|
Name |
Accession |
Description |
Interval |
E-value |
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
14-527 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 601.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 14 FAPEKYNIISEIEKySHI---PDKKAILYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELY 90
Cdd:COG0365 3 FVGGRLNIAYNCLD-RHAegrGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 91 IAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIA---------LEPFTVEFEKI-KEYDALTKFVIAG------QKDG 154
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITadgglrggkVIDLKEKVDEAlEELPSLEHVIVVGrtgadvPMEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 155 WISLEAEKENASNKLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWV 234
Cdd:COG0365 162 DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 235 WSPFLSVLGSGATAFVFNGRF---SPETYLELLQKYQINVLCCTPTEYRMMAK--LQNLNDYDLTHLHSAVSAGEPLNRE 309
Cdd:COG0365 242 SYIVYGPLLNGATVVLYEGRPdfpDPGRLWELIEKYGVTVFFTAPTAIRALMKagDEPLKKYDLSSLRLLGSAGEPLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 310 VVEQFKKYFNLTVRDGYGQTEST-LLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLPALFKGY 388
Cdd:COG0365 322 VWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 389 YKEPERTAKAQTGK---YYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGN 465
Cdd:COG0365 402 WNDPERYRETYFGRfpgWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQ 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441463764 466 IVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAE 527
Cdd:COG0365 482 VVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
49-525 |
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: 566.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 49 VTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIale 128
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 129 pftvefekikeydaltkfviagqkdgwisleaekenasnklemadTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQM 208
Cdd:cd05972 78 ---------------------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 209 ApKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLGSGATAFVFNG-RFSPETYLELLQKYQINVLCCTPTEYRMMAKlQN 287
Cdd:cd05972 113 A-AYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGpRFDAERILELLERYGVTSFCGPPTAYRMLIK-QD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 288 LNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSV 367
Cdd:cd05972 191 LSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGREL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 368 PANTKGNIAVPLDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNH 447
Cdd:cd05972 271 PPGEEGDIAIKLPPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEH 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441463764 448 PAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:cd05972 351 PAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
15-525 |
3.13e-156 |
|
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: 456.57 E-value: 3.13e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 15 APEKYNIISEI-EKYSHI-PDKKAILYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIA 92
Cdd:cd05970 12 VPENFNFAYDVvDAMAKEyPDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 93 ALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIALEPFTV--EFEK-IKEYDALTKFVIAG--QKDGWISLEAEKENASN 167
Cdd:cd05970 92 LHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIpeEIEKaAPECPSKPKLVWVGdpVPEGWIDFRKLIKNASP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 168 KLEM----ADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMApKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLG 243
Cdd:cd05970 172 DFERptanSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTA-KYWQNVREGGLHLTVADTGWGKAVWGKIYGQWI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 244 SGATAFVFN-GRFSPETYLELLQKYQINVLCCTPTEYRMMAKlQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTV 322
Cdd:cd05970 251 AGAAVFVYDyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 323 RDGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLD--LP-ALFKGYYKEPERTAKAQ 399
Cdd:cd05970 330 MEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgKPvGLFGGYYKDAEKTAEVW 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 400 TGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVIL-QDHTA 478
Cdd:cd05970 410 HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLaKGYEP 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1441463764 479 GdDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:cd05970 490 S-EELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
16-527 |
3.98e-148 |
|
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: 435.74 E-value: 3.98e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 16 PEKYNIISEI-------EKYSHIPDKKAILYHNTEGEDISVTYQQLIEQSNKVGNVLASH-GLSKGDKVLIMMPRSIATY 87
Cdd:cd05928 2 PEYFNFASDVldqwadkEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 88 ELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIALEPFTVEFEKI-KEYDAL-TKFVIAGQ-KDGWISLEAEKEN 164
Cdd:cd05928 82 LVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVaSECPSLkTKLLVSEKsRDGWLNFKELLNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 165 ASNKLEMADT-TRDDMAILsYTSGTTGNPKAVTHCHGWGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLG 243
Cdd:cd05928 162 ASTEHHCVETgSQEPMAIY-FTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 244 SGATAFVFN-GRFSPETYLELLQKYQINVLCCTPTEYRMMAKlQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTV 322
Cdd:cd05928 241 QGACVFVHHlPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 323 RDGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAV---PLDLPALFKGYYKEPERTAKAQ 399
Cdd:cd05928 320 YEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkPIRPFGLFSGYVDNPEKTAATI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 400 TGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAG 479
Cdd:cd05928 400 RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLS 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1441463764 480 DD--TLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAE 527
Cdd:cd05928 480 HDpeQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKE 529
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
18-521 |
2.61e-142 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 422.38 E-value: 2.61e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 18 KYNIISE-IEKYSHIPDK-KAILYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIatyELYIA--- 92
Cdd:PRK04319 41 KVNIAYEaIDRHADGGRKdKVALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIP---ELYFAllg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 93 ALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIAlepfTVEFEKIKEYDALT--KFVI-----AGQKDGWISLEAEKENA 165
Cdd:PRK04319 118 ALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT----TPALLERKPADDLPslKHVLlvgedVEEGPGTLDFNALMEQA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 166 SNKLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMApKHWLCINEDDLVWATAAPGW----QKWVWSPFLSv 241
Cdd:PRK04319 194 SDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTG-KYVLDLHEDDVYWCTADPGWvtgtSYGIFAPWLN- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 242 lgsGATAFVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMAKL--QNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFN 319
Cdd:PRK04319 272 ---GATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAgdDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 320 LTVRDGYGQTES-TLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLPALFKGYYKEPERTAKA 398
Cdd:PRK04319 349 LPIHDNWWMTETgGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYESY 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 399 QTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTA 478
Cdd:PRK04319 429 FAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYE 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1441463764 479 GDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKI-RRV 521
Cdd:PRK04319 509 PSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKImRRV 552
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
32-530 |
1.16e-136 |
|
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: 403.42 E-value: 1.16e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:COG0318 13 PDRPALVF-----GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIAlepftvefekikeydaltkfviagqkdgwisleaekenasnklemadttrddmAILSYTSGTTGN 191
Cdd:COG0318 88 LAYILEDSGARALVT-----------------------------------------------------ALILYTSGTTGR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGwGFAHLQMAPKHWLCINEDDlVWATAAP-----GWqkwvWSPFLSVLGSGATAfVFNGRFSPETYLELLQK 266
Cdd:COG0318 115 PKGVMLTHR-NLLANAAAIAAALGLTPGD-VVLVALPlfhvfGL----TVGLLAPLLAGATL-VLLPRFDPERVLELIER 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 267 YQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLI--GFLKDTPQR 344
Cdd:COG0318 188 ERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVtvNPEDPGERR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 345 IGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRR 424
Cdd:COG0318 268 PGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV--RGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 425 DDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDdtlVKELQQFVKNEVAPYKYPREI 504
Cdd:COG0318 346 KDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELD---AEELRAFLRERLARYKVPRRV 422
|
490 500
....*....|....*....|....*.
gi 1441463764 505 EFVDDLPKTNSGKIRRVELRDAEIEK 530
Cdd:COG0318 423 EFVDELPRTASGKIDRRALRERYAAG 448
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
50-528 |
2.79e-131 |
|
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: 389.55 E-value: 2.79e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIALEp 129
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 130 ftvefekikeydaltkfviagqkdgwisleaekenasnklEMAD-TTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQM 208
Cdd:cd05969 81 ----------------------------------------ELYErTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 209 APKHwLCINEDDLVWATAAPGWQK----WVWSPFLSvlgsGATAFVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMAK 284
Cdd:cd05969 121 GKYV-LDLHPDDIYWCTADPGWVTgtvyGIWAPWLN----GVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 285 L--QNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTES-TLLIGFLKDTPQRIGSMGKGIPGSSVTVVD 361
Cdd:cd05969 196 EgdELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgSIMIANYPCMPIKPGSMGKPLPGVKAAVVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 362 DEGNSVPANTKGNIAVPLDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVE 441
Cdd:cd05969 276 ENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 442 DALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRV 521
Cdd:cd05969 356 SALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRR 435
|
....*..
gi 1441463764 522 ELRDAEI 528
Cdd:cd05969 436 VLKAKEL 442
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-525 |
1.51e-115 |
|
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: 349.04 E-value: 1.51e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 49 VTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIALE 128
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 129 PftvefekikeydaltkfviagqkdgwisleaekenasnklemadttrDDMAILSYTSGTTGNPKAVTHCHGWGFAHL-- 206
Cdd:cd05971 87 S-----------------------------------------------DDPALIIYTSGTTGPPKGALHAHRVLLGHLpg 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 207 -QMApkHWLCINEDDLVWATAapgwqKWVWspfLSVLGSGATAFVFNG---------RFSPETYLELLQKYQINVLCCTP 276
Cdd:cd05971 120 vQFP--FNLFPRDGDLYWTPA-----DWAW---IGGLLDVLLPSLYFGvpvlahrmtKFDPKAALDLMSRYGVTTAFLPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 277 TEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIGFLKDT-PQRIGSMGKGIPGS 355
Cdd:cd05971 190 TALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSALfPIKPGSMGKPIPGH 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 356 SVTVVDDEGNSVPANTKGNIAVPLDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTI 435
Cdd:cd05971 270 RVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 436 GPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNS 515
Cdd:cd05971 350 GPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTAT 429
|
490
....*....|
gi 1441463764 516 GKIRRVELRD 525
Cdd:cd05971 430 GKIRRRELRA 439
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-527 |
5.11e-115 |
|
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: 347.63 E-value: 5.11e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 49 VTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGeinaviale 128
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 129 pftvefekikeydaltKFVIAGQKDgwisleaekenasnklemaDTTRDDMAILSYTSGTTGNPKAVTHCH-GWGFAHLq 207
Cdd:cd05974 72 ----------------GAVYAAVDE-------------------NTHADDPMLLYFTSGTTSKPKLVEHTHrSYPVGHL- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 208 mAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLGSGATAFVFN-GRFSPETYLELLQKYQINVLCCTPTEYRMMAKlQ 286
Cdd:cd05974 116 -STMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNyARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ-Q 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 287 NLNDYDlTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNS 366
Cdd:cd05974 194 DLASFD-VKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 367 VpanTKGNIAVPL--DLPA-LFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDA 443
Cdd:cd05974 273 A---TEGEVALDLgdTRPVgLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 444 LTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVdDLPKTNSGKIRRVEL 523
Cdd:cd05974 350 LIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVEL 428
|
....
