDAlkGTLVKTLREVRPTAFMGVPRVWekiqekmkavgaksgtlkrkiaswakgvgletnlKLMGGESPSPLFYRLAKKl 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 202 ----------------CLAGGEALNSDVRDKWknqTGLEI--HEGYGQSE-----TVLICGNFRgstikSGSMGKASPPY 258
Cdd:cd05933 309 vfkkvrkalgldrcqkFFTGAAPISRETLEFF---LSLNIpiMELYGMSEtsgphTISNPQAYR-----LLSCGKALPGC 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 259 DVQIVDEEGNvlppgKEGNIAIRIKPtrpfcLFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFVGRNDD-VINS 336
Cdd:cd05933 381 KTKIHNPDAD-----GIGEICFWGRH-----VFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITA 450
|
410
....*....|....*.
gi 1958647527 337 SSYRIGPVEVESALAE 352
Cdd:cd05933 451 GGENVPPVPIEDAVKK 466
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
243-434 |
1.07e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.92 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 243 GSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKE-GNIAIRIKptrpfCLFNCYLDNpektAASEQGDFYITGDRAHMDED 321
Cdd:PRK05851 339 SGARRHAVLGNPIPGMEVRISPGDGAAGVAGREiGEIEIRGA-----SMMSGYLGQ----APIDPDDWFPTGDLGYLVDG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 322 GYFwFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGevVKAFIVLSPAYVSHDPEALTRELQEHVKT 401
Cdd:PRK05851 410 GLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRVAS 486
|
170 180 190
....*....|....*....|....*....|....*
gi 1958647527 402 VTApyKYPRKVAFIS--ELPKTVSGKILRSKLRNQ 434
Cdd:PRK05851 487 ECG--VVPSDVVFVApgSLPRTSSGKLRRLAVKRS 519
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
82-391 |
3.63e-05 |
|
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: 46.05 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 82 DSMAIYFTSGTTGTPKMVEHSQ---CSYGLGFVASGRRLMALTESDifwnttdtgwvkaawTLFS--------------- 143
Cdd:cd05927 115 DLATICYTSGTTGNPKGVMLTHgniVSNVAGVFKILEILNKINPTD---------------VYISylplahifervveal 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 144 AWANGACVFVHelpQVDAQTILNTLCRFPITTICCVPTLF-RLL------VQED--LTR--------YKFQCLRH----- 201
Cdd:cd05927 180 FLYHGAKIGFY---SGDIRLLLDDIKALKPTVFPGVPRVLnRIYdkifnkVQAKgpLKRklfnfalnYKLAELRSgvvra 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 202 ----------------------CLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTIKsGSMGKASPPY 258
Cdd:cd05927 257 spfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTaGATLTLPGDTSV-GHVGGPLPCA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 259 DVQIVD-EEGN--VLPPGKEGNIAIRikptrPFCLFNCYLDNPEKTA-ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVI 334
Cdd:cd05927 336 EVKLVDvPEMNydAKDPNPRGEVCIR-----GPNVFSGYYKDPEKTAeALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIF 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958647527 335 NSS--SYrIGPVEVESALAEHPAVLESAVvsspdpiRGEVVKAFIVlspAYVSHDPEAL 391
Cdd:cd05927 411 KLSqgEY-VAPEKIENIYARSPFVAQIFV-------YGDSLKSFLV---AIVVPDPDVL 458
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
310-431 |
4.16e-05 |
|
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: 45.59 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 310 YITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLES------------AVVS--SPDPIRGEVVKA 375
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPDDESF 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958647527 376 FIVLSPAYVSHDPEA--------LTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:cd17647 454 AQEDVPKEVSTDPIVkgligyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
89-404 |
6.09e-05 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 44.92 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 89 TSGTTGTPKMVEHSQ--CSYGLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLF-SAWANGACVFvhelP----QVDA 161
Cdd:cd05913 86 SSGTTGKPTVVGYTKndLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHyGAERLGALVI----PagggNTER 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 162 QtiLNTLCRFPITTICCVPTLFRLL---VQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLIC 238
Cdd:cd05913 162 Q--LQLIKDFGPTVLCCTPSYALYLaeeAEEEGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 239 GNFrgSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRI--KPTRPFClfncyldnpektaaseqgdFYITGD- 314
Cdd:cd05913 240 VAF--ECEEKDGLHIWEDHFIPEIIDpETGEPVPPGEVGELVFTTltKEAMPLI-------------------RYRTRDi 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 315 -----------RAHMDEDGyfwFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESA--VVSSPDPIRGEVVKafIVLSP 381
Cdd:cd05913 299 trllpgpcpcgRTHRRIDR---ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYqlILTRQEHLDELTIK--VEVRP 373
|
330 340
....*....|....*....|....
gi 1958647527 382 AYVSHDP-EALTRELQEHVKTVTA 404
Cdd:cd05913 374 EADDDEKlEALKQRLERHIKSVLG 397
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
199-436 |
1.28e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 40.95 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 199 LRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETvliCGnfrGSTI-------KSGSMGKASPPYDVQI--VDEEG-N 268
Cdd:PLN02430 385 LRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LG---PTTLgfpdemcMLGTVGAPAVYNELRLeeVPEMGyD 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 269 VLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVE-VE 347
Cdd:PLN02430 459 PLGEPPRGEICVRGK-----CLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEyLE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 348 SALAEHPAVLESAVVsspdpirGEVVKAFIVlspAYVSHDPEALTR--ELQEHVKTVTAPYKYPR-KVAFISELPKTVSg 424
Cdd:PLN02430 534 NVYGQNPIVEDIWVY-------GDSFKSMLV---AVVVPNEENTNKwaKDNGFTGSFEELCSLPElKEHILSELKSTAE- 602
|
250
....*....|..
gi 1958647527 425 kilRSKLRNQEW 436
Cdd:PLN02430 603 ---KNKLRGFEY 611
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
328-434 |
1.62e-03 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 40.52 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 328 GRNDDVINSssyriGPVeVESALAEHPAVLESAVVSSPDPIRGEVVKAFivlspayVSHDPEALTRELQEHVKTVTAPyK 407
Cdd:PRK09188 233 GTGDRIDNE-----APA-IQAALKSDPAVSDVAIALFSLPAKGVGLYAF-------VEAELPADEKSLRARLAGAKPP-K 298
|
90 100 110
....*....|....*....|....*....|.
gi 1958647527 408 YPRKVAFISELPKTVSGK----ILRSKLRNQ 434
Cdd:PRK09188 299 PPEHIQPVAALPRDADGTvrddILRLIAMNQ 329
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
310-431 |
2.64e-03 |
|
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: 40.43 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647527 310 YITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLE----------------SAVVSSPDPirgEVV 373
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnvtlvrrdkdeeptlvSYIVPQDKS---DEL 756
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647527 374 KAFIVLSPAYVSHDP--------EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 431
Cdd:TIGR03443 757 EEFKSEVDDEESSDPvvkglikyRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| |
