|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
42-569 |
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: 907.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 42 PEEFNFASDVLDYWAQMEEEGKRGPSPAFWWVNGQGDEIKWSFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEWW 121
Cdd:cd05928 2 PEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 122 LVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPDLKTKLVVSDHSHEGWLDFCSLIKS 201
Cdd:cd05928 82 LVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 202 ASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAFRSYIPSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTS 281
Cdd:cd05928 162 ASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 282 GCTVFIHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHE 361
Cdd:cd05928 242 GACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 362 VYGQSETGISSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRIKPTRPLGLFMEYENSPESTSEVECG 441
Cdd:cd05928 322 GYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 442 DFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLSHD 521
Cdd:cd05928 402 DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 18381087 522 QEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKE 569
Cdd:cd05928 482 PEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKE 529
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
82-566 |
0e+00 |
|
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: 531.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 82 WSFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTT 161
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 162 ASlvpevesvasecpdlktklvvsdhshegwldfcsliksaspdhtcikskmkDPMAIFFTSGTTGYPKMAKHNQGLAFr 241
Cdd:cd05972 80 AE---------------------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPL- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 242 SYIPSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVL 321
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 322 QQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIKRGSIGKAILPFDLQIIDEKG 401
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 402 NILPPNTEGYIGIRIKptrPLGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVE 481
Cdd:cd05972 268 RELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 482 NALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIK 561
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*
gi 18381087 562 RKELR 566
Cdd:cd05972 423 RVELR 427
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
35-569 |
1.82e-180 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 520.82 E-value: 1.82e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 35 RWndhDSPEEFNFASDVLDYWAQmeeegKRGPSPAFWWVNGQGDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALIL 114
Cdd:COG0365 1 RW---FVGGRLNIAYNCLDRHAE-----GRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRAL-GVKKGDRVAIYL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 115 PRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLV---------PEVESVASECPDLKTKLVV- 184
Cdd:COG0365 72 PNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLEHVIVVg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 185 ---SDHSHEGWLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQG--LAFRSYipSCRKLLKLKTSDIL 259
Cdd:COG0365 152 rtgADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGgyLVHAAT--TAKYVLDLKPGDVF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 260 WCMSDPGWILATVGCLIEPWTSGCTVFIHH-LPQF-DPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLR---FPTLE 334
Cdd:COG0365 230 WCTADIGWATGHSYIVYGPLLNGATVVLYEgRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKkydLSSLR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 335 HCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETG-ISSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIG 413
Cdd:COG0365 310 LLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 414 IRikptRPL-GLFMEYENSPESTSEV---ECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPA 489
Cdd:COG0365 390 IK----GPWpGMFRGYWNDPERYRETyfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 490 VAESAVVSSPDKDRGEVVKAFIVLNPEFlsHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKE 569
Cdd:COG0365 466 VAEAAVVGVPDEIRGQVVKAFVVLKPGV--EPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
40-569 |
3.09e-169 |
|
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: 491.24 E-value: 3.09e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 40 DSPEEFNFASDVLDYWAQMEEEgkrgpSPAFWWVNGQGDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPE 119
Cdd:cd05970 11 NVPENFNFAYDVVDAMAKEYPD-----KLALVWCDDAGEERIFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 120 WWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA-SLVPE-VESVASECPDLKTKLVVSDHSHEGWLDFCS 197
Cdd:cd05970 85 FWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAeDNIPEeIEKAAPECPSKPKLVWVGDPVPEGWIDFRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 198 LIKSASPD----HTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAFrSYIPSCRKLLKLKTSDILWCMSDPGWILATVG 273
Cdd:cd05970 165 LIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPL-GHIVTAKYWQNVREGGLHLTVADTGWGKAVWG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 274 CLIEPWTSGCTVFIHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQ 353
Cdd:cd05970 244 KIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 354 RTGLSIHEVYGQSETGISSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRIKPTRPLGLFMEYENSPE 433
Cdd:cd05970 324 KTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 434 STSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVL 513
Cdd:cd05970 404 KTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVL 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 18381087 514 NPEFlsHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKE 569
Cdd:cd05970 484 AKGY--EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
61-571 |
2.19e-114 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 351.50 E-value: 2.19e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 61 EGKRGPSPAFWWVNGQGDEiKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQ 140
Cdd:PRK04319 54 DGGRKDKVALRYLDASRKE-KYTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 141 LKAKDILYRIQISRAKAIVTTASLVPEVesVASECPDLKTKLVVSDH--SHEGWLDFCSLIKSASPDHTCIKSKMKDPMA 218
Cdd:PRK04319 132 FMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDveEGPGTLDFNALMEQASDEFDIEWTDREDGAI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 219 IFFTSGTTGYPKMAKHNQGLAFRSYIpSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHHlPQFDPKVI 298
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHNAMLQHYQ-TGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDG-GRFSPERW 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 299 VEVLFKYPITQCLAAPGVYRMVLQQKT---SNLRFPTLEHCTTGGESLLPEEYeQWKQRT-GLSIHEVYGQSETG-ISSA 373
Cdd:PRK04319 288 YRILEDYKVTVWYTAPTAIRMLMGAGDdlvKKYDLSSLRHILSVGEPLNPEVV-RWGMKVfGLPIHDNWWMTETGgIMIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 374 TLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIriKPTRPlGLFMEYENSPESTSEVECGDFYNSGDRATID 453
Cdd:PRK04319 367 NYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMD 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 454 EEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlsHDQEQLIKELQHHV 533
Cdd:PRK04319 444 EDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGY--EPSEELKEEIRGFV 521
|
490 500 510
....*....|....*....|....*....|....*...
gi 18381087 534 KSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKEFG 571
Cdd:PRK04319 522 KKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWELG 559
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
76-566 |
2.07e-111 |
|
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: 339.79 E-value: 2.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 76 QGDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRA 155
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 156 KAIVTTASlvpevesvasecpdlktklvvsdhshegwldfcsliksaspdhtcikskmKDPMAIFFTSGTTGYPKMAKHn 235
Cdd:cd05971 80 SALVTDGS--------------------------------------------------DDPALIIYTSGTTGPPKGALH- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 236 qglAFR---SYIPSCRKLLKL--KTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHHLPQFDPKVIVEVLFKYPITQC 310
Cdd:cd05971 109 ---AHRvllGHLPGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 311 LAAPGVYRMVLQQKTSNLRFP-TLEHCTTGGESLlPEEYEQWKQRT-GLSIHEVYGQSETGI---SSATLreMKIKRGSI 385
Cdd:cd05971 186 FLPPTALKMMRQQGEQLKHAQvKLRAIATGGESL-GEELLGWAREQfGVEVNEFYGQTECNLvigNCSAL--FPIKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 386 GKAILPFDLQIIDEKGNILPPNTEGYIGIRikptRPLGL-FMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRG 464
Cdd:cd05971 263 GKPIPGHRVAIVDDNGTPLPPGEVGEIAVE----LPDPVaFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 465 DDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLshDQEQLIKELQHHVKSVTAPYKYPR 544
Cdd:cd05971 339 DDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPR 416
|
490 500
....*....|....*....|..
gi 18381087 545 KVEFVSELPKTVTGKIKRKELR 566
Cdd:cd05971 417 EIEFVNELPRTATGKIRRRELR 438
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
82-569 |
3.16e-106 |
|
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: 326.38 E-value: 3.16e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 82 WSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTT 161
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSL-GVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 162 ASLVPevesvasecpdlktklvvsdhshegwldfcsliksaspdhtciKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAFR 241
Cdd:cd05969 80 EELYE-------------------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 242 SYIpSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHHlPQFDPKVIVEVLFKYPITQCLAAPGVYRMVL 321
Cdd:cd05969 117 YYF-TGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 322 QQKTSNLR---FPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETG-ISSATLREMKIKRGSIGKAILPFDLQII 397
Cdd:cd05969 195 KEGDELARkydLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSMGKPLPGVKAAVV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 398 DEKGNILPPNTEGYIGIriKPTRPlGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGP 477
Cdd:cd05969 275 DENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 478 VEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlsHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVT 557
Cdd:cd05969 352 FEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF--EPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRS 429
|
490
....*....|..
gi 18381087 558 GKIKRKELRNKE 569
Cdd:cd05969 430 GKIMRRVLKAKE 441
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
50-566 |
1.71e-105 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 324.84 E-value: 1.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 50 DVLDYWAQmeeegKRGPSPAFWWvngqgDEIKWSFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEWWLVTVGCMR 129
Cdd:COG0318 3 DLLRRAAA-----RHPDRPALVF-----GGRRLTYAELDARARRLAAALRA-LGVGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 130 TGIIFMPGTTQLKAKDILYRIQISRAKAIVTtaslvpevesvasecpdlktklvvsdhshegwldfcsliksaspdhtci 209
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 210 kskmkdpMAIFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIhh 289
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHR-NLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL-- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 290 LPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQ-KTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSET 368
Cdd:COG0318 173 LPRFDPERVLELIERERVTVLFGVPTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTET 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 369 G--ISSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRikptrPLGLFMEYENSPESTSEVECGDFYNS 446
Cdd:COG0318 253 SpvVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDGWLRT 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 447 GDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlSHDQEQLI 526
Cdd:COG0318 328 GDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGA-ELDAEELR 406
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 18381087 527 KELQHHVksvtAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:COG0318 407 AFLRERL----ARYKVPRRVEFVDELPRTASGKIDRRALR 442
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-569 |
2.62e-101 |
|
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: 313.35 E-value: 2.62e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANvFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAkaivtta 162
Cdd:cd05974 2 SFAEMSARSSRVAN-FLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 slvpevesvasecpdlkTKLVVSDHSHEgwldfcsliksaspdhtcikskmKDPMAIFFTSGTTGYPKMAKHNQglafRS 242
Cdd:cd05974 74 -----------------VYAAVDENTHA-----------------------DDPMLLYFTSGTTSKPKLVEHTH----RS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 243 YiP----SCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHHLPQFDPKVIVEVLFKYPITQCLAAPGVYR 318
Cdd:cd05974 110 Y-PvghlSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 319 MVLQQKTSNLRFPTLEHCTtGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIKRGSIGKAILPFDLQIID 398
Cdd:cd05974 189 MLIQQDLASFDVKLREVVG-AGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLD 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 399 EKGNilpPNTEGYIGIRIKPTRPLGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPV 478
Cdd:cd05974 268 PDGA---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 479 EVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEflSHDQEQLIKELQHHVKSVTAPYKYPRKVEFVsELPKTVTG 558
Cdd:cd05974 345 ELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG--YEPSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISG 421
|
490
....*....|.
gi 18381087 559 KIKRKELRNKE 569
Cdd:cd05974 422 KIRRVELRRRE 432
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
215-561 |
9.04e-93 |
|
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: 288.03 E-value: 9.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSDILWCMSDPGWILAtVGCLIEPWTSGCTVFIHhlPQFD 294
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHR-NLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLL--PKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 295 PKVIVEVLFKYPITQCLAAPGVYRMVLQQ-KTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSA 373
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKApESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 374 TLR--EMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRIKptrplGLFMEYENSPESTSEVECGDFYNSGDRAT 451
Cdd:cd04433 157 TGPpdDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGP-----SVMKGYWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 452 IDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEflshdQEQLIKELQH 531
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG-----ADLDAEELRA 306
|
330 340 350
....*....|....*....|....*....|
gi 18381087 532 HVKSVTAPYKYPRKVEFVSELPKTVTGKIK 561
Cdd:cd04433 307 HVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-567 |
2.21e-92 |
|
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: 290.57 E-value: 2.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA 162
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 slvpevesvasecpdlktklvvsDHSHEgwLDfcsliksaspdhtcikskmKDPMAIFFTSGTTGYPKMAKH--NQGLAF 240
Cdd:cd05973 81 -----------------------ANRHK--LD-------------------SDPFVMMFTSGTTGLPKGVPVplRALAAF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 241 RSYIpscRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHHLPqFDPKVIVEVLFKYPITQCLAAPGVYRMV 320
Cdd:cd05973 117 GAYL---RDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 321 LQQKTSNLRFPT--LEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETG--ISSATLREMKIKRGSIGKAILPFDLQI 396
Cdd:cd05973 193 MAAGAEVPARPKgrLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGmvLANHHALEHPVHAGSAGRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 397 IDEKGNILPPNTEGYIGIRIKPTrPLGLFMEYENSPESTSEvecGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIG 476
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIDIANS-PLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 477 PVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlsHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTV 556
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGH--EGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTP 426
|
490
....*....|.
gi 18381087 557 TGKIKRKELRN 567
Cdd:cd05973 427 SGKIQRFLLRR 437
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
63-566 |
6.01e-87 |
|
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: 277.14 E-value: 6.01e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 63 KRGPSPAFWWvngqgDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLK 142
Cdd:cd05936 11 RFPDKTALIF-----MGRKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 143 AKDILYRIQISRAKAIVTTASLvpevesvasecpdlkTKLVVSDHSHEGWldfcsliKSASPDhtcikskmkDPMAIFFT 222
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSF---------------TDLLAAGAPLGER-------VALTPE---------DVAVLQYT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 223 SGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTS--DILWCmsdpgwILA-------TVGCLIePWTSGCTVFIhhLPQF 293
Cdd:cd05936 134 SGTTGVPKGAMLTHR-NLVANALQIKAWLEDLLEgdDVVLA------ALPlfhvfglTVALLL-PLALGATIVL--IPRF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 294 DPKVIVEVLFKYPITQCLAAPGVYRMVLQQKT-SNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETG-IS 371
Cdd:cd05936 204 RPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEfKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 372 SATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVECGDFYNSGDRAT 451
Cdd:cd05936 284 AVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-GPQVMKG----YWNRPEETAEAFVDGWLRTGDIGY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 452 IDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNP-EFLSHDqeqlikELQ 530
Cdd:cd05936 359 MDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEgASLTEE------EII 432
|
490 500 510
....*....|....*....|....*....|....*.
gi 18381087 531 HHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd05936 433 AFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
49-566 |
3.35e-85 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 274.37 E-value: 3.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 49 SDVLDYWAQmeeegKRGPSPAFWWvngqgDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCM 128
Cdd:PRK06187 9 GRILRHGAR-----KHPDKEAVYF-----DGRRTTYAELDERVNRLANALRAL-GVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 129 RTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPDLKTKLVVSD----HSHEGWLDFCSLIKSASP 204
Cdd:PRK06187 78 KIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDgpaaPLAPEVGEYEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 205 DHTCIKSKMKDPMAIFFTSGTTGYPK--MAKHNQglaFRSYIPSCRKLLKLKTSD-ILWCMsdPGWILATVGCLIEPWTS 281
Cdd:PRK06187 158 TFDFPDIDENDAAAMLYTSGTTGHPKgvVLSHRN---LFLHSLAVCAWLKLSRDDvYLVIV--PMFHVHAWGLPYLALMA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 282 GCTVFIHHlpQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLR-FPTLEHCTTGGESLLPEEYEQWKQRTGLSIH 360
Cdd:PRK06187 233 GAKQVIPR--RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVdFSSLRLVIYGGAALPPALLREFKEKFGIDLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 361 EVYGQSETG--ISSATLRE----MKIKRGSIGKAILPFDLQIIDEKGNILPPNTE--GYIGIRiKPTRPLGlfmeYENSP 432
Cdd:PRK06187 311 QGYGMTETSpvVSVLPPEDqlpgQWTKRRSAGRPLPGVEARIVDDDGDELPPDGGevGEIIVR-GPWLMQG----YWNRP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 433 ESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIV 512
Cdd:PRK06187 386 EATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 18381087 513 LNPeflshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK06187 466 LKP-----GATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
43-566 |
2.76e-82 |
|
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: 266.16 E-value: 2.76e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 43 EEFNFASDVLDywaqmEEEGKRGPSPAFwwVNGQGdeiKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWL 122
Cdd:cd05959 1 EKYNAATLVDL-----NLNEGRGDKTAF--IDDAG---SLTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 123 VTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVA-SECPDLKTKLVVSDHSHE-GWLDFCSLIK 200
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALtKSEHTLVVLIVSGGAGPEaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 201 SASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQglafRSYIPSC----RKLLKLKTSDIlwCMSDPGWILA-TVG-C 274
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLH----ADIYWTAelyaRNVLGIREDDV--CFSAAKLFFAyGLGnS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 275 LIEPWTSGCTVFIhhLPQF-DPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLR-FPTLEHCTTGGESLLPEEYEQWK 352
Cdd:cd05959 224 LTFPLSVGATTVL--MPERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRdLSSLRLCVSAGEALPAEVGERWK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 353 QRTGLSIHEVYGQSETGISSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRIKPTRPLglfmeYENSP 432
Cdd:cd05959 302 ARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM-----YWNNR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 433 ESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIV 512
Cdd:cd05959 377 DKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVV 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 18381087 513 LNPEFlsHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd05959 457 LRPGY--EDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
79-566 |
2.29e-76 |
|
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: 248.93 E-value: 2.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 79 EIKWSFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQisraKAI 158
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD----KAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 159 VTTASLVPEVESVasecpdlktklvvsdhshegwldfcsliksaspDHTCIkskmkdpmaIFFTSGTTGYPKMAKHnqgl 238
Cdd:cd05958 84 ITVALCAHALTAS---------------------------------DDICI---------LAFTSGTTGAPKATMH---- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 239 AFRSYIPSC----RKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIhhLPQFDPKVIVEVLFKYPITQCLAAP 314
Cdd:cd05958 118 FHRDPLASAdryaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 315 GVYRMVL------QQKTSNLRFptlehCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIKRGSIGKA 388
Cdd:cd05958 196 TAYRAMLahpdaaGPDLSSLRK-----CVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 389 ILPFDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGLFmeyenspESTSEVECGDFYN-SGDRATIDEEGYIWFLGRGDDV 467
Cdd:cd05958 271 VPGYEAKVVDDEGNPVPDGTIGRLAVR-GPTGCRYLA-------DKRQRTYVQGGWNiTGDTYSRDPDGYFRHQGRSDDM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 468 INASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLShdQEQLIKELQHHVKSVTAPYKYPRKVE 547
Cdd:cd05958 343 IVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAIE 420
|
490
....*....|....*....
gi 18381087 548 FVSELPKTVTGKIKRKELR 566
Cdd:cd05958 421 FVTELPRTATGKLQRFALR 439
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
46-567 |
3.02e-75 |
|
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: 250.56 E-value: 3.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 46 NFASDVLDYWAQmeeegKRGPSPAFWWVNGQGDEIK-WSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVT 124
Cdd:cd05966 53 NISYNCLDRHLK-----ERGDKVAIIWEGDEPDQSRtITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 125 VGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTAS---------LVPEVESVASECPDLKTKLVVSDHSH-----E 190
Cdd:cd05966 127 LACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGgyrggkvipLKEIVDEALEKCPSVEKVLVVKRTGGevpmtE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 191 G---WLDfcSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQG--LAFRSYipSCRKLLKLKTSDILWCMSDP 265
Cdd:cd05966 207 GrdlWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGgyLLYAAT--TFKYVFDYHPDDIYWCTADI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 266 GWILATVGCLIEPWTSGCTVFIHH-LPQF-DPKVIVEVLFKYPITQCLAAPGVYRMVLQQ-----KTSNLRfpTLEHCTT 338
Cdd:cd05966 283 GWITGHSYIVYGPLANGATTVMFEgTPTYpDPGRYWDIVEKHKVTIFYTAPTAIRALMKFgdewvKKHDLS--SLRVLGS 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 339 GGESLLPEEYEqW------KQRtgLSIHEVYGQSETG---IS---SATlremKIKRGSigkAILPF---DLQIIDEKGNI 403
Cdd:cd05966 361 VGEPINPEAWM-WyyevigKER--CPIVDTWWQTETGgimITplpGAT----PLKPGS---ATRPFfgiEPAILDEEGNE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 404 LPPNTEGYIGIRikptRPL-GLFMEYENSPESTSEV---ECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVE 479
Cdd:cd05966 431 VEGEVEGYLVIK----RPWpGMARTIYGDHERYEDTyfsKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAE 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 480 VENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlsHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGK 559
Cdd:cd05966 507 VESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGE--EPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGK 584
|
....*...
gi 18381087 560 IKRKELRN 567
Cdd:cd05966 585 IMRRILRK 592
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
83-568 |
7.73e-73 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 241.73 E-value: 7.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA 162
Cdd:PRK07656 32 TYAELNARVRRAAAALAAL-GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SLVPEVESVASECPDLKTKLVV----SDHSHEGWLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPK--MAKHNQ 236
Cdd:PRK07656 111 LFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKgaMLTHRQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 237 GL-AFRSYIpscrKLLKLKTSDiLWCMSDP---------GWIlatvGCLIepwtSGCTVFIHhlPQFDPKVIVEVLFKYP 306
Cdd:PRK07656 191 LLsNAADWA----EYLGLTEGD-RYLAANPffhvfgykaGVN----APLM----RGATILPL--PVFDPDEVFRLIETER 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 307 ITQCLAAPGVYRMVLQQ-KTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLS-IHEVYGQSE-TGIssATL----REMK 379
Cdd:PRK07656 256 ITVLPGPPTMYNSLLQHpDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEaSGV--TTFnrldDDRK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 380 IKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVECGD-FYNSGDRATIDEEGYI 458
Cdd:PRK07656 334 TVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR-GPNVMKG----YYDDPEATAAAIDADgWLHTGDLGRLDEEGYL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 459 WFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlSHDQEQLIkelqHHVKSVTA 538
Cdd:PRK07656 409 YIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGA-ELTEEELI----AYCREHLA 483
|
490 500 510
....*....|....*....|....*....|
gi 18381087 539 PYKYPRKVEFVSELPKTVTGKIKRKELRNK 568
Cdd:PRK07656 484 KYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
83-566 |
8.61e-72 |
|
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: 236.59 E-value: 8.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA 162
Cdd:cd05919 12 TYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SlvpevesvasecpdlktklvvsdhshegwlDFCSLIksaspdhtcikskmkdpmaifFTSGTTGYPKMAKHnqglAFRS 242
Cdd:cd05919 91 D------------------------------DIAYLL---------------------YSSGTTGPPKGVMH----AHRD 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 243 YIPSC----RKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHHLPQfDPKVIVEVLFKYPITQCLAAPGVYR 318
Cdd:cd05919 116 PLLFAdamaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 319 MVLQQKTSNLR-FPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIKRGSIGKAILPFDLQII 397
Cdd:cd05919 195 NLLDSCAGSPDaLRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 398 DEKGNILPPNTEGYIGIRIKptrplGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGP 477
Cdd:cd05919 275 DEEGHTIPPGEEGDLLVRGP-----SAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 478 VEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLShdQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVT 557
Cdd:cd05919 350 VEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAP--QESLARDIHRHLLERLSAHKVPRRIAFVDELPRTAT 427
|
....*....
gi 18381087 558 GKIKRKELR 566
Cdd:cd05919 428 GKLQRFKLR 436
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
20-560 |
1.55e-71 |
|
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: 240.17 E-value: 1.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 20 PTQLHRRLFSRVGAP--RWNDHDSpeeFNFASDVLDYWAQmeeegKRGPSPAFWWVNGQGDEIK-WSFRKLRDLTCRTAN 96
Cdd:cd17634 28 PYQKVKNTSFAPGAPsiKWFEDAT---LNLAANALDRHLR-----ENGDRTAIIYEGDDTSQSRtISYRELHREVCRFAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 97 VFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVT---------TASLVPE 167
Cdd:cd17634 100 TLLDL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITadggvragrSVPLKKN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 168 V-ESVASECPDLKTKLVV----SDHSHEG--WLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAF 240
Cdd:cd17634 179 VdDALNPNVTSVEHVIVLkrtgSDIDWQEgrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 241 RSYIPSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHH-LPQF-DPKVIVEVLFKYPITQCLAAPGVYR 318
Cdd:cd17634 259 VYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 319 MVLQQKTSNLR---FPTLEHCTTGGESLLPEEYEQWKQRTGLS---IHEVYGQSETGISSATLREMKI--KRGSIGKAIL 390
Cdd:cd17634 339 ALMAAGDDAIEgtdRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTETGGFMITPLPGAIelKAGSATRPVF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 391 PFDLQIIDEKGNILPPNTEGYIGIRIK-PTRPLGLFM---EYENSPESTSEvecgDFYNSGDRATIDEEGYIWFLGRGDD 466
Cdd:cd17634 419 GVQPAVVDNEGHPQPGGTEGNLVITDPwPGQTRTLFGdheRFEQTYFSTFK----GMYFSGDGARRDEDGYYWITGRSDD 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 467 VINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLshDQEQLIKELQHHVKSVTAPYKYPRKV 546
Cdd:cd17634 495 VINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVV 572
|
570
....*....|....
gi 18381087 547 EFVSELPKTVTGKI 560
Cdd:cd17634 573 HWVDSLPKTRSGKI 586
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
77-566 |
3.39e-71 |
|
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: 240.23 E-value: 3.39e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 77 GDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAK 156
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AIVTT---------ASLVPEVESVASECPD-LKTKLVV------SDHSHEG---WLDFcsLIKSASPDHTCIKSKMKDPM 217
Cdd:TIGR02188 163 LVITAdeglrggkvIPLKAIVDEALEKCPVsVEHVLVVrrtgnpVVPWVEGrdvWWHD--LMAKASAYCEPEPMDSEDPL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 218 AIFFTSGTTGYPKMAKHNQGlafrSYI----PSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHH-LPQ 292
Cdd:TIGR02188 241 FILYTSGSTGKPKGVLHTTG----GYLlyaaMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEgVPT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 293 F-DPKVIVEVLFKYPITQCLAAPGVYRMVLQQ--------KTSNLRfptLEHctTGGESLLPEEYEqW------KQRTgl 357
Cdd:TIGR02188 317 YpDPGRFWEIIEKHKVTIFYTAPTAIRALMRLgdewvkkhDLSSLR---LLG--SVGEPINPEAWM-WyykvvgKERC-- 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 358 SIHEVYGQSETG---ISS---ATlrEMKikrgsIGKAILPF---DLQIIDEKGNILP-PNTEGYIGIRIK-PTRPLGLFM 426
Cdd:TIGR02188 389 PIVDTWWQTETGgimITPlpgAT--PTK-----PGSATLPFfgiEPAVVDEEGNPVEgPGEGGYLVIKQPwPGMLRTIYG 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 427 EYENSPES-TSEVEcgDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGE 505
Cdd:TIGR02188 462 DHERFVDTyFSPFP--GYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQ 539
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18381087 506 VVKAFIVLNPEFLSHDqeQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:TIGR02188 540 AIYAFVTLKDGYEPDD--ELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLR 598
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
77-469 |
4.29e-68 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 226.42 E-value: 4.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 77 GDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAK 156
Cdd:pfam00501 17 GEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AIVTTASL-VPEVESVASECPDLKTKLVVSDHSH--EGWLDFCSLIKSASPdHTCIKSKMKDPMAIFFTSGTTGYPKMAK 233
Cdd:pfam00501 96 VLITDDALkLEELLEALGKLEVVKLVLVLDRDPVlkEEPLPEEAKPADVPP-PPPPPPDPDDLAYIIYTSGTTGKPKGVM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 234 HNQG--LAF-RSYIPSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCT-VFIHHLPQFDPKVIVEVLFKYPITQ 309
Cdd:pfam00501 175 LTHRnlVANvLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATvVLPPGFPALDPAALLELIERYKVTV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 310 CLAAPGVYRMVLQQKT-SNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIK---RGSI 385
Cdd:pfam00501 255 LYGVPTLLNMLLEAGApKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDlrsLGSV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 386 GKAILPFDLQIIDEK-GNILPPNTEGYIGIRikptRPlGLFMEYENSPESTSEV-ECGDFYNSGDRATIDEEGYIWFLGR 463
Cdd:pfam00501 335 GRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAfDEDGWYRTGDLGRRDEDGYLEIVGR 409
|
....*.
gi 18381087 464 GDDVIN 469
Cdd:pfam00501 410 KKDQIK 415
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
43-566 |
1.67e-67 |
|
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: 227.41 E-value: 1.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 43 EEFNFASDVLDywaQMEEEGkRGPSPAFwwVNGQGdeiKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWL 122
Cdd:TIGR02262 1 EKYNAAEDLLD---RNVVEG-RGGKTAF--IDDIS---SLSYGELEAQVRRLAAALRRL-GVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 123 VTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPDLKTKLVVSDhSHEGWLDFCSLIKSA 202
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGR-PEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 203 SPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAFRSYIPSCRKLLKLKTSDIlwCMSDPGWILA-TVG-CLIEPWT 280
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDV--CFSAAKLFFAyGLGnALTFPMS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 281 SGCT-VFIHHLPQfdPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLRFP-TLEHCTTGGESLlPEEYEQ-WKQRTGL 357
Cdd:TIGR02262 228 VGATtVLMGERPT--PDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQvRLRLCTSAGEAL-PAEVGQrWQARFGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 358 SIHEVYGQSETGISSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSE 437
Cdd:TIGR02262 305 DIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS-GPSSATM----YWNNRAKSRD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 438 VECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPef 517
Cdd:TIGR02262 380 TFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRP-- 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 18381087 518 lshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:TIGR02262 458 ---GQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
78-560 |
1.68e-67 |
|
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: 225.18 E-value: 1.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 78 DEIKWSFRKLRDLTCRTANVFeQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKA 157
Cdd:cd17631 17 GGRSLTYAELDERVNRLAHAL-RALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 158 IVttaslvpevesvasecpdlktklvvsdhshegwldfcsliksaspdhtcikskmKDPMAIFFTSGTTGYPKMAKHNQG 237
Cdd:cd17631 96 LF------------------------------------------------------DDLALLMYTSGTTGRPKGAMLTHR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 238 ---------LAFRSYIPSCRKLLKLKTSDIlwcmsdpgwilATVGCLIEP--WTSGCTVFihhLPQFDPKVIVEVLFKYP 306
Cdd:cd17631 122 nllwnavnaLAALDLGPDDVLLVVAPLFHI-----------GGLGVFTLPtlLRGGTVVI---LRKFDPETVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 307 ITQCLAAPGVYRMVLQQ-KTSNLRFPTLEHCTTGGeSLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLR--EMKIKRG 383
Cdd:cd17631 188 VTSFFLVPTMIQALLQHpRFATTDLSSLRAVIYGG-APMPERLLRALQARGVKFVQGYGMTETSPGVTFLSpeDHRRKLG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 384 SIGKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTrplgLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGR 463
Cdd:cd17631 267 SAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GPH----VMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 464 GDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPeflshDQEQLIKELQHHVKSVTAPYKYP 543
Cdd:cd17631 342 KKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP-----GAELDEDELIAHCRERLARYKIP 416
|
490
....*....|....*..
gi 18381087 544 RKVEFVSELPKTVTGKI 560
Cdd:cd17631 417 KSVEFVDALPRNATGKI 433
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
44-567 |
2.37e-67 |
|
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: 229.89 E-value: 2.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 44 EFNFASDVLDYWAqmeeEGKRGPSPAFWWVNG-QGDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWL 122
Cdd:cd05967 48 RLNTCYNALDRHV----EAGRGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVLRKL-GVVKGDRVIIYMPMIPEAAI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 123 VTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTtAS----------LVPEVESVASEC------------PDLKT 180
Cdd:cd05967 123 AMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVT-AScgiepgkvvpYKPLLDKALELSghkphhvlvlnrPQVPA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 181 KLVVsdhsHEGWLDFCSLIKSASPdHTCIKSKMKDPMAIFFTSGTTGYPK-MAKHNQGLAFRSYIpSCRKLLKLKTSDIL 259
Cdd:cd05967 202 DLTK----PGRDLDWSELLAKAEP-VDCVPVAATDPLYILYTSGTTGKPKgVVRDNGGHAVALNW-SMRNIYGIKPGDVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 260 WCMSDPGWIlatVG-CLI--EPWTSGCT-VFIHHLPQF--DPKVIVEVLFKYPITQCLAAPGVYRMVLQQKT--SNLR-- 329
Cdd:cd05967 276 WAASDVGWV---VGhSYIvyGPLLHGATtVLYEGKPVGtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPdgKYIKky 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 330 -FPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSAT----LREMKIKRGSIGKAILPFDLQIIDEKGNIL 404
Cdd:cd05967 353 dLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITAnpvgLEPLPIKAGSPGKPVPGYQVQVLDEDGEPV 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 405 PPNTEGYIGIRIkPTRPlGLFMEYENSPESTSEVECGDF---YNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVE 481
Cdd:cd05967 433 GPNELGNIVIKL-PLPP-GCLLTLWKNDERFKKLYLSKFpgyYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEME 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 482 NALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIK 561
Cdd:cd05967 511 ESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG-VKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKIL 589
|
....*.
gi 18381087 562 RKELRN 567
Cdd:cd05967 590 RRTLRK 595
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
83-565 |
3.86e-65 |
|
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: 218.89 E-value: 3.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANvFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA 162
Cdd:cd05935 3 TYLELLEVVKKLAS-FLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SLvpevesvasecpdlktklvvsdhshegwldfcsliksaspdhtcikskmKDPMAIFFTSGTTGYPKMAKHNQGLAFRS 242
Cdd:cd05935 82 EL-------------------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 243 YIPSCRkllklktsdilWCMSDPGWI-LAT---------VGCLIEPWTSGCTVFIhhLPQFDPKVIVEVLFKYPITQCLA 312
Cdd:cd05935 113 ALQSAV-----------WTGLTPSDViLAClplfhvtgfVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 313 APGVYRMVLQQKTSNLR-FPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETgISSATLREM-KIKRGSIGKAIL 390
Cdd:cd05935 180 IPTMLVDLLATPEFKTRdLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTET-MSQTHTNPPlRPKLQCLGIP*F 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 391 PFDLQIID-EKGNILPPNTEGYIGIRiKPTrplgLFMEYENSPESTSE--VECG--DFYNSGDRATIDEEGYIWFLGRGD 465
Cdd:cd05935 259 GVDARVIDiETGRELPPNEVGEIVVR-GPQ----IFKGYWNRPEETEEsfIEIKgrRFFRTGDLGYMDEEGYFFFVDRVK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 466 DVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLSHDQEQLIKELqhhVKSVTAPYKYPRK 545
Cdd:cd05935 334 RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIIEW---AREQMAAYKYPRE 410
|
490 500
....*....|....*....|
gi 18381087 546 VEFVSELPKTVTGKIKRKEL 565
Cdd:cd05935 411 VEFVDELPRSASGKILWRLL 430
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
81-566 |
3.37e-64 |
|
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: 216.00 E-value: 3.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 81 KWSFRKLRDLTCRTANVFeQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVT 160
Cdd:cd05934 3 RWTYAELLRESARIAAAL-AALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 161 taslvpevesvasecpdlktklvvsdhshegwldfcsliksaspdhtcikskmkDPMAIFFTSGTTGYPK--MAKHNQgL 238
Cdd:cd05934 82 ------------------------------------------------------DPASILYTSGTTGPPKgvVITHAN-L 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 239 AFRSYIPSCRklLKLKTSDILW-----------CMSdpgWILAtvgcliepWTSGCTVFIhhLPQFDPKVIVEVLFKYPI 307
Cdd:cd05934 107 TFAGYYSARR--FGLGEDDVYLtvlplfhinaqAVS---VLAA--------LSVGATLVL--LPRFSASRFWSDVRRYGA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 308 TQCLAAPGVYRMVLQQKTSN------LRFptlehctTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIK 381
Cdd:cd05934 172 TVTNYLGAMLSYLLAQPPSPddrahrLRA-------AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRR 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 382 RGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRikPTRPLGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFL 461
Cdd:cd05934 245 PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 462 GRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNP-EFLSHDqeqlikELQHHVKSVTAPY 540
Cdd:cd05934 323 DRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPgETLDPE------ELFAFCEGQLAYF 396
|
490 500
....*....|....*....|....*.