gi 1441463764 524 RDAE 527
Cdd:cd05974 429 RRRE 432
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
17-524 |
2.09e-105 |
|
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: 325.48 E-value: 2.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 17 EKYNIISEI--EKYSHIPDKKAILYHNTegediSVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAAL 94
Cdd:cd05959 1 EKYNAATLVdlNLNEGRGDKTAFIDDAG-----SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 95 KLGVAIIPCSEMLRTKDLQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFVI-----AGQKDGWISLEAEKENASNKL 169
Cdd:cd05959 76 RAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLivsggAGPEAGALLLAELVAAEAEQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 170 EMADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMAPKHWLCINEDDLVWATA----APGWQKWVWSPFlsvlGSG 245
Cdd:cd05959 156 KPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAklffAYGLGNSLTFPL----SVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 246 ATAFVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDG 325
Cdd:cd05959 232 ATTVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 326 YGQTEstLLIGFLKDTPQRI--GSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKY 403
Cdd:cd05959 312 IGSTE--MLHIFLSNRPGRVryGTTGKPVPGYEVELRDEDGGDVADGEPGELYV--RGPSSATMYWNNRDKTRDTFQGEW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 404 YITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTL 483
Cdd:cd05959 388 TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEAL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1441463764 484 VKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:cd05959 468 EEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-524 |
1.46e-104 |
|
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: 320.62 E-value: 1.46e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPcsemLRTkdlqyrithgeinaviALEP 129
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQP----LFT----------------AFGP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 130 FTVEfEKIKEYDAltKFVIAgqkdgwisleaekeNASNKLEMADttrdDMAILSYTSGTTGNPKAVTH----CHGWGfAH 205
Cdd:cd05973 62 KAIE-HRLRTSGA--RLVVT--------------DAANRHKLDS----DPFVMMFTSGTTGLPKGVPVplraLAAFG-AY 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 206 LQMApkhwLCINEDDLVWATAAPGWQKWVWSPFLSVLGSGATAFVFNGRFSPETYLELLQKYQINVLCCTPTEYRM-MAK 284
Cdd:cd05973 120 LRDA----VDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLlMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 285 LQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIG--FLKDTPQRIGSMGKGIPGSSVTVVDD 362
Cdd:cd05973 196 GAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLAnhHALEHPVHAGSAGRAMPGWRVAVLDD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 363 EGNSVPANTKGNIAVPLDLPAL--FKGYYKEPERTAkaqTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEV 440
Cdd:cd05973 276 DGDELGPGEPGRLAIDIANSPLmwFRGYQLPDTPAI---DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 441 EDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:cd05973 353 ESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
....
gi 1441463764 521 VELR 524
Cdd:cd05973 433 FLLR 436
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
32-524 |
3.39e-103 |
|
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: 318.35 E-value: 3.39e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHntegeDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd05936 13 PDKTALIFM-----GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFTvefekikeyDALtkfviagqkdgwisleaekENASNKLEMADTTRDDMAILSYTSGTTGN 191
Cdd:cd05936 88 LEHILNDSGAKALIVAVSFT---------DLL-------------------AAGAPLGERVALTPEDVAVLQYTSGTTGV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGWGFAHLQMApKHWL--CINEDDLVWATAapgwqkwvwsPFLSVLGSGA--TAFVFNG-------RFSPETY 260
Cdd:cd05936 140 PKGAMLTHRNLVANALQI-KAWLedLLEGDDVVLAAL----------PLFHVFGLTValLLPLALGativlipRFRPIGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 261 LELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIGF-LK 339
Cdd:cd05936 209 LKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVnPL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 340 DTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFW 419
Cdd:cd05936 289 DGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWV--RGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 420 FEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtaGDDTLVKELQQFVKNEVAPYK 499
Cdd:cd05936 367 IVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKE---GASLTEEEIIAFCREQLAGYK 443
|
490 500
....*....|....*....|....*
gi 1441463764 500 YPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:cd05936 444 VPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
178-519 |
1.52e-102 |
|
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: 311.91 E-value: 1.52e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 178 DMAILSYTSGTTGNPKAVTHCHGwGFAHLQMAPKHWLCINEDDLVWATAAPGWQkWVWSPFLSVLGSGATAFVFnGRFSP 257
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHR-NLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL-PKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 258 ETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTE--STLLI 335
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTEtgGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 336 GFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDD 415
Cdd:cd04433 158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVV--RGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 416 GYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtaGDDTLVKELQQFVKNEV 495
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP---GADLDAEELRAHVRERL 312
|
330 340
....*....|....*....|....
gi 1441463764 496 APYKYPREIEFVDDLPKTNSGKIR 519
Cdd:cd04433 313 APYKVPRRVVFVDALPRTASGKID 336
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
46-524 |
1.59e-100 |
|
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: 310.56 E-value: 1.59e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 46 DISVTYQQLIEQSNKVGNVL-ASHGLSKGDKVLIMMPRSIATYELYIAALKLG---VAIIPcseMLRTKDLQYRITHGEI 121
Cdd:cd05958 8 EREWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGaiaVATMP---LLRPKELAYILDKARI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 122 navialepftvefekikeydalTKFVIAGQKdgwisleaekenasnklemadTTRDDMAILSYTSGTTGNPKAVTHCHGW 201
Cdd:cd05958 85 ----------------------TVALCAHAL---------------------TASDDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 202 GFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLGSGATAFVFNGRfSPETYLELLQKYQINVLCCTPTEYRM 281
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA-TPDLLLSAIARYKPTVLFTAPTAYRA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 282 MAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTEstLLIGFLKDTPQ--RIGSMGKGIPGSSVTV 359
Cdd:cd05958 201 MLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTE--MFHIFISARPGdaRPGATGKPVPGYEAKV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 360 VDDEGNSVPANTKGNIAVpldlpalfKG----YYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTI 435
Cdd:cd05958 279 VDDEGNPVPDGTIGRLAV--------RGptgcRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 436 GPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNS 515
Cdd:cd05958 351 APPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTAT 430
|
....*....
gi 1441463764 516 GKIRRVELR 524
Cdd:cd05958 431 GKLQRFALR 439
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
46-524 |
1.02e-98 |
|
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: 305.54 E-value: 1.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 46 DISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVI 125
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 126 alepftvefekikeydaltkfviagqkdgwisleaekenasnklemadTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAH 205
Cdd:cd05919 88 ------------------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 206 LQMAPKHWLCINEDDLVWATA----APGWQKWVWSPflsvLGSGATAFVFNGRFSPETYLELLQKYQINVLCCTPTEYRM 281
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAkmffGYGLGNSLWFP----LAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYAN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 282 MAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLigFLKDTPQ--RIGSMGKGIPGSSVTV 359
Cdd:cd05919 196 LLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHI--FLSNRPGawRLGSTGRPVPGYEIRL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 360 VDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFE 439
Cdd:cd05919 274 VDEEGHTIPPGEEGDLLV--RGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 440 VEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIR 519
Cdd:cd05919 352 VESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQ 431
|
....*
gi 1441463764 520 RVELR 524
Cdd:cd05919 432 RFKLR 436
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
32-525 |
3.64e-97 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 304.42 E-value: 3.64e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK06187 20 PDKEAVYF-----DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFVI-------AGQKDGWISLEAEKENASNKLEMADTTRDDMAILSY 184
Cdd:PRK06187 95 IAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIvegdgpaAPLAPEVGEYEELLAAASDTFDFPDIDENDAAAMLY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 185 TSGTTGNPKAVTHCHGWGFAHLqMAPKHWLCINEDD--LVWA----TAAPGWqkwvwsPFLSVLgSGATAfVFNGRFSPE 258
Cdd:PRK06187 175 TSGTTGHPKGVVLSHRNLFLHS-LAVCAWLKLSRDDvyLVIVpmfhVHAWGL------PYLALM-AGAKQ-VIPRRFDPE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 259 TYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIGFL 338
Cdd:PRK06187 246 NLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 339 KDTPQ------RIGSMGKGIPGSSVTVVDDEGNSVPANTK--GNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLA 410
Cdd:PRK06187 326 PPEDQlpgqwtKRRSAGRPLPGVEARIVDDDGDELPPDGGevGEIIV--RGPWLMQGYWNRPEATAETIDGGWLHTGDVG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 411 HVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtaGDDTLVKELQQF 490
Cdd:PRK06187 404 YIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKP---GATLDAKELRAF 480
|
490 500 510
....*....|....*....|....*....|....*
gi 1441463764 491 VKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK06187 481 LRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
29-520 |
1.84e-94 |
|
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: 294.52 E-value: 1.84e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 29 SHIPDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPcsemlr 108
Cdd:cd17631 6 RRHPDRTALVF-----GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 109 tkdLQYRITHGEINAVIAlepftvefekikeyDALTKFVIagqkdgwisleaekenasnklemadttrDDMAILSYTSGT 188
Cdd:cd17631 75 ---LNFRLTPPEVAYILA--------------DSGAKVLF----------------------------DDLALLMYTSGT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 189 TGNPKAVTHCHGWGFAHLQMAPKHWlCINEDDlVWATAAP-----GWQKWVwspfLSVLGSGATAfVFNGRFSPETYLEL 263
Cdd:cd17631 110 TGRPKGAMLTHRNLLWNAVNALAAL-DLGPDD-VLLVVAPlfhigGLGVFT----LPTLLRGGTV-VILRKFDPETVLDL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 264 LQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKyFNLTVRDGYGQTESTLLIGFL--KDT 341
Cdd:cd17631 183 IERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTFLspEDH 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 342 PQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFE 421
Cdd:cd17631 262 RRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVV--RGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 422 GRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTlvkELQQFVKNEVAPYKYP 501
Cdd:cd17631 340 DRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDED---ELIAHCRERLARYKIP 416
|
490
....*....|....*....
gi 1441463764 502 REIEFVDDLPKTNSGKIRR 520
Cdd:cd17631 417 KSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
32-431 |
7.07e-88 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 276.89 E-value: 7.07e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhnteGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:pfam00501 9 PDKTALEV----GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFTVE-FEKIKEYDALTKFVIAGQKDGWISLEAEKENASNK----LEMADTTRDDMAILSYTS 186
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEeLLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAdvppPPPPPPDPDDLAYIIYTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 187 GTTGNPKAVTHCHG---WGFAHLQMAPKHWLCINEDDLVWATA----APGWQKWVWSPFLsvlgSGATAFVFNG--RFSP 257
Cdd:pfam00501 165 GTTGKPKGVMLTHRnlvANVLSIKRVRPRGFGLGPDDRVLSTLplfhDFGLSLGLLGPLL----AGATVVLPPGfpALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 258 ETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTEST--LLI 335
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTgvVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 336 GFLKDTPQR-IGSMGKGIPGSSVTVVDDE-GNSVPANTKGNIAVplDLPALFKGYYKEPERTAKA-QTGKYYITGDLAHV 412
Cdd:pfam00501 321 PLPLDEDLRsLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCV--RGPGVMKGYLNDPELTAEAfDEDGWYRTGDLGRR 398
|
410
....*....|....*....
gi 1441463764 413 DDDGYFWFEGRRDDIIISS 431
Cdd:pfam00501 399 DEDGYLEIVGRKKDQIKLG 417
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
32-525 |
1.01e-86 |
|
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: 279.83 E-value: 1.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntEGEDIS----VTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIatyELYIAAL---KLGVA----- 99
Cdd:cd05966 67 GDKVAIIW---EGDEPDqsrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIP---ELVIAMLacaRIGAVhsvvf 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 100 -----------IIPC-SEMLRTKDLQYR----ITHGEInAVIALE-PFTVE----FEKIKeydalTKFVIAGQKDGWISL 158
Cdd:cd05966 141 agfsaesladrINDAqCKLVITADGGYRggkvIPLKEI-VDEALEkCPSVEkvlvVKRTG-----GEVPMTEGRDLWWHD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 159 EAEKENASNKLEMADTtrDDMAILSYTSGTTGNPKAVTHCHGwGFA-HLQMAPKHWLCINEDDLVWATAAPGW----QKW 233
Cdd:cd05966 215 LMAKQSPECEPEWMDS--EDPLFILYTSGSTGKPKGVVHTTG-GYLlYAATTFKYVFDYHPDDIYWCTADIGWitghSYI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 234 VWSPflsvLGSGATAFVFNGRFS---PETYLELLQKYQINVLCCTPTEYRMMAKLQN--LNDYDLTHLHSAVSAGEPLNR 308
Cdd:cd05966 292 VYGP----LANGATTVMFEGTPTypdPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDewVKKHDLSSLRVLGSVGEPINP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 309 EVVEQFKKY---FNLTVRDGYGQTES-----TLLIGFlkdTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLD 380
Cdd:cd05966 368 EAWMWYYEVigkERCPIVDTWWQTETggimiTPLPGA---TPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRP 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 381 LPALFKGYYKEPERTAKAQTGK---YYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVA 457
Cdd:cd05966 445 WPGMARTIYGDHERYEDTYFSKfpgYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVG 524
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1441463764 458 KPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKI-RRVeLRD 525
Cdd:cd05966 525 RPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKImRRI-LRK 592
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
48-526 |
9.45e-85 |
|
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: 271.71 E-value: 9.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 48 SVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIAL 127
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 128 EPFTVEFEK-IKEYDALTKFVIAGQKD-GWISLEAEKENASNKLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAH 205
Cdd:TIGR02262 110 GALLPVIKAaLGKSPHLEHRVVVGRPEaGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 206 LQMAPKHWLCINEDDLVWATA----APGWQKWVWSPflsvLGSGATAFVFNGRFSPETYLELLQKYQINVLCCTPTEYRM 281
Cdd:TIGR02262 190 AELYARNTLGIREDDVCFSAAklffAYGLGNALTFP----MSVGATTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 282 MAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTEstLLIGFLKDTPQRI--GSMGKGIPGSSVTV 359
Cdd:TIGR02262 266 MLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTE--MLHIFLSNLPGDVryGTSGKPVPGYRLRL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 360 VDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFE 439
Cdd:TIGR02262 344 VGDGGQDVADGEPGELLI--SGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 440 VEDALTNHPAVKECAVVAKpHDIRGNIV-KAFVILQdhtAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKI 518
Cdd:TIGR02262 422 IESALIQHPAVLEAAVVGV-ADEDGLIKpKAFVVLR---PGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKI 497
|
....*...
gi 1441463764 519 RRVELRDA 526
Cdd:TIGR02262 498 QRFKLREG 505
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-524 |
3.14e-84 |
|
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: 267.62 E-value: 3.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIAlep 129
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 130 ftvefekikeydaltkfviagqkdgwisleaekenasnklemadttrdDMAILSYTSGTTGNPKAV--THCHgWGFAHLQ 207
Cdd:cd05934 82 ------------------------------------------------DPASILYTSGTTGPPKGVviTHAN-LTFAGYY 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 208 MApkHWLCINEDDlVWATAAP----GWQKWVWSPFLSVlgsGATaFVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMA 283
Cdd:cd05934 113 SA--RRFGLGEDD-VYLTVLPlfhiNAQAVSVLAALSV---GAT-LVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 284 KlQNLNDYDLTH-LHSAVSAGEPlnREVVEQFKKYFNLTVRDGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVDD 362
Cdd:cd05934 186 A-QPPSPDDRAHrLRAAYGAPNP--PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 363 EGNSVPANTKGNIAV-PLDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVE 441
Cdd:cd05934 263 DGQELPAGEPGELVIrGLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 442 DALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtaGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRV 521
Cdd:cd05934 343 RAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRP---GETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKA 419
|
...
gi 1441463764 522 ELR 524
Cdd:cd05934 420 QLR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
48-518 |
9.55e-81 |
|
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: 260.61 E-value: 9.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 48 SVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIAL 127
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 128 EPFtveFEKIKEydALTK-------FVIAGQKDGWISLE-----AEKENASNKLEMADTTRDDMAILSYTSGTTGNPKAV 195
Cdd:cd05911 90 PDG---LEKVKE--AAKElgpkdkiIVLDDKPDGVLSIEdllspTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 196 --THcHGWGFAHLQMAPKHWLCINEDD-------LVWATAAPGWqkwVWSPFLsvlgsGATAFVFNgRFSPETYLELLQK 266
Cdd:cd05911 165 clSH-RNLIANLSQVQTFLYGNDGSNDvilgflpLYHIYGLFTT---LASLLN-----GATVIIMP-KFDSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 267 YQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYF-NLTVRDGYGQTESTLLIGFLKDTPQRI 345
Cdd:cd05911 235 YKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFpNATIKQGYGMTETGGILTVNPDGDDKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 346 GSMGKGIPGSSVTVVDDEGNS-VPANTKGNIAVplDLPALFKGYYKEPERTAKAQT-GKYYITGDLAHVDDDGYFWFEGR 423
Cdd:cd05911 315 GSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICV--RGPQVMKGYYNNPEATKETFDeDGWLHTGDIGYFDEDGYLYIVDR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 424 RDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtaGDDTLVKELQQFVKNEVAPYKYPR- 502
Cdd:cd05911 393 KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKP---GEKLTEKEVKDYVAKKVASYKQLRg 469
|
490
....*....|....*.