gi 18381087 541 KYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd05934 397 KVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
81-560 |
7.73e-63 |
|
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: 214.38 E-value: 7.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 81 KWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVT 160
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 161 TASLVPEVESvASECPDLKTKLVVSDHSHEGWLDFCSLIKSASPDH-----TCIKSKMKDPMAIFFTSGTTGYPK--MAK 233
Cdd:cd05911 89 DPDGLEKVKE-AAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEdedlpPPLKDGKDDTAAILYSSGTTGLPKgvCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 234 HNqGLAFRSYIPSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTsGCTVFIHhlPQFDPKVIVEVLFKYPITQCLAA 313
Cdd:cd05911 168 HR-NLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIM--PKFDSELFLDLIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 314 PGVyrMVLQQKTSNL---RFPTLEHCTTGGESLLPEEYEQWKQRTGLS-IHEVYGQSETGISSATLREMKIKRGSIGKaI 389
Cdd:cd05911 244 PPI--AAALAKSPLLdkyDLSSLRVILSGGAPLSKELQELLAKRFPNAtIKQGYGMTETGGILTVNPDGDDKPGSVGR-L 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 390 LP-FDLQIIDEKGN-ILPPNTEGYIGIRIkPTRPLGlfmeYENSPESTSEVECGD-FYNSGDRATIDEEGYIWFLGRGDD 466
Cdd:cd05911 321 LPnVEAKIVDDDGKdSLGPNEPGEICVRG-PQVMKG----YYNNPEATKETFDEDgWLHTGDIGYFDEDGYLYIVDRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 467 VINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLSHDqeqliKELQHHVKSVTAPYKYPRK- 545
Cdd:cd05911 396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE-----KEVKDYVAKKVASYKQLRGg 470
|
490
....*....|....*
gi 18381087 546 VEFVSELPKTVTGKI 560
Cdd:cd05911 471 VVFVDEIPKSASGKI 485
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
77-566 |
2.25e-61 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 213.85 E-value: 2.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 77 GDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGII-------FmpgttqlKAKDILYR 149
Cdd:PRK00174 94 GDSRKITYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvvfggF-------SAEALADR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 150 IQISRAKAIVT---------TASLVPEVESVASECPDLKTKLVV-----SDHSHEG---WLDfcSLIKSASPDHTCIKSK 212
Cdd:PRK00174 166 IIDAGAKLVITadegvrggkPIPLKANVDEALANCPSVEKVIVVrrtggDVDWVEGrdlWWH--ELVAGASDECEPEPMD 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 213 MKDPMAIFFTSGTTGYPKMAKHNQG--LAFRSYipSCRKLLKLKTSDILWCMSDPGWILA----TVGcliePWTSGCTVF 286
Cdd:PRK00174 244 AEDPLFILYTSGSTGKPKGVLHTTGgyLVYAAM--TMKYVFDYKDGDVYWCTADVGWVTGhsyiVYG----PLANGATTL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 287 IHH-LPQF-DPKVIVEVLFKYPITQCLAAPGVYRM--------VLQQKTSNLRfptLEHctTGGESLLPEEYEqWkqrtg 356
Cdd:PRK00174 318 MFEgVPNYpDPGRFWEVIDKHKVTIFYTAPTAIRAlmkegdehPKKYDLSSLR---LLG--SVGEPINPEAWE-W----- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 357 lsIHEVYG-----------QSETG---IS---SATlremKIKRGSigkAILPF---DLQIIDEKGNILPPNTEGYIGIri 416
Cdd:PRK00174 387 --YYKVVGgercpivdtwwQTETGgimITplpGAT----PLKPGS---ATRPLpgiQPAVVDEEGNPLEGGEGGNLVI-- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 417 kpTRP-----LGLFmeyeNSPESTSEV---ECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHP 488
Cdd:PRK00174 456 --KDPwpgmmRTIY----GDHERFVKTyfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP 529
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18381087 489 AVAESAVVSSPDKDRGEVVKAFIVLNPEFlsHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK00174 530 KVAEAAVVGRPDDIKGQGIYAFVTLKGGE--EPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
83-573 |
5.54e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 208.28 E-value: 5.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA 162
Cdd:PRK08314 37 SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SLVPEVESVASEC----------------------PD-LKTKLVVSDHSHEGWLDFCSLIKS--------ASPDHTCIks 211
Cdd:PRK08314 117 ELAPKVAPAVGNLrlrhvivaqysdylpaepeiavPAwLRAEPPLQALAPGGVVAWKEALAAglappphtAGPDDLAV-- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 212 kmkdpmaIFFTSGTTGYPK--MAKHnqglafRSYIPSCrkllklkTSDILWCMSDPGWI-LAT---------VGCLIEPW 279
Cdd:PRK08314 195 -------LPYTSGTTGVPKgcMHTH------RTVMANA-------VGSVLWSNSTPESVvLAVlplfhvtgmVHSMNAPI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 280 TSGCTVFIhhLPQFDPKVIVEVLFKYPIT----------QCLAAPGVYRMVLqqktSNLRfptlehCTTGGESLLPEEY- 348
Cdd:PRK08314 255 YAGATVVL--MPRWDREAAARLIERYRVThwtniptmvvDFLASPGLAERDL----SSLR------YIGGGGAAMPEAVa 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 349 EQWKQRTGLSIHEVYGQSETGISSATLREMKIKRGSIGKAILPFDLQIID-EKGNILPPNTEGYIGIRikptrplG--LF 425
Cdd:PRK08314 323 ERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH-------GpqVF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 426 MEYENSPESTS----EVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDK 501
Cdd:PRK08314 396 KGYWNRPEATAeafiEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDP 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18381087 502 DRGEVVKAFIVLNPEFLSHDQEQlikELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKEFGQL 573
Cdd:PRK08314 476 RRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARA 544
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
79-567 |
1.13e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 204.01 E-value: 1.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 79 EIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAI 158
Cdd:PRK08316 34 DRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 159 VTTASLVPEVESVASECPDLKTKL--VVSDHSHE-GWLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHN 235
Cdd:PRK08316 113 LVDPALAPTAEAALALLPVDTLILslVLGGREAPgGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 236 QGLAFRSYIpSCRKLLKLKTSDI-LWCMsdPGWILATVGCLIEPWTS-GCTVFIhhLPQFDPKVIVEVLFKYPITQCLAA 313
Cdd:PRK08316 193 HRALIAEYV-SCIVAGDMSADDIpLHAL--PLYHCAQLDVFLGPYLYvGATNVI--LDAPDPELILRTIEAERITSFFAP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 314 PGVYRMVLQQK---TSNLRfpTLEHCTTGGeSLLPEE-YEQWKQR-TGLSIHEVYGQSETGISSATLR--EMKIKRGSIG 386
Cdd:PRK08316 268 PTVWISLLRHPdfdTRDLS--SLRKGYYGA-SIMPVEvLKELRERlPGLRFYNCYGQTEIAPLATVLGpeEHLRRPGSAG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 387 KAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTrplgLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDD 466
Cdd:PRK08316 345 RPVLNVETRVVDDDGNDVAPGEVGEIVHR-SPQ----LMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 467 VINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSHDQEQLIKelqhHVKSVTAPYKYPRKV 546
Cdd:PRK08316 420 MIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG-ATVTEDELIA----HCRARLAGFKVPKRV 494
|
490 500
....*....|....*....|.
gi 18381087 547 EFVSELPKTVTGKIKRKELRN 567
Cdd:PRK08316 495 IFVDELPRNPSGKILKRELRE 515
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
77-571 |
3.39e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 203.47 E-value: 3.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 77 GDEIKWsfRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAK 156
Cdd:PRK07786 40 GNTTTW--RELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AIVTTASLVPEVESVASECPDLKTKLVVSDHSHEGWLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMA--KH 234
Cdd:PRK07786 117 VVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAvlTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 235 N--QGLAFrsyipSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHHLPQFDPKVIVEVLFKYPITQCLA 312
Cdd:PRK07786 197 AnlTGQAM-----TCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGIFL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 313 APGVYRMVLQQKTSNLRFPTLEHCTTGG----ESLLPEEYEQWKqrtGLSIHEVYGQSE-TGISSATLREMKI-KRGSIG 386
Cdd:PRK07786 272 VPAQWQAVCAEQQARPRDLALRVLSWGAapasDTLLRQMAATFP---EAQILAAFGQTEmSPVTCMLLGEDAIrKLGSVG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 387 KAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTrplgLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDD 466
Cdd:PRK07786 349 KVIPTVAARVVDENMNDVPVGEVGEIVYR-APT----LMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 467 VINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEflshDQEQLIKELQHHVKSVTAPYKYPRKV 546
Cdd:PRK07786 424 MIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND----DAALTLEDLAEFLTDRLARYKHPKAL 499
|
490 500
....*....|....*....|....*
gi 18381087 547 EFVSELPKTVTGKIKRKELRnKEFG 571
Cdd:PRK07786 500 EIVDALPRNPAGKVLKTELR-ERYG 523
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
215-567 |
4.53e-57 |
|
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: 197.90 E-value: 4.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPKMAKHNQglafRSYIPSCRKLLKL----KTSDILWCMsdP-----GWILAtvgcLIEPWTSGCTV 285
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTH----ANLAANVRALVDAwrwtEDDVLLHVL--PlhhvhGLVNA----LLCPLFAGASV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 286 fiHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQ---QKTSNLRFPTLEHC------TTGGESLLPEEYEQWKQRTG 356
Cdd:cd05941 160 --EFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQyyeAHFTDPQFARAAAAerlrlmVSGSAALPVPTLEEWEAITG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 357 LSIHEVYGQSETGISSATLREMKIKRGSIGKAILPFDLQIIDEKGN-ILPPNTEGYIGIRiKPTrplgLFMEYENSPEST 435
Cdd:cd05941 238 HTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GPS----VFKEYWNKPEAT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 436 SEVECGD-FYNSGDRATIDEEGYIWFLGRG-DDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVL 513
Cdd:cd05941 313 KEEFTDDgWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVL 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 18381087 514 NPEFLSHDQEQLIkelqHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:cd05941 393 RAGAAALSLEELK----EWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
77-567 |
5.26e-56 |
|
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: 196.38 E-value: 5.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 77 GDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAK 156
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AIVT-TASLVPEVESVASECP-------DLKTKLVVSDHSHEGWLDFCSLIKSASPdhtciKSKMKDPMAIFFTSGTTGY 228
Cdd:cd05926 89 LVLTpKGELGPASRAASKLGLailelalDVGVLIRAPSAESLSNLLADKKNAKSEG-----VPLPDDLALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 229 PKMA--KHNQGLAFRSYIpscRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHhlPQFDPKVIVEVLFKYP 306
Cdd:cd05926 164 PKGVplTHRNLAASATNI---TNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLP--PRFSASTFWPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 307 ITQCLAAPGVYRMVLQQKTSNLR--FPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETG--ISSATLREMKIKR 382
Cdd:cd05926 239 ATWYTAVPTIHQILLNRPEPNPEspPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 383 GSIGKAILPfDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEV-ECGDFYNSGDRATIDEEGYIWFL 461
Cdd:cd05926 319 GSVGKPVGV-EVRILDEDGEILPPGVVGEICLR-GPNVTRG----YLNNPEANAEAaFKDGWFRTGDLGYLDADGYLFLT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 462 GRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNpEFLSHDQEQLIKELQHHVksvtAPYK 541
Cdd:cd05926 393 GRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLR-EGASVTEEELRAFCRKHL----AAFK 467
|
490 500
....*....|....*....|....*.
gi 18381087 542 YPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:cd05926 468 VPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
49-565 |
8.75e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 191.79 E-value: 8.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 49 SDVLDYWAQmeeegKRGPSPAFWWVngqGDEIkwSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCM 128
Cdd:PRK06178 36 TEYLRAWAR-----ERPQRPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVFLPNCPQFHIVFFGIL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 129 RTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPdLKTKLVVSDH--------------------S 188
Cdd:PRK06178 105 KLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETS-LRHVIVTSLAdvlpaeptlplpdslraprlA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 189 HEGWLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAFRSYIPSCRKLLKLKTSDILWCMSDPGWI 268
Cdd:PRK06178 184 AAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 269 LATVGCLIEPWTSGCTVFIhhLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLR-FPTLEH--CTTGGESLLP 345
Cdd:PRK06178 264 AGENFGLLFPLFSGATLVL--LARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYdLSSLRQvrVVSFVKKLNP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 346 EEYEQWKQRTGLSIHEV-YGQSETGISSA----------TLREMKIKRGsigkaiLPF---DLQIID-EKGNILPPNTEG 410
Cdd:PRK06178 342 DYRQRWRALTGSVLAEAaWGMTETHTCDTftagfqdddfDLLSQPVFVG------LPVpgtEFKICDfETGELLPLGAEG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 411 YIGIRiKPTrplgLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAV 490
Cdd:PRK06178 416 EIVVR-TPS----LLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAV 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18381087 491 AESAVVSSPDKDRGEVVKAFIVLNPEflsHDQEQliKELQHHVKSVTAPYKYPrKVEFVSELPKTVTGKIKRKEL 565
Cdd:PRK06178 491 LGSAVVGRPDPDKGQVPVAFVQLKPG---ADLTA--AALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
83-565 |
9.12e-54 |
|
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: 190.52 E-value: 9.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA 162
Cdd:cd05904 34 TYAELERRVRRLAAGLAKR-GGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SLVPEVesvasecPDLKTKLVVSDHSHEGWLDFCSLIKSASPDHTCiKSKMK--DPMAIFFTSGTTGYPK--MAKHnqgl 238
Cdd:cd05904 113 ELAEKL-------ASLALPVVLLDSAEFDSLSFSDLLFEADEAEPP-VVVIKqdDVAALLYSSGTTGRSKgvMLTH---- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 239 afRSYIPSCRKLLKLKTSDilwcMSDPGWILATV---------GCLIEPWTSGCTVFIhhLPQFDPKVIVEVLFKYPITQ 309
Cdd:cd05904 181 --RNLIAMVAQFVAGEGSN----SDSEDVFLCVLpmfhiyglsSFALGLLRLGATVVV--MPRFDLEELLAAIERYKVTH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 310 CLAAPG-VYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLS-IHEVYGQSE-TGISSATL--REMKIKRGS 384
Cdd:cd05904 253 LPVVPPiVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVdLGQGYGMTEsTGVVAMCFapEKDRAKYGS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 385 IGKaILP-FDLQIID-EKGNILPPNTEGYIGIRiKPTrplglFM-EYENSPESTSEVECGD-FYNSGDRATIDEEGYIWF 460
Cdd:cd05904 333 VGR-LVPnVEAKIVDpETGESLPPNQTGELWIR-GPS-----IMkGYLNNPEATAATIDKEgWLHTGDLCYIDEDGYLFI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 461 LGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEflSHDQEQLIKELqhhVKSVTAPY 540
Cdd:cd05904 406 VDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG--SSLTEDEIMDF---VAKQVAPY 480
|
490 500
....*....|....*....|....*
gi 18381087 541 KYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd05904 481 KKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
82-568 |
2.80e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 188.96 E-value: 2.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 82 WSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTT 161
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 162 ASLVPEVESVASECPDLKTKLVVSDHSHEGWLDFCSLIKSAS----PDHTCikskmKDPMAifFTSGTTGYPKMAK---- 233
Cdd:PRK08276 91 AALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPdtpiADETA-----GADML--YSSGTTGRPKGIKrplp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 234 HNQ-----------GLAFRSYIPSCRKLLK---LKTSDILWCMSdpgwILATvgcliepwtsGCTVFIhhLPQFDPKVIV 299
Cdd:PRK08276 164 GLDpdeapgmmlalLGFGMYGGPDSVYLSPaplYHTAPLRFGMS----ALAL----------GGTVVV--MEKFDAEEAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 300 EVLFKYPITQCLAAPGVY-RMV-LQQKT------SNLRF------PtlehCttggesllPEEYEQ-----WkqrtGLSIH 360
Cdd:PRK08276 228 ALIERYRVTHSQLVPTMFvRMLkLPEEVrarydvSSLRVaihaaaP----C--------PVEVKRamidwW----GPIIH 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 361 EVYGQSET-GISSATLREMKIKRGSIGKAILPfDLQIIDEKGNILPPNTEGYIGIRikptRPLGLFmEYENSPESTSEVE 439
Cdd:PRK08276 292 EYYASSEGgGVTVITSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE----MDGYPF-EYHNDPEKTAAAR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 440 CG-DFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAfiVLNPEFL 518
Cdd:PRK08276 366 NPhGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQPADG 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 18381087 519 SHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNK 568
Cdd:PRK08276 444 ADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
82-566 |
3.44e-52 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 188.63 E-value: 3.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 82 WSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFmPGTTQLKAKDILYRIQISRAKAIVTT 161
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSL-GVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVTL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 162 AS-----LVPEVESVASECPDLKTKLVV-----------------SDHSHEGWLDFCSLIKSASPDHTCIKSKMK--DPM 217
Cdd:PRK07529 137 GPfpgtdIWQKVAEVLAALPELRTVVEVdlarylpgpkrlavpliRRKAHARILDFDAELARQPGDRLFSGRPIGpdDVA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 218 AIFFTSGTTGYPKMAKHNQG-LAFRSYIPScrKLLKLKTSDILWCmsdpGWIL----ATVGCLIEPWTSGCTVFIHHlPQ 292
Cdd:PRK07529 217 AYFHTGGTTGMPKLAQHTHGnEVANAWLGA--LLLGLGPGDTVFC----GLPLfhvnALLVTGLAPLARGAHVVLAT-PQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 293 --FDPKV------IVEvlfKYPITQCLAAPGVYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYG 364
Cdd:PRK07529 290 gyRGPGVianfwkIVE---RYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 365 QSE-TGISSATLREMKIKRGSIGkaiLPFDLQ-----IIDEKGNIL---PPNTEGYIGIRiKPtrplGLFMEYENSPEST 435
Cdd:PRK07529 367 LTEaTCVSSVNPPDGERRIGSVG---LRLPYQrvrvvILDDAGRYLrdcAVDEVGVLCIA-GP----NVFSGYLEAAHNK 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 436 SEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNP 515
Cdd:PRK07529 439 GLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKP 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 18381087 516 EflSHDQEQlikELQHHVKSVTA-PYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK07529 519 G--ASATEA---ELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
76-566 |
2.40e-51 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 184.12 E-value: 2.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 76 QGDEIKWSFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRA 155
Cdd:PRK08008 32 GGVVRRYSYLELNEEINRTANLFYS-LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 156 KAIVTTASLVPEVESVASECPD-LKTKLVVSDHSHE--GWLDFCSLiKSASPDHTCIKSKMK--DPMAIFFTSGTTGYPK 230
Cdd:PRK08008 111 SLLVTSAQFYPMYRQIQQEDATpLRHICLTRVALPAddGVSSFTQL-KAQQPATLCYAPPLStdDTAEILFTSGTTSRPK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 231 ---MAKHNqgLAFRSYIPS--CRkllkLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVfihhlpqfdpkVIVE----- 300
Cdd:PRK08008 190 gvvITHYN--LRFAGYYSAwqCA----LRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATF-----------VLLEkysar 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 301 ------VLFKYPITQCLaaPGVYR-MVLQQKTSNLRfptlEHCTTGGESLLP---EEYEQWKQRTGLSIHEVYGQSETGI 370
Cdd:PRK08008 253 afwgqvCKYRATITECI--PMMIRtLMVQPPSANDR----QHCLREVMFYLNlsdQEKDAFEERFGVRLLTSYGMTETIV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 371 SSATLREMKIKR-GSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRIKPTRPLglFMEYENSPESTSEVECGD-FYNSGD 448
Cdd:PRK08008 327 GIIGDRPGDKRRwPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTI--FKEYYLDPKATAKVLEADgWLHTGD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 449 RATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNP-EFLShdQEQLIK 527
Cdd:PRK08008 405 TGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEgETLS--EEEFFA 482
|
490 500 510
....*....|....*....|....*....|....*....
gi 18381087 528 ELQHHVksvtAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK08008 483 FCEQNM----AKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
46-572 |
2.62e-51 |
|
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: 185.77 E-value: 2.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 46 NFASDVLDYWaqmeeEGKRGPSPAFWWVNGQGDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTV 125
Cdd:cd05968 61 NIVEQLLDKW-----LADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRAL-GVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 126 GCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTT---------ASLVPEVESVASECPDLKTKLVV-----SDHSHEG 191
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgreVNLKEEADKACAQCPTVEKVVVVrhlgnDFTPAKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 192 WLDFCSLIKSASPDHTCiKSKMKDPMAIFFTSGTTGYPKMAKHNQG-----LAFRSYIPscrklLKLKTSDILWCMSDPG 266
Cdd:cd05968 215 RDLSYDEEKETAGDGAE-RTESEDPLMIIYTSGTTGKPKGTVHVHAgfplkAAQDMYFQ-----FDLKPGDLLTWFTDLG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 267 WILAtvgcliePW------TSGCTVFIHH-LPQFD-PKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLR---FPTLEH 335
Cdd:cd05968 289 WMMG-------PWlifgglILGATMVLYDgAPDHPkADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNahdLSSLRV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 336 CTTGGESLLPEEYeQWKQRTGLSIH----------EVYGqsetGISSATLREmKIKRGSIGKAILPFDLQIIDEKGNILP 405
Cdd:cd05968 362 LGSTGEPWNPEPW-NWLFETVGKGRnpiinysggtEISG----GILGNVLIK-PIKPSSFNGPVPGMKADVLDESGKPAR 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 406 PnTEGYIGIRiKP----TRPlglFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVE 481
Cdd:cd05968 436 P-EVGELVLL-APwpgmTRG---FWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 482 NALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlsHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIK 561
Cdd:cd05968 511 SVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGV--TPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVM 588
|
570
....*....|.
gi 18381087 562 RKELRNKEFGQ 572
Cdd:cd05968 589 RRVIRAAYLGK 599
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
77-566 |
2.43e-49 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 178.15 E-value: 2.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 77 GDEIKWSFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAK 156
Cdd:PRK07514 24 PDGLRYTYGDLDAASARLANLLVA-LGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AIVTTASLVPEVESVASECPdlkTKLVVS-DHSHEGwldfcSLIKSA---SPDHTCIKSKMKDPMAIFFTSGTTGYPK-- 230
Cdd:PRK07514 103 LVVCDPANFAWLSKIAAAAG---APHVETlDADGTG-----SLLEAAaaaPDDFETVPRGADDLAAILYTSGTTGRSKga 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 231 MAKH----NQGLAFRSYipscrklLKLKTSDILWCMSdP-----GWILATVGCLIepwtSGCTVFIhhLPQFDPKVIVE- 300
Cdd:PRK07514 175 MLSHgnllSNALTLVDY-------WRFTPDDVLIHAL-PifhthGLFVATNVALL----AGASMIF--LPKFDPDAVLAl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 301 -----VLFKYPI--TQCLAAPGVYRmvlqQKTSNLRFptlehCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSA 373
Cdd:PRK07514 241 mpratVMMGVPTfyTRLLQEPRLTR----EAAAHMRL-----FISGSAPLLAETHREFQERTGHAILERYGMTETNMNTS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 374 TLREMKIKRGSIGKAiLP-FDLQIID-EKGNILPPnteGYIG-IRIK-PTrplgLFMEYENSPESTSEVECGD-FYNSGD 448
Cdd:PRK07514 312 NPYDGERRAGTVGFP-LPgVSLRVTDpETGAELPP---GEIGmIEVKgPN----VFKGYWRMPEKTAEEFRADgFFITGD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 449 RATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlSHDQEQLIKE 528
Cdd:PRK07514 384 LGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGA-ALDEAAILAA 462
|
490 500 510
....*....|....*....|....*....|....*...
gi 18381087 529 LqhhvKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK07514 463 L----KGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
77-567 |
3.22e-49 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 177.74 E-value: 3.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 77 GDEIKWSFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAK 156
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AIVTTaslvPEVESVASEcpdLKTKLVVSdhsHEGWLDFCSLIKSASPDHTCIKSKmKDPMAIFFTSGTTGYPKMAKHNQ 236
Cdd:PRK06839 103 VLFVE----KTFQNMALS---MQKVSYVQ---RVISITSLKEIEDRKIDNFVEKNE-SASFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 237 GLAFRSYIPSCRKLlKLKTSDILWCMSdPGWILATVGCLIEP-WTSGCTVFIHHlpQFDPKVIVEVLFKYPITQCLAAPG 315
Cdd:PRK06839 172 ENMFWNALNNTFAI-DLTMHDRSIVLL-PLFHIGGIGLFAFPtLFAGGVIIVPR--KFEPTKALSMIEKHKVTVVMGVPT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 316 VYRMVLQqkTSNLRFPTLEHCT--TGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIKR--GSIGKAILP 391
Cdd:PRK06839 248 IHQALIN--CSKFETTNLQSVRwfYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARRkvGSIGKPVLF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 392 FDLQIIDEKGNILPPNTEGYIGIRiKPTrplgLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINAS 471
Cdd:PRK06839 326 CDYELIDENKNKVEVGEVGELLIR-GPN----VMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 472 GYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLSHDqeqliKELQHHVKSVTAPYKYPRKVEFVSE 551
Cdd:PRK06839 401 GENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE-----KDVIEHCRLFLAKYKIPKEIVFLKE 475
|
490
....*....|....*.
gi 18381087 552 LPKTVTGKIKRKELRN 567
Cdd:PRK06839 476 LPKNATGKIQKAQLVN 491
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
63-566 |
3.34e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 178.26 E-value: 3.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 63 KRGPS-PAFWWvngqgDEIKWSFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEWWLV-----TVGCMRTGIIFMp 136
Cdd:PRK06188 23 KRYPDrPALVL-----GDTRLTYGQLADRISRYIQAFEA-LGLGTGDAVALLSLNRPEVLMAigaaqLAGLRRTALHPL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 137 GTTQlkakDILYRIQISRAKA-IVTTASLVPEVESVASECPDLKTKLVVSDHshEGWLDFCSLIKSASPDHTCIKSKMKD 215
Cdd:PRK06188 96 GSLD----DHAYVLEDAGISTlIVDPAPFVERALALLARVPSLKHVLTLGPV--PDGVDLLAAAAKFGPAPLVAAALPPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 216 PMAIFFTSGTTGYPK--MAKHNQGLAFRSyipscrkllklktsdilWCMSDPGW-----ILATV------GCLIEP--WT 280
Cdd:PRK06188 170 IAGLAYTGGTTGKPKgvMGTHRSIATMAQ-----------------IQLAEWEWpadprFLMCTplshagGAFFLPtlLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 281 SGCTVFihhLPQFDPKVIVEVLFKYPITQCLAAPG-VYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSI 359
Cdd:PRK06188 233 GGTVIV---LAKFDPAEVLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 360 HEVYGQSETGISSATLRE-----MKIKR-GSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRikptRPLgLFMEYENSPE 433
Cdd:PRK06188 310 AQYYGQTEAPMVITYLRKrdhdpDDPKRlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVR----GPL-VMDGYWNRPE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 434 STSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVL 513
Cdd:PRK06188 385 ETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVL 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 18381087 514 NPEfLSHDQEqlikELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK06188 465 RPG-AAVDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
83-568 |
2.11e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 176.04 E-value: 2.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQIcGLQQGDHLALIL---PRVPEwwlVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIV 159
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 160 TTASLVPEVESVASECPDLKTKLVV-SDHSHEGWLDFCSLIKSASPdhTCIKSK-MKDPMaiFFTSGTTGYPKMAK---- 233
Cdd:PRK13391 102 TSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPA--TPIADEsLGTDM--LYSSGTTGRPKGIKrplp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 234 HNQGLAFRSYIPSCRKLLKLKTSDILWC-----MSDPgwiLATVGCLIepwTSGCTVFIhhLPQFDPKVIVEVLFKYPIT 308
Cdd:PRK13391 178 EQPPDTPLPLTAFLQRLWGFRSDMVYLSpaplyHSAP---QRAVMLVI---RLGGTVIV--MEHFDAEQYLALIEEYGVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 309 QCLAAPGVY-RMVLQQKTSNLRF--PTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSE-TGISSATLREMKIKRGS 384
Cdd:PRK13391 250 HTQLVPTMFsRMLKLPEEVRDKYdlSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEgLGFTACDSEEWLAHPGT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 385 IGKAILPfDLQIIDEKGNILPPNTEGYIGIRIkptrplGLFMEYENSPESTSEV--ECGDFYNSGDRATIDEEGYIWFLG 462
Cdd:PRK13391 330 VGRAMFG-DLHILDDDGAELPPGEPGTIWFEG------GRPFEYLNDPAKTAEArhPDGTWSTVGDIGYVDEDGYLYLTD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 463 RGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAfiVLNPEFLSHDQEQLIKELQHHVKSVTAPYKY 542
Cdd:PRK13391 403 RAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKA--VVQPVDGVDPGPALAAELIAFCRQRLSRQKC 480
|
490 500
....*....|....*....|....*.