gi 1441463764 503 EIEFVDDLPKTNSGKI 518
Cdd:cd05911 470 GVVFVDEIPKSASGKI 485
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
32-518 |
2.88e-78 |
|
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: 257.12 E-value: 2.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTEGEDI-SVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTK 110
Cdd:cd17634 67 GDRTAIIYEGDDTSQSrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 111 DLQYRITHGEINAVIALEPF-----TVEFEKIKEyDAL---------------TKFVIAGQKDGWISLEAEKENASNKLE 170
Cdd:cd17634 147 AVAGRIIDSSSRLLITADGGvragrSVPLKKNVD-DALnpnvtsvehvivlkrTGSDIDWQEGRDLWWRDLIAKASPEHQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 171 MADTTRDDMAILSYTSGTTGNPKAVTHCHGwGFA-HLQMAPKHWLCINEDDLVWATAAPGWQkwVWSPFL--SVLGSGAT 247
Cdd:cd17634 226 PEAMNAEDPLFILYTSGTTGKPKGVLHTTG-GYLvYAATTMKYVFDYGPGDIYWCTADVGWV--TGHSYLlyGPLACGAT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 248 AFVFNGRF---SPETYLELLQKYQINVLCCTPTEYRMMAKLQN--LNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLT- 321
Cdd:cd17634 303 TLLYEGVPnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDdaIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEk 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 322 --VRDGYGQTES-----TLLIGFLkdtPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLPALFKGYYKEPER 394
Cdd:cd17634 383 cpVVDTWWQTETggfmiTPLPGAI---ELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHER 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 395 ---TAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFV 471
Cdd:cd17634 460 feqTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYV 539
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1441463764 472 ILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKI 518
Cdd:cd17634 540 VLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
32-530 |
7.27e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 254.88 E-value: 7.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTEgedisVTYQQLIEQSNKVGNVLASH-GLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTK 110
Cdd:PRK08314 24 PDKTAIVFYGRA-----ISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 111 DLQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFVIAGQKDG-----------WISLEAEKENASNKLEMA------- 172
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDYlpaepeiavpaWLRAEPPLQALAPGGVVAwkealaa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 173 -------DTTRDDMAILSYTSGTTGNPKAVTHCHGwGFAHLQMAPKHWLCINEDDLVWATAapgwqkwvwsPFLSVLG-- 243
Cdd:PRK08314 179 glappphTAGPDDLAVLPYTSGTTGVPKGCMHTHR-TVMANAVGSVLWSNSTPESVVLAVL----------PLFHVTGmv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 244 --------SGATaFVFNGRFSPETYLELLQKYQINVLCCTPTeyrMMAKL---QNLNDYDLTHLHSAVSAGEPLNREVVE 312
Cdd:PRK08314 248 hsmnapiyAGAT-VVLMPRWDREAAARLIERYRVTHWTNIPT---MVVDFlasPGLAERDLSSLRYIGGGGAAMPEAVAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 313 QFKKYFNLTVRDGYGQTEStllIGFLKDTP-QRIGSMGKGIPGSSVT--VVD-DEGNSVPANTKGNIAVplDLPALFKGY 388
Cdd:PRK08314 324 RLKELTGLDYVEGYGLTET---MAQTHSNPpDRPKLQCLGIPTFGVDarVIDpETLEELPPGEVGEIVV--HGPQVFKGY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 389 YKEPERTAKAQT---GK-YYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRG 464
Cdd:PRK08314 399 WNRPEATAEAFIeidGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRG 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1441463764 465 NIVKAFVILQDHTAGdDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAEIEK 530
Cdd:PRK08314 479 ETVKAVVVLRPEARG-KTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKAR 543
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
33-525 |
7.17e-77 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 254.68 E-value: 7.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 33 DKKAILYhntEGEDIS----VTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIatyELYIAAL---KLGVA------ 99
Cdd:PRK00174 82 DKVAIIW---EGDDPGdsrkITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIP---EAAVAMLacaRIGAVhsvvfg 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 100 ----------IIPC-SEMLRTKDLQYRithGeiNAVIALEPfTVEfEKIKEYDALTKfVI----AGQK-------DGWIS 157
Cdd:PRK00174 156 gfsaealadrIIDAgAKLVITADEGVR---G--GKPIPLKA-NVD-EALANCPSVEK-VIvvrrTGGDvdwvegrDLWWH 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 158 LEAEKENASNKLEMADTtrDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMAPKHWLCINEDDLVWATAAPGW----QKW 233
Cdd:PRK00174 228 ELVAGASDECEPEPMDA--EDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWvtghSYI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 234 VWSPflsvLGSGATAFVF--------NGRFSpetylELLQKYQINVLCCTPTEYRMMAKL--QNLNDYDLTHLHSAVSAG 303
Cdd:PRK00174 306 VYGP----LANGATTLMFegvpnypdPGRFW-----EVIDKHKVTIFYTAPTAIRALMKEgdEHPKKYDLSSLRLLGSVG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 304 EPLNREVVEQFKKYF---NLTVRDGYGQTES-----TLLIGFlkdTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNI 375
Cdd:PRK00174 377 EPINPEAWEWYYKVVggeRCPIVDTWWQTETggimiTPLPGA---TPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNL 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 376 AVPLDLPALFKGYYKEPERTAKAQTGKY---YITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKE 452
Cdd:PRK00174 454 VIKDPWPGMMRTIYGDHERFVKTYFSTFkgmYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAE 533
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441463764 453 CAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKI-RRVeLRD 525
Cdd:PRK00174 534 AAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKImRRI-LRK 606
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
32-531 |
1.64e-75 |
|
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: 250.31 E-value: 1.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTE-GEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGvAIipCSEML--- 107
Cdd:cd05967 65 GDQIALIYDSPVtGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIG-AI--HSVVFggf 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 108 RTKDLQYRITHGEINAVIALEpFTVEFEKIKEY-----DALT------KFVIAGQKDgwiSLEAEKENASNKL----EMA 172
Cdd:cd05967 142 AAKELASRIDDAKPKLIVTAS-CGIEPGKVVPYkplldKALElsghkpHHVLVLNRP---QVPADLTKPGRDLdwseLLA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 173 DTTRDDMA---------ILsYTSGTTGNPKAVTHCHGwGFA-HLQMAPKHWLCINEDDLVWATAAPGW----QKWVWSPF 238
Cdd:cd05967 218 KAEPVDCVpvaatdplyIL-YTSGTTGKPKGVVRDNG-GHAvALNWSMRNIYGIKPGDVWWAASDVGWvvghSYIVYGPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 239 LSvlgsGATAFVFNGRFS----PETYLELLQKYQINVLCCTPTEYRMMAKL----QNLNDYDLTHLHSAVSAGEPLNREV 310
Cdd:cd05967 296 LH----GATTVLYEGKPVgtpdPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpdgKYIKKYDLSSLRTLFLAGERLDPPT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 311 VEQFKKYFNLTVRDGYGQTES-----TLLIGfLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDL-PAL 384
Cdd:cd05967 372 LEWAENTLGVPVIDHWWQTETgwpitANPVG-LEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGC 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 385 FKGYYKEPERTAKAQTGK---YYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHD 461
Cdd:cd05967 451 LLTLWKNDERFKKLYLSKfpgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDE 530
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441463764 462 IRGNIVKAFVILQDH-TAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD-AEIEKW 531
Cdd:cd05967 531 LKGQVPLGLVVLKEGvKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKiADGEDY 602
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
32-525 |
2.13e-75 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 247.51 E-value: 2.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRS----IATYelyiAALKLGVAIIPCSEML 107
Cdd:PRK07656 19 GDKEAYVF-----GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSphwvIAAL----GALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 108 RTKDLQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFVIAGQKDGWISLEAEKENASNKLEMADTTR-------DDMA 180
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAErapevdpDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 181 ILSYTSGTTGNPKAVThchgwgFAHLQM--APKHW---LCINEDDLVWATaapgwqkwvwSPFLSVLG----------SG 245
Cdd:PRK07656 170 DILFTSGTTGRPKGAM------LTHRQLlsNAADWaeyLGLTEGDRYLAA----------NPFFHVFGykagvnaplmRG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 246 ATAFVFNgRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNL-TVRD 324
Cdd:PRK07656 234 ATILPLP-VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVdIVLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 325 GYGQTESTLLIGF--LKDTPQRI-GSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTG 401
Cdd:PRK07656 313 GYGLSEASGVTTFnrLDDDRKTVaGTIGTAIAGVENKIVNELGEEVPVGEVGELLV--RGPNVMKGYYDDPEATAAAIDA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 402 KYYI-TGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGD 480
Cdd:PRK07656 391 DGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELT 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1441463764 481 DtlvKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK07656 471 E---EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
48-520 |
8.73e-74 |
|
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: 240.84 E-value: 8.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 48 SVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIAL 127
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 128 epftvefekikeydaltkfviagqkdgwisleaekenasnklemadTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLq 207
Cdd:cd05935 81 ----------------------------------------------SELDDLALIPYTSGTTGLPKGCMHTHFSAAANA- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 208 MAPKHWLCINEDDLVWATAapgwqkwvwsPFLSVLG----------SGATaFVFNGRFSPETYLELLQKYQINVLCCTPT 277
Cdd:cd05935 114 LQSAVWTGLTPSDVILACL----------PLFHVTGfvgslntavyVGGT-YVLMARWDRETALELIEKYKVTFWTNIPT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 278 EYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIGFlkDTPQRIGSMGKGIPGSSV 357
Cdd:cd05935 183 MLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHT--NPPLRPKLQCLGIP*FGV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 358 T--VVDDE-GNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQT----GKYYITGDLAHVDDDGYFWFEGRRDDIIIS 430
Cdd:cd05935 261 DarVIDIEtGRELPPNEVGEIVV--RGPQIFKGYWNRPEETEESFIeikgRRFFRTGDLGYMDEEGYFFFVDRVKRMINV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 431 SGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTlVKELQQFVKNEVAPYKYPREIEFVDDL 510
Cdd:cd05935 339 SGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVT-EEDIIEWAREQMAAYKYPREVEFVDEL 417
|
490
....*....|
gi 1441463764 511 PKTNSGKIRR 520
Cdd:cd05935 418 PRSASGKILW 427
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
44-533 |
1.13e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 239.81 E-value: 1.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 44 GEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINA 123
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 124 VI---ALEPFTVEFEKIKEYDALTKFVIAGQKDGWISLEAEKENASNKLEMADTTRDDMAilsYTSGTTGNPKAV----T 196
Cdd:PRK08276 87 LIvsaALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGADML---YSSGTTGRPKGIkrplP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 197 HCHGWGFAHLQMA-PKHWLCINEDDLVWATA-----APGwqkwVWSpfLSVLGSGATAfVFNGRFSPETYLELLQKYQIN 270
Cdd:PRK08276 164 GLDPDEAPGMMLAlLGFGMYGGPDSVYLSPAplyhtAPL----RFG--MSALALGGTV-VVMEKFDAEEALALIERYRVT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 271 VLCCTPTEYRMMAKL--QNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTEStllIGFLKDTPQ----R 344
Cdd:PRK08276 237 HSQLVPTMFVRMLKLpeEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEG---GGVTVITSEdwlaH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 345 IGSMGKGIPGSsVTVVDDEGNSVPANTKGNIAVPLDLPAlFKgYYKEPERTAKAQTGKYYIT-GDLAHVDDDGYFWFEGR 423
Cdd:PRK08276 314 PGSVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYP-FE-YHNDPEKTAAARNPHGWVTvGDVGYLDEDGYLYLTDR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 424 RDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPRE 503
Cdd:PRK08276 391 KSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRS 470
|
490 500 510
....*....|....*....|....*....|
gi 1441463764 504 IEFVDDLPKTNSGKIRRVELRDAEIEKWQQ 533
Cdd:PRK08276 471 IDFEDELPRTPTGKLYKRRLRDRYWEGRQR 500
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
32-523 |
4.50e-72 |
|
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: 236.66 E-value: 4.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPcsemLrtkD 111
Cdd:cd05930 1 PDAVAVVD-----GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVP----L---D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQY---RITHgeinaVIAlepftvefekikeyDALTKFVIagqkdgwisleaekenasnklemadTTRDDMAILSYTSGT 188
Cdd:cd05930 69 PSYpaeRLAY-----ILE--------------DSGAKLVL-------------------------TDPDDLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 189 TGNPKAV--THChgwGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSvLGSGATAFVF--NGRFSPETYLELL 264
Cdd:cd05930 105 TGKPKGVmvEHR---GLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGA-LLAGATLVVLpeEVRKDPEALADLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 265 QKYQINVLCCTPTEYRMMakLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYF-NLTVRDGYGQTESTLLIGFLKDTPQ 343
Cdd:cd05930 181 AEEGITVLHLTPSLLRLL--LQELELAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVDATYYRVPPD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 344 RIGSM----GKGIPGSSVTVVDDEGNSVPANTKGNIAV--PldlpALFKGYYKEPERTAK-------AQTGKYYITGDLA 410
Cdd:cd05930 259 DEEDGrvpiGRPIPNTRVYVLDENLRPVPPGVPGELYIggA----GLARGYLNRPELTAErfvpnpfGPGERMYRTGDLV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 411 HVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtaGDDTLVKELQQF 490
Cdd:cd05930 335 RWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE---GGELDEEELRAH 411
|
490 500 510
....*....|....*....|....*....|...