gi 18381087 543 PRKVEFVSELPKTVTGKIKRKELRNK 568
Cdd:PRK13391 481 PRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
51-567 |
1.03e-47 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 174.94 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 51 VLDYWAQmeeEGKRGPSPAFWwVNGQGDeiKWSFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEWWLVTVGCMRT 130
Cdd:PRK06087 25 LADYWQQ---TARAMPDKIAV-VDNHGA--SYTYSALDHAASRLANWLLA-KGIEPGDRVAFQLPGWCEFTIIYLACLKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 131 GIIFMPGTTQLKAKDILYRIQISRAKAIVT-----TASLVPEVESVASECPDLKTKLVVSDHSHE-GWLDFCSLIKSASP 204
Cdd:PRK06087 98 GAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGVDKLAPAtSSLSLSQIIADYEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 205 DHTCIKSKMKDPMAIFFTSGTTGYPK--MAKHNQGLAF-RSYIpscrKLLKLKTSDILWCMSDPGWILATVGCLIEPWTS 281
Cdd:PRK06087 178 LTTAITTHGDELAAVLFTSGTEGLPKgvMLTHNNILASeRAYC----ARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 282 GCTVFIhhLPQFDPKVIVEVLFKYPITQCLAA-PGVYRMVLQQKTSNLRFPTLEHCTTGGeSLLPEEYEQWKQRTGLSIH 360
Cdd:PRK06087 254 GARSVL--LDIFTPDACLALLEQQRCTCMLGAtPFIYDLLNLLEKQPADLSALRFFLCGG-TTIPKKVARECQQRGIKLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 361 EVYGQSETGISSATLREMKIKR--GSIGKAILPFDLQIIDEKGNILPPNTEGYigiriKPTRPLGLFMEYENSPESTSEV 438
Cdd:PRK06087 331 SVYGSTESSPHAVVNLDDPLSRfmHTDGYAAAGVEIKVVDEARKTLPPGCEGE-----EASRGPNVFMGYLDEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 439 --ECGDFYnSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPE 516
Cdd:PRK06087 406 ldEEGWYY-SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAP 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 18381087 517 FLSHDQEQLIKELQhhvKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:PRK06087 485 HHSLTLEEVVAFFS---RKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
103-566 |
3.25e-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: 171.47 E-value: 3.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 103 GLQQGDHLALILPRVPEW-WL---VTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPDL 178
Cdd:cd05922 14 GGVRGERVVLILPNRFTYiELsfaVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 179 KTKLVVsdhshEGWLDFCSLIKSASPDHtcikskmKDPMAIFFTSGTTGYPK--MAKHNQGLAFRSYIpscRKLLKLKTS 256
Cdd:cd05922 94 GTVLDA-----DGIRAARASAPAHEVSH-------EDLALLLYTSGSTGSPKlvRLSHQNLLANARSI---AEYLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 257 DILWCMSDPGWILATvGCLIEPWTSGCTVFIHHLPQFDPKVIvEVLFKYPITQCLAAPGVYRMVLQQKTSNLRFPTLEHC 336
Cdd:cd05922 159 DRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVLDDAFW-EDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 337 TTGGESLLPEEYEQWKQR-TGLSIHEVYGQSETGISSATLREMKIKR--GSIGKAILPFDLQIIDEKGNILPPNTEGYIG 413
Cdd:cd05922 237 TQAGGRLPQETIARLRELlPGAQVYVMYGQTEATRRMTYLPPERILEkpGSIGLAIPGGEFEILDDDGTPTPPGEPGEIV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 414 irikPTRPLGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAES 493
Cdd:cd05922 317 ----HRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18381087 494 AVVSSPDkDRGEVVKAFIVLNPEFLSHDqeqlikeLQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd05922 393 AAVGLPD-PLGEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
49-566 |
6.31e-47 |
|
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: 172.25 E-value: 6.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 49 SDVLDYWAQmeeegKRGPSPAFwwVNGqgdEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCM 128
Cdd:COG1021 28 GDLLRRRAE-----RHPDRIAV--VDG---ERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 129 RTGII---FMPGttqLKAKDILYRIQISRAKAIVTTAS-----LVPEVESVASECPDLKTKLVVSDHshEGWLDFCSLIK 200
Cdd:COG1021 97 RAGAIpvfALPA---HRRAEISHFAEQSEAVAYIIPDRhrgfdYRALARELQAEVPSLRHVLVVGDA--GEFTSLDALLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 201 SASpDHTCIKSKMKDPmAIFFTS-GTTGYPKMA--KHNQGL-AFRSYIPSCRkllkLKTSDILWC---------MSDPGw 267
Cdd:COG1021 172 APA-DLSEPRPDPDDV-AFFQLSgGTTGLPKLIprTHDDYLySVRASAEICG----LDADTVYLAalpaahnfpLSSPG- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 268 ILATVgcliepWTSGCTVFihhLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQ-QKTSNLRFPTLEHCTTGGESLLPE 346
Cdd:COG1021 245 VLGVL------YAGGTVVL---APDPSPDTAFPLIERERVTVTALVPPLALLWLDaAERSRYDLSSLRVLQVGGAKLSPE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 347 EYEQWKQRTGLSIHEVYGQSEtGISSATL----REMKIkrGSIGKAILPFD-LQIIDEKGNILPPNTEGYIGIRiKPTRP 421
Cdd:COG1021 316 LARRVRPALGCTLQQVFGMAE-GLVNYTRlddpEEVIL--TTQGRPISPDDeVRIVDEDGNPVPPGEVGELLTR-GPYTI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 422 LGlfmeYENSPESTSEVECGD-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPD 500
Cdd:COG1021 392 RG----YYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPD 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18381087 501 KDRGEVVKAFIVLNPEFLShdqeqlIKELQHHVKSV-TAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:COG1021 468 EYLGERSCAFVVPRGEPLT------LAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALR 528
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
74-567 |
1.16e-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: 171.27 E-value: 1.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 74 NGQGDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILprvpewW-----LVT---VGCMrtGIIFMPGTTQLKAKD 145
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLA------WnthrhLELyyaVPGM--GAVLHTINPRLFPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 146 ILYRIQISRAKAIVTTASLVPEVESVASECPDLKTKLVVSDHSH------EGWLDFCSLIKSASPDHTCIKSKMKDPMAI 219
Cdd:cd12119 89 IAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 220 FFTSGTTGYPK--MAKHNQgLAFRSYIPSCRKLLKLKTSDILWCMSdP-----GWILATVGcliePWTSGCTVfihhLPQ 292
Cdd:cd12119 169 CYTSGTTGNPKgvVYSHRS-LVLHAMAALLTDGLGLSESDVVLPVV-PmfhvnAWGLPYAA----AMVGAKLV----LPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 293 --FDPKVIVEVLFKYPITQCLAAPGVYRMVLQ-QKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRtGLSIHEVYGQSETG 369
Cdd:cd12119 239 pyLDPASLAELIEREGVTFAAGVPTVWQGLLDhLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 370 --ISSATL--------REMKI-KRGSIGKAILPFDLQIIDEKGNILP--PNTEGYIGIRiKPTrplgLFMEYENSPESTS 436
Cdd:cd12119 318 plGTVARPpsehsnlsEDEQLaLRAKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVR-GPW----VTKSYYKNDEESE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 437 EVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPe 516
Cdd:cd12119 393 ALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKE- 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 18381087 517 flshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:cd12119 472 ----GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
78-565 |
3.59e-46 |
|
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: 168.09 E-value: 3.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 78 DEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWwLVTV-GCMRTGIIFMPGTTQLKAKDILYRIQISRAK 156
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEM-VVAIlAVLKAGAAYVPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AIVTTASlvpevesvasecpdlktklvvsdhshegwldfcsliksaspdhtcikskmkDPMAIFFTSGTTGYPK--MAKH 234
Cdd:cd05930 87 LVLTDPD---------------------------------------------------DLAYVIYTSGSTGKPKgvMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 235 nQGLAfrSYIPSCRKLLKLKTSDILWCMSDPGWILAtVGCLIEPWTSGCTVfiHHLPQ---FDPKVIVEVLFKYPITQCL 311
Cdd:cd05930 116 -RGLV--NLLLWMQEAYPLTPGDRVLQFTSFSFDVS-VWEIFGALLAGATL--VVLPEevrKDPEALADLLAEEGITVLH 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 312 AAPGVYRMVLQQkTSNLRFPTLEHCTTGGESLLPEEYEQWKQR-TGLSIHEVYGQSETGISSAT--LREMKIKRGS--IG 386
Cdd:cd05930 190 LTPSLLRLLLQE-LELAALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDATYyrVPPDDEEDGRvpIG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 387 KAILPFDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEYENSPESTSEVECGD-------FYNSGDRATIDEEGY 457
Cdd:cd05930 269 RPIPNTRVYVLDENLRPVPPGVPGelYIG-------GAGLARGYLNRPELTAERFVPNpfgpgerMYRTGDLVRWLPDGN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 458 IWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPeflshDQEQLIKELQHHVKSVT 537
Cdd:cd05930 342 LEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE-----GGELDEEELRAHLAERL 416
|
490 500
....*....|....*....|....*...
gi 18381087 538 APYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd05930 417 PDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
209-566 |
4.55e-46 |
|
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: 167.14 E-value: 4.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 209 IKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAFRSYIpSCRKLLKLkTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIH 288
Cdd:cd05912 72 SDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAI-GSALNLGL-TEDDNWLCALPLFHISGLSILMRSVIYGMTVYLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 289 hlPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQ----KTSNLRFPTLehcttGGESLLPEEYEQWKQRtGLSIHEVYG 364
Cdd:cd05912 150 --DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEIlgegYPNNLRCILL-----GGGPAPKPLLEQCKEK-GIPVYQSYG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 365 QSETGISSATL--REMKIKRGSIGKAILPFDLQIIDEKGnilPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVECGD 442
Cdd:cd05912 222 MTETCSQIVTLspEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLK-GPNVTKG----YLNRPDATEESFENG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 443 FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlshDQ 522
Cdd:cd05912 294 WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SE 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 18381087 523 EQLIKELQHHVksvtAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd05912 371 EELIAYCSEKL----AKYKVPKKIYFVDELPRTASGKLLRHELK 410
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
79-566 |
5.22e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 167.64 E-value: 5.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 79 EIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAI 158
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 159 VTTA------------SLVPEV------ESVASECPDLKTKLVVSDHSHEGWLDFCSLIK-------------SASPDHt 207
Cdd:PRK12583 122 ICADafktsdyhamlqELLPGLaegqpgALACERLPELRGVVSLAPAPPPGFLAWHELQArgetvsrealaerQASLDR- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 208 cikskmKDPMAIFFTSGTTGYPKMA--KHNQGLAfRSYIPSCRklLKLKTSDILwCMSDP-----GWILATVGCLiepwT 280
Cdd:PRK12583 201 ------DDPINIQYTSGTTGFPKGAtlSHHNILN-NGYFVAES--LGLTEHDRL-CVPVPlyhcfGMVLANLGCM----T 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 281 SGCTVFIhhlPQ--FDPKVIVEVLFKypiTQCLAAPGVYRMVLQQKT----SNLRFPTLEHCTTGGESLLPEEYeqwkQR 354
Cdd:PRK12583 267 VGACLVY---PNeaFDPLATLQAVEE---ERCTALYGVPTMFIAELDhpqrGNFDLSSLRTGIMAGAPCPIEVM----RR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 355 TGLSIH--EV---YGQSETG-ISSATLRE--MKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGirikpTRPLGLFM 426
Cdd:PRK12583 337 VMDEMHmaEVqiaYGMTETSpVSLQTTAAddLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC-----TRGYSVMK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 427 EYENSPESTSEVECGD-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGE 505
Cdd:PRK12583 412 GYWNNPEATAESIDEDgWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGE 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18381087 506 VVKAFIVLNPeflshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK12583 492 EIVAWVRLHP-----GHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
215-566 |
6.54e-45 |
|
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: 162.45 E-value: 6.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPKMA---KHNqgLAFRSYIPSCRklLKLKTSDILwCMSDP-----GWILATVGCLiepwTSGCT-V 285
Cdd:cd05917 3 DVINIQFTSGTTGSPKGAtltHHN--IVNNGYFIGER--LGLTEQDRL-CIPVPlfhcfGSVLGVLACL----THGATmV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 286 FIHhlPQFDPKVIVEVLFKypiTQCLAAPGVYRMVL----QQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLS-IH 360
Cdd:cd05917 74 FPS--PSFDPLAVLEAIEK---EKCTALHGVPTMFIaeleHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKdVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 361 EVYGQSETG-ISSATLREMKIKR--GSIGKAILPFDLQIIDEKGNILPP-NTEGYIGIRikptrPLGLFMEYENSPESTS 436
Cdd:cd05917 149 IAYGMTETSpVSTQTRTDDSIEKrvNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEKTA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 437 EVECGD-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNP 515
Cdd:cd05917 224 EAIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKE 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 18381087 516 EflshdQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd05917 304 G-----AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
79-567 |
5.23e-44 |
|
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: 163.24 E-value: 5.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 79 EIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAI 158
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 159 VTtaslvpevesvasecpdlktklvvsDHSHEgwldFCSLIKSASPDHTCIKSKMK-DPMAIFFTSGTTGYPK-MAKHNQ 236
Cdd:cd12118 106 FV-------------------------DREFE----YEDLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKgVVYHHR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 237 GlafrSYIPSCRKLL--KLKTSDI-LWCMSD---PGWilatvgCLiePWT----SGCTVFihhLPQFDPKVIVEVLFKYP 306
Cdd:cd12118 157 G----AYLNALANILewEMKQHPVyLWTLPMfhcNGW------CF--PWTvaavGGTNVC---LRKVDAKAIYDLIEKHK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 307 ITQCLAAPGVYRMVLQQKTSNLR-FPTLEHCTTGGeSLLPEEYEQWKQRTGLSIHEVYGQSET----------------- 368
Cdd:cd12118 222 VTHFCGAPTVLNMLANAPPSDARpLPHRVHVMTAG-APPPAAVLAKMEELGFDVTHVYGLTETygpatvcawkpewdelp 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 369 -----------GISSATLREMKIKRGSIGKAIlPFDLQIIDE---KGNILppnTEGYigirikptrplglfmeYENsPES 434
Cdd:cd12118 301 teerarlkarqGVRYVGLEEVDVLDPETMKPV-PRDGKTIGEivfRGNIV---MKGY----------------LKN-PEA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 435 TSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLN 514
Cdd:cd12118 360 TAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELK 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 18381087 515 PeflshDQEQLIKELQHHVKSVTAPYKYPRKVEFvSELPKTVTGKIKRKELRN 567
Cdd:cd12118 440 E-----GAKVTEEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
83-566 |
3.92e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 158.25 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA 162
Cdd:PRK13390 26 SYRQLDDDSAALARVLYD-AGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SLvpevESVASEC-PDLKTKLVVSDHShEGWLDFCSLIKSASPDHTcikskmKDP--MAIFFTSGTTGYPKMAKHNqgLA 239
Cdd:PRK13390 105 AL----DGLAAKVgADLPLRLSFGGEI-DGFGSFEAALAGAGPRLT------EQPcgAVMLYSSGTTGFPKGIQPD--LP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 240 FRSY-------IPSCRKLLKLKTSDILWCmSDPGWILATVgcliePWTS-----GCTVFIHHlpQFDPKVIVEVLFKYPI 307
Cdd:PRK13390 172 GRDVdapgdpiVAIARAFYDISESDIYYS-SAPIYHAAPL-----RWCSmvhalGGTVVLAK--RFDAQATLGHVERYRI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 308 TQCLAAPGVY-RMVLQQKTSNLRF--PTLE---HCTTGGESLLPEEYEQWkqrTGLSIHEVYGQSET-GISSATLREMKI 380
Cdd:PRK13390 244 TVTQMVPTMFvRLLKLDADVRTRYdvSSLRaviHAAAPCPVDVKHAMIDW---LGPIVYEYYSSTEAhGMTFIDSPDWLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 381 KRGSIGKAILPfDLQIIDEKGNILPPnteGYIG-IRIKPTRplgLFMEYENSPESTSEVE--CGDFYNS-GDRATIDEEG 456
Cdd:PRK13390 321 HPGSVGRSVLG-DLHICDDDGNELPA---GRIGtVYFERDR---LPFRYLNDPEKTAAAQhpAHPFWTTvGDLGSVDEDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 457 YIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlsHDQEQLIKELQHHVKSV 536
Cdd:PRK13390 394 YLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI--RGSDELARELIDYTRSR 471
|
490 500 510
....*....|....*....|....*....|
gi 18381087 537 TAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK13390 472 IAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
219-569 |
1.09e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 157.78 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 219 IFFTSGTTGYPKMAKHNQ--GLA----FRSYIPSCRKLLKLKTSDIL--WcmsdpGWILATVGCLIepwtsGCTVFIHHl 290
Cdd:PRK07788 212 VILTSGTTGTPKGAPRPEpsPLAplagLLSRVPFRAGETTLLPAPMFhaT-----GWAHLTLAMAL-----GSTVVLRR- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 291 pQFDPKVIVEVLFKYPITQCLAAPG-VYRMV-----LQQK--TSNLRFptlehCTTGGESLLPEEYEQWKQRTGLSIHEV 362
Cdd:PRK07788 281 -RFDPEATLEDIAKHKATALVVVPVmLSRILdlgpeVLAKydTSSLKI-----IFVSGSALSPELATRALEAFGPVLYNL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 363 YGQSETGISS-ATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNT------------EGYIGIRIKPTrplglfmeye 429
Cdd:PRK07788 355 YGSTEVAFATiATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVvgrifvgngfpfEGYTDGRDKQI---------- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 430 nspestseveCGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKA 509
Cdd:PRK07788 425 ----------IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRA 494
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 510 FIVLNPeflshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKE 569
Cdd:PRK07788 495 FVVKAP-----GAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
77-565 |
1.57e-41 |
|
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: 155.45 E-value: 1.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 77 GDEIKWSFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAK 156
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIA-LGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AivttaslvpevesvasecpdlktkLVVSDhshegwldfcsliksasPDHTCIkskmkdpmaIFFTSGTTGYPK--MAKH 234
Cdd:cd05907 80 A------------------------LFVED-----------------PDDLAT---------IIYTSGTTGRPKgvMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 235 NQglaFRSYIPSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTvfIHHLPqfDPKVIVEVLFKYPITQCLAAP 314
Cdd:cd05907 110 RN---ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGAR--IYFAS--SAETLLDDLSEVRPTVFLAVP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 315 GVYRMV----LQQKTSNLR--------FPTLEHCTTGGeSLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIKR 382
Cdd:cd05907 183 RVWEKVyaaiKVKAVPGLKrklfdlavGGRLRFAASGG-APLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 383 GSIGKAILPFDLQIiDEKGNILppntegyigirikpTRPLGLFMEYENSPESTSEVECGD-FYNSGDRATIDEEGYIWFL 461
Cdd:cd05907 262 GTVGKPLPGVEVRI-ADDGEIL--------------VRGPNVMLGYYKNPEATAEALDADgWLHTGDLGEIDEDGFLHIT 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 462 GRGDDVI-NASGYRIGPVEVENALAEHPAVAESAVVSspdkDRGEVVKAFIVLNPEFLSH----------------DQEQ 524
Cdd:cd05907 327 GRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG----DGRPFLVALIVPDPEALEAwaeehgiaytdvaelaANPA 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 18381087 525 LIKELQHHVKSVTA---PYKYPRKVEFVSElPKTV-------TGKIKRKEL 565
Cdd:cd05907 403 VRAEIEAAVEAANArlsRYEQIKKFLLLPE-PFTIengeltpTLKLKRPVI 452
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
83-573 |
1.98e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 157.62 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA 162
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SLVPEVESV----------ASECPDL--------------KTKLVVSDHSHEGWLDFCS-LIKSASPDHTCIKSKMKDPM 217
Cdd:PRK05677 131 NMAHLAEKVlpktgvkhviVTEVADMlpplkrllinavvkHVKKMVPAYHLPQAVKFNDaLAKGAGQPVTEANPQADDVA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 218 AIFFTSGTTGYPKMAKhnqgLAFRSYIPS---CRKLLKLKTSDILWCMSDP---GWILA-TVGCLIEPWTSGCTVFIHH- 289
Cdd:PRK05677 211 VLQYTGGTTGVAKGAM----LTHRNLVANmlqCRALMGSNLNEGCEILIAPlplYHIYAfTFHCMAMMLIGNHNILISNp 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 290 --LPQFdpkviVEVLFKYPITQCLAAPGVYRMVLQQKT-SNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQS 366
Cdd:PRK05677 287 rdLPAM-----VKELGKWKFSGFVGLNTLFVALCNNEAfRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 367 ETGiSSATLREMK-IKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVECGD-FY 444
Cdd:PRK05677 362 ETS-PVVSVNPSQaIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK-GPQVMKG----YWQRPEATDEILDSDgWL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 445 NSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSHDQEQ 524
Cdd:PRK05677 436 KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG-ETLTKEQ 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 18381087 525 LikeLQHHVKSVTApYKYPRKVEFVSELPKTVTGKIKRKELRNKEFGQL 573
Cdd:PRK05677 515 V---MEHMRANLTG-YKVPKAVEFRDELPTTNVGKILRRELRDEELKKA 559
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
60-573 |
2.65e-41 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 158.52 E-value: 2.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 60 EEGKRGPSPAFWWVNGQGDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTT 139
Cdd:PLN02654 99 EAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDV-GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 140 QLKAKDILYRIQISRAKAIVTT-----------------ASLVPEVESVAS--ECPDLKTKLVVSDHS---HEG----WL 193
Cdd:PLN02654 178 GFSAESLAQRIVDCKPKVVITCnavkrgpktinlkdivdAALDESAKNGVSvgICLTYENQLAMKREDtkwQEGrdvwWQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 194 DFCSLIKSASPDHTCiksKMKDPMAIFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKL-LKLKTSDILWCMSDPGWILATV 272
Cdd:PLN02654 258 DVVPNYPTKCEVEWV---DAEDPLFLLYTSGSTGKPKGVLHTTG-GYMVYTATTFKYaFDYKPTDVYWCTADCGWITGHS 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 273 GCLIEPWTSGCTVFIHH-LPQF-DPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNL-RFP--TLEHCTTGGESLLPEE 347
Cdd:PLN02654 334 YVTYGPMLNGATVLVFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVtRHSrkSLRVLGSVGEPINPSA 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 348 YEQWKQRTGLS---IHEVYGQSETG--ISSATLREMKIKRGSigkAILPF-DLQ--IIDEKGNILPPNTEGYIGIRIK-P 418
Cdd:PLN02654 414 WRWFFNVVGDSrcpISDTWWQTETGgfMITPLPGAWPQKPGS---ATFPFfGVQpvIVDEKGKEIEGECSGYLCVKKSwP 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 419 TRPLGLFMEYENSpESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSS 498
Cdd:PLN02654 491 GAFRTLYGDHERY-ETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGI 569
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18381087 499 PDKDRGEVVKAFIVLNpEFLSHdQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKEFGQL 573
Cdd:PLN02654 570 EHEVKGQGIYAFVTLV-EGVPY-SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQL 642
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
63-566 |
1.02e-40 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 156.26 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 63 KRGPSPAFWWVNGQGDEIK-WSFRKLRDLTCRTANVFeQICGLQQGDHLALILPRVPEWWLVTVGCMRTGII-------F 134
Cdd:PRK10524 65 KRPEQLALIAVSTETDEERtYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsvvfggF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 135 MPGTTQLKAKDILYRIQIS-----RAKAIVTTASLVPEVESVASECPdlkTKLVVSDHShegwLDFCSLIKSASPDHTCI 209
Cdd:PRK10524 144 ASHSLAARIDDAKPVLIVSadagsRGGKVVPYKPLLDEAIALAQHKP---RHVLLVDRG----LAPMARVAGRDVDYATL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 210 KSKMKD------------PMAIFFTSGTTGYPKMAKHNQG---LAFRSyipSCRKLLKLKTSDILWCMSDPGWILATVGC 274
Cdd:PRK10524 217 RAQHLGarvpvewlesnePSYILYTSGTTGKPKGVQRDTGgyaVALAT---SMDTIFGGKAGETFFCASDIGWVVGHSYI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 275 LIEPWTSGC-TVFIHHLP-QFDPKV---IVEvlfKYPITQCLAAPGVYRMVLQQKTSNLR---FPTLEHCTTGGESLlPE 346
Cdd:PRK10524 294 VYAPLLAGMaTIMYEGLPtRPDAGIwwrIVE---KYKVNRMFSAPTAIRVLKKQDPALLRkhdLSSLRALFLAGEPL-DE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 347 EYEQWKQRT-GLSIHEVYGQSETG---ISSA-TLREMKIKRGSIGKAILPFDLQIIDEK-GNILPPNTEGYIGIRikPTR 420
Cdd:PRK10524 370 PTASWISEAlGVPVIDNYWQTETGwpiLAIArGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIE--GPL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 421 PLGlFME--------YENSPESTSEVECgdfYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAE 492
Cdd:PRK10524 448 PPG-CMQtvwgdddrFVKTYWSLFGRQV---YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAE 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18381087 493 SAVVSSPDKDRGEVVKAFIVLNPEFLSHDQEQ---LIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK10524 524 VAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
81-572 |
1.06e-40 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 153.96 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 81 KWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVT 160
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLAAL-GVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 161 TASLVPEVESVASecpdlktklvvsdhshegwLDFCSLIKSASPDHTCIKS-KMKDPMAIFFTSGTTGYPKMAKHNQGLA 239
Cdd:PRK03640 106 DDDFEAKLIPGIS-------------------VKFAELMNGPKEEAEIQEEfDLDEVATIMYTSGTTGKPKGVIQTYGNH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 240 FRSYIPSCrklLKLK-TSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHhlPQFDPKVIVEVLFKYPITqclAAPGVYR 318
Cdd:PRK03640 167 WWSAVGSA---LNLGlTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLV--EKFDAEKINKLLQTGGVT---IISVVST 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 319 MV--LQQKTSNLRFPTLEHCT-TGG----ESLLpeeyEQWKQRtGLSIHEVYGQSETGISSATL--REMKIKRGSIGKAI 389
Cdd:PRK03640 239 MLqrLLERLGEGTYPSSFRCMlLGGgpapKPLL----EQCKEK-GIPVYQSYGMTETASQIVTLspEDALTKLGSAGKPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 390 LPFDLQIIDEkGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVIN 469
Cdd:PRK03640 314 FPCELKIEKD-GVVVPPFEEGEIVVK-GPNVTKG----YLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLII 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 470 ASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlshDQEqlikELQHHVKSVTAPYKYPRKVEFV 549
Cdd:PRK03640 388 SGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEV---TEE----ELRHFCEEKLAKYKVPKRFYFV 460
|
490 500
....*....|....*....|...
gi 18381087 550 SELPKTVTGKIKRKELRNKEFGQ 572
Cdd:PRK03640 461 EELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
83-566 |
1.09e-40 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 155.21 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQIcGLQQGDHLALilpRVPEWWLVTV---GCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIV 159
Cdd:PRK13295 57 TYRELAALVDRVAVGLARL-GVGRGDVVSC---QLPNWWEFTVlylACSRIGAVLNPLMPIFRERELSFMLKHAESKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 160 ttaslVPE----------VESVASECPDLKTKLVVSDHSHEGWLD-FCSLIKSASPDHTCIKSKMK----DPMAIFFTSG 224
Cdd:PRK13295 133 -----VPKtfrgfdhaamARRLRPELPALRHVVVVGGDGADSFEAlLITPAWEQEPDAPAILARLRpgpdDVTQLIYTSG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 225 TTGYPKMAKHNQGLAFRSYIPsCRKLLKLKTSDILWcMSDP-----GWILAtvgcLIEPWTSGCTVFIhhLPQFDPKVIV 299
Cdd:PRK13295 208 TTGEPKGVMHTANTLMANIVP-YAERLGLGADDVIL-MASPmahqtGFMYG----LMMPVMLGATAVL--QDIWDPARAA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 300 EVLFKYPITQCLAA-PGVYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREM 378
Cdd:PRK13295 280 ELIRTEGVTFTMAStPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 379 KIKR--GSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRikptrPLGLFMEYENSPESTSEVECGdFYNSGDRATIDEEG 456
Cdd:PRK13295 360 PDERasTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVR-----GCSNFGGYLKRPQLNGTDADG-WFDTGDLARIDADG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 457 YIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSHDQEQLIKELQHHvkSV 536
Cdd:PRK13295 434 YIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPG-QSLDFEEMVEFLKAQ--KV 510
|
490 500 510
....*....|....*....|....*....|
gi 18381087 537 TAPYkYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK13295 511 AKQY-IPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
290-562 |
4.36e-40 |
|
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: 148.57 E-value: 4.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 290 LPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQ-KTSNLRFPTLEHcTTGGESllPEEYEQWKQRTGLSIHEVYGQSET 368
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAaEKSGVDLSSLRH-VLGLDA--PETIQRFEETTGATFWSLYGQTET 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 369 GiSSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRikptRPLgLFMEYENSPESTSEVECGDFYNSGD 448
Cdd:cd17637 149 S-GLVTLSPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVR----GPL-VFQGYWNLPELTAYTFRNGWHHTGD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 449 RATIDEEGYIWFLGRG--DDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlSHDQEQLI 526
Cdd:cd17637 223 LGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGA-TLTADELI 301
|
250 260 270
....*....|....*....|....*....|....*.
gi 18381087 527 KelqhHVKSVTAPYKYPRKVEFVSELPKTVTGKIKR 562
Cdd:cd17637 302 E----FVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
80-566 |
6.68e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 153.04 E-value: 6.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 80 IKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIV 159
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLLAL-GIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 160 TTAS------------LVPEVES------VASECPDLKTKLVVSDHSHEGWLDFCSLIKSASPDH----TCIKSKMK--D 215
Cdd:PRK08315 121 AADGfkdsdyvamlyeLAPELATcepgqlQSARLPELRRVIFLGDEKHPGMLNFDELLALGRAVDdaelAARQATLDpdD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 216 PMAIFFTSGTTGYPK--MAKH----NQGLafrsYIPSCrklLKLKTSDILwCMSDP-----GWILATVGCLiepwTSGCT 284
Cdd:PRK08315 201 PINIQYTSGTTGFPKgaTLTHrnilNNGY----FIGEA---MKLTEEDRL-CIPVPlyhcfGMVLGNLACV----THGAT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 285 -VFIhhLPQFDPKVIVEVLFKypiTQCLAAPGVYRM---VLQQKT------SNLRfptlehctTG---GeSLLPEE-YEQ 350
Cdd:PRK08315 269 mVYP--GEGFDPLATLAAVEE---ERCTALYGVPTMfiaELDHPDfarfdlSSLR--------TGimaG-SPCPIEvMKR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 351 WKQRTGLSihEV---YGQSETG-ISSATLREMKIKR--GSIGKAiLPF-DLQIID-EKGNILPPNTEGYIGirikpTRPL 422
Cdd:PRK08315 335 VIDKMHMS--EVtiaYGMTETSpVSTQTRTDDPLEKrvTTVGRA-LPHlEVKIVDpETGETVPRGEQGELC-----TRGY 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 423 GLFMEYENSPESTSEVECGD-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDK 501
Cdd:PRK08315 407 SVMKGYWNDPEKTAEAIDADgWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDE 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18381087 502 DRGEVVKAFIVLNP-EFLSHDqeqlikELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK08315 487 KYGEEVCAWIILRPgATLTEE------DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
271-567 |
7.12e-40 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 152.87 E-value: 7.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 271 TVGCLIEPWTSGCTVFIHHlPQfDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKT-SNLRFPTLEHCTTGGESLLPEEYE 349
Cdd:PRK07059 268 TVCGLLGMRTGGRNILIPN-PR-DIPGFIKELKKYQVHIFPAVNTLYNALLNNPDfDKLDFSKLIVANGGGMAVQRPVAE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 350 QWKQRTGLSIHEVYGQSETGiSSATLREMKIKR--GSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfme 427
Cdd:PRK07059 346 RWLEMTGCPITEGYGLSETS-PVATCNPVDATEfsGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR-GPQVMAG---- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 428 YENSPESTSEVECGD-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEV 506
Cdd:PRK07059 420 YWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEA 499
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18381087 507 VKAFIVlnpeflSHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:PRK07059 500 VKLFVV------KKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
83-569 |
8.75e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 152.88 E-value: 8.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA 162
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKL-GVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SLVPEVESVAS----------ECPDL---------------KTKLVVSDHSHEGWLDFCSLIKSASPDHTCIKSKMKDPM 217
Cdd:PRK06710 130 LVFPRVTNVQSatkiehvivtRIADFlpfpknllypfvqkkQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 218 AIFFTSGTTGYPK--MAKHnqglafrsyipscRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHH------ 289
Cdd:PRK06710 210 LLQYTGGTTGFPKgvMLTH-------------KNLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLsimqgy 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 290 ----LPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKT-SNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYG 364
Cdd:PRK06710 277 kmvlIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 365 QSETG--ISSATLREMKIKrGSIGKAILPFDLQIID-EKGNILPPNTEGYIGIRiKPTrplgLFMEYENSPESTSEVECG 441
Cdd:PRK06710 357 LTESSpvTHSNFLWEKRVP-GSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK-GPQ----IMKGYWNKPEETAAVLQD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 442 DFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNpeflsHD 521
Cdd:PRK06710 431 GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK-----EG 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 18381087 522 QEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKE 569
Cdd:PRK06710 506 TECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
83-566 |
1.74e-39 |
|
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: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQIcGLQQGDHLALILPrvpEWWLVTV---GCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIV 159
Cdd:cd05903 3 TYSELDTRADRLAAGLAAL-GVGPGDVVAFQLP---NWWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKVFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 160 TTASLvpevesvasecpdlktklvvSDHSHEgwldfcsliksASPDHTCikskmkdpmAIFFTSGTTGYPKMAKHNQGLA 239
Cdd:cd05903 79 VPERF--------------------RQFDPA-----------AMPDAVA---------LLLFTSGTTGEPKGVMHSHNTL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 240 FRSYIPSCRKLlKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVfiHHLPQFDPKVIVEVLFKYPITQCLAA-PGVYR 318
Cdd:cd05903 119 SASIRQYAERL-GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTFMMGAtPFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 319 MVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETG--ISSATLREMKIKRGSIGKAILPFDLQI 396
Cdd:cd05903 196 LLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPgaVTSITPAPEDRRLYTDGRPLPGVEIKV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 397 IDEKGNILPPNTEGYIGIRiKPTrplgLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIG 476
Cdd:cd05903 276 VDDTGATLAPGVEGELLSR-GPS----VFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 477 PVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVL-NPEFLSHDqeqlikELQHHVKSV-TAPYKYPRKVEFVSELPK 554
Cdd:cd05903 351 VLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTkSGALLTFD------ELVAYLDRQgVAKQYWPERLVHVDDLPR 424
|
490
....*....|..
gi 18381087 555 TVTGKIKRKELR 566
Cdd:cd05903 425 TPSGKVQKFRLR 436
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
83-569 |
2.08e-39 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 151.74 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA 162
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SLVPEVESVASECP----------DL----KTKLVvsdhshegwlDFC-SLIKSASPdhtciksKMKDPMAIFF------ 221
Cdd:PRK08974 130 NFAHTLEKVVFKTPvkhviltrmgDQlstaKGTLV----------NFVvKYIKRLVP-------KYHLPDAISFrsalhk 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 222 ---------------------TSGTTGYPK--MAKH-----NQGLAFRSYIPScrkllkLKTSDILWCMSDPGW-ILA-T 271
Cdd:PRK08974 193 grrmqyvkpelvpedlaflqyTGGTTGVAKgaMLTHrnmlaNLEQAKAAYGPL------LHPGKELVVTALPLYhIFAlT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 272 VGCLIEPWTSGCTVFIHHlPQFDPKVIVEvLFKYPITqclAAPGV---YRMVLQQKT-SNLRFPTLEHCTTGGESLLPEE 347
Cdd:PRK08974 267 VNCLLFIELGGQNLLITN-PRDIPGFVKE-LKKYPFT---AITGVntlFNALLNNEEfQELDFSSLKLSVGGGMAVQQAV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 348 YEQWKQRTGLSIHEVYGQSETG-ISSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfm 426
Cdd:PRK08974 342 AERWVKLTGQYLLEGYGLTECSpLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK-GPQVMLG--- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 427 eYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEV 506
Cdd:PRK08974 418 -YWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18381087 507 VKAFIVLNPEFLShdQEQLIKELQHHVKSvtapYKYPRKVEFVSELPKTVTGKIKRKELRNKE 569
Cdd:PRK08974 497 VKIFVVKKDPSLT--EEELITHCRRHLTG----YKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
340-567 |
2.89e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 149.75 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 340 GESLLP-EEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTE--GYIGIRi 416
Cdd:PRK07787 249 GSAALPvPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVR- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 417 KPTrplgLFMEYENSPESTSEVECGD-FYNSGDRATIDEEGYIWFLGR-GDDVINASGYRIGPVEVENALAEHPAVAESA 494
Cdd:PRK07787 328 GPT----LFDGYLNRPDATAAAFTADgWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAA 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18381087 495 VVSSPDKDRGEVVKAFIVLNPEFlshDQEQLIKelqhHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:PRK07787 404 VVGVPDDDLGQRIVAYVVGADDV---AADELID----FVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
166-568 |
3.66e-39 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 150.68 E-value: 3.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 166 PEVESVASECPDLKTKLVVSDHSHEGWLDfcSLIKS---ASPDHTCIKSKMkdpmaIFFTSGTTGYPKMAKHNqglAFRS 242
Cdd:PRK13382 152 ATVDRALADCPQATRIVAWTDEDHDLTVE--VLIAAhagQRPEPTGRKGRV-----ILLTSGTTGTPKGARRS---GPGG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 243 YIPscrklLKLKTSDILWCMSDPGWILATvgcLIEPW---------TSGCTVFIHHlpQFDPKVIVEVLFKYPITQCLAA 313
Cdd:PRK13382 222 IGT-----LKAILDRTPWRAEEPTVIVAP---MFHAWgfsqlvlaaSLACTIVTRR--RFDPEATLDLIDRHRATGLAVV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 314 PGVYRMVLQQKTSNLR---FPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETG-ISSATLREMKIKRGSIGKAI 389
Cdd:PRK13382 292 PVMFDRIMDLPAEVRNrysGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGmIATATPADLRAAPDTAGRPA 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 390 LPFDLQIIDEKGNILPPNTEGYIGIRIKPtrplgLFMEYenSPESTSEVECGdFYNSGDRATIDEEGYIWFLGRGDDVIN 469
Cdd:PRK13382 372 EGTEIRILDQDFREVPTGEVGTIFVRNDT-----QFDGY--TSGSTKDFHDG-FMASGDVGYLDENGRLFVVGRDDEMIV 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 470 ASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSHDQEqlikELQHHVKSVTAPYKYPRKVEFV 549
Cdd:PRK13382 444 SGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG-ASATPE----TLKQHVRDNLANYKVPRDIVVL 518
|
410
....*....|....*....