gi 1441463764 491 VKNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd05930 412 LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
32-525 |
9.01e-69 |
|
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: 229.51 E-value: 9.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILyhnTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd05926 1 PDAPALV---VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIAlePFTVEFEKIKeydALTKFVIAGQKDGWIS------LEAEKENASNKLEMADTTR-----DDMA 180
Cdd:cd05926 78 FEFYLADLGSKLVLT--PKGELGPASR---AASKLGLAILELALDVgvliraPSAESLSNLLADKKNAKSEgvplpDDLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 181 ILSYTSGTTGNPKAV--THchgwgfAHLQMAPKHW---LCINEDDLVWATAapgwqkwvwsPF----------LSVLGSG 245
Cdd:cd05926 153 LILHTSGTTGRPKGVplTH------RNLAASATNItntYKLTPDDRTLVVM----------PLfhvhglvaslLSTLAAG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 246 ATAfVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYD-LTHLHSAVSAGEPLNREVVEQFKKYFNLTVRD 324
Cdd:cd05926 217 GSV-VLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 325 GYGQTESTLLIGF--LKDTPQRIGSMGKGIpGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAK-AQTG 401
Cdd:cd05926 296 AYGMTEAAHQMTSnpLPPGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEIC--LRGPNVTRGYLNNPEANAEaAFKD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 402 KYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDD 481
Cdd:cd05926 373 GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTE 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1441463764 482 tlvKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:cd05926 453 ---EELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
48-523 |
2.19e-66 |
|
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: 223.27 E-value: 2.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 48 SVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRIThgEINAVIAl 127
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVK--DSGAKLA- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 128 epFTV--EFEKIKEYDALTkfVIAGQ--KDGWISLEAEKENASNKLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGWGF 203
Cdd:cd05904 109 --FTTaeLAEKLASLALPV--VLLDSaeFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 204 AHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPF-LSVLGSGATAFVFnGRFSPETYLELLQKYQINVLCCTPTEYRMM 282
Cdd:cd05904 185 AMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFaLGLLRLGATVVVM-PRFDLEELLAAIERYKVTHLPVVPPIVLAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 283 AKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYF-NLTVRDGYGQTEST--LLIGFLKD-TPQRIGSMGKGIPGSSVT 358
Cdd:cd05904 264 VKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTgvVAMCFAPEkDRAKYGSVGRLVPNVEAK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 359 VVD-DEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYI-TGDLAHVDDDGYFWFEGRRDDIIISSGYTIG 436
Cdd:cd05904 344 IVDpETGESLPPNQTGELWI--RGPSIMKGYLNNPEATAATIDKEGWLhTGDLCYIDEDGYLFIVDRLKELIKYKGFQVA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 437 PFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSG 516
Cdd:cd05904 422 PAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRK---PGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSG 498
|
....*..
gi 1441463764 517 KIRRVEL 523
Cdd:cd05904 499 KILRKEL 505
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
9-526 |
3.02e-66 |
|
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: 225.83 E-value: 3.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 9 QKSALFAPEKYNIISEIEKYS--HIPDKKAILYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIAT 86
Cdd:cd05968 50 PWAAWFVGGRMNIVEQLLDKWlaDTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 87 YELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIALEPFT---------VEFEKIKEYDALTKFVI----AGQKD 153
Cdd:cd05968 130 VPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTrrgrevnlkEEADKACAQCPTVEKVVvvrhLGNDF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 154 GW-----ISLEAEKENASNKLEmaDTTRDDMAILSYTSGTTGNPKAVTHCHGwGFAhLQMAPKHWLCIN---EDDLVWAT 225
Cdd:cd05968 210 TPakgrdLSYDEEKETAGDGAE--RTESEDPLMIIYTSGTTGKPKGTVHVHA-GFP-LKAAQDMYFQFDlkpGDLLTWFT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 226 AApgwqKWVWSPFLsVLGS---GATAFVFNG---RFSPETYLELLQKYQINVLCCTPTEYR--MMAKLQNLNDYDLTHLH 297
Cdd:cd05968 286 DL----GWMMGPWL-IFGGlilGATMVLYDGapdHPKADRLWRMVEDHEITHLGLSPTLIRalKPRGDAPVNAHDLSSLR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 298 SAVSAGEPLNREVVeqfkKYFNLTVRDGY-------GQTE-STLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPa 369
Cdd:cd05968 361 VLGSTGEPWNPEPW----NWLFETVGKGRnpiinysGGTEiSGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPAR- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 370 NTKGNIAVPLDLPALFKGYYKEPERTAKAQTGKY---YITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTN 446
Cdd:cd05968 436 PEVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNA 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 447 HPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDA 526
Cdd:cd05968 516 HPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAA 595
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
30-525 |
3.04e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 223.66 E-value: 3.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 30 HIPDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRT 109
Cdd:PRK08316 23 RYPDKTALVF-----GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 110 KDLQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFVIAGQ------KDGWISLEAEKENASNKLEMADTTRDDMAILS 183
Cdd:PRK08316 98 EELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVlggreaPGGWLDFADWAEAGSVAEPDVELADDDLAQIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 184 YTSGTTGNPKAVTHCHGwGFAHLQMAPKHWLCINEDDLVWAtAAPGW---QKWVW-SPFLSVlgsGATAFVFNGRfSPET 259
Cdd:PRK08316 178 YTSGTESLPKGAMLTHR-ALIAEYVSCIVAGDMSADDIPLH-ALPLYhcaQLDVFlGPYLYV---GATNVILDAP-DPEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 260 YLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYF-NLTVRDGYGQTEstllIGFL 338
Cdd:PRK08316 252 ILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTE----IAPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 339 ------KDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAKAQTGKYYITGDLAHV 412
Cdd:PRK08316 328 atvlgpEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIV--HRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 413 DDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtAGDDTLVKELQQFVK 492
Cdd:PRK08316 406 DEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPK---AGATVTEDELIAHCR 482
|
490 500 510
....*....|....*....|....*....|...
gi 1441463764 493 NEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK08316 483 ARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
21-524 |
3.40e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 220.63 E-value: 3.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 21 IISEIEKYshiPDKKAILyhnteGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAI 100
Cdd:PRK06188 18 LVSALKRY---PDRPALV-----LGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 101 IPCSEMLRTKDLQYRITHGEINA-VIALEPFTVEFEKIKE-YDALTKFVIAGQKDGWISLEAEKENASNKLEMADTTRDD 178
Cdd:PRK06188 90 TALHPLGSLDDHAYVLEDAGISTlIVDPAPFVERALALLArVPSLKHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 179 MAILSYTSGTTGNPKAVTHCH--GWGFAHLQMAPKHWlcinEDDLVWATAAP-----GwqkwvwSPFLSVLGSGATAFVF 251
Cdd:PRK06188 170 IAGLAYTGGTTGKPKGVMGTHrsIATMAQIQLAEWEW----PADPRFLMCTPlshagG------AFFLPTLLRGGTVIVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 252 NGrFSPETYLELLQKYQINVLCCTPTE-YRMMaKLQNLNDYDLTHLHSAVSAGEPLN----REVVEQFKKYFNLTvrdgY 326
Cdd:PRK06188 240 AK-FDPAEVLRAIEEQRITATFLVPTMiYALL-DHPDLRTRDLSSLETVYYGASPMSpvrlAEAIERFGPIFAQY----Y 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 327 GQTESTLLIGFLK------DTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAV--PLdlpaLFKGYYKEPERTAKA 398
Cdd:PRK06188 314 GQTEAPMVITYLRkrdhdpDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVrgPL----VMDGYWNRPEETAEA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 399 QTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtA 478
Cdd:PRK06188 390 FRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLR---P 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1441463764 479 GDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PRK06188 467 GAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
32-525 |
7.37e-65 |
|
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: 218.71 E-value: 7.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHntegeDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd12118 18 PDRTSIVYG-----DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFtvefekikEYDALtkfvIAGQKDGWISLEAEKENasnklemadttrdDMAILSYTSGTTGN 191
Cdd:cd12118 93 IAFILRHSEAKVLFVDREF--------EYEDL----LAEGDPDFEWIPPADEW-------------DPIALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGWGFAHLQMAPKHWLCinEDDLVWATAAP-----GWQkWVWSPFlsvlGSGATAfVFNGRFSPETYLELLQK 266
Cdd:cd12118 148 PKGVVYHHRGAYLNALANILEWEM--KQHPVYLWTLPmfhcnGWC-FPWTVA----AVGGTN-VCLRKVDAKAIYDLIEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 267 YQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKyFNLTVRDGYGQTEST--LLIGFLKD---- 340
Cdd:cd12118 220 HKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEE-LGFDVTHVYGLTETYgpATVCAWKPewde 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 341 --TPQRIGSM---GKGIPGSS-VTVVDDEGN-SVPANTK--------GNIavpldlpaLFKGYYKEPERTAKAQTGKYYI 405
Cdd:cd12118 299 lpTEERARLKarqGVRYVGLEeVDVLDPETMkPVPRDGKtigeivfrGNI--------VMKGYLKNPEATAEAFRGGWFH 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 406 TGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtaGDDTLVK 485
Cdd:cd12118 371 SGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKE---GAKVTEE 447
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1441463764 486 ELQQFVKNEVAPYKYPREIEFvDDLPKTNSGKIRRVELRD 525
Cdd:cd12118 448 EIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
48-525 |
1.48e-63 |
|
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: 214.08 E-value: 1.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 48 SVTYQQLIEQSNKVGNVL-ASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIa 126
Cdd:cd05941 11 SITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 127 lepftvefekikeydaltkfviagqkdgwisleaekenasnklemadttrdDMAILSYTSGTTGNPKAVTHCHGWGFAHL 206
Cdd:cd05941 90 ---------------------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 207 QMAPKHWLCINED------------DLVWATAAPGWqkwvwspflsvlgSGATaFVFNGRFSPETYLELLQKYQINVLCC 274
Cdd:cd05941 119 RALVDAWRWTEDDvllhvlplhhvhGLVNALLCPLF-------------AGAS-VEFLPKFDPKEVAISRLMPSITVFMG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 275 TPTEYRMMAKLQNLNDYDLTHLHSA--------VSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIGFLKDTPQRIG 346
Cdd:cd05941 185 VPTIYTRLLQYYEAHFTDPQFARAAaaerlrlmVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 347 SMGKGIPGSSVTVVDDEGNS-VPANTKGNIAVplDLPALFKGYYKEPERTAKAQTG-KYYITGDLAHVDDDGYFWFEGR- 423
Cdd:cd05941 265 TVGMPLPGVQARIVDEETGEpLPRGEVGEIQV--RGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVDEDGYYWILGRs 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 424 RDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLvkELQQFVKNEVAPYKYPRE 503
Cdd:cd05941 343 SVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLE--ELKEWAKQRLAPYKRPRR 420
|
490 500
....*....|....*....|..