gi 18381087 550 SELPKTVTGKIKRKELRNK 568
Cdd:PRK13382 519 DELPRGATGKILRRELQAR 537
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
215-565 |
5.74e-39 |
|
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: 148.55 E-value: 5.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSDILWCMSDPGWILAtVGCLIEPWTSGCTVFIhhLP--- 291
Cdd:cd05945 98 DNAYIIFTSGSTGRPKGVQISHD-NLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLS-VMDLYPALASGATLVP--VPrda 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 292 QFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNL-RFPTLEHCTTGGESLLPEEYEQWKQRT-GLSIHEVYGQSETG 369
Cdd:cd05945 174 TADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPeSLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEAT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 370 ISSATL---REM--KIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEV----EC 440
Cdd:cd05945 254 VAVTYIevtPEVldGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVIS-GPSVSKG----YLNNPEKTAAAffpdEG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 441 GDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPeflsH 520
Cdd:cd05945 329 QRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP----G 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 18381087 521 DQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd05945 405 AEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
104-567 |
6.47e-39 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 150.41 E-value: 6.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 104 LQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECP------- 176
Cdd:PRK08751 73 LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPvkqvitt 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 177 ---DL--------------KTKLVVSDHSHEGWLDFCSLIKSASpDHTCIKSKMK-DPMAIF-FTSGTTGYPKMAKhnqg 237
Cdd:PRK08751 153 glgDMlgfpkaalvnfvvkYVKKLVPEYRINGAIRFREALALGR-KHSMPTLQIEpDDIAFLqYTGGTTGVAKGAM---- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 238 LAFRSYIPScrkllklktsdilwcMSDPGWILATVGCLIEpwtsGCTVFIHHLPQF------------------------ 293
Cdd:PRK08751 228 LTHRNLVAN---------------MQQAHQWLAGTGKLEE----GCEVVITALPLYhifaltanglvfmkiggcnhlisn 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 294 --DPKVIVEVLFKYPITQCLAAPGVYRMVLQQKT-SNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETG- 369
Cdd:PRK08751 289 prDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGfDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSp 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 370 ---ISSATLREMKikrGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVECGD-FYN 445
Cdd:PRK08751 369 aacINPLTLKEYN---GSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK-GPQVMKG----YWKRPEETAKVMDADgWLH 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 446 SGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVlnpeflSHDQEQL 525
Cdd:PRK08751 441 TGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------KKDPALT 514
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 18381087 526 IKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:PRK08751 515 AEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
77-565 |
9.45e-39 |
|
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: 148.63 E-value: 9.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 77 GDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAK 156
Cdd:cd05920 36 DGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AIVttaslVPEVES----------VASECPDLktklvvsdhshegwldfcsliksaspdhtcikskmkdpmAIFFTS-GT 225
Cdd:cd05920 115 AYI-----VPDRHAgfdhralareLAESIPEV---------------------------------------ALFLLSgGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 226 TGYPKMA--KHNQ-GLAFRSYIPSCRkllkLKTSDILWC---------MSDPGwILATVgcliepWTSGCTVFIhhlPQF 293
Cdd:cd05920 151 TGTPKLIprTHNDyAYNVRASAEVCG----LDQDTVYLAvlpaahnfpLACPG-VLGTL------LAGGRVVLA---PDP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 294 DPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLRFP-TLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISS 372
Cdd:cd05920 217 SPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLsSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 373 ATLRE-MKIKRGSIGKAILPFD-LQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVECGD-FYNSGDR 449
Cdd:cd05920 297 TRLDDpDEVIIHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTR-GPYTIRG----YYRAPEHNARAFTPDgFYRTGDL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 450 ATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLSHDQ-EQLIKE 528
Cdd:cd05920 372 VRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQlRRFLRE 451
|
490 500 510
....*....|....*....|....*....|....*..
gi 18381087 529 LQhhvksvTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd05920 452 RG------LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
79-566 |
9.48e-39 |
|
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: 149.21 E-value: 9.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 79 EIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAI 158
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALKKY-GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 159 VTTASLVPEVESVASECPDLKTKLVV-SDHSHEGWLDFCSLIKSASPDHTCIKS-------KMKDPMAIFFTSGTTGYPK 230
Cdd:cd17642 121 FCSKKGLQKVLNVQKKLKIIKTIIILdSKEDYKGYQCLYTFITQNLPPGFNEYDfkppsfdRDEQVALIMNSSGSTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 231 --MAKHNQGLAFRSyipSCRKllklktsDILWCMSDPGWILATV-------GCLIEPWTSGCTVFIHHLPQFDPKVIVEV 301
Cdd:cd17642 201 gvQLTHKNIVARFS---HARD-------PIFGNQIIPDTAILTVipfhhgfGMFTTLGYLICGFRVVLMYKFEEELFLRS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 302 LFKYPITQCLAAPGVyrMVLQQKTSNLR---FPTLEHCTTGGESLLPEEYEQWKQRTGLS-IHEVYGQSETGISSATLRE 377
Cdd:cd17642 271 LQDYKVQSALLVPTL--FAFFAKSTLVDkydLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 378 MKIKRGSIGKAILPFDLQIID-EKGNILPPNTEGYIGIRIKptrplGLFMEYENSPESTSEVECGD-FYNSGDRATIDEE 455
Cdd:cd17642 349 GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGP-----MIMKGYVNNPEATKALIDKDgWLHSGDIAYYDED 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 456 GYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVlnpefLSHDQEQLIKELQHHVKS 535
Cdd:cd17642 424 GHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV-----LEAGKTMTEKEVMDYVAS 498
|
490 500 510
....*....|....*....|....*....|..
gi 18381087 536 VTAPYKYPR-KVEFVSELPKTVTGKIKRKELR 566
Cdd:cd17642 499 QVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
50-568 |
1.38e-37 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 146.78 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 50 DVLDYWAQmeeegKRGPSPAFWWVNGqGDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMR 129
Cdd:COG1022 15 DLLRRRAA-----RFPDRVALREKED-GIWQSLTWAEFAERVRALAAGLLAL-GVKPGDRVAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 130 TGIIFMP-GTTQLkAKDILYRIQISRAKAIVT-TASLVPEVESVASECPDLKtKLVVSD--------------------- 186
Cdd:COG1022 88 AGAVTVPiYPTSS-AEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLR-HIVVLDprglrddprllsldellalgr 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 187 -HSHEGWLDfcSLIKSASPDhtcikskmkDPMAIFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSDI------L 259
Cdd:COG1022 166 eVADPAELE--ARRAAVKPD---------DLATIIYTSGTTGRPKGVMLTHR-NLLSNARALLERLPLGPGDRtlsflpL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 260 WcmsdpgWILA---TVGCLIepwtSGCTV--------FIHHLPQFDPKVIVEV------------------------LFK 304
Cdd:COG1022 234 A------HVFErtvSYYALA----AGATVafaespdtLAEDLREVKPTFMLAVprvwekvyagiqakaeeagglkrkLFR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 305 YPITQCLAA----------PGVYRMV-----------LQQKT-SNLRFptlehCTTGGESLlPEEYEQWKQRTGLSIHEV 362
Cdd:COG1022 304 WALAVGRRYararlagkspSLLLRLKhaladklvfskLREALgGRLRF-----AVSGGAAL-GPELARFFRALGIPVLEG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 363 YGQSET-GISSATlREMKIKRGSIGKAILPFDLQIiDEKGNILppntegyigirikpTRPLGLFMEYENSPESTSEVECG 441
Cdd:COG1022 378 YGLTETsPVITVN-RPGDNRIGTVGPPLPGVEVKI-AEDGEIL--------------VRGPNVMKGYYKNPEATAEAFDA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 442 D-FYNSGDRATIDEEGYIWFLGRGDDVI-NASGYRIGPVEVENALAEHPAVAESAVVsspdkdrGE----VVkAFIVLNP 515
Cdd:COG1022 442 DgWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALIVPDF 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 516 EFLSH----------------DQEQLIKELQHHVKSVT---APYKYPRKVEFvseLPK---------TVTGKIKRKELRN 567
Cdd:COG1022 514 EALGEwaeenglpytsyaelaQDPEVRALIQEEVDRANaglSRAEQIKRFRL---LPKeftiengelTPTLKLKRKVILE 590
|
.
gi 18381087 568 K 568
Cdd:COG1022 591 K 591
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
83-495 |
1.53e-37 |
|
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: 143.56 E-value: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPgttqLkakDILY---RIQI----SRA 155
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP----L---DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 156 KAIVTTASLVPEVESVASEcpdlktklvvsdHSHEGWLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPK--MAK 233
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLP------------VILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKgvVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 234 HnQGLAfrSYIPSCRKLLKLKTSDILWCMSDPGW------ILAtvgcliePWTSGCTVFI--HHLPQFDPKVIVEVLFKY 305
Cdd:TIGR01733 142 H-RSLV--NLLAWLARRYGLDPDDRVLQFASLSFdasveeIFG-------ALLAGATLVVppEDEERDDAALLAALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 306 PITQCLAAPGVYRMVLQQKTSNLrfPTLEHCTTGGESLLPEEYEQWKQRTG-LSIHEVYGQSETGISSATLR-----EMK 379
Cdd:TIGR01733 212 PVTVLNLTPSLLALLAAALPPAL--ASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLvdpddAPR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 380 IKRGSIGKAILPFDLQIIDEKGNILPPNTEG--YIGIRikptrplGLFMEYENSPESTSEV---------ECGDFYNSGD 448
Cdd:TIGR01733 290 ESPVPIGRPLANTRLYVLDDDLRPVPVGVVGelYIGGP-------GVARGYLNRPELTAERfvpdpfaggDGARLYRTGD 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 18381087 449 RATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAV 495
Cdd:TIGR01733 363 LVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
93-566 |
1.66e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 145.61 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 93 RTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASL-------V 165
Cdd:PRK12406 23 RAAGGLAAL-GVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLlhglasaL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 166 PE---VESVASEcPDLKTKLVVSDHSH---EGWLDFCSLIKSASPDHTCIKSKmkdPMAIFFTSGTTGYPK--------- 230
Cdd:PRK12406 102 PAgvtVLSVPTP-PEIAAAYRISPALLtppAGAIDWEGWLAQQEPYDGPPVPQ---PQSMIYTSGTTGHPKgvrraaptp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 231 --------MAKHNQGLafrsyIPSCRKLlklktsdilwcMSDPGWILATVGCLIEPWTSGCTVFIhhLPQFDPKVIVEVL 302
Cdd:PRK12406 178 eqaaaaeqMRALIYGL-----KPGIRAL-----------LTGPLYHSAPNAYGLRAGRLGGVLVL--QPRFDPEELLQLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 303 FKYPITQCLAAPGVYRMVLQ--------QKTSNLRFptlehcTTGGESLLPEEYEQ-----WkqrtGLSIHEVYGQSETG 369
Cdd:PRK12406 240 ERHRITHMHMVPTMFIRLLKlpeevrakYDVSSLRH------VIHAAAPCPADVKRamiewW----GPVIYEYYGSTESG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 370 -ISSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRIkPTRPLglfMEYENSPESTSEVECGDFYNSGD 448
Cdd:PRK12406 310 aVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI-AGNPD---FTYHNKPEKRAEIDRGGFITSGD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 449 RATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSHDQEQLIKE 528
Cdd:PRK12406 386 VGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG-ATLDEADIRAQ 464
|
490 500 510
....*....|....*....|....*....|....*...
gi 18381087 529 LQHHVksvtAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK12406 465 LKARL----AGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
103-568 |
1.82e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 145.03 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 103 GLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVttaslvpeVESVASECPDLKTKL 182
Cdd:PRK06145 48 GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL--------VDEEFDAIVALETPK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 183 VVSDHSHEGwlDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQG-LAFRSYIPSCRklLKLKTSDILWC 261
Cdd:PRK06145 120 IVIDAAAQA--DSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGnLHWKSIDHVIA--LGLTASERLLV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 262 MSDpgwiLATVGCLIEP-----WTSGcTVFIHHlpQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNlRF--PTLE 334
Cdd:PRK06145 196 VGP----LYHVGAFDLPgiavlWVGG-TLRIHR--EFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRD-RFdlDSLA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 335 HCTTGGESLlPEEYEQWKQR--TGLSIHEVYGQSETgISSATL----REMKiKRGSIGKAILPFDLQIIDEKGNILPPNT 408
Cdd:PRK06145 268 WCIGGGEKT-PESRIRDFTRvfTRARYIDAYGLTET-CSGDTLmeagREIE-KIGSTGRALAHVEIRIADGAGRWLPPNM 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 409 EGYIGIR-IKPTRplglfmEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEH 487
Cdd:PRK06145 345 KGEICMRgPKVTK------GYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 488 PAVAESAVVSSPDKDRGEVVKAFIVLNPeflshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:PRK06145 419 PEVAEAAVIGVHDDRWGERITAVVVLNP-----GATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
.
gi 18381087 568 K 568
Cdd:PRK06145 494 E 494
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
78-566 |
6.39e-37 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 144.13 E-value: 6.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 78 DEIKWSFRKLRDLTCRTANVFeQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKA 157
Cdd:PRK06155 43 GGTRWTYAEAARAAAAAAHAL-AAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 158 IVTTASLVPEVESVASECPDLKTKLVVSDHSHEGW---LDFCSLIKSASPdHTCIKSKMKDPMAIFFTSGTTGYPKMAKH 234
Cdd:PRK06155 122 LVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpagWSTAPLPPLDAP-APAAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 235 NQGLAFRSYIPSCRkLLKLKTSDILwCMSDPGWILATVGCLIEPWTSGCTVFIhhLPQFDPKVIVEVLFKYPITQCLAAP 314
Cdd:PRK06155 201 PHAQFYWWGRNSAE-DLEIGADDVL-YTTLPLFHTNALNAFFQALLAGATYVL--EPRFSASGFWPAVRRHGATVTYLLG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 315 GVYRMVLQQ-KTSNLRFPTLEHCTTGGESllPEEYEQWKQRTGLSIHEVYGQSETG-ISSATLREMKikRGSIGKAILPF 392
Cdd:PRK06155 277 AMVSILLSQpARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNfVIAVTHGSQR--PGSMGRLAPGF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 393 DLQIIDEKGNILPPNTEGYIGIRIKPtrPLGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASG 472
Cdd:PRK06155 353 EARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 473 YRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSHDQEQLIKelqhHVKSVTAPYKYPRKVEFVSEL 552
Cdd:PRK06155 431 ENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG-TALEPVALVR----HCEPRLAYFAVPRYVEFVAAL 505
|
490
....*....|....
gi 18381087 553 PKTVTGKIKRKELR 566
Cdd:PRK06155 506 PKTENGKVQKFVLR 519
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
349-566 |
8.31e-37 |
|
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: 142.90 E-value: 8.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 349 EQWKQRTGLSIHEVYGQSE----TGISSAtlrEMKIKRGSIGKAILPfDLQIIDEKGNILPPNTEGYIGIRIKPTrplgl 424
Cdd:cd05929 262 EQWIDWGGPIIWEYYGGTEgqglTIINGE---EWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG----- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 425 fMEYENSPESTSE-VECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDR 503
Cdd:cd05929 333 -FEYTNDPEKTAAaRNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEEL 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18381087 504 GEVVKAfiVLNPEFLSHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd05929 412 GQRVHA--VVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
83-567 |
1.21e-36 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 143.81 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIV--- 159
Cdd:PRK12492 51 SYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVyln 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 160 TTASLVPEVesvaseCPDLKTKLVVSDH------SHEGWL--DFCSLIKSASPD--------------------HTCIKS 211
Cdd:PRK12492 131 MFGKLVQEV------LPDTGIEYLIEAKmgdllpAAKGWLvnTVVDKVKKMVPAyhlpqavpfkqalrqgrglsLKPVPV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 212 KMKDPMAIFFTSGTTGYPK--MAKHNQGLA--------FRSYIPSCRKLLKlKTSDILWCMSDPGWILA-TVGCLIEPWT 280
Cdd:PRK12492 205 GLDDIAVLQYTGGTTGLAKgaMLTHGNLVAnmlqvracLSQLGPDGQPLMK-EGQEVMIAPLPLYHIYAfTANCMCMMVS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 281 SGCTVFIHHlPQFDPKVIVEvLFKYPITQCLAAPGVYRMVLQQKT-SNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSI 359
Cdd:PRK12492 284 GNHNVLITN-PRDIPGFIKE-LGKWRFSALLGLNTLFVALMDHPGfKDLDFSALKLTNSGGTALVKATAERWEQLTGCTI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 360 HEVYGQSETG-ISSATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEV 438
Cdd:PRK12492 362 VEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIK-GPQVMKG----YWQQPEATAEA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 439 -ECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEF 517
Cdd:PRK12492 437 lDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPG 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 18381087 518 LShdqeqlIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:PRK12492 517 LS------VEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
54-566 |
1.15e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 140.91 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 54 YWAQMEEEGKRgpsPAFWWVNGQGdeikwSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGII 133
Cdd:PRK05605 38 YDNAVARFGDR---PALDFFGATT-----TYAELGKQVRRAAAGLRAL-GVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 134 FMPGTTQLKAKDILYRIQISRAK-AIV--TTASLVPE------VESVAS-----------------ECPDLKTKLVVSDH 187
Cdd:PRK05605 109 VVEHNPLYTAHELEHPFEDHGARvAIVwdKVAPTVERlrrttpLETIVSvnmiaampllqrlalrlPIPALRKARAALTG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 188 SHEGWLDFCSLIKSASPDHTCIKS----KMKDPMAIFFTSGTTGYPK---------MAKHNQGLAfrsYIPSCRKllklk 254
Cdd:PRK05605 189 PAPGTVPWETLVDAAIGGDGSDVShprpTPDDVALILYTSGTTGKPKgaqlthrnlFANAAQGKA---WVPGLGD----- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 255 tsdilwcmsDPGWILA----------TVGCLIEPWTSGCTVFihhLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQ- 323
Cdd:PRK05605 261 ---------GPERVLAalpmfhayglTLCLTLAVSIGGELVL---LPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAa 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 324 KTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETG-ISSATlrEMKIKR--GSIGkaiLPF---DLQII 397
Cdd:PRK05605 329 EERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGN--PMSDDRrpGYVG---VPFpdtEVRIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 398 DEK--GNILPPNTEGYIGIRiKPTRplglFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRI 475
Cdd:PRK05605 404 DPEdpDETMPDGEEGELLVR-GPQV----FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 476 GPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSHDQEQLikeLQHHVKSVTApYKYPRKVEFVSELPKT 555
Cdd:PRK05605 479 YPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEGL---RAYCREHLTR-YKVPRRFYHVDELPRD 553
|
570
....*....|.
gi 18381087 556 VTGKIKRKELR 566
Cdd:PRK05605 554 QLGKVRRREVR 564
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
215-566 |
1.22e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 137.23 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPKMAKHNQ-GLAFRSYIPScrKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCT-VFIHHLPQ 292
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHsNEVYNAWMLA--LNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHvVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 293 FDPKVIVE---VLFKYPITQCLAAPGVYRMVLQ----QKTSNLRFptlehcTTGGESLLPEE-YEQWKQRTGLSIHEVYG 364
Cdd:cd05944 81 RNPGLFDNfwkLVERYRITSLSTVPTVYAALLQvpvnADISSLRF------AMSGAAPLPVElRARFEDATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 365 QSE-TGISSATLREMKIKRGSIGKAiLPFDLQ---IIDEKGNILPPNTEGYIGIRIKPTRplGLFMEYENSPESTSEVEC 440
Cdd:cd05944 155 LTEaTCLVAVNPPDGPKRPGSVGLR-LPYARVrikVLDGVGRLLRDCAPDEVGEICVAGP--GVFGGYLYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 441 GDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSH 520
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG-AVV 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 18381087 521 DQEQLIKELQHHVKSVTApykYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd05944 311 EEEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
103-568 |
1.77e-35 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 141.71 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 103 GLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVE-SVASECPDLktk 181
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQpSRVAEAAEL--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 182 lvVSDHSHEGWLDFCSLIKSASPDHTcikskmkdpmaifFTSGTTGYPKMAKHNQGLAFRSYIPSCRKLLKLKTSDILWC 261
Cdd:PRK06060 128 --MSEAARVAPGGYEPMGGDALAYAT-------------YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLC 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 262 MSDPGWILATVGCLIEPWTSGCTVFIHHLP-----------QFDPKVIVEVlfkypitqclaaPGVYRMVLQQKTSNlRF 330
Cdd:PRK06060 193 SARMYFAYGLGNSVWFPLATGGSAVINSAPvtpeaaailsaRFGPSVLYGV------------PNFFARVIDSCSPD-SF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 331 PTLEHCTTGGESLLPEEYEQWKQR-TGLSIHEVYGQSETGIS--SATLREMKIkrGSIGKAILPFDLQIIDEKGNILPPN 407
Cdd:PRK06060 260 RSLRCVVSAGEALELGLAERLMEFfGGIPILDGIGSTEVGQTfvSNRVDEWRL--GTLGRVLPPYEIRVVAPDGTTAGPG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 408 TEGYIGIRiKPTrplgLFMEYENSPESTseVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEH 487
Cdd:PRK06060 338 VEGDLWVR-GPA----IAKGYWNRPDSP--VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIED 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 488 PAVAESAVVSSPDKDRGEVVKAFIVlnPEFLSHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:PRK06060 411 EAVAEAAVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRK 488
|
.
gi 18381087 568 K 568
Cdd:PRK06060 489 Q 489
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
76-559 |
2.46e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 139.64 E-value: 2.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 76 QGDEiKWSFRKLRDLTCRTANVF-EQicGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISR 154
Cdd:PRK07798 24 CGDR-RLTYAELEERANRLAHYLiAQ--GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 155 AKAIVTTASLVPEVESVASECPDLKTKLVVSDHSHE----GWLDFCSLIKSASPDHTCIKSKMKDpMAIFFTSGTTGYPK 230
Cdd:PRK07798 101 AVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNdllpGAVDYEDALAAGSPERDFGERSPDD-LYLLYTGGTTGMPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 231 --MAKHNQ-------GLAFRS--YIPSCRKLLKLKTSD--ILWCMSDP----GWILATVGCLiepwTSGCTVFIHHLPQF 293
Cdd:PRK07798 180 gvMWRQEDifrvllgGRDFATgePIEDEEELAKRAAAGpgMRRFPAPPlmhgAGQWAAFAAL----FSGQTVVLLPDVRF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 294 DP----------KVIVEVL----FKYPITQCLAAPGVYRmvlqqkTSNLRfpTLehcTTGGESLLPEEYEQW-KQRTGLS 358
Cdd:PRK07798 256 DAdevwrtiereKVNVITIvgdaMARPLLDALEARGPYD------LSSLF--AI---ASGGALFSPSVKEALlELLPNVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 359 IHEVYGQSETG-ISSATlremkIKRGSIGKAILPFDLQ----IIDEKGNILPPNtEGYIG-IRIKPTRPLGlfmeYENSP 432
Cdd:PRK07798 325 LTDSIGSSETGfGGSGT-----VAKGAVHTGGPRFTIGprtvVLDEDGNPVEPG-SGEIGwIARRGHIPLG----YYKDP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 433 ESTS----EVEcGDFYN-SGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVV 507
Cdd:PRK07798 395 EKTAetfpTID-GVRYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEV 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 18381087 508 KAFIVLNPEfLSHDQEqlikELQHHVKSVTAPYKYPRKVEFVSELPKTVTGK 559
Cdd:PRK07798 474 VAVVQLREG-ARPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
83-565 |
1.16e-34 |
|
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: 137.02 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVF-EQicGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTT 161
Cdd:cd17646 25 TYRELDERANRLAHLLrAR--GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 162 ASLVPEveSVASECPDLKTKLVVSDHSHEGwldfcsLIKSASPDHtcikskmkdPMAIFFTSGTTGYPK--MAKHnQGLA 239
Cdd:cd17646 103 ADLAAR--LPAGGDVALLGDEALAAPPATP------PLVPPRPDN---------LAYVIYTSGSTGRPKgvMVTH-AGIV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 240 FR--------SYIPSCRKLLKLKTS-DI-LWCMSdpgWILATVGCLIEPWTSGCTvfihhlpqfDPKVIVEVLFKYPITQ 309
Cdd:cd17646 165 NRllwmqdeyPLGPGDRVLQKTPLSfDVsVWELF---WPLVAGARLVVARPGGHR---------DPAYLAALIREHGVTT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 310 CLAAPGVYRMVLQQKTSNlRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGI--SSATLREMKIKRG-SIG 386
Cdd:cd17646 233 CHFVPSMLRVFLAEPAAG-SCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIdvTHWPVRGPAETPSvPIG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 387 KAILPFDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEYENSPESTSEVECGD-------FYNSGDRATIDEEGY 457
Cdd:cd17646 312 RPVPNTRLYVLDDALRPVPVGVPGelYLG-------GVQLARGYLGRPALTAERFVPDpfgpgsrMYRTGDLARWRPDGA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 458 IWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLSHDQEqlikELQHHVKSVT 537
Cdd:cd17646 385 LEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTA----ALRAHLAERL 460
|
490 500
....*....|....*....|....*...
gi 18381087 538 APYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd17646 461 PEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
103-566 |
1.17e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 137.48 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 103 GLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPDLKtkL 182
Cdd:PRK07470 53 GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLT--H 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 183 VVSDHSHEGWLDFCSLI--------KSASPDHtcikskmKDPMAIFFTSGTTGYPKMA--KHNQgLAFrsyipscrkLLK 252
Cdd:PRK07470 131 VVAIGGARAGLDYEALVarhlgarvANAAVDH-------DDPCWFFFTSGTTGRPKAAvlTHGQ-MAF---------VIT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 253 LKTSDILwcmsdPGWILATVGCLIEPWTSGCTvfIHHLPQ--------------FDPKVIVEVLFKYPITQCLAAPGVYR 318
Cdd:PRK07470 194 NHLADLM-----PGTTEQDASLVVAPLSHGAG--IHQLCQvargaatvllpserFDPAEVWALVERHRVTNLFTVPTILK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 319 M------VLQQKTSNLRfptleHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSE-TG---ISSATLREMK----IKRGS 384
Cdd:PRK07470 267 MlvehpaVDRYDHSSLR-----YVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEvTGnitVLPPALHDAEdgpdARIGT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 385 IGKAILPFDLQIIDEKGNILPPNTEGYIGIRikptrPLGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRG 464
Cdd:PRK07470 342 CGFERTGMEVQIQDDEGRELPPGETGEICVI-----GPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 465 DDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNpEFLSHDQEQLIKELQHHVksvtAPYKYPR 544
Cdd:PRK07470 417 SDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVAR-DGAPVDEAELLAWLDGKV----ARYKLPK 491
|
490 500
....*....|....*....|..
gi 18381087 545 KVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK07470 492 RFFFWDALPKSGYGKITKKMVR 513
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
80-566 |
1.32e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 136.86 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 80 IKWSFRKLRDLTCRTANVFEQIcGLQQGDHLAlILPRVPEWWLVT-VGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAI 158
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRR-GCVDGERLA-VLARNSVWLVALhFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 159 V---TTASLVPEVESVAsecpdlktklvvsdhshegwlDFCSLIKSASPDHTciKSKMKD-PMAIFFTSGTTGYPKMAKH 234
Cdd:PRK09088 99 LgddAVAAGRTDVEDLA---------------------AFIASADALEPADT--PSIPPErVSLILFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 235 NQGLAFRSYIPSCRkLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHhlPQFDPKVIVEVL--FKYPITQCLA 312
Cdd:PRK09088 156 SERNLQQTAHNFGV-LGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVS--NGFEPKRTLGRLgdPALGITHYFC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 313 APGVYRMVLQQKT---SNLRfpTLEHCTTGGESLLPEEYEQWKQRtGLSIHEVYGQSETGI---SSATLREMKIKRGSIG 386
Cdd:PRK09088 233 VPQMAQAFRAQPGfdaAALR--HLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTvfgMSVDCDVIRAKAGAAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 387 KAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTrplgLFMEYENSPESTSEVECGD-FYNSGDRATIDEEGYIWFLGRGD 465
Cdd:PRK09088 310 IPTPTVQTRVVDDQGNDCPAGVPGELLLR-GPN----LSPGYWRRPQATARAFTGDgWFRTGDIARRDADGFFWVVDRKK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 466 DVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEflshdQEQLIKELQHHVKSVTAPYKYPRK 545
Cdd:PRK09088 385 DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-----APLDLERIRSHLSTRLAKYKVPKH 459
|
490 500
....*....|....*....|.
gi 18381087 546 VEFVSELPKTVTGKIKRKELR 566
Cdd:PRK09088 460 LRLVDALPRTASGKLQKARLR 480
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
214-562 |
2.38e-34 |
|
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: 133.15 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 214 KDPMAIFFTSGTTGYPKMAKHNQGLAFRSYIPSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHHLPQF 293
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 294 dpKVIVEVLFKYPIT-QCLAAPGVYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGisS 372
Cdd:cd17635 81 --KSLFKILTTNAVTtTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETG--T 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 373 ATLREM---KIKRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVECGDFYNSGDR 449
Cdd:cd17635 157 ALCLPTdddSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIK-SPANMLG----YWNNPERTAEVLIDGWVNTGDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 450 ATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEflshDQEQLIKEL 529
Cdd:cd17635 232 GERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE----LDENAIRAL 307
|
330 340 350
....*....|....*....|....*....|...
gi 18381087 530 QHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKR 562
Cdd:cd17635 308 KHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
219-562 |
3.71e-34 |
|
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: 132.24 E-value: 3.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 219 IFFTSGTTGYPK--MAKHNQGLAFRSYIPSCRKLlklkTSDILWCMSDP-----GWILATVGCLIepwtSGCTVFIHHLp 291
Cdd:cd17638 5 IMFTSGTTGRSKgvMCAHRQTLRAAAAWADCADL----TEDDRYLIINPffhtfGYKAGIVACLL----TGATVVPVAV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 292 qFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQ-KTSNLRFPTLEHCTTGGESLLPEEYEqwKQRTGLSIHEV---YGQSE 367
Cdd:cd17638 76 -FDVDAILEAIERERITVLPGPPTLFQSLLDHpGRKKFDLSSLRAAVTGAATVPVELVR--RMRSELGFETVltaYGLTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 368 TGIssATLRE----MKIKRGSIGKAILPFDLQIIDEkGNILppntegyigirikpTRPLGLFMEYENSPESTSE-VECGD 442
Cdd:cd17638 153 AGV--ATMCRpgddAETVATTCGRACPGFEVRIADD-GEVL--------------VRGYNVMQGYLDDPEATAEaIDADG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 443 FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSHDQ 522
Cdd:cd17638 216 WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG-VTLTE 294
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 18381087 523 EQLIKELQHHVksvtAPYKYPRKVEFVSELPKTVTGKIKR 562
Cdd:cd17638 295 EDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
89-568 |
1.12e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 134.72 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 89 DLTCRTANVFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEV 168
Cdd:PLN02246 57 ELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 169 ESVASEcPDLKtkLVVSDHSHEGWLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPK--MAKHnqglafRSYIPS 246
Cdd:PLN02246 137 KGLAED-DGVT--VVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKgvMLTH------KGLVTS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 247 CRKL-------LKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIhhLPQFDPKVIVEVLFKYPITqclAAPGVYRM 319
Cdd:PLN02246 208 VAQQvdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI--MPKFEIGALLELIQRHKVT---IAPFVPPI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 320 VL---------QQKTSNLRFptlehcTTGGESLLPEEYEQwKQRTGLS---IHEVYGQSETG----ISSATLRE-MKIKR 382
Cdd:PLN02246 283 VLaiakspvveKYDLSSIRM------VLSGAAPLGKELED-AFRAKLPnavLGQGYGMTEAGpvlaMCLAFAKEpFPVKS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 383 GSIGKAILPFDLQIID-EKGNILPPNTEGYIGIRikptrplG--LFMEYENSPESTSE-VECGDFYNSGDRATIDEEGYI 458
Cdd:PLN02246 356 GSCGTVVRNAELKIVDpETGASLPRNQPGEICIR-------GpqIMKGYLNDPEATANtIDKDGWLHTGDIGYIDDDDEL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 459 WFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEF-LSHDQeqlIKelQHHVKSVT 537
Cdd:PLN02246 429 FIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSeITEDE---IK--QFVAKQVV 503
|
490 500 510
....*....|....*....|....*....|.
gi 18381087 538 ApYKYPRKVEFVSELPKTVTGKIKRKELRNK 568
Cdd:PLN02246 504 F-YKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
87-568 |
3.67e-33 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 133.57 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 87 LRDlTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVP 166
Cdd:PLN02330 62 VRD-TRRFAKALRSL-GLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 167 EVESVasECPdlktKLVVSDHSHEGWLDFCSLIKSA-----SPDHTCIKSKmkDPMAIFFTSGTTGYPK--MAKHnqgla 239
Cdd:PLN02330 140 KVKGL--GLP----VIVLGEEKIEGAVNWKELLEAAdragdTSDNEEILQT--DLCALPFSSGTTGISKgvMLTH----- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 240 fRSYIPS-CRKLLKLKTSDIlwcmsdpGWIlATVGCL----IEPWTSGCTVFIHH------LPQFDPKVIVEVLFKYPIT 308
Cdd:PLN02330 207 -RNLVANlCSSLFSVGPEMI-------GQV-VTLGLIpffhIYGITGICCATLRNkgkvvvMSRFELRTFLNALITQEVS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 309 QCLAAPGVYRMVLQQ---KTSNLRFPTLEHCTTGGESLLPEEYEQWKQR-TGLSIHEVYGQSETGISSATLREMK----- 379
Cdd:PLN02330 278 FAPIVPPIILNLVKNpivEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITLTHGDPEkghgi 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 380 IKRGSIGkAILP-FDLQIID-EKGNILPPNTEGYIGIRIKPTRpLGLFMeyeNSPESTSEVECGDFYNSGDRATIDEEGY 457
Cdd:PLN02330 358 AKKNSVG-FILPnLEVKFIDpDTGRSLPKNTPGELCVRSQCVM-QGYYN---NKEETDRTIDEDGWLHTGDIGYIDDDGD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 458 IWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEflSHDQEQLIKElqhHVKSVT 537
Cdd:PLN02330 433 IFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPK--AKESEEDILN---FVAANV 507
|
490 500 510
....*....|....*....|....*....|.
gi 18381087 538 APYKYPRKVEFVSELPKTVTGKIKRKELRNK 568
Cdd:PLN02330 508 AHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
79-568 |
9.33e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 131.99 E-value: 9.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 79 EIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAI 158
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 159 VTTASLVPEVESVASECPDLKTKLV-VSDHSHE-----GWLDFCSLIKSASPDHTCIKSKMK-DPMAIFFTSGTTGYPK- 230
Cdd:PRK08162 120 IVDTEFAEVAREALALLPGPKPLVIdVDDPEYPggrfiGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKg 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 231 MAKHNQGlafrSYIPSCRKLLKL---KTSDILWCMsdP-----GWilatvgCLiePWT----SGCTVFihhLPQFDPKVI 298
Cdd:PRK08162 200 VVYHHRG----AYLNALSNILAWgmpKHPVYLWTL--PmfhcnGW------CF--PWTvaarAGTNVC---LRKVDPKLI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 299 VEVLFKYPITQCLAAPGVYRMVL---QQKTSNLRFPTleHCTTGGESLLPEEYEQWKQRtGLSIHEVYGQSET------- 368
Cdd:PRK08162 263 FDLIREHGVTHYCGAPIVLSALInapAEWRAGIDHPV--HAMVAGAAPPAAVIAKMEEI-GFDLTHVYGLTETygpatvc 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 369 -------GISSATLREMKIKRGsigkaiLPFDLQiidEKGNILPPNT----------EGYIGIRikptrplG-LFME-YE 429
Cdd:PRK08162 340 awqpewdALPLDERAQLKARQG------VRYPLQ---EGVTVLDPDTmqpvpadgetIGEIMFR-------GnIVMKgYL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 430 NSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKA 509
Cdd:PRK08162 404 KNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCA 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 18381087 510 FIVLNPEfLSHDQEQLIKelqhHVKSVTAPYKYPRKVEFvSELPKTVTGKIKRKELRNK 568
Cdd:PRK08162 484 FVELKDG-ASATEEEIIA----HCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
53-566 |
1.68e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 131.40 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 53 DYWAQMEEEGKRGPSPAFWwvngQGDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGI 132
Cdd:PRK06164 11 TLASLLDAHARARPDAVAL----IDEDRPLSRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 133 IFMPGTTQLKAKDILYRIQISRAKAIVTTAS-----LVPEVESVA-SECPDLKTKLVVSDHSHE-------GWLDFCSLI 199
Cdd:PRK06164 86 TVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidFAAILAAVPpDALPPLRAIAVVDDAADAtpapapgARVQLFALP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 200 KSASPDHTCIKSKMKDPMAIFFT-SGTTGYPKMAKHNQGLAFRsYIPSCRKLLKLKTSDILWCMSdP-----GW--ILAT 271
Cdd:PRK06164 166 DPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLR-HARAIARAYGYDPGAVLLAAL-PfcgvfGFstLLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 272 VgcliepwTSGCTVfiHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLRFPTLEHCttGGESLLP--EEYE 349
Cdd:PRK06164 244 L-------AGGAPL--VCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF--GFASFAPalGELA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 350 QWKQRTGLSIHEVYGQSET----GISSATLREmKIKRGSIGKAILP-FDLQIID-EKGNILPPNTEGYIGIRiKPtrplG 423
Cdd:PRK06164 313 ALARARGVPLTGLYGSSEVqalvALQPATDPV-SVRIEGGGRPASPeARVRARDpQDGALLPDGESGEIEIR-AP----S 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 424 LFMEYENSPESTSEVECGD-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKD 502
Cdd:PRK06164 387 LMRGYLDNPDATARALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDG 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18381087 503 RGEVVkAFIVLNPEfLSHDQEQLIKelqhHVKSVTAPYKYPRKVEFVSELPKTVTG---KIKRKELR 566
Cdd:PRK06164 467 KTVPV-AFVIPTDG-ASPDEAGLMA----ACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
77-566 |
4.98e-32 |
|
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: 129.39 E-value: 4.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 77 GDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAK 156
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AIVTTASLVPEVESVAsecpdlktklvvsdhsHEGWLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPK--MAKH 234
Cdd:cd17651 95 LVLTHPALAGELAVEL----------------VAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKgvVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 235 ----NQGLAFRSYIPSCRKLLKLKTSDILWCMSdpGW-ILATVGcliepwTSGCTVFIHHLPQFDPKVIVEVLFKYPITQ 309
Cdd:cd17651 159 rslaNLVAWQARASSLGPGARTLQFAGLGFDVS--VQeIFSTLC------AGATLVLPPEEVRTDPPALAAWLDEQRISR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 310 CLAAPGVYRMVLQQKTSNLRFP-TLEHCTTGGESL-LPEEYEQW-KQRTGLSIHEVYGQSETGISSA-TLREMKIKRG-- 383
Cdd:cd17651 231 VFLPTVALRALAEHGRPLGVRLaALRYLLTGGEQLvLTEDLREFcAGLPGLRLHNHYGPTETHVVTAlSLPGDPAAWPap 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 384 -SIGKAILPFDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEYENSPESTSE-------VECGDFYNSGDRATID 453
Cdd:cd17651 311 pPIGRPIDNTRVYVLDAALRPVPPGVPGelYIG-------GAGLARGYLNRPELTAErfvpdpfVPGARMYRTGDLARWL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 454 EEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEflshdQEQLIKELQHHV 533
Cdd:cd17651 384 PDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE-----APVDAAELRAAL 458
|
490 500 510
....*....|....*....|....*....|...
gi 18381087 534 KSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd17651 459 ATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
208-566 |
7.33e-32 |
|
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: 128.99 E-value: 7.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 208 CIKSKMKDPMAIFFTSGTTGYPK--MAKHNQGLAFRSyipSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTV 285
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKgvVLSHKNLLANVE---QITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 286 FIHHLPqFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNlRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQ 365
Cdd:cd05909 218 VFHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARAAHPE-DFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 366 SETG-ISSATLREMKIKRGSIGKAILPFDLQIIDEKGNI-LPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVECGDF 443
Cdd:cd05909 296 TECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVR-GPNVMLG----YLNEPELTSFAFGDGW 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 444 YNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEH-PAVAESAVVSSPDKDRGEVVKAFIVLnpeflsHDQ 522
Cdd:cd05909 371 YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTT------TDT 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 18381087 523 EQLikELQHHVKSVTAPYKY-PRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd05909 445 DPS--SLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLK 487
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
83-566 |
1.16e-31 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 129.19 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIfmpgTTQLKAKDILYRIqisRAKAIVTTA 162
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGI----VTTMNPSSSLGEI---KKRVVDCSV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SLVPEVESVASECPDLKTKLV-VSDHSHegwldFCSLIKSASPDHTCIKS----------KMKDPMAIFFTSGTTGYPKM 231
Cdd:PLN02574 141 GLAFTSPENVEKLSPLGVPVIgVPENYD-----FDSKRIEFPKFYELIKEdfdfvpkpviKQDDVAAIMYSSGTTGASKG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 232 AKhnqgLAFRSYIPSCRKLLKLKTSDILWCMSDP------------GWILATVGCLiepwTSGCTVFIhhLPQFDPKVIV 299
Cdd:PLN02574 216 VV----LTHRNLIAMVELFVRFEASQYEYPGSDNvylaalpmfhiyGLSLFVVGLL----SLGSTIVV--MRRFDASDMV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 300 EVLFKYPITQCLAAPGVYrMVLQQKTSNL---RFPTLEHCTTGGESLLPEEYEQWKQR-TGLSIHEVYGQSE-TGISSAT 374
Cdd:PLN02574 286 KVIDRFKVTHFPVVPPIL-MALTKKAKGVcgeVLKSLKQVSCGAAPLSGKFIQDFVQTlPHVDFIQGYGMTEsTAVGTRG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 375 LREMKIKR-GSIGKAILPFDLQIID-EKGNILPPNTEGYIGIRiKPtrplGLFMEYENSPEST-SEVECGDFYNSGDRAT 451
Cdd:PLN02574 365 FNTEKLSKySSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ-GP----GVMKGYLNNPKATqSTIDKDGWLRTGDIAY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 452 IDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPE-FLShdQEQLIkelq 530
Cdd:PLN02574 440 FDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGsTLS--QEAVI---- 513
|
490 500 510
....*....|....*....|....*....|....*.
gi 18381087 531 HHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PLN02574 514 NYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
103-565 |
3.23e-31 |
|
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: 126.93 E-value: 3.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 103 GLQQGDHLALILPRVPEwwLVTV--GCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVesvasecPDLKT 180
Cdd:cd12117 43 GVGPGDVVGVLAERSPE--LVVAllAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRA-------GGLEV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 181 KLVVSDHSHEGwldfcslikSASPDHTCIKSkmkDPMA-IFFTSGTTGYPK--MAKHN--QGLAF-RSYIPscrkllkLK 254
Cdd:cd12117 114 AVVIDEALDAG---------PAGNPAVPVSP---DDLAyVMYTSGSTGRPKgvAVTHRgvVRLVKnTNYVT-------LG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 255 TSDILWCMSDPGWILATvgclIEPWTS----GCTVFIHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSnlRF 330
Cdd:cd12117 175 PDDRVLQTSPLAFDAST----FEIWGAllngARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADEDPE--CF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 331 PTLEHCTTGGESLLPEEYEQWKQRT-GLSIHEVYGQSETGISSAT--LREMKIKRGS--IGKAILPFDLQIIDEKGNILP 405
Cdd:cd12117 249 AGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTTFTTShvVTELDEVAGSipIGRPIANTRVYVLDEDGRPVP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 406 PNTEG--YIGIRikptrplGLFMEYENSPESTSE--VEC-----GDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIG 476
Cdd:cd12117 329 PGVPGelYVGGD-------GLALGYLNRPALTAErfVADpfgpgERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 477 PVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSHDqeqlikELQHHVKSVTAPYKYPRKVEFVSELPKTV 556
Cdd:cd12117 402 LGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA-LDAA------ELRAFLRERLPAYMVPAAFVVLDELPLTA 474
|
....*....
gi 18381087 557 TGKIKRKEL 565
Cdd:cd12117 475 NGKVDRRAL 483
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
80-565 |
7.16e-31 |
|
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: 126.08 E-value: 7.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 80 IKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIV 159
Cdd:cd05923 27 LRLTYSELRARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 160 TTASLVPEVESVASECPDLKTKLVVSDHSHEgwldfcslikSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAkhnqGLA 239
Cdd:cd05923 106 IAVDAQVMDAIFQSGVRVLALSDLVGLGEPE----------SAGPLIEDPPREPEQPAFVFYTSGTTGLPKGA----VIP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 240 FRS------YIPSCRKLLKLKTSDILWCMsdP-----GWILATVGCLIepwtsgCTVFIHHLPQFDPKVIVEVLFKYPIT 308
Cdd:cd05923 172 QRAaesrvlFMSTQAGLRHGRHNVVLGLM--PlyhviGFFAVLVAALA------LDGTYVVVEEFDPADALKLIEQERVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 309 QCLAAPGVYRMVLQQKT-SNLRFPTLEHCTTGGESL---LPEEYEQWKQRTGLSIhevYGQSETGISsatLREMKIKRGS 384
Cdd:cd05923 244 SLFATPTHLDALAAAAEfAGLKLSSLRHVTFAGATMpdaVLERVNQHLPGEKVNI---YGTTEAMNS---LYMRDARTGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 385 IGKAILPFDLQIIDEKGN---ILPPNTEGYIGIRIKPTRPlglFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFL 461
Cdd:cd05923 318 EMRPGFFSEVRIVRIGGSpdeALANGEEGELIVAAAADAA---FTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRIL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 462 GRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLSHDqeqlikEL-QHHVKSVTAPY 540
Cdd:cd05923 395 GRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAD------ELdQFCRASELADF 468
|
490 500
....*....|....*....|....*
gi 18381087 541 KYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd05923 469 KRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
219-566 |
1.29e-30 |
|
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: 124.79 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 219 IFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSD-ILWCMS---DpgwilATVGCLIEPWTSGCTVFIHHLPQF- 293
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHG-PLAAHCQATAERYGLTPGDrELQFASfnfD-----GAHEQLLPPLICGACVVLRPDELWa 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 294 DPKVIVEVLFKYPITQCLAAPGVYRMVLQQ--KTSNLRFPTLEHCTTGGESLLPEEYEQWkQRTGLSIHEVYGQSETGIS 371
Cdd:cd17649 173 SADELAEMVRELGVTVLDLPPAYLQQLAEEadRTGDGRPPSLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEATVT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 372 S-ATLREMKIKRGS----IGKAILPFDLQIIDEKGNILPPNTEG--YIGIRikptrplGLFMEYENSPESTSE------- 437
Cdd:cd17649 252 PlVWKCEAGAARAGasmpIGRPLGGRSAYILDADLNPVPVGVTGelYIGGE-------GLARGYLGRPELTAErfvpdpf 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 438 -VECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVkAFIVL-NP 515
Cdd:cd17649 325 gAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLrAA 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 18381087 516 EFLSHDQEQLIKelqhHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd17649 404 AAQPELRAQLRT----ALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
211-565 |
2.14e-30 |
|
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: 124.36 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 211 SKMKDPMAIFFTSGTTGYPK--MAKHnQGL-----AFRSYIPSCRKLLKLKTSDILWcmsDpgwilATVGCLIEPWTSGC 283
Cdd:cd17655 134 SKSDDLAYVIYTSGSTGKPKgvMIEH-RGVvnlveWANKVIYQGEHLRVALFASISF---D-----ASVTEIFASLLSGN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 284 TVFIH-HLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVlqQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLS--IH 360
Cdd:cd17655 205 TLYIVrKETVLDGQALTQYIRQNRITIIDLTPAHLKLL--DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNptIT 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 361 EVYGQSET--GISSATLREMKIKRGS--IGKAILPFDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEYENSPES 434
Cdd:cd17655 283 NAYGPTETtvDASIYQYEPETDQQVSvpIGKPLGNTRIYILDQYGRPQPVGVAGelYIG-------GEGVARGYLNRPEL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 435 TSE-------VECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVV 507
Cdd:cd17655 356 TAEkfvddpfVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYL 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 18381087 508 KAFIVLNPEFlshDQEQLIKELQHHVKSVTAPyKYPRKVEfvsELPKTVTGKIKRKEL 565
Cdd:cd17655 436 CAYIVSEKEL---PVAQLREFLARELPDYMIP-SYFIKLD---EIPLTPNGKVDRKAL 486
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
103-568 |
4.16e-30 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 124.57 E-value: 4.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 103 GLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPDLKTK- 181
Cdd:PLN02479 66 SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKKSs 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 182 ------LVVSDHSHE----------GWLDFCSLIKSASPDHTCIKSKMK-DPMAIFFTSGTTGYPK-MAKHNQGlafrSY 243
Cdd:PLN02479 146 fkppllIVIGDPTCDpkslqyalgkGAIEYEKFLETGDPEFAWKPPADEwQSIALGYTSGTTASPKgVVLHHRG----AY 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 244 IPSCRKLLklktsdiLWCMSDPG---WILATVGC--LIEPW-------TSGCtvfihhLPQFDPKVIVEVLFKYPITQCL 311
Cdd:PLN02479 222 LMALSNAL-------IWGMNEGAvylWTLPMFHCngWCFTWtlaalcgTNIC------LRQVTAKAIYSAIANYGVTHFC 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 312 AAPGVYRMVLQQKTSN--LRFPTLEHCTTGGESLLPEEYEQWKQRtGLSIHEVYGQSETgISSATLREMKIKRGSigkai 389
Cdd:PLN02479 289 AAPVVLNTIVNAPKSEtiLPLPRVVHVMTAGAAPPPSVLFAMSEK-GFRVTHTYGLSET-YGPSTVCAWKPEWDS----- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 390 LPFD------------------LQIIDEKGNILPP---NTEGYIGIRIKptrplGLFMEYENSPESTSEVECGDFYNSGD 448
Cdd:PLN02479 362 LPPEeqarlnarqgvryiglegLDVVDTKTMKPVPadgKTMGEIVMRGN-----MVMKGYLKNPKANEEAFANGWFHSGD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 449 RATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLSHDQEQLIKE 528
Cdd:PLN02479 437 LGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAED 516
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 18381087 529 LQHHVKSVTAPYKYPRKVEFvSELPKTVTGKIKRKELRNK 568
Cdd:PLN02479 517 IMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
215-562 |
3.33e-29 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 117.89 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPKMAKHNQglafRSYIPSC---RKLLKLKTSDILWCmsdPGWI---LATVGCLIEPWTSGCtvfIH 288
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSE----RSWIESFvcnEDLFNISGEDAILA---PGPLshsLFLYGAISALYLGGT---FI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 289 HLPQFDPKVIVEVLFKYPITQCLAAPgvyrMVLQQKTSnlrfpTLEHCT------TGGESLLPEEYEQWKQRT-GLSIHE 361
Cdd:cd17633 71 GQRKFNPKSWIRKINQYNATVIYLVP----TMLQALAR-----TLEPESkiksifSSGQKLFESTKKKLKNIFpKANLIE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 362 VYGQSETGISSATLREMKIKRGSIGKailPF---DLQIIDEKGNILppnteGYIGIRiKPTRPLGLFMEYENSPESTSEV 438
Cdd:cd17633 142 FYGTSELSFITYNFNQESRPPNSVGR---PFpnvEIEIRNADGGEI-----GKIFVK-SEMVFSGYVRGGFSNPDGWMSV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 439 ecgdfynsGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNpefl 518
Cdd:cd17633 213 --------GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD---- 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 18381087 519 SHDQEQLIKELQHHVKSvtapYKYPRKVEFVSELPKTVTGKIKR 562
Cdd:cd17633 281 KLTYKQLKRFLKQKLSR----YEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
78-565 |
5.76e-29 |
|
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: 120.09 E-value: 5.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 78 DEIKWSFRKLRDLTCRTANVFeQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKA 157
Cdd:cd12116 9 DDRSLSYAELDERANRLAARL-RARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 158 IVTTaslvPEVESVASECPDLKTKLVVSDHshegwLDFCSLIKSASPDhtcikskmkDPMAIFFTSGTTGYPK--MAKHN 235
Cdd:cd12116 88 VLTD----DALPDRLPAGLPVLLLALAAAA-----AAPAAPRTPVSPD---------DLAYVIYTSGSTGRPKgvVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 236 QGLAFRSyipSCRKLLKLKTSDILWCMSDPGWILATVGCLIePWTSGCTVFIhhLP---QFDPKVIVEVLFKYPITQCLA 312
Cdd:cd12116 150 NLVNFLH---SMRERLGLGPGDRLLAVTTYAFDISLLELLL-PLLAGARVVI--APretQRDPEALARLIEAHSITVMQA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 313 APGVYRMVLQQKTSNLRFPTLeHCttGGESLLPEEYEQWKQRTGlSIHEVYGQSETGI-SSATLREMKIKRGSIGKAILP 391
Cdd:cd12116 224 TPATWRMLLDAGWQGRAGLTA-LC--GGEALPPDLAARLLSRVG-SLWNLYGPTETTIwSTAARVTAAAGPIPIGRPLAN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 392 FDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEYENSPESTSEV--------ECGDFYNSGDRATIDEEGYIWFL 461
Cdd:cd12116 300 TQVYVLDAALRPVPPGVPGelYIG-------GDGVAQGYLGRPALTAERfvpdpfagPGSRLYRTGDLVRRRADGRLEYL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 462 GRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVkAFIVLnPEFLSHDqeqlIKELQHHVKSVTAPYK 541
Cdd:cd12116 373 GRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPD----AAALRAHLRATLPAYM 446
|
490 500
....*....|....*....|....
gi 18381087 542 YPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd12116 447 VPSAFVRLDALPLTANGKLDRKAL 470
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
219-568 |
6.21e-29 |
|
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: 117.43 E-value: 6.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 219 IFFTSGTTGYPKMAKHN--QGLAFRSyipSCRKLLKLKTSDiLWCMSDPGWILATVGCLIEPWTSGCTVfihHLPQFDPK 296
Cdd:cd17630 5 VILTSGSTGTPKAVVHTaaNLLASAA---GLHSRLGFGGGD-SWLLSLPLYHVGGLAILVRSLLAGAEL---VLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 297 VIVEVLfKYPITQCLAAPGVYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRtGLSIHEVYGQSETGISSATLR 376
Cdd:cd17630 78 LAEDLA-PPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVATKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 377 EMKIKRGSIGKAiLPFDLQIIDEKGNILPpntegyigirikptRPLGLFMEYENSPESTSEVECGDFYnSGDRATIDEEG 456
Cdd:cd17630 156 PDGFGRGGVGVL-LPGRELRIVEDGEIWV--------------GGASLAMGYLRGQLVPEFNEDGWFT-TKDLGELHADG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 457 YIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEflsHDQEQLIKelqhHVKSV 536
Cdd:cd17630 220 RLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP---ADPAELRA----WLKDK 292
|
330 340 350
....*....|....*....|....*....|..
gi 18381087 537 TAPYKYPRKVEFVSELPKTVTGKIKRKELRNK 568
Cdd:cd17630 293 LARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
215-559 |
8.76e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 117.87 E-value: 8.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPK--MAKHNQ---------GLAFRSYIPSCRKLL-KLKTSDILWCMSDP-----GWILATVGclie 277
Cdd:cd05924 4 DDLYILYTGGTTGMPKgvMWRQEDifrmlmggaDFGTGEFTPSEDAHKaAAAAAGTVMFPAPPlmhgtGSWTAFGG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 278 pWTSGCTVFIHHlPQFDPK--------------VIVEVLFKYPITQCLAAPGVYRMvlqqktsnlrfPTLEHCTTGGESL 343
Cdd:cd05924 80 -LLGGQTVVLPD-DRFDPEevwrtiekhkvtsmTIVGDAMARPLIDALRDAGPYDL-----------SSLFAISSGGALL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 344 LPEEYEQW-KQRTGLSIHEVYGQSETG-ISSATLREMKIKRGSigKAILPFDLQIIDEKGNILPPNTE--GYIGIR--Ik 417
Cdd:cd05924 147 SPEVKQGLlELVPNITLVDAFGSSETGfTGSGHSAGSGPETGP--FTRANPDTVVLDDDGRVVPPGSGgvGWIARRghI- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 418 ptrPLGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVS 497
Cdd:cd05924 224 ---PLGYYGDEAKTAETFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVG 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18381087 498 SPDKDRGEVVKAFIVLNPEFlSHDQEqlikELQHHVKSVTAPYKYPRKVEFVSELPKTVTGK 559
Cdd:cd05924 301 RPDERWGQEVVAVVQLREGA-GVDLE----ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
76-562 |
8.93e-29 |
|
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: 119.47 E-value: 8.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 76 QGDEIKWSFRKLRDLTCRTANVFEqICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRA 155
Cdd:cd05914 2 YYGGEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 156 KAIvttaslvpevesvasecpdlktklvvsdhshegwldFCSliksaspdhtciksKMKDPMAIFFTSGTTGYPK--MAK 233
Cdd:cd05914 81 KAI------------------------------------FVS--------------DEDDVALINYTSGTTGNSKgvMLT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 234 HNQglaFRSYIPSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTV-FIHHLP----------QFDPKVIVEVL 302
Cdd:cd05914 111 YRN---IVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVvFLDKIPsakiialafaQVTPTLGVPVP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 303 F-------KYPITQCLAAPGVYRM---VLQQKTSNLRFPTLEHCTTG-------GESLLPEEYEQWKQRTGLSIHEVYGQ 365
Cdd:cd05914 188 LviekifkMDIIPKLTLKKFKFKLakkINNRKIRKLAFKKVHEAFGGnikefviGGAKINPDVEEFLRTIGFPYTIGYGM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 366 SETG--ISSAtlREMKIKRGSIGKAILPFDLQIIDEKgnilPPNTEGYIGIRIKptrplGLFMEYENSPESTSEV--ECG 441
Cdd:cd05914 268 TETApiISYS--PPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGP-----NVMKGYYKNPEATAEAfdKDG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 442 DFYnSGDRATIDEEGYIWFLGRGDDVI-NASGYRIGPVEVENALAEHPAVAESAVVSSPDKdrgevVKAFIVLNPEFL-- 518
Cdd:cd05914 337 WFH-TGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKK-----LVALAYIDPDFLdv 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 18381087 519 -----SHDQEQLIKELQHHVKSVTAPYKYPRKVEFV-SELPKTVTGKIKR 562
Cdd:cd05914 411 kalkqRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
110-565 |
8.05e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 119.68 E-value: 8.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 110 LALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESvasecPDLKTKLVVSdhSH 189
Cdd:PRK12316 4604 VGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPI-----PDGLASLALD--RD 4676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 190 EGWLDFcsliksasPDHTCIKSKMKDPMA-IFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSDILWCMSDPGWI 268
Cdd:PRK12316 4677 EDWEGF--------PAHDPAVRLHPDNLAyVIYTSGSTGRPKGVAVSHG-SLVNHLHATGERYELTPDDRVLQFMSFSFD 4747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 269 LATVGcLIEPWTSGCTVFIHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEY 348
Cdd:PRK12316 4748 GSHEG-LYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASY 4826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 349 EQ-WKQRTGLSIHEVYGQSETGISSATLREMKIKRGS-----IGKAILPFDLQIIDEKGNILPPNTEG--YIGIRikptr 420
Cdd:PRK12316 4827 DLaWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGaaympIGTPLGNRSGYVLDGQLNPLPVGVAGelYLGGE----- 4901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 421 plGLFMEYENSPESTSE--------VECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAE 492
Cdd:PRK12316 4902 --GVARGYLERPALTAErfvpdpfgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE 4979
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18381087 493 SAVVSSPDKDRGEVVKAFIVLNPEFLSHDQEQ--LIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:PRK12316 4980 AVVIAQEGAVGKQLVGYVVPQDPALADADEAQaeLRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
79-566 |
9.13e-28 |
|
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: 117.15 E-value: 9.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 79 EIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAI 158
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRAL-GVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 159 VTTAslvpEVESVASECPDLKTKLVVSDHSHEGWLDFCSLIKSASPDHTCIKSKMK-DPMAIFFTSGTTGYPKMAKHN-Q 236
Cdd:cd05915 101 LFDP----NLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPErAACGMAYTTGTTGLPKGVVYShR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 237 GLAFRSYIPSCRKLLKLKTSDILWCMSD----PGWilatvgCLIEPWTSGCTVFIHHLPQFDPKVIVEVLFKYPITQCLA 312
Cdd:cd05915 177 ALVLHSLAASLVDGTALSEKDVVLPVVPmfhvNAW------CLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 313 APGVYRMVLQQKTSNLR-FPTLEHCTTGGESLlPEEYEQWKQRTGLSIHEVYGQSET-GISSA--------TLREMKIKR 382
Cdd:cd05915 251 VPTVWLALADYLESTGHrLKTLRRLVVGGSAA-PRSLIARFERMGVEVRQGYGLTETsPVVVQnfvkshleSLSEEEKLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 383 GSIGKAILPFDlqiidEKGNILPPNT-----EGYIgIRIKPTRPLGLFMEYENSPESTSEVEC-GDFYNSGDRATIDEEG 456
Cdd:cd05915 330 LKAKTGLPIPL-----VRLRVADEEGrpvpkDGKA-LGEVQLKGPWITGGYYGNEEATRSALTpDGFFRTGDIAVWDEEG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 457 YIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEflSHDQEQLIKELQHHVKSV 536
Cdd:cd05915 404 YVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGE--KPTPEELNEHLLKAGFAK 481
|
490 500 510
....*....|....*....|....*....|
gi 18381087 537 TApykYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:cd05915 482 WQ---LPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
479-559 |
1.96e-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: 105.32 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 479 EVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPeflshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTG 558
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 18381087 559 K 559
Cdd:pfam13193 76 K 76
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
79-566 |
2.12e-27 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 116.24 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 79 EIKWSFRKLRDLTCRTANVFEQiCGLQQGDhLALI-LPRVPEWWLVTVGCMRTGI-----IFMPGTTQLKAkdilYRIQI 152
Cdd:PRK10946 46 ERQFSYRELNQASDNLACSLRR-QGIKPGD-TALVqLGNVAEFYITFFALLKLGVapvnaLFSHQRSELNA----YASQI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 153 -------SRAKAIVTTASLVpevESVASECPDLktkLVVSDHSHEGWLDFCSLIKSASPDHTCIKSKmKDPMAIFFTSG- 224
Cdd:PRK10946 120 epalliaDRQHALFSDDDFL---NTLVAEHSSL---RVVLLLNDDGEHSLDDAINHPAEDFTATPSP-ADEVAFFQLSGg 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 225 TTGYPKMA--KHNqglafrSYIPSCRK---LLKLKTSDILWC---------MSDPG--WILATVGCLI---EPWTSGCTV 285
Cdd:PRK10946 193 STGTPKLIprTHN------DYYYSVRRsveICGFTPQTRYLCalpaahnypMSSPGalGVFLAGGTVVlapDPSATLCFP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 286 FIHH--------LPqfdPKVIVEVlfkypitQCLAAPGvYRMVLQqktsnlrfpTLEHCTTGGESLLPEEYEQWKQRTGL 357
Cdd:PRK10946 267 LIEKhqvnvtalVP---PAVSLWL-------QAIAEGG-SRAQLA---------SLKLLQVGGARLSETLARRIPAELGC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 358 SIHEVYGQSEtGISSATLREMKIKR--GSIGKAILPFD-LQIIDEKGNILPPNTEGYIGIRIKPTrplglFMEYENSPES 434
Cdd:PRK10946 327 QLQQVFGMAE-GLVNYTRLDDSDERifTTQGRPMSPDDeVWVADADGNPLPQGEVGRLMTRGPYT-----FRGYYKSPQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 435 TSEVECGD-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVL 513
Cdd:PRK10946 401 NASAFDANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 18381087 514 N-----PEFLSHDQEQLIkelqhhvksvtAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK10946 481 KeplkaVQLRRFLREQGI-----------AEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
103-566 |
4.11e-27 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 115.67 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 103 GLQQGDHLAlILPRVPEW---WLVTVGCMrtGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLV---PEVESvaSECP 176
Cdd:PLN02860 53 GLRNGDVVA-IAALNSDLyleWLLAVACA--GGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSswyEELQN--DRLP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 177 DLKTKLVVSDHSHEGWLDFCSL----------IKSASPDHtciKSKMKDPMAIFFTSGTTGYPK--MAKHN----QGLAF 240
Cdd:PLN02860 128 SLMWQVFLESPSSSVFIFLNSFlttemlkqraLGTTELDY---AWAPDDAVLICFTSGTTGRPKgvTISHSalivQSLAK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 241 RSYIPSCRKLLKLKTSDIlwCMsdpgwILATVGCLIEPWTSGCTVFIhhlPQFDPKVIVEVLFKYPITQCLAAPGVYRMV 320
Cdd:PLN02860 205 IAIVGYGEDDVYLHTAPL--CH-----IGGLSSALAMLMVGACHVLL---PKFDAKAALQAIKQHNVTSMITVPAMMADL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 321 L---QQKTSNLRFPTLEHCTTGGES----LLPEEYEQWKQRTGLSiheVYGQSETgISSATLREMKIKRGSIGKAILPFD 393
Cdd:PLN02860 275 IsltRKSMTWKVFPSVRKILNGGGSlssrLLPDAKKLFPNAKLFS---AYGMTEA-CSSLTFMTLHDPTLESPKQTLQTV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 394 LQIIDEKGNIL--------PPNTEgyigIRIKP----------TRPLGLFMEYENSPESTSEVECGDFY-NSGDRATIDE 454
Cdd:PLN02860 351 NQTKSSSVHQPqgvcvgkpAPHVE----LKIGLdessrvgrilTRGPHVMLGYWGQNSETASVLSNDGWlDTGDIGWIDK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 455 EGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFL-SHDQEQLIK------ 527
Cdd:PLN02860 427 AGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIwSDNEKENAKknltls 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 18381087 528 --ELQHHV--KSVTApYKYPRK-VEFVSELPKTVTGKIKRKELR 566
Cdd:PLN02860 507 seTLRHHCreKNLSR-FKIPKLfVQWRKPFPLTTTGKIRRDEVR 549
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
103-566 |
9.07e-27 |
|
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: 115.72 E-value: 9.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 103 GLQQGDHLALILPRVPEWwLVTV-GCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVesvasecPDLKTK 181
Cdd:COG1020 522 GVGPGDLVGVCLERSLEM-VVALlAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL-------PELGVP 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 182 LVVSDHSHEGWLDFCSLIKSASPDHTcikskmkdpmA-IFFTSGTTGYPK--MAKHnQGLAfrSYIPSCRKLLKLKTSD- 257
Cdd:COG1020 594 VLALDALALAAEPATNPPVPVTPDDL----------AyVIYTSGSTGRPKgvMVEH-RALV--NLLAWMQRRYGLGPGDr 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 258 ILWCMS---DpgwilATVGCLIEPWTSGCTVFIhhLPQ---FDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLrfP 331
Cdd:COG1020 661 VLQFASlsfD-----ASVWEIFGALLSGATLVL--APPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEAL--P 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 332 TLEHCTTGGESLLPEEYEQWKQRT-GLSIHEVYGQSETGISSAT--LREMKIKRGS--IGKAILPFDLQIIDEKGNILPP 406
Cdd:COG1020 732 SLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYyeVTPPDADGGSvpIGRPIANTRVYVLDAHLQPVPV 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 407 NTEG--YI-GIrikptrplGLFMEYENSPESTSE--VEC-----GD-FYNSGDRATIDEEGYIWFLGRGDD-V-INasGY 473
Cdd:COG1020 812 GVPGelYIgGA--------GLARGYLNRPELTAErfVADpfgfpGArLYRTGDLARWLPDGNLEFLGRADDqVkIR--GF 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 474 RIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEflshdQEQLIKELQHHVKSVTAPYKYPRKVEFVSELP 553
Cdd:COG1020 882 RIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG-----AAAAAALLRLALALLLPPYMVPAAVVLLLPLP 956
|
490
....*....|...