gi 1441463764 504 IEFVDDLPKTNSGKIRRVELRD 525
Cdd:cd05941 421 LILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
48-524 |
1.53e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 216.95 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 48 SVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVI-- 125
Cdd:PRK07786 42 TTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVte 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 126 -ALEPFTVEFEKIKEydALTKFVIAG--QKDGWISLEAEKENASNKLEMADTTRDDMAILSYTSGTTGNPKavthchGWG 202
Cdd:PRK07786 122 aALAPVATAVRDIVP--LLSTVVVAGgsSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPK------GAV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 203 FAHLQMAPKHWLCI------NEDDLvwataapgwqKWVWSPFLSV--LGSGATAFVFN--------GRFSPETYLELLQK 266
Cdd:PRK07786 194 LTHANLTGQAMTCLrtngadINSDV----------GFVGVPLFHIagIGSMLPGLLLGaptviyplGAFDPGQLLDVLEA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 267 YQINVLCCTPTEYRMMAKLQNLNDYDLThLH----SAVSAGEPLNREVVEQFKKYFNLTVrdgYGQTE----STLLIGfl 338
Cdd:PRK07786 264 EKVTGIFLVPAQWQAVCAEQQARPRDLA-LRvlswGAAPASDTLLRQMAATFPEAQILAA---FGQTEmspvTCMLLG-- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 339 KDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYF 418
Cdd:PRK07786 338 EDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIV--YRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYV 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 419 WFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtAGDDTLVKELQQFVKNEVAPY 498
Cdd:PRK07786 416 WVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN--DDAALTLEDLAEFLTDRLARY 493
|
490 500
....*....|....*....|....*.
gi 1441463764 499 KYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PRK07786 494 KHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
32-525 |
5.27e-63 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 214.55 E-value: 5.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTeGEdiSVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK13391 11 PDKPAVIMAST-GE--VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVI----ALEpftVEFEKIKEYDALTKFVIA---GQKDGWISLEAEKENASnklemaDTTRDDMAI--- 181
Cdd:PRK13391 88 AAYIVDDSGARALItsaaKLD---VARALLKQCPGVRHRLVLdgdGELEGFVGYAEAVAGLP------ATPIADESLgtd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 182 LSYTSGTTGNPKAVthchgwgFAHL-QMAPKHWLCINE---------DDLVWATAAP----GWQKWVwspfLSVLGSGAT 247
Cdd:PRK13391 159 MLYSSGTTGRPKGI-------KRPLpEQPPDTPLPLTAflqrlwgfrSDMVYLSPAPlyhsAPQRAV----MLVIRLGGT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 248 AFVFNgRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQN--LNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDG 325
Cdd:PRK13391 228 VIVME-HFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEevRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 326 YGQTEStllIGFLK-DTPQ---RIGSMGKGIPGSsVTVVDDEGNSVPANTKGNIavpldlpaLFKG-----YYKEPERTA 396
Cdd:PRK13391 307 YAATEG---LGFTAcDSEEwlaHPGTVGRAMFGD-LHILDDDGAELPPGEPGTI--------WFEGgrpfeYLNDPAKTA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 397 KAQT--GKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQ 474
Cdd:PRK13391 375 EARHpdGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPV 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1441463764 475 DHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK13391 455 DGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
48-525 |
1.09e-62 |
|
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: 211.05 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 48 SVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPcsemlrtkdLQYRITHGEINavial 127
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVL---------LNTRLTPNELA----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 128 epftvefekikeydaltkfviagqkdgwisleaekenasNKLEMADTTRDDMAILSYTSGTTGNPKAVthchgwgfahLQ 207
Cdd:cd05912 67 ---------------------------------------FQLKDSDVKLDDIATIMYTSGTTGKPKGV----------QQ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 208 MAPKHW---------LCINEDDlVWATAAPGWQKWVWSPFLSVLGSGATAFVFNgRFSPETYLELLQKYQINVLCCTPTe 278
Cdd:cd05912 98 TFGNHWwsaigsalnLGLTEDD-NWLCALPLFHISGLSILMRSVIYGMTVYLVD-KFDAEQVLHLINSGKVTIISVVPT- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 279 yrMMAKL-QNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYfNLTVRDGYGQTESTLLIGFLK--DTPQRIGSMGKGIPGS 355
Cdd:cd05912 175 --MLQRLlEILGEGYPNNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCSQIVTLSpeDALNKIGSAGKPLFPV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 356 SVTVVDDEGnsvPANTKGNIAvpLDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTI 435
Cdd:cd05912 252 ELKIEDDGQ---PPYEVGEIL--LKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENI 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 436 GPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtagDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNS 515
Cdd:cd05912 327 YPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE-----RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTAS 401
|
490
....*....|
gi 1441463764 516 GKIRRVELRD 525
Cdd:cd05912 402 GKLLRHELKQ 411
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-524 |
5.50e-62 |
|
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: 209.93 E-value: 5.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 48 SVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIAL 127
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 128 EPFtvefekikeydaltkfviaGQKDgwisleaekenasnKLEMADttrdDMAILSYTSGTTGNPKAVTHCHGWGFAHLQ 207
Cdd:cd05903 81 ERF-------------------RQFD--------------PAAMPD----AVALLLFTSGTTGEPKGVMHSHNTLSASIR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 208 MAPKHWLcINEDDLVWaTAAP-----GWQKWVWSPFLSvlgsGATAfVFNGRFSPETYLELLQKYQINVLCCTPTEYRMM 282
Cdd:cd05903 124 QYAERLG-LGPGDVFL-VASPmahqtGFVYGFTLPLLL----GAPV-VLQDIWDPDKALALMREHGVTFMMGATPFLTDL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 283 AKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIGFLKDTP--QRIGSMGKGIPGSSVTVV 360
Cdd:cd05903 197 LNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedRRLYTDGRPLPGVEIKVV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 361 DDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEV 440
Cdd:cd05903 277 DDTGATLAPGVEGELLS--RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 441 EDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQD-HTAGDDTLVKELQqfvKNEVAPYKYPREIEFVDDLPKTNSGKIR 519
Cdd:cd05903 355 EDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSgALLTFDELVAYLD---RQGVAKQYWPERLVHVDDLPRTPSGKVQ 431
|
....*
gi 1441463764 520 RVELR 524
Cdd:cd05903 432 KFRLR 436
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
32-523 |
2.07e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 211.82 E-value: 2.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTEgedisVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK06178 47 PQRPAIIFYGHV-----ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFVIAGQKD----------------------GWISLEAEKENASNKL 169
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADvlpaeptlplpdslraprlaaaGAIDLLPALRACTAPV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 170 EMADTTRDDMAILSYTSGTTGNPKAVTHCHGwgfahlqmapkhwlcinedDLVWATAA------PGWQKWVWSPFLSV-- 241
Cdd:PRK06178 202 PLPPPALDALAALNYTGGTTGMPKGCEHTQR-------------------DMVYTAAAayavavVGGEDSVFLSFLPEfw 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 242 -----------LGSGATaFVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHS--AVSAGEPLNR 308
Cdd:PRK06178 263 iagenfgllfpLFSGAT-LVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQvrVVSFVKKLNP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 309 EVVEQFKKYFNLTVRDG-YGQTES----TLLIGFLKDTPQRIGS---MGKGIPGSSVTVVD-DEGNSVPANTKGNIAVpl 379
Cdd:PRK06178 342 DYRQRWRALTGSVLAEAaWGMTEThtcdTFTAGFQDDDFDLLSQpvfVGLPVPGTEFKICDfETGELLPLGAEGEIVV-- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 380 DLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKP 459
Cdd:PRK06178 420 RTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRP 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441463764 460 HDIRGNIVKAFVILQDhtaGDDTLVKELQQFVKNEVAPYKYPrEIEFVDDLPKTNSGKIRRVEL 523
Cdd:PRK06178 500 DPDKGQVPVAFVQLKP---GADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
46-525 |
3.44e-61 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 211.03 E-value: 3.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 46 DISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPrSIATYELYIAA-LKLGVAIIPCSEMLRTKDLQYRITHGEINAV 124
Cdd:PRK07059 46 GKAITYGELDELSRALAAWLQSRGLAKGARVAIMMP-NVLQYPVAIAAvLRAGYVVVNVNPLYTPRELEHQLKDSGAEAI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 125 IALEPFTVEFEKIKEYDALTKFVIAGQKD-----GWI---------------SL-------EAEKENASNKLEMADTTRD 177
Cdd:PRK07059 125 VVLENFATTVQQVLAKTAVKHVVVASMGDllgfkGHIvnfvvrrvkkmvpawSLpghvrfnDALAEGARQTFKPVKLGPD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 178 DMAILSYTSGTTGNPKAVTHCHGWGFA-----HLQMAPKHWLCINEDDLVWATAAPGWQKWVWS--PFLSVLGSGATAFV 250
Cdd:PRK07059 205 DVAFLQYTGGTTGVSKGATLLHRNIVAnvlqmEAWLQPAFEKKPRPDQLNFVCALPLYHIFALTvcGLLGMRTGGRNILI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 251 FNGRFSPeTYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTE 330
Cdd:PRK07059 285 PNPRDIP-GFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 331 -STLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGK-YYITGD 408
Cdd:PRK07059 364 tSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICI--RGPQVMAGYWNRPDETAKVMTADgFFRTGD 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 409 LAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDtlvkELQ 488
Cdd:PRK07059 442 VGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEE----DVK 517
|
490 500 510
....*....|....*....|....*....|....*..