gi 18381087 554 KTVTGKIKRKELR 566
Cdd:COG1020 957 LTGNGKLDRLALP 969
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
103-563 |
1.35e-26 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 113.83 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 103 GLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPDLKTKL 182
Cdd:PRK05852 64 GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 183 VVSDHSHEGWLDfCSLIKSASPDH--TCIKSKMKDPMAIFFTSGTTGYPKM---AKHNQGLAFRSYIPSCRKLLKLKTSD 257
Cdd:PRK05852 144 GGDSGPSGGTLS-VHLDAATEPTPatSTPEGLRPDDAMIMFTGGTTGLPKMvpwTHANIASSVRAIITGYRLSPRDATVA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 258 ILWCMSDPGWILATVGCLiepwTSGCTVFIHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQ--------QKTSNLR 329
Cdd:PRK05852 223 VMPLYHGHGLIAALLATL----ASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLEraatepsgRKPAALR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 330 FptLEHCTTggeSLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIKR--------GSIGKAILPfDLQIIDEKG 401
Cdd:PRK05852 299 F--IRSCSA---PLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQtenpvvstGLVGRSTGA-QIRIVGSDG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 402 NILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVE 481
Cdd:PRK05852 373 LPLPAGAVGEVWLR-GTTVVRG----YLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 482 NALAEHPAVAESAVVSSPDKDRGEVVKAFIVlnPEFLSHDQEQlikELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIK 561
Cdd:PRK05852 448 GVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAPPTAE---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLD 522
|
..
gi 18381087 562 RK 563
Cdd:PRK05852 523 RR 524
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
219-565 |
2.11e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 113.17 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 219 IFFTSGTTGYPKMAKHNQGLafRSYIPSCRKLL---KLKTSDILwCMSDPGWILATVGCLIEPWTSGCTVFIHHlpQFDP 295
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRAPQL--RSAVGVWVTILdrtRLRTGSRI-SVAMPMFHGLGLGMLMLTIALGGTVLTHR--HFDA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 296 KVIVEVLFKYPITQCLAAPGVYRMVLQ---QKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISS 372
Cdd:PRK13383 254 EAALAQASLHRADAFTAVPVVLARILElppRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGA 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 373 -ATLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEG--YIGIRIKPTRPLGlfmeyenspeSTSEVECGDFYNSGDR 449
Cdd:PRK13383 334 lATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGriFVGGELAGTRYTD----------GGGKAVVDGMTSTGDM 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 450 ATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEfLSHDQEQlikeL 529
Cdd:PRK13383 404 GYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ----L 478
|
330 340 350
....*....|....*....|....*....|....*.
gi 18381087 530 QHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:PRK13383 479 RDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
89-567 |
2.37e-26 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 113.19 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 89 DLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEV 168
Cdd:PLN03102 47 DRCCRLAASLISL-NITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 169 ESVASECPDLKTKL---VVSDH---------SHEgwLDFCSLIKSASPDHTCIKSKMK-----DPMAIFFTSGTTGYPKM 231
Cdd:PLN03102 126 REVLHLLSSEDSNLnlpVIFIHeidfpkrpsSEE--LDYECLIQRGEPTPSLVARMFRiqdehDPISLNYTSGTTADPKG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 232 AKHNQGLAFRSYIpscrkllklkTSDILWCMSD-PG--WILATVGC--LIEPWTS----GCTVFIHHLPQfdPKVIVEVL 302
Cdd:PLN03102 204 VVISHRGAYLSTL----------SAIIGWEMGTcPVylWTLPMFHCngWTFTWGTaargGTSVCMRHVTA--PEIYKNIE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 303 FkYPITQCLAAPGVYRMVLQQKTSNL--RFPTLeHCTTGGESLlPEEYEQWKQRTGLSIHEVYGQSET------------ 368
Cdd:PLN03102 272 M-HNVTHMCCVPTVFNILLKGNSLDLspRSGPV-HVLTGGSPP-PAALVKKVQRLGFQVMHAYGLTEAtgpvlfcewqde 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 369 ----------------GISSATLREMKIKRGSIGKAIlPFDLQIIDE---KGNILppnTEGYIgirikptrplglfmeye 429
Cdd:PLN03102 349 wnrlpenqqmelkarqGVSILGLADVDVKNKETQESV-PRDGKTMGEiviKGSSI---MKGYL----------------- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 430 NSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKA 509
Cdd:PLN03102 408 KNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCA 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18381087 510 FIVL--NPEFLSHDQEQLI---KELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:PLN03102 488 FVVLekGETTKEDRVDKLVtreRDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
345-566 |
3.75e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 112.47 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 345 PEEYEQWKQRTGLSIHEVYGQSETGISSAtlREMKIKRGSIGKaiLPFDLQIID-EKGNILPP---------NTEGYIGI 414
Cdd:PRK07867 279 PGDIARFARRFGCVVVDGFGSTEGGVAIT--RTPDTPPGALGP--LPPGVAIVDpDTGTECPPaedadgrllNADEAIGE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 415 RIKPTRPlGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESA 494
Cdd:PRK07867 355 LVNTAGP-GGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVA 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18381087 495 VVSSPDKDRGEVVKAFIVLNP--EFlshDQEQLIKELqhHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK07867 434 VYAVPDPVVGDQVMAALVLAPgaKF---DPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
83-567 |
6.47e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 111.02 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQICGLQQgdHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTA 162
Cdd:PRK07638 28 TYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SLVPEVesvasecPDLKTKLVVSDHSHEgwldfcsLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAFRS 242
Cdd:PRK07638 106 YKLNDL-------PDEEGRVIEIDEWKR-------MIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 243 YIPSCRKLLKLKTSDILWcmsdPG------WILATVGCLIepwtSGCTVFIhhLPQFDPKVIVEVLFKYPITQCLAAPGV 316
Cdd:PRK07638 172 FDCNVHDFHMKREDSVLI----AGtlvhslFLYGAISTLY----VGQTVHL--MRKFIPNQVLDKLETENISVMYTVPTM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 317 YRMVLQQKtsnlRFPtlEHCTT---GGESLLPEEYEQWKQR-TGLSIHEVYGQSETG-ISSATLREMKIKRGSIGKAILP 391
Cdd:PRK07638 242 LESLYKEN----RVI--ENKMKiisSGAKWEAEAKEKIKNIfPYAKLYEFYGASELSfVTALVDEESERRPNSVGRPFHN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 392 FDLQIIDEKGNILPPNTEGYIGIRiKPTRplglFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINAS 471
Cdd:PRK07638 316 VQVRICNEAGEEVQKGEIGTVYVK-SPQF----FMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 472 GYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIvlnpeflshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSE 551
Cdd:PRK07638 391 GINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKEWHFVDE 461
|
490
....*....|....*.
gi 18381087 552 LPKTVTGKIKRKELRN 567
Cdd:PRK07638 462 IPYTNSGKIARMEAKS 477
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
106-565 |
1.17e-25 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 110.87 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 106 QGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAI-------VTTASLVPEVESVASECPDL 178
Cdd:PRK05857 65 RGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAAlvapgskMASSAVPEALHSIPVIAVDI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 179 KTKLVVSDHSHEgwLDFcsliKSASPDhtcikSKMKDPMAIFFTSGTTGYPKMAK-------------HNQGLAFRSYIP 245
Cdd:PRK05857 145 AAVTRESEHSLD--AAS----LAGNAD-----QGSEDPLAMIFTSGTTGEPKAVLlanrtffavpdilQKEGLNWVTWVV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 246 SCRKLLKLKTSDI--LWcmsdpgWILatvGCLIEpwTSGCTVFIHHLPQfdpkvIVEVLFKYPI-TQCLAAPGVYRMVLQ 322
Cdd:PRK05857 214 GETTYSPLPATHIggLW------WIL---TCLMH--GGLCVTGGENTTS-----LLEILTTNAVaTTCLVPTLLSKLVSE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 323 QKTSNLRFPTLEHCTTGGESLLPEEYeQWKQRTGLSIHEVYGQSETGISSATLRE-----MKIKRGSIGKAILPFDLQII 397
Cdd:PRK05857 278 LKSANATVPSLRLVGYGGSRAIAADV-RFIEATGVRTAQVYGLSETGCTALCLPTddgsiVKIEAGAVGRPYPGVDVYLA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 398 DEKGNilPPNTEG------YIGIRIK-PTRPLGlfmeYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINA 470
Cdd:PRK05857 357 ATDGI--GPTAPGagpsasFGTLWIKsPANMLG----YWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIIC 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 471 SGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLSHDQEQLIKELQHHVKSVTAPYKYPRKVEFVS 550
Cdd:PRK05857 431 GGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVT 510
|
490
....*....|....*
gi 18381087 551 ELPKTVTGKIKRKEL 565
Cdd:PRK05857 511 DIPRTQSGKVMRASL 525
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
215-565 |
1.92e-25 |
|
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: 109.32 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPK--MAKHNQGLAfrsyipscrkLLKlKTSDILWCMSDPGWILATVGC----LIEPW----TSGCT 284
Cdd:cd17643 94 DLAYVIYTSGSTGRPKgvVVSHANVLA----------LFA-ATQRWFGFNEDDVWTLFHSYAfdfsVWEIWgallHGGRL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 285 VFIHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLR-FPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEV- 362
Cdd:cd17643 163 VVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRdPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLv 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 363 --YGQSETGISSaTLREMK------IKRGSIGKAILPFDLQIIDEKGNILPPNTEG--YIGiriKPTRPLGlfmeYENSP 432
Cdd:cd17643 243 nmYGITETTVHV-TFRPLDaadlpaAAASPIGRPLPGLRVYVLDADGRPVPPGVVGelYVS---GAGVARG----YLGRP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 433 ESTSEVECGD--------FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRG 504
Cdd:cd17643 315 ELTAERFVANpfggpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGD 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18381087 505 EVVKAFIVLNPEflshdQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd17643 395 TRLVAYVVADDG-----AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-565 |
4.32e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 111.02 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 35 RWNdhdsPEEFNFASD-VLDYWAQMEEEGKRGPSPAFwwvngqgDEIKWSFRKLRDLTCRTANV-FEQicGLQQGDHLAL 112
Cdd:PRK12467 501 RWN----APATEYAPDcVHQLIEAQARQHPERPALVF-------GEQVLSYAELNRQANRLAHVlIAA--GVGPDVLVGI 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 113 ILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVT---TASLVPEVESVASECPDLKTKLVVSDHSH 189
Cdd:PRK12467 568 AVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTqshLLAQLPVPAGLRSLCLDEPADLLCGYSGH 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 190 EGWLDFcsliksaSPDHTCIkskmkdpmaIFFTSGTTGYPK--MAKHNqglAFRSYIPSCRKLLKLKTSDILWCMSDPGW 267
Cdd:PRK12467 648 NPEVAL-------DPDNLAY---------VIYTSGSTGQPKgvAISHG---ALANYVCVIAERLQLAADDSMLMVSTFAF 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 268 ILAtVGCLIEPWTSGCTVfiHHLPQ---FDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLrfPTLEHCTT-GGESL 343
Cdd:PRK12467 709 DLG-VTELFGALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL--PRPQRALVcGGEAL 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 344 LPEEYEQWKQ-RTGLSIHEVYGQSETGISSATLR----EMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEG--YIGiri 416
Cdd:PRK12467 784 QVDLLARVRAlGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGelYIG--- 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 417 kptrPLGLFMEYENSPESTSE--------VECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHP 488
Cdd:PRK12467 861 ----GAGLARGYHRRPALTAErfvpdpfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQP 936
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18381087 489 AVAESAVVSSPDKDRGEVVkAFIVlnPEFLSHDQEQLIK--ELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:PRK12467 937 GVREAVVLAQPGDAGLQLV-AYLV--PAAVADGAEHQATrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
81-565 |
5.56e-25 |
|
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: 108.33 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 81 KWSFRKLRDLTCRTANVFeQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVT 160
Cdd:cd17656 13 KLTYRELNERSNQLARFL-REKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 161 TASLvpevesvASECPDLKTKLVVSDhshegwldfcSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPK--MAKHNQG- 237
Cdd:cd17656 92 QRHL-------KSKLSFNKSTILLED----------PSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKgvQLEHKNMv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 238 --LAF---RSYIPSCRKLLKLKTSDILWCMSDpgwILATvgcliepWTSGCTVFI-HHLPQFDPKVIVEVLFKYPITQCL 311
Cdd:cd17656 155 nlLHFereKTNINFSDKVLQFATCSFDVCYQE---IFST-------LLSGGTLYIiREETKRDVEQLFDLVKRHNIEVVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 312 AAPGVYRMVLQQKTSNLRFPT-LEHCTTGGESL-LPEEYEQWKQRTGLSIHEVYGQSETGISSA-------TLREMKikr 382
Cdd:cd17656 225 LPVAFLKFIFSEREFINRFPTcVKHIITAGEQLvITNEFKEMLHEHNVHLHNHYGPSETHVVTTytinpeaEIPELP--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 383 gSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRikptrPLGLFMEYENSPESTSEVECGD-------FYNSGDRATIDEE 455
Cdd:cd17656 302 -PIGKPISNTWIYILDQEQQLQPQGIVGELYIS-----GASVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 456 GYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLnpeflshDQEQLIKELQHHVKS 535
Cdd:cd17656 376 GNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM-------EQELNISQLREYLAK 448
|
490 500 510
....*....|....*....|....*....|
gi 18381087 536 VTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd17656 449 QLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
215-565 |
1.49e-24 |
|
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: 106.63 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPK--MAKHNQGLAFrsyipscrkllklktsdILWCMSD------PGWILATVGC-------LIEPW 279
Cdd:cd12115 106 DLAYVIYTSGSTGRPKgvAIEHRNAAAF-----------------LQWAAAAfsaeelAGVLASTSICfdlsvfeLFGPL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 280 TSGCTVFI----HHLPQFDPKVIVEVLFKYP--ITQCLAAPGVYRMVlqqKTSNLrfptlehcttGGESLLPEEYEQWKQ 353
Cdd:cd12115 169 ATGGKVVLadnvLALPDLPAAAEVTLINTVPsaAAELLRHDALPASV---RVVNL----------AGEPLPRDLVQRLYA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 354 RTGLS-IHEVYGQSE-TGISSATLREMKIKRG-SIGKAILPFDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEY 428
Cdd:cd12115 236 RLQVErVVNLYGPSEdTTYSTVAPVPPGASGEvSIGRPLANTQAYVLDRALQPVPLGVPGelYIG-------GAGVARGY 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 429 ENSPESTSEVECGD-------FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDK 501
Cdd:cd12115 309 LGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDA 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18381087 502 DRGEVVKAFIVLNPEFLShdqeqLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd12115 389 AGERRLVAYIVAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
83-566 |
1.85e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 107.14 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQIcGLQQGDHLALI---LPRVPEWWLvtvGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIV 159
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIawnTWRHLEAWY---GIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 160 TTASLVPEVESVASECPDLKTKLVVSDHSH------EGWLDFCSLIKSASPDhtcIKSKMKD---PMAIFFTSGTTGYPK 230
Cdd:PRK06018 117 TDLTFVPILEKIADKLPSVERYVVLTDAAHmpqttlKNAVAYEEWIAEADGD---FAWKTFDentAAGMCYTSGTTGDPK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 231 --MAKHNQGLaFRSYIPSCRKLLKLKTSDIL-----------W--CMSDPGwilatVGC-LIEPwtsGCtvfihhlpQFD 294
Cdd:PRK06018 194 gvLYSHRSNV-LHALMANNGDALGTSAADTMlpvvplfhansWgiAFSAPS-----MGTkLVMP---GA--------KLD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 295 PKVIVEVLFKYPITQCLAAPGVYRMVLQQ-KTSNLRFPTLEHCTTGGeSLLPEEYEQWKQRTGLSIHEVYGQSET----- 368
Cdd:PRK06018 257 GASVYELLDTEKVTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGG-SAMPRSMIKAFEDMGVEVRHAWGMTEMsplgt 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 369 ------GISSATLRE-MKIKRGSiGKAILPFDLQIIDEKGNILP--PNTEGYIGIRikptrplGLFMEYENSPESTSEVE 439
Cdd:PRK06018 336 laalkpPFSKLPGDArLDVLQKQ-GYPPFGVEMKITDDAGKELPwdGKTFGRLKVR-------GPAVAAAYYRVDGEILD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 440 CGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPefls 519
Cdd:PRK06018 408 DDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKP---- 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 18381087 520 hDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK06018 484 -GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
163-566 |
2.23e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 107.10 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 163 SLVPEVESVASECPDLKTKLVVSDHSH-----EGWLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMA--KHN 235
Cdd:PRK07008 120 TFLPLVDALAPQCPNVKGWVAMTDAAHlpagsTPLLCYETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGAlySHR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 236 QGL--AFRSYIPSCrklLKLKTSDILWcmsdP--------GWIL----ATVGC-LIEPWtsgctvfihhlPQFDPKVIVE 300
Cdd:PRK07008 200 STVlhAYGAALPDA---MGLSARDAVL----PvvpmfhvnAWGLpysaPLTGAkLVLPG-----------PDLDGKSLYE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 301 VLFKYPITQCLAAPGVYRMVLQQ-KTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGI--SSATLR- 376
Cdd:PRK07008 262 LIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPlgTLCKLKw 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 377 ---------EMKIkRGSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRIKPTRPLGLFMEYENSPESTsevecgDFYNSG 447
Cdd:PRK07008 342 khsqlpldeQRKL-LEKQGRVIYGVDMKIVGDDGRELPWDGKAFGDLQVRGPWVIDRYFRGDASPLVD------GWFPTG 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 448 DRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEF-LSHDqeqli 526
Cdd:PRK07008 415 DVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAeVTRE----- 489
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 18381087 527 kELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK07008 490 -ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
281-558 |
3.44e-24 |
|
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: 103.54 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 281 SGCTVFIhhlPQFDPKVIVEVLFKYPITQC-LAAPGVYRMVLQQKT-----SNLRFPTLEHcttGGESLLPEEYEQWKQR 354
Cdd:cd17636 66 GGTNVFV---RRVDAEEVLELIEAERCTHAfLLPPTIDQIVELNADglydlSSLRSSPAAP---EWNDMATVDTSPWGRK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 355 TGLsihevYGQSETGiSSATLREMKIKRGSIGKAILPF-DLQIIDEKGNILPPNTEGYIGIRiKPTRPLGlfmeYENSPE 433
Cdd:cd17636 140 PGG-----YGQTEVM-GLATFAALGGGAIGGAGRPSPLvQVRILDEDGREVPDGEVGEIVAR-GPTVMAG----YWNRPE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 434 STSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVL 513
Cdd:cd17636 209 VNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVL 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 18381087 514 NPeflshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTG 558
Cdd:cd17636 289 KP-----GASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
59-565 |
5.73e-24 |
|
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: 104.94 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 59 EEEGKRGPSPAFWWVNGQgdeiKWSFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGT 138
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQ----SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 139 TQLKAKDILYRIQISRAKAIVTTASlvpevesvasecpdlktklvvsdhshegwldfcsliksaspdhtcikskmkDPMA 218
Cdd:cd17645 80 PDYPGERIAYMLADSSAKILLTNPD---------------------------------------------------DLAY 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 219 IFFTSGTTGYPK--MAKHNQGLAFRSYIPSCRKLLKLKTSDILWCMSDPGWILAtvgcLIEPWTSGCTVfiHHLPQfDPK 296
Cdd:cd17645 109 VIYTSGSTGLPKgvMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWE----IFPHLTAGAAL--HVVPS-ERR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 297 VIVEVLFKY----PITQCLAAPGVYRMVLQQKTSNLRFptlehCTTGGESLlpeeyeQWKQRTGLSIHEVYGQSETGISs 372
Cdd:cd17645 182 LDLDALNDYfnqeGITISFLPTGAAEQFMQLDNQSLRV-----LLTGGDKL------KKIERKGYKLVNNYGPTENTVV- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 373 ATLREMKIKRGS--IGKAILPFDLQIIDEKGNILPPNTEGYIGIRIKptrplGLFMEYENSPESTSEVECGD-------F 443
Cdd:cd17645 250 ATSFEIDKPYANipIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE-----GLARGYLNRPELTAEKFIVHpfvpgerM 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 444 YNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLnpeflshDQE 523
Cdd:cd17645 325 YRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA-------PEE 397
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 18381087 524 QLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd17645 398 IPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
219-565 |
1.20e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.58 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 219 IFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSDILWCMSdPGWILATVGCLIEPWTSGCTVFIHHLPQF-DPKV 297
Cdd:PRK12316 3201 VIYTSGSTGKPKGVGIRHS-ALSNHLCWMQQAYGLGVGDRVLQFT-TFSFDVFVEELFWPLMSGARVVLAGPEDWrDPAL 3278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 298 IVEVLFKYPITQCLAAPGVYRMVLQQKTSNlRFPTLEHCTTGGESLLPEEYEQWKqrTGLSIHEVYGQSETGISSATLRE 377
Cdd:PRK12316 3279 LVELINSEGVDVLHAYPSMLQAFLEEEDAH-RCTSLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEATITVTHWQC 3355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 378 MKIKRGS--IGKAILPFDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEYENSPESTSE-------VECGDFYNS 446
Cdd:PRK12316 3356 VEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGelYLG-------GEGLARGYHNRPGLTAErfvpdpfVPGERLYRT 3428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 447 GDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSspdkDRGEVVKAFIVLNPEflshdQEQLI 526
Cdd:PRK12316 3429 GDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE-----AGDLR 3499
|
330 340 350
....*....|....*....|....*....|....*....
gi 18381087 527 KELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:PRK12316 3500 EALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
74-568 |
4.94e-23 |
|
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: 102.55 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 74 NGQGDEIKWSfrKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQIS 153
Cdd:cd05932 1 GGQVVEFTWG--EVADKARRLAAALRAL-GLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 154 RAKAIV--------TTASLVPE-VESVASECPDlktklvvSDHSHEGWLDfcsLIKSASPDHTCIKSKMKDPMAIFFTSG 224
Cdd:cd05932 78 ESKALFvgklddwkAMAPGVPEgLISISLPPPS-------AANCQYQWDD---LIAQHPPLEERPTRFPEQLATLIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 225 TTGYPKMAKHNqglaFRSYIPSCRKL---LKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTV--------FIHHLPQF 293
Cdd:cd05932 148 TTGQPKGVMLT----FGSFAWAAQAGiehIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesldtFVEDVQRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 294 DPKviveVLFKYPITQCLAAPGVYRMVLQQKTSN-LRFPT--------------LEHC--TTGGESLLPEEYEQWKQRTG 356
Cdd:cd05932 224 RPT----LFFSVPRLWTKFQQGVQDKIPQQKLNLlLKIPVvnslvkrkvlkglgLDQCrlAGCGSAPVPPALLEWYRSLG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 357 LSIHEVYGQSETGISSATLREMKIKRGSIGKAiLPfDLQI-IDEKGNILppntegyigirikpTRPLGLFMEYENSPEST 435
Cdd:cd05932 300 LNILEAYGMTENFAYSHLNYPGRDKIGTVGNA-GP-GVEVrISEDGEIL--------------VRSPALMMGYYKDPEAT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 436 SEVECGD-FYNSGDRATIDEEGYIWFLGRGDDVINAS-GYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVL 513
Cdd:cd05932 364 AEAFTADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLSEEA 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18381087 514 NPEFLSHDQEQLIKELQHHVKSVTA---PYKYPRKVEFVSElPKTV-------TGKIKRKELRNK 568
Cdd:cd05932 444 RLRADAFARAELEASLRAHLARVNStldSHEQLAGIVVVKD-PWSIdngiltpTLKIKRNVLEKA 507
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
182-566 |
1.49e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 101.26 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 182 LVVSDHShegWLDFCSLIKSASPdHTCIKskMKDPMAIFFTSGTTGYPKMAKHNQG-LAFRSYIPSCRklLKLKTSDILW 260
Cdd:PRK13388 124 LDVDTPA---YAELVAAAGALTP-HREVD--AMDPFMLIFTSGTTGAPKAVRCSHGrLAFAGRALTER--FGLTRDDVCY 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 261 CmSDP---------GW--ILATVGCLIEPWTSGCTVFihhLPqfDPKVIVEVLFKY---PITQCLAAPGvyrmvLQQKTS 326
Cdd:PRK13388 196 V-SMPlfhsnavmaGWapAVASGAAVALPAKFSASGF---LD--DVRRYGATYFNYvgkPLAYILATPE-----RPDDAD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 327 NlrfpTLEHcTTGGESLlPEEYEQWKQRTGLSIHEVYGQSETGISsaTLREMKIKRGSIGKailPFDLQII--------- 397
Cdd:PRK13388 265 N----PLRV-AFGNEAS-PRDIAEFSRRFGCQVEDGYGSSEGAVI--VVREPGTPPGSIGR---GAPGVAIynpetltec 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 398 -----DEKGNILppNTEGYIGiRIKPTRPLGLFMEYENSPESTSEVECGDFYNSGDRATIDEEGYIWFLGRGDDVINASG 472
Cdd:PRK13388 334 avarfDAHGALL--NADEAIG-ELVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDG 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 473 YRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNP----------EFLsHDQEQLikelqhhvksvtAPYKY 542
Cdd:PRK13388 411 ENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDgatfdpdafaAFL-AAQPDL------------GTKAW 477
|
410 420
....*....|....*....|....
gi 18381087 543 PRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK13388 478 PRYVRIAADLPSTATNKVLKRELI 501
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
219-565 |
1.52e-22 |
|
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: 100.97 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 219 IFFTSGTTGYPK--MAKHNqglAFRSYIPSCRKLLKLKTSD-ILWCMS---DpgwilATVGCLIEPWTSGCTVFIH-HLP 291
Cdd:cd17644 111 VIYTSGSTGKPKgvMIEHQ---SLVNLSHGLIKEYGITSSDrVLQFASiafD-----VAAEEIYVTLLSGATLVLRpEEM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 292 QFDPKVIVEVLFKYPITqCLAAPGVYRMVLQQKTSNLRFPTLEH---CTTGGESLLPEEYEQWKQRTGLSIH--EVYGQS 366
Cdd:cd17644 183 RSSLEDFVQYIQQWQLT-VLSLPPAYWHLLVLELLLSTIDLPSSlrlVIVGGEAVQPELVRQWQKNVGNFIQliNVYGPT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 367 ETGISSA-----TLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEYENSPESTSE-- 437
Cdd:cd17644 262 EATIAATvcrltQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGelHIG-------GVGLARGYLNRPELTAEkf 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 438 -------VECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAF 510
Cdd:cd17644 335 ishpfnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAY 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 18381087 511 IVlnPEFlshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd17644 415 IV--PHY---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
83-570 |
2.48e-22 |
|
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: 100.83 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 83 SFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEW---W--LVTVGCMrtgIIFMPgtTQLKAKDILYRIQISRAKA 157
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWlgLAKLGCP---VAFLN--TNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 158 IVTTASLVPEVESVaseCPDLKTK----LVVSDHS-HEGWLDFCSLIKSASPDHTCI----KSKMKDPMAIFFTSGTTGY 228
Cdd:cd05938 82 LVVAPELQEAVEEV---LPALRADgvsvWYLSHTSnTEGVISLLDKVDAASDEPVPAslraHVTIKSPALYIYTSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 229 PKMAK--HNQGLAFRSYIPSCrkllKLKTSDI------LWCMSdpGWILATVGCLiepwTSGCTVFIHhlPQFDPKVIVE 300
Cdd:cd05938 159 PKAARisHLRVLQCSGFLSLC----GVTADDViyitlpLYHSS--GFLLGIGGCI----ELGATCVLK--PKFSASQFWD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 301 VLFKYPITqclaapgvyrmVLQQKTSNLRF-----PTLEHCT-----TGGESLLPEEYEQWKQRTG-LSIHEVYGQSETG 369
Cdd:cd05938 227 DCRKHNVT-----------VIQYIGELLRYlcnqpQSPNDRDhkvrlAIGNGLRADVWREFLRRFGpIRIREFYGSTEGN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 370 ISsatLREMKIKRGSIGKA------ILPFDL---------QIIDEKGNILPPNTeGYIGIRIKPTRPLGLFMEYENSPES 434
Cdd:cd05938 296 IG---FFNYTGKIGAVGRVsylyklLFPFELikfdvekeePVRDAQGFCIPVAK-GEPGLLVAKITQQSPFLGYAGDKEQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 435 TSE------VECGD-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAV--VSSPDKDrGE 505
Cdd:cd05938 372 TEKkllrdvFKKGDvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPGHE-GR 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18381087 506 VVKAFIVLNP--EFlshDQEQLIKelqhHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKEF 570
Cdd:cd05938 451 IGMAAVKLKPghEF---DGKKLYQ----HVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEEGF 510
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
95-567 |
4.50e-22 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 100.24 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 95 ANVFEQICGLQQGDHLALILPRVPEWW--LVTVGCMrtGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVA 172
Cdd:PRK05620 52 AHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 173 SECPDLKTKLVVSDH----------SHEGWLDFCSLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKmakhnqGLAFrs 242
Cdd:PRK05620 130 KECPCVRAVVFIGPSdadsaaahmpEGIKVYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPK------GVVY-- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 243 yipSCRKL----LKLKTSD---------ILWCMsdPGWILATVGCLIEPWTSGcTVFIHHLPQFDPKVIVEVLFKYPITQ 309
Cdd:PRK05620 202 ---SHRSLylqsLSLRTTDslavthgesFLCCV--PIYHVLSWGVPLAAFMSG-TPLVFPGPDLSAPTLAKIIATAMPRV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 310 CLAAPGVY--RMVLQQKTSNLRFpTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSET-----------GISSATLR 376
Cdd:PRK05620 276 AHGVPTLWiqLMVHYLKNPPERM-SLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETspvgtvarppsGVSGEARW 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 377 EMKIKRGSIGKAIlpfDLQIIDEkGNILPPN--TEGYIGIRiKPTRPLGLF---MEYENSPEST---SEVECGD------ 442
Cdd:PRK05620 355 AYRVSQGRFPASL---EYRIVND-GQVMESTdrNEGEIQVR-GNWVTASYYhspTEEGGGAASTfrgEDVEDANdrftad 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 443 -FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNP--EFLS 519
Cdd:PRK05620 430 gWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPgiEPTR 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 18381087 520 HDQEQLIKELQHHVKSVTAPYKYprkvEFVSELPKTVTGKIKRKELRN 567
Cdd:PRK05620 510 ETAERLRDQLRDRLPNWMLPEYW----TFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
122-568 |
4.71e-22 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 99.58 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 122 LVT-VGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESV----ASECPDLKTKLVVSDHSHegwldfc 196
Cdd:PRK04813 66 LATfLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEILGIpvitLDELKDIFATGNPYDFDH------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 197 sliksaspdhtCIKSKmkDPMAIFFTSGTTGYPKMAK--HNQGLAFRSyipscrkllklktsdilWCMSD------PGW- 267
Cdd:PRK04813 139 -----------AVKGD--DNYYIIFTSGTTGKPKGVQisHDNLVSFTN-----------------WMLEDfalpegPQFl 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 268 ----------ILATVGCLiepwTSGCTVFIhhLPQ---FDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLR-FPTL 333
Cdd:PRK04813 189 nqapysfdlsVMDLYPTL----ASGGTLVA--LPKdmtANFKQLFETLPQLPINVWVSTPSFADMCLLDPSFNEEhLPNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 334 EH---CttgGESLLPEEYEQWKQRTGLS-IHEVYGQSET--GISS-ATLREM--KIKRGSIGKAILPFDLQIIDEKGNIL 404
Cdd:PRK04813 263 THflfC---GEELPHKTAKKLLERFPSAtIYNTYGPTEAtvAVTSiEITDEMldQYKRLPIGYAKPDSPLLIIDEEGTKL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 405 PPNTEGYIGIrIKPTRPLGlfmeYENSPESTSEVecgdF--------YNSGDRATIDEeGYIWFLGRGDDVINASGYRIG 476
Cdd:PRK04813 340 PDGEQGEIVI-SGPSVSKG----YLNNPEKTAEA----FftfdgqpaYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 477 PVEVENALAEHPAVAESAVVssPDKDRGEVVK--AFIVLNPeflsHDQE---QLIKELQHHVKSVTAPYKYPRKVEFVSE 551
Cdd:PRK04813 410 LEEIEQNLRQSSYVESAVVV--PYNKDHKVQYliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRKFIYRDS 483
|
490
....*....|....*..
gi 18381087 552 LPKTVTGKIKRKELRNK 568
Cdd:PRK04813 484 LPLTPNGKIDRKALIEE 500
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
73-567 |
6.67e-22 |
|
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: 98.54 E-value: 6.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 73 VNGQGDEIkwSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQI 152
Cdd:cd17653 16 VESLGGSL--TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 153 SRAKAIVTTASlvpevesvasecpdlktklvvsdhshegwldfcsliksasPDhtcikskmkDPMAIFFTSGTTGYPK-- 230
Cdd:cd17653 93 SGATLLLTTDS----------------------------------------PD---------DLAYIIFTSGSTGIPKgv 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 231 MAKHnQGLAfrSYIPSCRKLLKLKTSD-ILWCMS---DP--GWILATVGcliepwtSGCTVFI--HHLPQFDPKVIVEVL 302
Cdd:cd17653 124 MVPH-RGVL--NYVSQPPARLDVGPGSrVAQVLSiafDAciGEIFSTLC-------NGGTLVLadPSDPFAHVARTVDAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 303 fkyPITqclaaPGVYRMVLQQktsnlRFPTLEHCTTGGESLLPEEYEQWKQrtGLSIHEVYGQSETGISSATLREMKIKR 382
Cdd:cd17653 194 ---MST-----PSILSTLSPQ-----DFPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 383 GSIGKAILPFDLQIIDEKGNILPPNTEGYIGIRikptrPLGLFMEYENSPESTSE--VECGD-----FYNSGDRATIDEE 455
Cdd:cd17653 259 VTIGKPIPNSTCYILDADLQPVPEGVVGEICIS-----GVQVARGYLGNPALTASkfVPDPFwpgsrMYRTGDYGRWTED 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 456 GYIWFLGRGDDVINASGYRIG-PVEVENALAEHPAVAESAVVSSpdkdrGEVVKAFIVlnPEflSHDQEQLIKELQHHVK 534
Cdd:cd17653 334 GGLEFLGREDNQVKVRGFRINlEEIEEVVLQSQPEVTQAAAIVV-----NGRLVAFVT--PE--TVDVDGLRSELAKHLP 404
|
490 500 510
....*....|....*....|....*....|...
gi 18381087 535 SvtapYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:cd17653 405 S----YAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
78-565 |
9.10e-22 |
|
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: 98.50 E-value: 9.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 78 DEIKWSFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMP-GTTQLKAkdilyriqisRAK 156
Cdd:cd12114 9 GDGTLTYGELAERARRVAGALKA-AGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPvDIDQPAA----------RRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AIVTTASLvpevesvasecpdlktKLVVSDH--SHEGWLDFCSLIKSASPDHT-----CIKSKMKDPMAIFFTSGTTGYP 229
Cdd:cd12114 78 AILADAGA----------------RLVLTDGpdAQLDVAVFDVLILDLDALAApapppPVDVAPDDLAYVIFTSGSTGTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 230 K--MAKHNqglAFRSYIPSCRKLLKLKTSDILWCMSDPGWILAtVGCLIEPWTSGCT-VFIHHLPQFDPKVIVEVLFKYP 306
Cdd:cd12114 142 KgvMISHR---AALNTILDINRRFAVGPDDRVLALSSLSFDLS-VYDIFGALSAGATlVLPDEARRRDPAHWAELIERHG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 307 ITQCLAAPGVYRMVL------QQKTSNLRFPTLehcttGGESL---LPEEYeqWKQRTGLSIHEVYGQSETGISSATLRE 377
Cdd:cd12114 218 VTLWNSVPALLEMLLdvleaaQALLPSLRLVLL-----SGDWIpldLPARL--RALAPDARLISLGGATEASIWSIYHPI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 378 MKIKR--GSI--GKailPFDLQ---IIDEKGNILPPNTEG--YIGIRikptrplGLFMEYENSPESTSE--VECGD---F 443
Cdd:cd12114 291 DEVPPdwRSIpyGR---PLANQryrVLDPRGRDCPDWVPGelWIGGR-------GVALGYLGDPELTAArfVTHPDgerL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 444 YNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDrGEVVKAFIVLNPEFLSHDQE 523
Cdd:cd12114 361 YRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG-GKRLAAFVVPDNDGTPIAPD 439
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 18381087 524 QLIKELQHHVKSvtapYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd12114 440 ALRAFLAQTLPA----YMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
110-573 |
1.36e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 100.03 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 110 LALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTaslvpevESVASECPdLKTKLVVSDHSH 189
Cdd:PRK12316 2056 VAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQ-------RHLLERLP-LPAGVARLPLDR 2127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 190 EGWLdfcslikSASPDHTCIKSKMKDPMA-IFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSD-ILWCMS---D 264
Cdd:PRK12316 2128 DAEW-------ADYPDTAPAVQLAGENLAyVIYTSGSTGLPKGVAVSHG-ALVAHCQAAGERYELSPADcELQFMSfsfD 2199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 265 pgwilATVGCLIEPWTSGCTVFIHHLPQFDPKVIVEVLFKYPITqCLAAPGVYrmvLQQKTSNL----RFPTLEHCTTGG 340
Cdd:PRK12316 2200 -----GAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVT-ILDFPPVY---LQQLAEHAerdgRPPAVRVYCFGG 2270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 341 ESLLPEEYEQWKQRT-GLSIHEVYGQSETGISSaTLREMKIKRGS------IGKAILPFDLQIIDEKGNILPPNTEG--Y 411
Cdd:PRK12316 2271 EAVPAASLRLAWEALrPVYLFNGYGPTEAVVTP-LLWKCRPQDPCgaayvpIGRALGNRRAYILDADLNLLAPGMAGelY 2349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 412 IGirikptrPLGLFMEYENSPESTSEVECGD--------FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENA 483
Cdd:PRK12316 2350 LG-------GEGLARGYLNRPGLTAERFVPDpfsasgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEAR 2422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 484 LAEHPAVAESAVVSSpDKDRGEVVKAFIVlnPEFLshdQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRK 563
Cdd:PRK12316 2423 LQAHPAVREAVVVAQ-DGASGKQLVAYVV--PDDA---AEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRK 2496
|
490
....*....|
gi 18381087 564 ELRNKEFGQL 573
Cdd:PRK12316 2497 ALPKPDVSQL 2506
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
81-570 |
1.46e-21 |
|
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: 97.88 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 81 KWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVT 160
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 161 taslvpevesvasecpDLKTKLvvsdhshegwldfcsliKSASPDH--TCIKSKMKDPMAIFFTSGTTGYPKMA--KHnq 236
Cdd:cd05939 82 ----------------NLLDPL-----------------LTQSSTEppSQDDVNFRDKLFYIYTSGTTGLPKAAviVH-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 237 glaFRSYIPSC--RKLLKLKTSDILW-CMS---DPGWILATVGCLIepwtSGCTVFIHHlpQFDPKVIVEVLFKYPITQC 310
Cdd:cd05939 127 ---SRYYRIAAgaYYAFGMRPEDVVYdCLPlyhSAGGIMGVGQALL----HGSTVVIRK--KFSASNFWDDCVKYNCTIV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 311 LAAPGVYRMVLQQKTS------NLRFPTlehcttgGESLLPEEYEQWKQRTGLS-IHEVYGQSEtgiSSATLREMKIKRG 383
Cdd:cd05939 198 QYIGEICRYLLAQPPSeeeqkhNVRLAV-------GNGLRPQIWEQFVRRFGIPqIGEFYGATE---GNSSLVNIDNHVG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 384 SIG--KAILPF--DLQII-----------DEKGNILP--PNTEGYIGIRIKPTRPLGLFMEYENSPESTSEV-----ECG 441
Cdd:cd05939 268 ACGfnSRILPSvyPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIardvfKKG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 442 D-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAV--VSSPdKDRGEVVKAFIVlNPEfL 518
Cdd:cd05939 348 DsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVP-GVEGRAGMAAIV-DPE-R 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 18381087 519 SHDQEQLIKELQhhvkSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKEF 570
Cdd:cd05939 425 KVDLDRFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGY 472
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
111-565 |
2.94e-21 |
|
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: 96.55 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 111 ALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASlvpevesvasecpdlktklvvsdhshe 190
Cdd:cd17652 41 ALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTTPD--------------------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 191 gwldfcsliksaspdhtcikskmkDPMAIFFTSGTTGYPK--MAKHnQGLAfrSYIPSCRKLLKLK-TSDILWCMSdPGW 267
Cdd:cd17652 94 ------------------------NLAYVIYTSGSTGRPKgvVVTH-RGLA--NLAAAQIAAFDVGpGSRVLQFAS-PSF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 268 IlATVGCLIEPWTSGCTVfihHLPQFDPKV----IVEVLFKYPITQCLAAPGVYRMVlqqKTSNLrfPTLEHCTTGGESL 343
Cdd:cd17652 146 D-ASVWELLMALLAGATL---VLAPAEELLpgepLADLLREHRITHVTLPPAALAAL---PPDDL--PDLRTLVVAGEAC 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 344 LPEEYEQWKQrtGLSIHEVYGQSETGISsATLREMKIKRGS--IGKAILPFDLQIIDEKGNILPPNTEG--YIGirikpt 419
Cdd:cd17652 217 PAELVDRWAP--GRRMINAYGPTETTVC-ATMAGPLPGGGVppIGRPVPGTRVYVLDARLRPVPPGVPGelYIA------ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 420 rPLGLFMEYENSPESTSE--VEC------GDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVA 491
Cdd:cd17652 288 -GAGLARGYLNRPGLTAErfVADpfgapgSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVA 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18381087 492 ESAVVSSPDKDRGEVVKAFIVLNPeflshDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd17652 367 EAVVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
215-567 |
6.58e-21 |
|
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: 96.07 E-value: 6.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPK--MAKHnqgLAFRSYIPSCRKLLKLKTSD-ILW--------CMSDpgwILATvgcliepWTSGC 283
Cdd:cd05918 107 DAAYVIFTSGSTGKPKgvVIEH---RALSTSALAHGRALGLTSESrVLQfasytfdvSILE---IFTT-------LAAGG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 284 TVFIhhLPQFD-----PKVIVEvlfkYPITQCLAAPGVYRMvLQQKTsnlrFPTLEHCTTGGESLLPEEYEQWKQRTGLs 358
Cdd:cd05918 174 CLCI--PSEEDrlndlAGFINR----LRVTWAFLTPSVARL-LDPED----VPSLRTLVLGGEALTQSDVDTWADRVRL- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 359 iHEVYGQSETGISSaTLREMKI--KRGSIGKAIlPFDLQIIDekgnilPPNTEGYIgirikptrPLG----LFME----- 427
Cdd:cd05918 242 -INAYGPAECTIAA-TVSPVVPstDPRNIGRPL-GATCWVVD------PDNHDRLV--------PIGavgeLLIEgpila 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 428 --YENSPESTSEV---------ECGD-----FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVA 491
Cdd:cd05918 305 rgYLNDPEKTAAAfiedpawlkQEGSgrgrrLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 492 ESAVV---SSPDKDRGEVVKAFIVLNPEFLSHDQEQ------------LIKELQHHVKSVTAPYKYPRKVEFVSELPKTV 556
Cdd:cd05918 385 KEVVVevvKPKDGSSSPQLVAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTA 464
|
410
....*....|.
gi 18381087 557 TGKIKRKELRN 567
Cdd:cd05918 465 SGKIDRRALRE 475
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
196-565 |
1.08e-20 |
|
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: 94.85 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 196 CSLIKSASPDHTCIKSKMKDPMA-IFFTSGTTGYPKMAK--HNqglAFRSYIPSCRKLLKLKTSDILWCMS----DPgwi 268
Cdd:cd17654 99 DNAPLSFTPEHRHFNIRTDECLAyVIHTSGTTGTPKIVAvpHK---CILPNIQHFRSLFNITSEDILFLTSpltfDP--- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 269 laTVGCLIEPWTSGCTVFI-HHLPQFDPKVIVEVLFKYPITQCL-AAPGVYRMVLQQ--------KTSNLRFPTLehctt 338
Cdd:cd17654 173 --SVVEIFLSLSSGATLLIvPTSVKVLPSKLADILFKRHRITVLqATPTLFRRFGSQsikstvlsATSSLRVLAL----- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 339 GGE---SLLpeEYEQWKQR-TGLSIHEVYGQSETGiSSATLREMKIKRGS--IGKAILPFDLQIIDEKGNILPPNTEGYI 412
Cdd:cd17654 246 GGEpfpSLV--ILSSWRGKgNRTRIFNIYGITEVS-CWALAYKVPEEDSPvqLGSPLLGTVIEVRDQNGSEGTGQVFLGG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 413 GIRIKPTRplglfmEYENSPESTsevecgdFYNSGDRATIdEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVaE 492
Cdd:cd17654 323 LNRVCILD------DEVTVPKGT-------MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-E 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18381087 493 SAVVSSPDKDRgevVKAFIVLNPeflSHDQEQliKELQHHVKSvtaPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd17654 388 SCAVTLSDQQR---LIAFIVGES---SSSRIH--KELQLTLLS---SHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
77-518 |
1.22e-20 |
|
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: 95.12 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 77 GDEIKWSFRKLRDLTCRTANvFEQICGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAK 156
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAA-GLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 AivttaslvpevesvasecpdlktkLVVSDHShegwldfcsliksaspdhtcikskmKDPMAIFFTSGTTGYPK--MAKH 234
Cdd:cd17640 80 A------------------------LVVENDS-------------------------DDLATIIYTSGTTGNPKgvMLTH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 235 nQGLAFRsyIPSCRKLLKLKTSDILWCMSdPGW---------ILATVGClIEPWTSgctvfIHHLPQ----FDPKVIVEV 301
Cdd:cd17640 111 -ANLLHQ--IRSLSDIVPPQPGDRFLSIL-PIWhsyersaeyFIFACGC-SQAYTS-----IRTLKDdlkrVKPHYIVSV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 302 ------LFKYPITQCLAAPGVYRMVLQQKTS--NLRFPTlehctTGGESLlPEEYEQWKQRTGLSIHEVYGQSETGISSA 373
Cdd:cd17640 181 prlwesLYSGIQKQVSKSSPIKQFLFLFFLSggIFKFGI-----SGGGAL-PPHVDTFFEAIGIEVLNGYGLTETSPVVS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 374 TLREMKIKRGSIGKAILPFDLQIIDEKGN-ILPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVECGD-FYNSGDRAT 451
Cdd:cd17640 255 ARRLKCNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVR-GPQVMKG----YYKNPEATSKVLDSDgWFNTGDLGW 329
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18381087 452 IDEEGYIWFLGRGDDVINAS-GYRIGPVEVENALAEHPAVAESAVVSSPDKDRGevvkAFIVLNPEFL 518
Cdd:cd17640 330 LTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG----ALIVPNFEEL 393
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-572 |
6.96e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.64 E-value: 6.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 36 WNDhdSPEEFNFASDVLDYWAQMEEEGKRGPSPAFwwvngqgDEIKWSFRKLRdltcRTANVFE---QICGLQQGDHLAL 112
Cdd:PRK12316 500 WNA--TAAEYPLQRGVHRLFEEQVERTPEAPALAF-------GEETLDYAELN----RRANRLAhalIERGVGPDVLVGV 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 113 ILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVesvasecpDLKTKLVVSDhshegw 192
Cdd:PRK12316 567 AMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL--------PLAAGVQVLD------ 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 193 LDFCSLIKSASPDHTCIKSKMKDPMA-IFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSDILwCMSDPGWILAT 271
Cdd:PRK12316 633 LDRPAAWLEGYSEENPGTELNPENLAyVIYTSGSTGKPKGAGNRHR-ALSNRLCWMQQAYGLGVGDTV-LQKTPFSFDVS 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 272 VGCLIEPWTSGCTvfIHHLPQ---FDPKVIVEVLFKYPITqclaapgVYRMVLQQKTSNLRFPTLEHCTT------GGES 342
Cdd:PRK12316 711 VWEFFWPLMSGAR--LVVAAPgdhRDPAKLVELINREGVD-------TLHFVPSMLQAFLQDEDVASCTSlrrivcSGEA 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 343 L---LPEEYEQWKQRTGLsiHEVYGQSETGISSA--TLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEG--YIGIR 415
Cdd:PRK12316 782 LpadAQEQVFAKLPQAGL--YNLYGPTEAAIDVThwTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGelYLAGR 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 416 ikptrplGLFMEYENSPESTSE-------VECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHP 488
Cdd:PRK12316 860 -------GLARGYHGRPGLTAErfvpspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 932
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 489 AVAESAVVSspdKDRGEVVkAFIVLNPEFLShdqeqLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNK 568
Cdd:PRK12316 933 WVREAAVLA---VDGKQLV-GYVVLESEGGD-----WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAP 1003
|
....
gi 18381087 569 EFGQ 572
Cdd:PRK12316 1004 EASV 1007
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
210-566 |
2.41e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 92.29 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 210 KSKMKDPMAIFFTSGTTGYPK--MAKHNQGLafrSYIPSCRKLLKLKTSDILwCMSDP-----GWILATVGCLIEpwtsG 282
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKgvMLSHHNIL---SNIEQISDVFNLRNDDVI-LSSLPffhsfGLTVTLWLPLLE----G 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 283 CTVfIHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVL-QQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHE 361
Cdd:PRK08633 850 IKV-VYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLrNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILE 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 362 VYGQSET-GISSATLREMKI---------KRGSIGKAILPFDLQIID-EKGNILPPNTEGYIGIRiKPTRPLGlfmeYEN 430
Cdd:PRK08633 929 GYGATETsPVASVNLPDVLAadfkrqtgsKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG-GPQVMKG----YLG 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 431 SPESTSEV----ECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEhpAVAES----AVVSSPDKD 502
Cdd:PRK08633 1004 DPEKTAEVikdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK--ALGGEevvfAVTAVPDEK 1081
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18381087 503 RGEVVkafIVLnpeflsHDQEQLIKE--LQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK08633 1082 KGEKL---VVL------HTCGAEDVEelKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLK 1138
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
219-565 |
2.49e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 92.92 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 219 IFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSDIlWCMSDPGWILATVGCLIEPWTSGCTVFI----HHLpqfD 294
Cdd:PRK12467 1723 VIYTSGSTGRPKGAGNRHG-ALVNRLCATQEAYQLSAADV-VLQFTSFAFDVSVWELFWPLINGARLVIappgAHR---D 1797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 295 PKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTG-LSIHEVYGQSETGISsA 373
Cdd:PRK12467 1798 PEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVD-V 1876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 374 TLRemKIKRGS--------IGKAILPFDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEYENSPESTSE------ 437
Cdd:PRK12467 1877 THW--TCRRKDlegrdsvpIGQPIANLSTYILDASLNPVPIGVAGelYLG-------GVGLARGYLNRPALTAErfvadp 1947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 438 --VECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSpDKDRGEVVKAFIV-LN 514
Cdd:PRK12467 1948 fgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVpTD 2026
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 18381087 515 PEFLSHDQEQ--LIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:PRK12467 2027 PGLVDDDEAQvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
445-565 |
2.76e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 90.48 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 445 NSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFlshDQEQ 524
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEI---DPVQ 370
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 18381087 525 LIKELQHHVksvtAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:PRK08308 371 LREWCIQHL----APYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
216-567 |
3.46e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 91.34 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 216 PMAIFFTSGTTGYPKMAKHNQG--LAFRSYIPSCRKLLKLKTsdILWCMSDPGWI--------LATVGCLIEPWTSGCTV 285
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNGphLVGLKYYWRSIIEKDIPT--VVFSHSSIGWVsfhgflygSLSLGNTFVMFEGGIIK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 286 FIHHLPQFdpkviVEVLFKYPITQCLAAPGVYRMVLQ------QKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTGLSI 359
Cdd:PTZ00237 334 NKHIEDDL-----WNTIEKHKVTHTLTLPKTIRYLIKtdpeatIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 360 HEVYGQSETGISSatLREMKIKRGSIGKAILPFDL---QIIDEKGNILPPNTEGYIGIRIkPTRPLGLFMEYENSpESTS 436
Cdd:PTZ00237 409 SRGYGQTEIGITY--LYCYGHINIPYNATGVPSIFikpSILSEDGKELNVNEIGEVAFKL-PMPPSFATTFYKND-EKFK 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 437 EV--ECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLN 514
Cdd:PTZ00237 485 QLfsKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLK 564
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 18381087 515 PEFLSH--DQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRN 567
Cdd:PTZ00237 565 QDQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
49-566 |
4.79e-19 |
|
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: 90.42 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 49 SDVLDYWAqmEEEGKRGPSpafwWVNGQGDEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPR----VPEWWlvt 124
Cdd:cd05906 13 LELLLRAA--ERGPTKGIT----YIDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 125 vGCMRTGII------FMPGTTQLKAKDILYRI-QISRAKAIVTTASLVPEVESVASECPdlktklvvsdhsHEGW-LDFC 196
Cdd:cd05906 83 -ACVLAGFVpapltvPPTYDEPNARLRKLRHIwQLLGSPVVLTDAELVAEFAGLETLSG------------LPGIrVLSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 197 SLIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQglafrsyipscRKLLKLKTSDILWCMSDPG-----WI-LA 270
Cdd:cd05906 150 EELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTH-----------RNILARSAGKIQHNGLTPQdvflnWVpLD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 271 TVGCLIE----PWTSGC-TVFIH--HLPQfDPKVIVEVLFKYPITQCLAAPGVYRMVLQQ------KT---SNLRFptle 334
Cdd:cd05906 219 HVGGLVElhlrAVYLGCqQVHVPteEILA-DPLRWLDLIDRYRVTITWAPNFAFALLNDLleeiedGTwdlSSLRY---- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 335 hCTTGGESLLPEEYEQWKQ---RTGL---SIHEVYGQSETG---ISSATLREMKIKRG----SIGKAILPFDLQIIDEKG 401
Cdd:cd05906 294 -LVNAGEAVVAKTIRRLLRllePYGLppdAIRPAFGMTETCsgvIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 402 NILPPNTEGYIGIRiKPTrplgLFMEYENSPESTSEVECGD-FYNSGDRATIDEeGYIWFLGRGDDVINASGYRIGPVEV 480
Cdd:cd05906 373 QLLPEGEVGRLQVR-GPV----VTKGYYNNPEANAEAFTEDgWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 481 ENALAEHPAVAES----AVVSSPDKDRGEVVkafIVLNPEFLSHDQ-EQLIKELQHHVK---SVTAPYKYPRKVEfvsEL 552
Cdd:cd05906 447 EAAVEEVPGVEPSftaaFAVRDPGAETEELA---IFFVPEYDLQDAlSETLRAIRSVVSrevGVSPAYLIPLPKE---EI 520
|
570
....*....|....
gi 18381087 553 PKTVTGKIKRKELR 566
Cdd:cd05906 521 PKTSLGKIQRSKLK 534
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
128-570 |
5.55e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 91.76 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 128 MRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASEcpdlkTKLVVSDHSHEGWLDFCSLIksaspdht 207
Cdd:PRK12467 3166 LKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGD-----TALTLDRLDLNGYSENNPST-------- 3232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 208 cikSKMKDPMA-IFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSD-ILWCMS---DPG-----WILATVGCLIe 277
Cdd:PRK12467 3233 ---RVMGENLAyVIYTSGSTGKPKGVGVRHG-ALANHLCWIAEAYELDANDrVLLFMSfsfDGAqerflWTLICGGCLV- 3307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 278 pwtsgctVFIHHLpqFDPKVIVEVLFKYPITQCLAAPGvYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWKQRTG- 356
Cdd:PRK12467 3308 -------VRDNDL--WDPEELWQAIHAHRISIACFPPA-YLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKp 3377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 357 LSIHEVYGQSETGISSATLREMKIKRGS-----IGKAILPFDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEYE 429
Cdd:PRK12467 3378 RGLTNGYGPTEAVVTVTLWKCGGDAVCEapyapIGRPVAGRSIYVLDGQLNPVPVGVAGelYIG-------GVGLARGYH 3450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 430 NSPESTSE-------VECGD-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSpDK 501
Cdd:PRK12467 3451 QRPSLTAErfvadpfSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DG 3529
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18381087 502 DRGEVVKAFIVLNPEflshdQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKEF 570
Cdd:PRK12467 3530 AGGKQLVAYVVPADP-----QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDA 3593
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
81-571 |
7.69e-19 |
|
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: 89.34 E-value: 7.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 81 KWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVt 160
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSL-GLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 161 taslvpevesvasecpdlktklvvsdhshegwLDFCSLIksaspdhtcikskmkdpmaifFTSGTTGYPKMAKHNQGLAF 240
Cdd:cd05940 81 --------------------------------VDAALYI---------------------YTSGTTGLPKAAIISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 241 RSYIPSCRKLLKLKTSDILWCMS---DPGWILATVGCLIepwtSGCTVFIHH---LPQFDPKVIVE--VLFKYPITQC-- 310
Cdd:cd05940 108 RGGAFFAGSGGALPSDVLYTCLPlyhSTALIVGWSACLA----SGATLVIRKkfsASNFWDDIRKYqaTIFQYIGELCry 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 311 -LAAPGV-------YRMVLqqktsnlrfptlehcttgGESLLPEEYEQWKQRTGL-SIHEVYGQSETGISSATLREmkiK 381
Cdd:cd05940 184 lLNQPPKpterkhkVRMIF------------------GNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFINFFG---K 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 382 RGSIGK-----------AILPFDLQ----IIDEKGNILPPNtEGYIGIRIKPTRPLGLFMEYENSPESTSEV-----ECG 441
Cdd:cd05940 243 PGAIGRnpsllrkvaplALVKYDLEsgepIRDAEGRCIKVP-RGEPGLLISRINPLEPFDGYTDPAATEKKIlrdvfKKG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 442 D-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAV--VSSPDKDrGEVVKAFIVLNPEfl 518
Cdd:cd05940 322 DaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTD-GRAGMAAIVLQPN-- 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 18381087 519 shdQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKEFG 571
Cdd:cd05940 399 ---EEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFD 448
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
49-571 |
1.40e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 89.16 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 49 SDVLDYWAQmeeegKRGPSPAfwwVNGQGDEIkwSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCM 128
Cdd:PRK08279 40 GDVFEEAAA-----RHPDRPA---LLFEDQSI--SYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 129 RTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPDLKTKLVVSD---HSHEGWLDFCSLIKSASPD 205
Cdd:PRK08279 109 KLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGdtlDDPEGYEDLAAAAAGAPTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 206 --HTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAFRSYIpSCRKLLKLKTSDILWC----------MSDPGWILATVG 273
Cdd:PRK08279 189 npASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-GFGGLLRLTPDDVLYCclplyhntggTVAWSSVLAAGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 274 CLI--------EPW----TSGCTVFIHhlpqfdpkvIVEVlfkypitqClaapgvyRMVLQQ-KTSNLRFPTLEHCTtgG 340
Cdd:PRK08279 268 TLAlrrkfsasRFWddvrRYRATAFQY---------IGEL--------C-------RYLLNQpPKPTDRDHRLRLMI--G 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 341 ESLLPEEYEQWKQRTGLS-IHEVYGQSETGISSATLREmkiKRGSIGK---------AILPFDLQ----IIDEKGNILPP 406
Cdd:PRK08279 322 NGLRPDIWDEFQQRFGIPrILEFYAASEGNVGFINVFN---FDGTVGRvplwlahpyAIVKYDVDtgepVRDADGRCIKV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 407 NTeGYIGIRIKPTRPLGLFMEYeNSPESTSEV------ECGD-FYNSGDRATIDEEGYIWFLGR-GDDvinasgYR---- 474
Cdd:PRK08279 399 KP-GEVGLLIGRITDRGPFDGY-TDPEASEKKilrdvfKKGDaWFNTGDLMRDDGFGHAQFVDRlGDT------FRwkge 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 475 -IGPVEVENALAEHPAVAESAV--VSSPDKDrGEVVKAFIVLnpeflsHDQEQL-IKELQHHVKSVTAPYKYPRKVEFVS 550
Cdd:PRK08279 471 nVATTEVENALSGFPGVEEAVVygVEVPGTD-GRAGMAAIVL------ADGAEFdLAALAAHLYERLPAYAVPLFVRLVP 543
|
570 580
....*....|....*....|.
gi 18381087 551 ELPKTVTGKIKRKELRNKEFG 571
Cdd:PRK08279 544 ELETTGTFKYRKVDLRKEGFD 564
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
82-568 |
3.72e-18 |
|
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: 87.49 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 82 WSFRKLRDLTCRTANVFEQICGLQQGDHLALILPRVPEW---W--LVTVGCMRTGIifmpgTTQLKAKDILYRIQISRAK 156
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFvflWlgLWSIGAAPAFI-----NYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 157 aivttaslvpevesvasecpdlktkLVVSDhshegwldfcsliksasPDhtcikskmkDPMAIFFTSGTTGYPKMAKHNQ 236
Cdd:cd05937 81 -------------------------FVIVD-----------------PD---------DPAILIYTSGTTGLPKAAAISW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 237 GLAFRSYIPSCRKLLKLKTSDILWCMS---DPGWILATVGCLIepwtSGCTVFIHH---LPQFDPKVIVE--VLFKYPIT 308
Cdd:cd05937 110 RRTLVTSNLLSHDLNLKNGDRTYTCMPlyhGTAAFLGACNCLM----SGGTLALSRkfsASQFWKDVRDSgaTIIQYVGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 309 QC---LAAPgvyrMVLQQKTSNLRFPTlehcttgGESLLPEEYEQWKQRTGLS-IHEVYGQSEtGISSATLREM------ 378
Cdd:cd05937 186 LCrylLSTP----PSPYDRDHKVRVAW-------GNGLRPDIWERFRERFNVPeIGEFYAATE-GVFALTNHNVgdfgag 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 379 KIK-RGSIGKAILPFDLQI--ID-EKGNIL-----------PPNTEGYIGIRIkPTRPLGLFMEYENSPESTSE------ 437
Cdd:cd05937 254 AIGhHGLIRRWKFENQVVLvkMDpETDDPIrdpktgfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESklvrdv 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 438 VECGD-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAV--VSSPDKDrGEVVKAFIVLN 514
Cdd:cd05937 333 FRKGDiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHD-GRAGCAAITLE 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 18381087 515 PEFLSHDQEQLiKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNK 568
Cdd:cd05937 412 ESSAVPTEFTK-SLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
215-565 |
4.53e-18 |
|
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: 86.75 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPK--MAKH----NQGLAFRSyipscRKLLKLKTSDILWCMSDPGWILAtvGCLIEPWTSGCTVFIh 288
Cdd:cd17650 94 DLAYVIYTSGTTGKPKgvMVEHrnvaHAAHAWRR-----EYELDSFPVRLLQMASFSFDVFA--GDFARSLLNGGTLVI- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 289 hLPQ---FDPKVIVEVLFKYPITQCLAAPGVYRMVLQQKTSN-LRFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEV-- 362
Cdd:cd17650 166 -CPDevkLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNgLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIIns 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 363 YGQSETGISSATLREMKIKRGS-----IGKAILPFDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEYENSPEST 435
Cdd:cd17650 245 YGVTEATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLDERLQPQPVGVAGelYIG-------GAGVARGYLNRPELT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 436 SE-------VECGDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVK 508
Cdd:cd17650 318 AErfvenpfAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLC 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18381087 509 AFIV----LNPEFLshdQEQLIKELqhhvksvtAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd17650 398 AYVVaaatLNTAEL---RAFLAKEL--------PSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
78-565 |
8.73e-18 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 87.41 E-value: 8.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 78 DEIKWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKA 157
Cdd:PRK10252 480 ARYQFSYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 158 IVTTASL---VPEVESVASECPDlkTKLVVSDHSHEGwldfcslikSASPDHTCIkskmkdpmaIFFTSGTTGYPK--MA 232
Cdd:PRK10252 559 LITTADQlprFADVPDLTSLCYN--APLAPQGAAPLQ---------LSQPHHTAY---------IIFTSGSTGRPKgvMV 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 233 KH----NQGLAFRSYIP--SCRKLLKlKTSdilwCMSDpgwilATVGCLIEPWTSGCTVFI-----HHlpqfDPKVIVEV 301
Cdd:PRK10252 619 GQtaivNRLLWMQNHYPltADDVVLQ-KTP----CSFD-----VSVWEFFWPFIAGAKLVMaepeaHR----DPLAMQQF 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 302 LFKYPITQCLAAPGVYRMVLQQKTSNLRFP---TLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGIS----SAT 374
Cdd:PRK10252 685 FAEYGVTTTHFVPSMLAAFVASLTPEGARQscaSLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDvswyPAF 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 375 LREMKIKRGS---IGKAILPFDLQIIDEKGNILPPNTEG--YI-GIRikptrplgLFMEYENSPESTSE-------VECG 441
Cdd:PRK10252 765 GEELAAVRGSsvpIGYPVWNTGLRILDARMRPVPPGVAGdlYLtGIQ--------LAQGYLGRPDLTASrfiadpfAPGE 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 442 DFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHP----AVAESAVVSSPDKDRGEVVK--AFIVlnp 515
Cdd:PRK10252 837 RMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQAAATGGDARQlvGYLV--- 913
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 18381087 516 eflSHDQEQL-IKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:PRK10252 914 ---SQSGLPLdTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
363-566 |
1.81e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 85.05 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 363 YGQSETGISSATLREMKIKRGSIGKA-ILPfDLQIIdekgniLPPNTEGYIGIRiKPTRPLGLFMEYENSPEstsevecg 441
Cdd:PRK07445 261 YGMTETASQIATLKPDDFLAGNNSSGqVLP-HAQIT------IPANQTGNITIQ-AQSLALGYYPQILDSQG-------- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 442 dFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEFLSHD 521
Cdd:PRK07445 325 -IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18381087 522 qeqlikELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK07445 404 ------ELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
46-560 |
4.17e-17 |
|
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: 84.63 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 46 NFASDVLdywaqmeeEGKRGPSPAFWWVNGQGDEIKWSFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEwwlVTV 125
Cdd:cd05943 71 NYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRA-LGVKPGDRVAGYLPNIPE---AVV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 126 GCMRT---GIIFMPGTTQLKAKDILYRI-QIsRAKAIVTTASLV---------PEVESVASECPDLKTKLVVS----DHS 188
Cdd:cd05943 139 AMLATasiGAIWSSCSPDFGVPGVLDRFgQI-EPKVLFAVDAYTyngkrhdvrEKVAELVKGLPSLLAVVVVPytvaAGQ 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 189 HEG--------WLDFCSLIKSASPDHTciKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAFRSYIpscrKLLKLKT----S 256
Cdd:cd05943 218 PDLskiakaltLEDFLATGAAGELEFE--PLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHL----KEHILHCdlrpG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 257 DILWCMSDPGWIL--ATVGCLIepwtSGCTVFIHHLPQFDPKVivEVLFKYP----ITQCLAAPGvYRMVLQQK----TS 326
Cdd:cd05943 292 DRLFYYTTCGWMMwnWLVSGLA----VGATIVLYDGSPFYPDT--NALWDLAdeegITVFGTSAK-YLDALEKAglkpAE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 327 NLRFPTLEHCTTGGESLLPEE----YEQWKQRTGLSihEVYGQseTGISSA---TLREMKIKRGSIGKAILPFDLQIIDE 399
Cdd:cd05943 365 THDLSSLRTILSTGSPLKPESfdyvYDHIKPDVLLA--SISGG--TDIISCfvgGNPLLPVYRGEIQCRGLGMAVEAFDE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 400 KGNILPpnteGYIG----IRIKPTRPLGL-------------FMEYENspestsevecgdFYNSGDRATIDEEGYIWFLG 462
Cdd:cd05943 441 EGKPVW----GEKGelvcTKPFPSMPVGFwndpdgsryraayFAKYPG------------VWAHGDWIEITPRGGVVILG 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 463 RGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNPEF-LSHDqeqLIKELQHHVKSVTAPYK 541
Cdd:cd05943 505 RSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVeLDDE---LRKRIRSTIRSALSPRH 581
|
570
....*....|....*....