gi 1441463764 489 QFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK07059 518 AFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
32-530 |
1.21e-60 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 207.51 E-value: 1.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK03640 16 PDRTAIEF-----EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFTVEFEkikeydaltkfviAGQKDGWISLEAEKENASNKLEMADTtrDDMAILSYTSGTTGN 191
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAKLI-------------PGISVKFAELMNGPKEEAEIQEEFDL--DEVATIMYTSGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVthchgwgfahLQMAPKHW---------LCINEDDlVWATAAP-----GwqkwvwspfLSVLGSGatafVFNG---- 253
Cdd:PRK03640 156 PKGV----------IQTYGNHWwsavgsalnLGLTEDD-CWLAAVPifhisG---------LSILMRS----VIYGmrvv 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 254 ---RFSPETYLELLQKYQINVLCCTPTeyrMMAKLqnLNDYDLTHLHSAVSA----GEPLNREVVEQFKKYfNLTVRDGY 326
Cdd:PRK03640 212 lveKFDAEKINKLLQTGGVTIISVVST---MLQRL--LERLGEGTYPSSFRCmllgGGPAPKPLLEQCKEK-GIPVYQSY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 327 GQTESTLLIGFL--KDTPQRIGSMGKGIPGSSVTVVDDeGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYY 404
Cdd:PRK03640 286 GMTETASQIVTLspEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVV--KGPNVTKGYLNREDATRETFQDGWF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 405 ITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILqDHTAGDDtlv 484
Cdd:PRK03640 363 KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK-SGEVTEE--- 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1441463764 485 kELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAEIEK 530
Cdd:PRK03640 439 -ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
32-524 |
3.85e-60 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 206.78 E-value: 3.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTeGEDISvtYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK13390 11 PDRPAVIVAET-GEQVS--YRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFTVEFEKIKEyDALTKFVIAGQKDGWISLEAEKENASNKLemadTTRDDMAILSYTSGTTGN 191
Cdd:PRK13390 88 ADYIVGDSGARVLVASAALDGLAAKVGA-DLPLRLSFGGEIDGFGSFEAALAGAGPRL----TEQPCGAVMLYSSGTTGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVT------HCHGWGFAHLQMApKHWLCINEDDlVWATAAPGWQK--WVWSPFLSVLGSgatAFVFNGRFSPETYLEL 263
Cdd:PRK13390 163 PKGIQpdlpgrDVDAPGDPIVAIA-RAFYDISESD-IYYSSAPIYHAapLRWCSMVHALGG---TVVLAKRFDAQATLGH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 264 LQKYQINVLCCTPTeyrMMAKLQNLND-----YDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIgfL 338
Cdd:PRK13390 238 VERYRITVTQMVPT---MFVRLLKLDAdvrtrYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHGMT--F 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 339 KDTPQRI---GSMGKGIPGSsVTVVDDEGNSVPANTKGNIAVPLDlpALFKGYYKEPERTAKAQ--TGKYYIT-GDLAHV 412
Cdd:PRK13390 313 IDSPDWLahpGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERD--RLPFRYLNDPEKTAAAQhpAHPFWTTvGDLGSV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 413 DDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVK 492
Cdd:PRK13390 390 DEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTR 469
|
490 500 510
....*....|....*....|....*....|..
gi 1441463764 493 NEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PRK13390 470 SRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
26-524 |
6.21e-60 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 206.46 E-value: 6.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 26 EKYShipDKKAILYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSE 105
Cdd:PRK08008 18 DVYG---HKTALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 106 MLRTKDLQYRITHGEINAVIALEPFTVEFEKIKEYDA--LTKFVIAG----QKDGWISLEAEKENASNKLEMADT-TRDD 178
Cdd:PRK08008 95 RLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDAtpLRHICLTRvalpADDGVSSFTQLKAQQPATLCYAPPlSTDD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 179 MAILSYTSGTTGNPKAV--THCHgWGFAHLQMApkhWLCINEDDLVWATAAPGW----QKWVWSPFLSVlgsGATaFVFN 252
Cdd:PRK08008 175 TAEILFTSGTTSRPKGVviTHYN-LRFAGYYSA---WQCALRDDDVYLTVMPAFhidcQCTAAMAAFSA---GAT-FVLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 253 GRFSPETYLELLQKYQINVLCCTPteyrMMAK---LQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQT 329
Cdd:PRK08008 247 EKYSARAFWGQVCKYRATITECIP----MMIRtlmVQPPSANDRQHCLREVMFYLNLSDQEKDAFEERFGVRLLTSYGMT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 330 EStlLIGFLKDTP---QRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPlDLPA--LFKGYYKEPERTAKAQTGK-Y 403
Cdd:PRK08008 323 ET--IVGIIGDRPgdkRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIK-GVPGktIFKEYYLDPKATAKVLEADgW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 404 YITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILqdhTAGDDTL 483
Cdd:PRK08008 400 LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVL---NEGETLS 476
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1441463764 484 VKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PRK08008 477 EEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
29-539 |
6.98e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 207.58 E-value: 6.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 29 SHIPDKKAILYHnteGEDIsvTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLR 108
Cdd:PRK06710 35 SRYPEKKALHFL---GKDI--TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 109 TKDLQYRITHGEINAVIALE---------------------------PF----TVEFEKIKEYDALTKFVIAGQKDGWIS 157
Cdd:PRK06710 110 ERELEYQLHDSGAKVILCLDlvfprvtnvqsatkiehvivtriadflPFpknlLYPFVQKKQSNLVVKVSESETIHLWNS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 158 LEAEKENAsnkLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMApKHWL--CINEDDLVWATAapgwqkwvw 235
Cdd:PRK06710 190 VEKEVNTG---VEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMG-VQWLynCKEGEEVVLGVL--------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 236 sPFLSVLGSGAT---------AFVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPL 306
Cdd:PRK06710 257 -PFFHVYGMTAVmnlsimqgyKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 307 NREVVEQFKKYFNLTVRDGYGQTESTLLI--GFL--KDTPqriGSMGKGIPGSSVTVVDDE-GNSVPANTKGNIAVplDL 381
Cdd:PRK06710 336 PVEVQEKFETVTGGKLVEGYGLTESSPVThsNFLweKRVP---GSIGVPWPDTEAMIMSLEtGEALPPGEIGEIVV--KG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 382 PALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHD 461
Cdd:PRK06710 411 PQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDP 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441463764 462 IRGNIVKAFVILQDHTAGDDtlvKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIrrveLRDAEIEKWQQQKDSNQ 539
Cdd:PRK06710 491 YRGETVKAFVVLKEGTECSE---EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKI----LRRVLIEEEKRKNEDEQ 561
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
25-525 |
1.88e-59 |
|
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: 205.84 E-value: 1.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 25 IEKYSHIPDKKAILYHNTEgedISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCS 104
Cdd:cd17642 24 MKRYASVPGTIAFTDAHTG---VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 105 EMLRTKDLQYRI----------THGEINAVIALEPFTVEFEKI---------KEYDALTKFvIAGQKDGWISLEAEKENA 165
Cdd:cd17642 101 DIYNERELDHSLniskptivfcSKKGLQKVLNVQKKLKIIKTIiildskedyKGYQCLYTF-ITQNLPPGFNEYDFKPPS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 166 SNKlemadttRDDMAILSYTSGTTGNPKAVTHCHG---WGFAHlQMAPKHWLCINEDDLVwATAAPGWQKWVWSPFLSVL 242
Cdd:cd17642 180 FDR-------DEQVALIMNSSGSTGLPKGVQLTHKnivARFSH-ARDPIFGNQIIPDTAI-LTVIPFHHGFGMFTTLGYL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 243 GSGATaFVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLT- 321
Cdd:cd17642 251 ICGFR-VVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPg 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 322 VRDGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVD-DEGNSVPANTKGNIAVPLDLpaLFKGYYKEPERTAKAQT 400
Cdd:cd17642 330 IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPM--IMKGYVNNPEATKALID 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 401 GKYYI-TGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtAG 479
Cdd:cd17642 408 KDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLE---AG 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1441463764 480 DDTLVKELQQFVKNEVAPYKYPR-EIEFVDDLPKTNSGKIRRVELRD 525
Cdd:cd17642 485 KTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
32-527 |
1.92e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 205.93 E-value: 1.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILyhnteGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIpcseMLRT-- 109
Cdd:PRK07788 63 PDRAALI-----DERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARII----LLNTgf 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 110 -----KDLQYRitHGeINAVIALEPFTVEFEKIKE----YDALTKFVIAG--QKDGWISLEAEKENASNKLEMADTTRDD 178
Cdd:PRK07788 134 sgpqlAEVAAR--EG-VKALVYDDEFTDLLSALPPdlgrLRAWGGNPDDDepSGSTDETLDDLIAGSSTAPLPKPPKPGG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 179 MAILsyTSGTTGNPKAVTHCHGWGFAHL-QMAPKHWLCINEDDLVwatAAPGWQKWVWSPFLSVLGSGATaFVFNGRFSP 257
Cdd:PRK07788 211 IVIL--TSGTTGTPKGAPRPEPSPLAPLaGLLSRVPFRAGETTLL---PAPMFHATGWAHLTLAMALGST-VVLRRRFDP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 258 ETYLELLQKYQINVLCCTPTEYRMMAKL--QNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTE-STLL 334
Cdd:PRK07788 285 EATLEDIAKHKATALVVVPVMLSRILDLgpEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvAFAT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 335 IGflkdTPQRI----GSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLPalFKGYykeperTA---KAQTGKYYITG 407
Cdd:PRK07788 365 IA----TPEDLaeapGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFP--FEGY------TDgrdKQIIDGLLSSG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 408 DLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDtlvKEL 487
Cdd:PRK07788 433 DVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE---DAI 509
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1441463764 488 QQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAE 527
Cdd:PRK07788 510 KDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-524 |
2.12e-59 |
|
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: 200.58 E-value: 2.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 DDMAILSYTSGTTGNPKAVTHCH------GWGFAH-LQMAPKHWLCIneddlvwataaPgwqkwvwSPF----------L 239
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHhnivnnGYFIGErLGLTEQDRLCI-----------P-------VPLfhcfgsvlgvL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 240 SVLGSGATAfVFNGR-FSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYF 318
Cdd:cd05917 64 ACLTHGATM-VFPSPsFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 319 NLT-VRDGYGQTESTLLI--GFLKDTP-QRIGSMGKGIPGSSVTVVDDEGNSVPA-NTKGNIAVPLDLpaLFKGYYKEPE 393
Cdd:cd05917 143 NMKdVTIAYGMTETSPVStqTRTDDSIeKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYS--VMKGYWNDPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 394 RTAKAQTG-KYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVI 472
Cdd:cd05917 221 KTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIR 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1441463764 473 LQDhtaGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:cd05917 301 LKE---GAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
50-526 |
6.68e-59 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 204.22 E-value: 6.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIALEP 129
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 130 FTVEFEKIKEYD-ALTKFVIAGQKDGWiSLEAEKENAS-----NKLEMADTTRDDMAILSYTSGTTGNPKAVTHCHG--- 200
Cdd:PRK06155 128 LLAALEAADPGDlPLPAVWLLDAPASV-SVPAGWSTAPlppldAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAqfy 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 201 -WGfahLQMApkHWLCINEDDlVWATAAPGWQKWVWSPFLSVLGSGATaFVFNGRFSPETYLELLQKYQinvlcCTPTEY 279
Cdd:PRK06155 207 wWG---RNSA--EDLEIGADD-VLYTTLPLFHTNALNAFFQALLAGAT-YVLEPRFSASGFWPAVRRHG-----ATVTYL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 280 --RMMAKL--QNLNDYDLTH-LHSAVSAGEPLnrEVVEQFKKYFNLTVRDGYGQTESTLLIGFLKDTpQRIGSMGKGIPG 354
Cdd:PRK06155 275 lgAMVSILlsQPARESDRAHrVRVALGPGVPA--ALHAAFRERFGVDLLDGYGSTETNFVIAVTHGS-QRPGSMGRLAPG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 355 SSVTVVDDEGNSVPANTKGNIAVPLDLP-ALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGY 433
Cdd:PRK06155 352 FEARVVDEHDQELPDGEPGELLLRADEPfAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 434 TIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTlvkELQQFVKNEVAPYKYPREIEFVDDLPKT 513
Cdd:PRK06155 432 NISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPV---ALVRHCEPRLAYFAVPRYVEFVAALPKT 508
|
490
....*....|...