gi 18381087 542 YPRKVEFVSELPKTVTGKI 560
Cdd:cd05943 582 VPAKIIAVPDIPRTLSGKK 600
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
103-524 |
7.24e-17 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 83.63 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 103 GLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIV-----------TTASLVPEVESV 171
Cdd:cd17641 32 GVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIaedeeqvdkllEIADRIPSVRYV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 172 ASECP---------------DLKTKLVVSDHSHEGWLDfcSLIKSASPDHTCIKSkmkdpmaifFTSGTTGYPKMAKhnq 236
Cdd:cd17641 112 IYCDPrgmrkyddprlisfeDVVALGRALDRRDPGLYE--REVAAGKGEDVAVLC---------TTSGTTGKPKLAM--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 237 gLAFRSYIPSCRKLL----KLKTSDILWCMSDPgWILATVGCLIEPWTSGCTVfihHLPQfDPKVIVEVLFKYPITQCLA 312
Cdd:cd17641 178 -LSHGNFLGHCAAYLaadpLGPGDEYVSVLPLP-WIGEQMYSVGQALVCGFIV---NFPE-EPETMMEDLREIGPTFVLL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 313 APGV------------------------------YRMVLQQKTSN------------------------LRFPTLEHCTT 338
Cdd:cd17641 252 PPRVwegiaadvrarmmdatpfkrfmfelgmklgLRALDRGKRGRpvslwlrlaswladallfrplrdrLGFSRLRSAAT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 339 GGESLLPEEYeQWKQRTGLSIHEVYGQSETGISSATLREMKIKRGSIGkaiLPF-DLQI-IDEKGNILppntegyigiri 416
Cdd:cd17641 332 GGAALGPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVG---VPFpGTEVrIDEVGEIL------------ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 417 kpTRPLGLFMEYENSPESTSEVECGD-FYNSGDRATIDEEGYIWFLGRGDDVIN-ASGYRIGPVEVENALAEHPAVAEsA 494
Cdd:cd17641 396 --VRSPGVFVGYYKNPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLKFSPYIAE-A 472
|
490 500 510
....*....|....*....|....*....|
gi 18381087 495 VVSSPDKDRgevVKAFIVLNPEFLSHDQEQ 524
Cdd:cd17641 473 VVLGAGRPY---LTAFICIDYAIVGKWAEQ 499
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
214-565 |
9.06e-17 |
|
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: 82.83 E-value: 9.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 214 KDPMAIFFTSGTTGYPK--MAKHnqglafRSYIPSCRKLLKLktsdilWCMSDPGW--ILATVGCLIEPW--------TS 281
Cdd:cd17648 94 TDLAYAIYTSGTTGKPKgvLVEH------GSVVNLRTSLSER------YFGRDNGDeaVLFFSNYVFDFFveqmtlalLN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 282 GCTVFIhhLPQ---FDPKVIVEVLFKYPITQCLAAPGVyrmvLQQKTSNlRFPTLEHCTTGGESLLPEEYEQWKQRTGLS 358
Cdd:cd17648 162 GQKLVV--PPDemrFDPDRFYAYINREKVTYLSGTPSV----LQQYDLA-RLPHLKRVDAAGEEFTAPVFEKLRSRFAGL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 359 IHEVYGQSETGISSATLREMKIKR--GSIGKAILPFDLQIIDEKGNILPPNTEG--YIGirikptrPLGLFMEYENSPES 434
Cdd:cd17648 235 IINAYGPTETTVTNHKRFFPGDQRfdKSLGRPVRNTKCYVLNDAMKRVPVGAVGelYLG-------GDGVARGYLNRPEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 435 T------------SEVECGDF---YNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSP 499
Cdd:cd17648 308 TaerflpnpfqteQERARGRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKE 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18381087 500 DKDRGEVVK-----AFIVLNPEFLShdqEQlikELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd17648 388 DASQAQSRIqkylvGYYLPEPGHVP---ES---DLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
428-572 |
2.77e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 77.39 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 428 YENSPESTSEVECGDFYNSgDRATIDEeGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVV 507
Cdd:PRK07824 221 YRNPVDPDPFAEPGWFRTD-DLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRV 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18381087 508 KAFIVLNPEflshdQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRnKEFGQ 572
Cdd:PRK07824 299 VAAVVGDGG-----PAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV-RRFAG 357
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
322-565 |
4.39e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.98 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 322 QQKTSNLRFptlehCTTGGESLLPEEYEQWKQR-TGLSIHEVYGQSETGISS-ATLREMKIKRGS----IGKAILPFDLQ 395
Cdd:PRK05691 2444 QGEQLPVRM-----CITGGEALTGEHLQRIRQAfAPQLFFNAYGPTETVVMPlACLAPEQLEEGAasvpIGRVVGARVAY 2518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 396 IIDEKGNILPPNTEG--YIGirikptrPLGLFMEYENSPESTSE--------VECGDFYNSGDRATIDEEGYIWFLGRGD 465
Cdd:PRK05691 2519 ILDADLALVPQGATGelYVG-------GAGLAQGYHDRPGLTAErfvadpfaADGGRLYRTGDLVRLRADGLVEYVGRID 2591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 466 DVINASGYRIGPVEVENALAEHPAVAEsAVVSSPDKDRGEVVKAFIVLNPEFLSHDQEQLIKE-LQHHVKSVTAPYKYPR 544
Cdd:PRK05691 2592 HQVKIRGFRIELGEIESRLLEHPAVRE-AVVLALDTPSGKQLAGYLVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVPA 2670
|
250 260
....*....|....*....|.
gi 18381087 545 KVEFVSELPKTVTGKIKRKEL 565
Cdd:PRK05691 2671 HLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
110-565 |
7.62e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 7.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 110 LALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPdlktklVVSDHSH 189
Cdd:PRK05691 1184 VAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSA------IALDSLH 1257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 190 -EGWldfcsliksasPDHTCIKSKMKDPMA-IFFTSGTTGYPKMAKHNQGlAFRSYIPSCRKLLKLKTSDILWCMSDPGW 267
Cdd:PRK05691 1258 lDSW-----------PSQAPGLHLHGDNLAyVIYTSGSTGQPKGVGNTHA-ALAERLQWMQATYALDDSDVLMQKAPISF 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 268 ILATVGCLIePWTSGCTVFI-----HHlpqfDPKVIVEVLFKYPITQCLAAPGVYRMVLQQktsnlrfPTLEHCT----- 337
Cdd:PRK05691 1326 DVSVWECFW-PLITGCRLVLagpgeHR----DPQRIAELVQQYGVTTLHFVPPLLQLFIDE-------PLAAACTslrrl 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 338 -TGGESLLPEEYEQWKQR-TGLSIHEVYGQSETGISSA--TLREMKIKRGSIGKAILPFDLQIIDEKGNILPPNTEG--Y 411
Cdd:PRK05691 1394 fSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAINVThwQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGelC 1473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 412 IGirikptrPLGLFMEYENSPESTSEVECGD--------FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENA 483
Cdd:PRK05691 1474 IG-------GAGLARGYLGRPALTAERFVPDplgedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQAR 1546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 484 LAEHPAVAESAVVSSPDKDRGEVVKAFIvlnpefLSHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRK 563
Cdd:PRK05691 1547 LLAQPGVAQAAVLVREGAAGAQLVGYYT------GEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRR 1620
|
..
gi 18381087 564 EL 565
Cdd:PRK05691 1621 AL 1622
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
215-532 |
1.30e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 73.39 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 215 DPMAIFFTSGTTGYPKMAKHNQGLaFRSYIPSCRKLLKLKtsdilwcmsdPGWI-LAT--VGCLIEPWTSGCTVfihhLP 291
Cdd:PRK09274 175 DMAAILFTSGSTGTPKGVVYTHGM-FEAQIEALREDYGIE----------PGEIdLPTfpLFALFGPALGMTSV----IP 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 292 QFD--------PKVIVEVLFKYPITQCLAAPGVYRMVLQQ-KTSNLRFPTLEHCTTGG-----------ESLLPEEYEqw 351
Cdd:PRK09274 240 DMDptrpatvdPAKLFAAIERYGVTNLFGSPALLERLGRYgEANGIKLPSLRRVISAGapvpiavierfRAMLPPDAE-- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 352 kqrtglsIHEVYGQSET-GISSATLREMKIKRGSI---------GKAILPFDLQIID---------EKGNILPPNTEGYI 412
Cdd:PRK09274 318 -------ILTPYGATEAlPISSIESREILFATRAAtdngagicvGRPVDGVEVRIIAisdapipewDDALRLATGEIGEI 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 413 GIRiKP--TRplglfmEYENSPESTSEV----ECGDFYN-SGDRATIDEEGYIWFLGR-GDDVINASGyRIGPVEVENAL 484
Cdd:PRK09274 391 VVA-GPmvTR------SYYNRPEATRLAkipdGQGDVWHrMGDLGYLDAQGRLWFCGRkAHRVETAGG-TLYTIPCERIF 462
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 18381087 485 AEHPAVAESAVVSSPDKdrGEVVKAFIV-LNPEfLSHDQEQLIKELQHH 532
Cdd:PRK09274 463 NTHPGVKRSALVGVGVP--GAQRPVLCVeLEPG-VACSKSALYQELRAL 508
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
46-560 |
4.53e-13 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 72.14 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 46 NFASDVLdywaqmeeEGKRGPSPAFWWVNGQGDEIKWSFRKLRDLTCRTANVFEQiCGLQQGDHLALILPRVPEwwlvtv 125
Cdd:PRK03584 87 NYAENLL--------RHRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRA-LGVGPGDRVAAYLPNIPE------ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 126 gcmrtGIIFMPGTTQLKA-----------KDILYRIQISRAKAIVTTA---------SLVPEVESVASECPDLKtKLVVS 185
Cdd:PRK03584 152 -----TVVAMLATASLGAiwsscspdfgvQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELRAALPSLE-HVVVV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 186 DHSHEG-----------WLDFCSLIKSASP-------DHtcikskmkdPMAIFFTSGTTGYPKMAKHNQG------Lafr 241
Cdd:PRK03584 226 PYLGPAaaaaalpgallWEDFLAPAEAAELefepvpfDH---------PLWILYSSGTTGLPKCIVHGHGgillehL--- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 242 syipscrKLLKL----KTSDILWCMSDPGWIL--ATVGCLIepwtSGCTVFIhhlpqFD-----PKVivEVLF------- 303
Cdd:PRK03584 294 -------KELGLhcdlGPGDRFFWYTTCGWMMwnWLVSGLL----VGATLVL-----YDgspfyPDP--NVLWdlaaeeg 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 304 --------KYpITQCLAA---PGvyrmvlqqKT---SNLRfpTLehCTTGgeSLLPEE-----YEQWKQRTGLSihevyg 364
Cdd:PRK03584 356 vtvfgtsaKY-LDACEKAglvPG--------EThdlSALR--TI--GSTG--SPLPPEgfdwvYEHVKADVWLA------ 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 365 qsetGISSAT---------LREMKIKRGSIGKAILPFDLQIIDEKGNILppntegyIGIR----IK---PTRPLGLFmey 428
Cdd:PRK03584 415 ----SISGGTdicscfvggNPLLPVYRGEIQCRGLGMAVEAWDEDGRPV-------VGEVgelvCTkpfPSMPLGFW--- 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 429 eNSPEstsevecGDFYNS------------GDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVV 496
Cdd:PRK03584 481 -NDPD-------GSRYRDayfdtfpgvwrhGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVI 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18381087 497 SSPDKDRGEVVKAFIVLNPEF-LShdqEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKI 560
Cdd:PRK03584 553 GQEWPDGDVRMPLFVVLAEGVtLD---DALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKK 614
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-496 |
5.97e-13 |
|
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: 70.95 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 199 IKSASPDHTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQGLaFRSYIPSCRKLLKLKTSDI------LWCMSDPGWILATV 272
Cdd:cd05910 70 LQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGT-FAAQIDALRQLYGIRPGEVdlatfpLFALFGPALGLTSV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 273 GCLIEPWTSGctvfihhlpQFDPKVIVEVLFKYPITQCLAAPGVYRMVLQQ-KTSNLRFPTLEHCTTGGESLLPEEYEQW 351
Cdd:cd05910 149 IPDMDPTRPA---------RADPQKLVGAIRQYGVSIVFGSPALLERVARYcAQHGITLPSLRRVLSAGAPVPIALAARL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 352 KQ--RTGLSIHEVYGQSET-GISSATLREMKIKRGS---------IGKAILPFDLQIID-------EKGNI--LPPNTEG 410
Cdd:cd05910 220 RKmlSDEAEILTPYGATEAlPVSSIGSRELLATTTAatsggagtcVGRPIPGVRVRIIEiddepiaEWDDTleLPRGEIG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 411 YI---GIRIKPTrplglfmeYENSPESTSEVECGD-----FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVEN 482
Cdd:cd05910 300 EItvtGPTVTPT--------YVNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVER 371
|
330
....*....|....
gi 18381087 483 ALAEHPAVAESAVV 496
Cdd:cd05910 372 VFNTHPGVRRSALV 385
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
125-573 |
8.88e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.74 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 125 VGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPDL-KTKLVVsdhshegWLDfcsLIKSAS 203
Cdd:PRK05691 3788 VGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQARALLDELGCAnRPRLLV-------WEE---VQAGEV 3857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 204 PDHTCIKSKMKDPMA-IFFTSGTTGYPK--MAK-----HNQglafRSYIPscrkLLKLKTSDILWCMSDPGWILATVGCL 275
Cdd:PRK05691 3858 ASHNPGIYSGPDNLAyVIYTSGSTGLPKgvMVEqrgmlNNQ----LSKVP----YLALSEADVIAQTASQSFDISVWQFL 3929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 276 IEPWTSGCTVFIHHLPQFDPKVIVEVLFKYPITQCLAAPGVYRMVL---QQKTSNLRF--PTlehcttgGESLLPEEYEQ 350
Cdd:PRK05691 3930 AAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLaedRQALDGLRWmlPT-------GEAMPPELARQ 4002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 351 WKQR-TGLSIHEVYGQSETGISSATLR-EMKIKRGS---IGKailPFD---LQIIDEKGNILPPNTEGYIGIRikptrPL 422
Cdd:PRK05691 4003 WLQRyPQIGLVNAYGPAECSDDVAFFRvDLASTRGSylpIGS---PTDnnrLYLLDEALELVPLGAVGELCVA-----GT 4074
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 423 GLFMEYENSPESTSEV-------ECGD-FYNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESA 494
Cdd:PRK05691 4075 GVGRGYVGDPLRTALAfvphpfgAPGErLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA 4154
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18381087 495 VVSSpDKDRGEVVKAFIVlnPEFLSHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKELRNKEFGQL 573
Cdd:PRK05691 4155 VAVQ-EGVNGKHLVGYLV--PHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQL 4230
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
198-560 |
2.42e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 69.99 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 198 LIKSASPDHTCIKSKMKDPMAIFFTSGTTGYPK--MAKHNQGLAFRSYIPScrkLLKLKTSDILWCmsdpgwILA----- 270
Cdd:PRK06814 777 LLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKgvVLSHRNLLANRAQVAA---RIDFSPEDKVFN------ALPvfhsf 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 271 --TVGCLIePWTSGCTVFIhhlpqfdpkvivevlfkYPitqclaAPGVYRMVLQ---QKTSNLRFPT------------- 332
Cdd:PRK06814 848 glTGGLVL-PLLSGVKVFL-----------------YP------SPLHYRIIPEliyDTNATILFGTdtflngyaryahp 903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 333 -----LEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETG--ISSATlrEMKIKRGSIGKaILPF------DLQIIDE 399
Cdd:PRK06814 904 ydfrsLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETApvIALNT--PMHNKAGTVGR-LLPGieyrlePVPGIDE 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 400 KGNIL--PPNT-EGYIgiriKPTRPlGLfmeYENSPEstsevecgDFYNSGDRATIDEEGYIWFLGRGDDVINASGYRIG 476
Cdd:PRK06814 981 GGRLFvrGPNVmLGYL----RAENP-GV---LEPPAD--------GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMIS 1044
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 477 PVEVENALAEHPAVAESAVVSSPDKDRGEVvkafIVLnpefLSHDQEQLIKELQHHVKSVTAPYKY-PRKVEFVSELPKT 555
Cdd:PRK06814 1045 LAAVEELAAELWPDALHAAVSIPDARKGER----IIL----LTTASDATRAAFLAHAKAAGASELMvPAEIITIDEIPLL 1116
|
....*
gi 18381087 556 VTGKI 560
Cdd:PRK06814 1117 GTGKI 1121
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
62-573 |
4.21e-11 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 65.87 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 62 GKRGPSPAFWWVNGQGDEI---KWSFRKLRDLTCRTANVFEQIcGLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGT 138
Cdd:PLN03052 186 SKTDDSIAIIWRDEGSDDLpvnRMTLSELRSQVSRVANALDAL-GFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 139 TQLKAKDILYRIQISRAKAIVTTA------------SLVPEVES-----VASECPDLKTKLVVSDHShegWLDFCSLIK- 200
Cdd:PLN03052 265 DSFAPSEIATRLKISKAKAIFTQDvivrggksiplySRVVEAKApkaivLPADGKSVRVKLREGDMS---WDDFLARANg 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 201 SASPD-HTCIKSKMKDPMAIFFTSGTTGYPKMAKHNQglafrsyipscrkLLKLKTSDILWCMSD--PGWILA---TVGC 274
Cdd:PLN03052 342 LRRPDeYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQ-------------LTPLRAAADAWAHLDirKGDIVCwptNLGW 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 275 LIEPW------TSGCTVFIHH-------LPQF--DPKV----IVEVLFK-YPITQClaapgvyrmvlqqkTSNLRFPTLE 334
Cdd:PLN03052 409 MMGPWlvyaslLNGATLALYNgsplgrgFAKFvqDAKVtmlgTVPSIVKtWKNTNC--------------MAGLDWSSIR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 335 HCTTGGESLLPEEYEQWKQRTGLS-IHEVYGQSETG---ISSATLREMKIkrGSIGKAILPFDLQIIDEKGNILPPNTEG 410
Cdd:PLN03052 475 CFGSTGEASSVDDYLWLMSRAGYKpIIEYCGGTELGggfVTGSLLQPQAF--AAFSTPAMGCKLFILDDSGNPYPDDAPC 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 411 yigirikpTRPLGLFMEYENSpesTSEVECGDFYN----------------SGDRATIDEEGYIWFLGRGDDVINASGYR 474
Cdd:PLN03052 553 --------TGELALFPLMFGA---SSTLLNADHYKvyfkgmpvfngkilrrHGDIFERTSGGYYRAHGRADDTMNLGGIK 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 475 IGPVEVENAL-AEHPAVAESAVVSSPDKDRG--EVVKAFIVLNPEFLSHDQEQLIKELQHHVKSVTAPYKYPRKVEFVSE 551
Cdd:PLN03052 622 VSSVEIERVCnAADESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPS 701
|
570 580
....*....|....*....|..
gi 18381087 552 LPKTVTGKIKRKELRnKEFGQL 573
Cdd:PLN03052 702 FPRTASNKVMRRVLR-QQLAQE 722
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
212-566 |
6.22e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 64.82 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 212 KMKDPMA-IFFTSGTTGYPK--MAKHNQglaFRSYIPSCRKLLKLKTSDILWcmsdpGWILAT-----VGCLIEPWTSGC 283
Cdd:cd05908 103 ELADELAfIQFSSGSTGDPKgvMLTHEN---LVHNMFAILNSTEWKTKDRIL-----SWMPLThdmglIAFHLAPLIAGM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 284 TVFIHHLPQF--DPKVIVEVLFKYPITQcLAAPGV-YRMVLQQ----KTSNLRFPTLEHCTTGGESLLPEEYEQWKQRT- 355
Cdd:cd05908 175 NQYLMPTRLFirRPILWLKKASEHKATI-VSSPNFgYKYFLKTlkpeKANDWDLSSIRMILNGAEPIDYELCHEFLDHMs 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 356 --GL---SIHEVYGQSET--GISSATLRE----------------------MKIKRG----SIGKAILPFDLQIIDEKGN 402
Cdd:cd05908 254 kyGLkrnAILPVYGLAEAsvGASLPKAQSpfktitlgrrhvthgepepevdKKDSECltfvEVGKPIDETDIRICDEDNK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 403 ILPPNTEGYIGIRIKPTRPlglfmEYENSPESTSEVECGD-FYNSGDRATI-DEEGYIwfLGRGDDVINASGYRIGPVEV 480
Cdd:cd05908 334 ILPDGYIGHIQIRGKNVTP-----GYYNNPEATAKVFTDDgWLKTGDLGFIrNGRLVI--TGREKDIIFVNGQNVYPHDI 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 481 ENALAEHPAVAESAVVS---SPDKDRGEVVKAFIVLNPEflSHDQEQLIKELQHHVKSVTApyKYPRKVEFVSELPKTVT 557
Cdd:cd05908 407 ERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRKS--EDDFYPLGKKIKKHLNKRGG--WQINEVLPIRRIPKTTS 482
|
....*....
gi 18381087 558 GKIKRKELR 566
Cdd:cd05908 483 GKVKRYELA 491
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
114-568 |
2.83e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 62.91 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 114 LPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTT------ASLVPEVESVASECP----------- 176
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQdvvlrgGRALPLYSKVVEAAPakaivlpaage 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 177 DLKTKLVVSDHShegWLDF---CSLIKSASPDH-TCIKSKMKDPMAIFFTSGTTGYPKMAKHNQGLAFRSYIPScRKLLK 252
Cdd:PLN03051 81 PVAVPLREQDLS---WCDFlgvAAAQGSVGGNEySPVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDG-WAHMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 253 LKTSDILWCMSDPGWILATVgCLIEPWTSGCTVFIHH-------LPQFDPKVIVEVLFKYPI-------TQCLAAPGVyr 318
Cdd:PLN03051 157 IQPGDVVCWPTNLGWMMGPW-LLYSAFLNGATLALYGgaplgrgFGKFVQDAGVTVLGLVPSivkawrhTGAFAMEGL-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 319 mvlqqKTSNLRFptleHCTTGgESLLPEEYEQWKQRTGLS--IHEVYGQSETG---ISSATLREMKIkrGSIGKAILPFD 393
Cdd:PLN03051 234 -----DWSKLRV----FASTG-EASAVDDVLWLSSVRGYYkpVIEYCGGTELAsgyISSTLLQPQAP--GAFSTASLGTR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 394 LQIIDEKGNILP--PNTEGYIGIRikpTRPLGLFMEYENSPESTSEVECGDFYNS--------GDRATIDEEGYIWFLGR 463
Cdd:PLN03051 302 FVLLNDNGVPYPddQPCVGEVALA---PPMLGASDRLLNADHDKVYYKGMPMYGSkgmplrrhGDIMKRTPGGYFCVQGR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 464 GDDVINASGYRIGPVEVENALAE-HPAVAESAVVSSPDKDRGE----VVKAFIVLNPEFLSHDQEQLIKELQHHVKSVTA 538
Cdd:PLN03051 379 ADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLN 458
|
490 500 510
....*....|....*....|....*....|
gi 18381087 539 PYKYPRKVEFVSELPKTVTGKIKRKELRNK 568
Cdd:PLN03051 459 PLFKVSRVKIVPELPRNASNKLLRRVLRDQ 488
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
105-567 |
3.39e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 59.72 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 105 QQGDHLALILPRVPEWWLVTVGC-MRTGIIFMPGTTQlKAKDILYRIQISRAKAIVTTASL------------VPEVESV 171
Cdd:PRK08043 253 VEGERIGLMLPNATISAAVIFGAsLRRRIPAMMNYTA-GVKGLTSAITAAEIKTIFTSRQFldkgklwhlpeqLTQVRWV 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 172 ASEcpDLKTKLVVSDhshEGWLdFCSLIksaSPDHTCIKSKMKDPMAIFFTSGTTGYPK--MAKHNQGLAFRSYIpscRK 249
Cdd:PRK08043 332 YLE--DLKDDVTTAD---KLWI-FAHLL---MPRLAQVKQQPEDAALILFTSGSEGHPKgvVHSHKSLLANVEQI---KT 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 250 LLKLKTSDILwcMSDPGWILA---TVGcLIEPWTSGCTVFIHHLPqFDPKVIVEVLFKYPITqclaapgvyrmVLQQKTS 326
Cdd:PRK08043 400 IADFTPNDRF--MSALPLFHSfglTVG-LFTPLLTGAEVFLYPSP-LHYRIVPELVYDRNCT-----------VLFGTST 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 327 NL----------RFPTLEHCTTGGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIKRGSIGKaILP-FDLQ 395
Cdd:PRK08043 465 FLgnyarfanpyDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGR-ILPgMDAR 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 396 IID----EKGNILP---PNT-EGYIGIRiKPTRplglfMEYENSPESTSEVECGdFYNSGDRATIDEEGYIWFLGRGDDV 467
Cdd:PRK08043 544 LLSvpgiEQGGRLQlkgPNImNGYLRVE-KPGV-----LEVPTAENARGEMERG-WYDTGDIVRFDEQGFVQIQGRAKRF 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 468 INASGYRIGPVEVEN-ALAEHPAvAESAVVSSPDKDRGEVVKAFivlnpeflSHDQEQLIKELQHHVKSVTAP-YKYPRK 545
Cdd:PRK08043 617 AKIAGEMVSLEMVEQlALGVSPD-KQHATAIKSDASKGEALVLF--------TTDSELTREKLQQYAREHGVPeLAVPRD 687
|
490 500
....*....|....*....|..
gi 18381087 546 VEFVSELPKTVTGKIKRKELRN 567
Cdd:PRK08043 688 IRYLKQLPLLGSGKPDFVTLKS 709
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
62-562 |
6.59e-09 |
|
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: 58.40 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 62 GKRGPSPAFWWVN-GQGDEIKWSFRKLRDLTCRTANVFEQICGlqQGDHLALILPRVPEWWLVTVGCMRTGII---FMPG 137
Cdd:cd05931 4 AARPDRPAYTFLDdEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 138 TTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASECPDLKTklvvsdhsheGWLDFCSLIKSASPDHTCIKSKMKDPM 217
Cdd:cd05931 82 TPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGT----------PRLLVVDLLPDTSAADWPPPSPDPDDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 218 AIF-FTSGTTGYPK--MAKHnqglafRSYIPSCRKLLKLktsdilwCMSDPGWILAT----------VGCLIEPWTSGCT 284
Cdd:cd05931 152 AYLqYTSGSTGTPKgvVVTH------RNLLANVRQIRRA-------YGLDPGDVVVSwlplyhdmglIGGLLTPLYSGGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 285 V-------FIHhlpqfDPKVIVEVLFKYPITqCLAAPG-----VYRMVLQQKTSNLRFPTLEHCTTGGESLLPEEYEQWK 352
Cdd:cd05931 219 SvlmspaaFLR-----RPLRWLRLISRYRAT-ISAAPNfaydlCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 353 QR---TGL---SIHEVYGQSE-----------TGISSATLREMKIKRG---------------SIGKAILPFDLQIIDEK 400
Cdd:cd05931 293 EAfapFGFrpeAFRPSYGLAEatlfvsggppgTGPVVLRVDRDALAGRavavaaddpaarelvSCGRPLPDQEVRIVDPE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 401 GNI-LPPNTEGYIGIRiKPTRPLGlfmeYENSPESTSEVEC-------GDFYNSGDRATIDEeGYIWFLGRGDDVINASG 472
Cdd:cd05931 373 TGReLPDGEVGEIWVR-GPSVASG----YWGRPEATAETFGalaatdeGGWLRTGDLGFLHD-GELYITGRLKDLIIVRG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 473 YRIGPVEVENALAE-HPAVAES--AVVSSPDKDRGEVVkAFIVLNPEFLSHDQEQLIKELQHHVKS---VTapykyPRKV 546
Cdd:cd05931 447 RNHYPQDIEATAEEaHPALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAVARehgVA-----PADV 520
|
570
....*....|....*...
gi 18381087 547 EFVS--ELPKTVTGKIKR 562
Cdd:cd05931 521 VLVRpgSIPRTSSGKIQR 538
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
384-562 |
8.00e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 55.00 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 384 SIGKAILPFDLQIIDEKGNILPPNTEGYIGIRIKPTRPLGLFMEyenSPESTseVECGDFYNSGDRATIDEEGYIWFLGR 463
Cdd:PRK07768 361 TLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLTMD---GFIPA--QDADGWLDTGDLGYLTEEGEVVVCGR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 464 GDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPdKDRGEVVKAFIVLNPEFLSHDQEQlIKELQHHVKS-VTAPYKY 542
Cdd:PRK07768 436 VKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVR-LDAGHSREGFAVAVESNAFEDPAE-VRRIRHQVAHeVVAEVGV 513
|
170 180
....*....|....*....|...
gi 18381087 543 -PRKVEFVS--ELPKTVTGKIKR 562
Cdd:PRK07768 514 rPRNVVVLGpgSIPKTPSGKLRR 536
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
386-567 |
1.99e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 53.86 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 386 GKAILPFDLQIIDEKGNILPPNTEGYIGIRiKPtrplGLFMEYENSPESTSEVECGDFYNSGDRATIdEEGYIWFLGRGD 465
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR-GP----SLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 466 DVINASGYRIGPVEVENALAEHPAV-AESAVVSSPDKDRGEVVKAFI---VLNPEflshDQEQLIKELQHHVKSVTApyk 541
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELrSGDAAAFSIAQENGEKIVLLVqcrISDEE----RRGQLIHALAALVRSEFG--- 534
|
170 180
....*....|....*....|....*...
gi 18381087 542 YPRKVEFVS--ELPKTVTGKIKRKELRN 567
Cdd:PRK09192 535 VEAAVELVPphSLPRTSSGKLSRAKAKK 562
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
438-567 |
7.76e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 51.69 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 438 VECGDFYNSGDRATIDEEGYIwFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGevVKAFIVLNPEF 517
Cdd:PRK05851 392 IDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEF 468
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18381087 518 LSHDQEQLIKELQHHVKSVTApyKYPRKVEFVS--ELPKTVTGKIKRKELRN 567
Cdd:PRK05851 469 RGPDEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
150-487 |
2.77e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 50.20 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 150 IQISRAKAIVTTASLVPEVESVASECPDLKTKLVVSD--HSHEGWLDFCSLIKSASPDHTC------IKSKMKDPMA-IF 220
Cdd:PRK06334 110 ANLVGVTHVLTSKQLMQHLAQTHGEDAEYPFSLIYMEevRKELSFWEKCRIGIYMSIPFEWlmrwfgVSDKDPEDVAvIL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 221 FTSGTTGYPKMA--KHNQGLAFRSyipSCRKLLKLKTSDILWCMSDPGWILATVGCLIEPWTSGCTVFIHHLPqFDPKVI 298
Cdd:PRK06334 190 FTSGTEKLPKGVplTHANLLANQR---ACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNP-LYPKKI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 299 VEVLFKYPITQCLAAPGVYRMVLQQ-KTSNLRFPTLEHCTTGGESLLPEEYEQ-WKQRTGLSIHEVYGQSETG--ISSAT 374
Cdd:PRK06334 266 VEMIDEAKVTFLGSTPVFFDYILKTaKKQESCLPSLRFVVIGGDAFKDSLYQEaLKTFPHIQLRQGYGTTECSpvITINT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 375 LREMKIKRgSIGKAILPFDLQIIDEKGNIlpPNTEGYIGIRIkpTRPLGLFMEYENSPESTSEVECG--DFYNSGDRATI 452
Cdd:PRK06334 346 VNSPKHES-CVGMPIRGMDVLIVSEETKV--PVSSGETGLVL--TRGTSLFSGYLGEDFGQGFVELGgeTWYVTGDLGYV 420
|
330 340 350
....*....|....*....|....*....|....*
gi 18381087 453 DEEGYIWFLGRGDDVINASGYRIGPVEVENALAEH 487
Cdd:PRK06334 421 DRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
333-496 |
2.89e-06 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 50.05 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 333 LEHCTT--GGESLLPEEYEQWKQRTGLSIHEVYGQSETGISSATLREMKIKRGSIGKAILPFDLQIIDekgnilpPNTEG 410
Cdd:cd05933 319 LDRCQKffTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHN-------PDADG 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 411 YIGIRIkptRPLGLFMEYENSPESTSE-VECGDFYNSGDRATIDEEGYIWFLGRGDD-VINASGYRIGPVEVENAL-AEH 487
Cdd:cd05933 392 IGEICF---WGRHVFMGYLNMEDKTEEaIDEDGWLHSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAVkKEL 468
|
....*....
gi 18381087 488 PAVAESAVV 496
Cdd:cd05933 469 PIISNAMLI 477
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
444-565 |
1.37e-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: 47.90 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 444 YNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVlnPEFLSHDQE 523
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIV--PRFDKPDDE 451
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18381087 524 ------------------------QLIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:cd17647 452 sfaqedvpkevstdpivkgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
444-565 |
3.53e-04 |
|
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: 43.51 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 444 YNSGDRATIDEEGYIWFLGRGDDVINASGYRIGPVEVENALAEHPAVAESAVVSSPDKDRGEVVKAFIVLNP------EF 517
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDksdeleEF 759
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18381087 518 LSHDQEQ---------------LIKELQHHVKSVTAPYKYPRKVEFVSELPKTVTGKIKRKEL 565
Cdd:TIGR03443 760 KSEVDDEessdpvvkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
103-230 |
4.40e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 43.29 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 103 GLQQGDHLALILPRVPEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLVPEVESVASEC-PDLKTK 181
Cdd:PLN02861 98 GVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLPKCsSNLKTI 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18381087 182 LVVSDHSHE-------------GWLDFCSLiksASPDHTCIKSKMKDPMAIFFTSGTTGYPK 230
Cdd:PLN02861 178 VSFGDVSSEqkeeaeelgvscfSWEEFSLM---GSLDCELPPKQKTDICTIMYTSGTTGEPK 236
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
462-566 |
5.51e-04 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 42.44 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 462 GRGDDVINasgyrIGPVEVEnALAEHPAVAESAVVSSPDKDRGEVVKAFIvlnpeflSHDQEQLIKELQHHVKSVTAPyK 541
Cdd:PRK09188 233 GTGDRIDN-----EAPAIQA-ALKSDPAVSDVAIALFSLPAKGVGLYAFV-------EAELPADEKSLRARLAGAKPP-K 298
|
90 100
....*....|....*....|....*
gi 18381087 542 YPRKVEFVSELPKTVTGKIKRKELR 566
Cdd:PRK09188 299 PPEHIQPVAALPRDADGTVRDDILR 323
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
118-237 |
4.75e-03 |
|
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: 39.89 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18381087 118 PEWWLVTVGCMRTGIIFMPGTTQLKAKDILYRIQISRAKAIVTTASLvpEVESvasecpdlktklvvsdhshegWLDFCS 197
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDAGV--KVYS---------------------LEEFEK 99
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 18381087 198 LIKSASPDHTciKSKMKDPMAIFFTSGTTGYPKMAKHNQG 237
Cdd:cd05927 100 LGKKNKVPPP--PPKPEDLATICYTSGTTGNPKGVMLTHG 137
|
|
| |