gi 1441463764 514 NSGKIRRVELRDA 526
Cdd:PRK06155 509 ENGKVQKFVLREQ 521
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
30-529 |
9.55e-59 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 204.24 E-value: 9.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 30 HIPDKKAILYHNtegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRT 109
Cdd:PRK12583 30 RFPDREALVVRH---QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 110 KDLQYRITHGEINAVIALEPFtvefeKIKEYDALTKFVIAGQKDG-----------------------------WISLEA 160
Cdd:PRK12583 107 SELEYALGQSGVRWVICADAF-----KTSDYHAMLQELLPGLAEGqpgalacerlpelrgvvslapapppgflaWHELQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 161 EKENASNK-LE--MADTTRDDMAILSYTSGTTGNPKAVTHCH------GWgFAHLQMApkhwlCINEDDLVwataapgwq 231
Cdd:PRK12583 182 RGETVSREaLAerQASLDRDDPINIQYTSGTTGFPKGATLSHhnilnnGY-FVAESLG-----LTEHDRLC--------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 232 kwVWSPF-------LSVLG---SGATAFVFNGRFSPETYLELLQKYQINVLCCTPTEYrmMAKLQN--LNDYDLTHLHSA 299
Cdd:PRK12583 247 --VPVPLyhcfgmvLANLGcmtVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMF--IAELDHpqRGNFDLSSLRTG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 300 VSAGEPLNREVVEQFKKYFNLT-VRDGYGQTES---TLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNI 375
Cdd:PRK12583 323 IMAGAPCPIEVMRRVMDEMHMAeVQIAYGMTETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGEL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 376 AVPLDLpaLFKGYYKEPERTAKAQTGKYYI-TGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECA 454
Cdd:PRK12583 403 CTRGYS--VMKGYWNNPEATAESIDEDGWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQ 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1441463764 455 VVAKPHDIRGNIVKAFVILQ-DHTAGDDtlvkELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAEIE 529
Cdd:PRK12583 481 VFGVPDEKYGEEIVAWVRLHpGHAASEE----ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIE 552
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
19-523 |
1.02e-58 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 202.78 E-value: 1.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 19 YNIISEIEKYSHI-PDKKAILyhnteGEDISVTYQQLIEQSNKVGNVLASH-GLSKGDKVLIMMPRSIATYELYIAALKL 96
Cdd:PRK06839 2 QGIAYWIEKRAYLhPDRIAII-----TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 97 GVAIIPCSEMLRTKDLQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFViagqkdgWISLEAEKENASnKLEMADTTR 176
Cdd:PRK06839 77 ECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVI-------SITSLKEIEDRK-IDNFVEKNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 DDMAILSYTSGTTGNPKAvthchgwgfAHLQMAPKHWLCINEDDLVWATAAPgwQKWVWSPFLSVLGSGATAF------- 249
Cdd:PRK06839 149 SASFIICYTSGTTGKPKG---------AVLTQENMFWNALNNTFAIDLTMHD--RSIVLLPLFHIGGIGLFAFptlfagg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 250 --VFNGRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYfNLTVRDGYG 327
Cdd:PRK06839 218 viIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 328 QTES--TLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYI 405
Cdd:PRK06839 297 MTETspTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLI--RGPNVMKEYWNRPDATEETIQDGWLC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 406 TGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtAGDDTLVK 485
Cdd:PRK06839 375 TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKK---SSSVLIEK 451
|
490 500 510
....*....|....*....|....*....|....*...
gi 1441463764 486 ELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:PRK06839 452 DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
30-525 |
1.16e-58 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 203.75 E-value: 1.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 30 HIPDKKAIL-YHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLR 108
Cdd:PRK13295 36 SCPDKTAVTaVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 109 TKDLQYRITHGEINAVIALEPFT-VEFEKI-----KEYDALTKFVIAGqKDGWISLEA-----EKENASNKLEMADTTR- 176
Cdd:PRK13295 116 ERELSFMLKHAESKVLVVPKTFRgFDHAAMarrlrPELPALRHVVVVG-GDGADSFEAllitpAWEQEPDAPAILARLRp 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 --DDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMAPKHwLCINEDDLVWATAAPGWQKWVWSPFLSVLGSGATAfVFNGR 254
Cdd:PRK13295 195 gpDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAER-LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATA-VLQDI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 255 FSPETYLELLQKYQIN-VLCCTP--TEyrmMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTES 331
Cdd:PRK13295 273 WDPARAAELIRTEGVTfTMASTPflTD---LTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 332 TLL-IGFLKDTPQR-IGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGkYYITGDL 409
Cdd:PRK13295 350 GAVtLTKLDDPDERaSTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQV--RGCSNFGGYLKRPQLNGTDADG-WFDTGDL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 410 AHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtAGDDTLVKELQQ 489
Cdd:PRK13295 427 ARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR---PGQSLDFEEMVE 503
|
490 500 510
....*....|....*....|....*....|....*..
gi 1441463764 490 FVKNE-VAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK13295 504 FLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
34-525 |
3.05e-57 |
|
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: 199.39 E-value: 3.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 34 KKAILYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQ 113
Cdd:cd12119 11 DREIVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 114 YRITHGEINAVIA-------LEPFTVEFEKIKEYDALTKFVIAGQKD--GWISLEAEKENASNKLEMADTTRDDMAILSY 184
Cdd:cd12119 91 YIINHAEDRVVFVdrdflplLEAIAPRLPTVEHVVVMTDDAAMPEPAgvGVLAYEELLAAESPEYDWPDFDENTAAAICY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 185 TSGTTGNPKAVTHCHGWGFAH-LQMAPKHWLCINEDDLVWAtAAPGWQKWVW-SPFLSVLgSGAtAFVFNGRF-SPETYL 261
Cdd:cd12119 171 TSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVVLP-VVPMFHVNAWgLPYAAAM-VGA-KLVLPGPYlDPASLA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 262 ELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFnLTVRDGYGQTE-------STLL 334
Cdd:cd12119 248 ELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERG-VRVIHAWGMTEtsplgtvARPP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 335 IGFLKDTPQ-----RIgSMGKGIPGSSVTVVDDEGNSVPA--NTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITG 407
Cdd:cd12119 327 SEHSNLSEDeqlalRA-KQGRPVPGVELRIVDDDGRELPWdgKAVGELQV--RGPWVTKSYYKNDEESEALTEDGWLRTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 408 DLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtaGDDTLVKEL 487
Cdd:cd12119 404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKE---GATVTAEEL 480
|
490 500 510
....*....|....*....|....*....|....*...
gi 1441463764 488 QQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:cd12119 481 LEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
65-526 |
9.33e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 198.34 E-value: 9.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 65 LASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSemlrtkdlqYRITHGEI---------NAVIALEPFTVEFE 135
Cdd:PRK07470 49 LAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN---------FRQTPDEVaylaeasgaRAMICHADFPEHAA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 136 KIKEYDALTKFVIA-GQKDGWISLEAE-KENASNKLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGwgfahlQMA---P 210
Cdd:PRK07470 120 AVRAASPDLTHVVAiGGARAGLDYEALvARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG------QMAfviT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 211 KHwLCinedDLVWATA--------APgwqkwvwspfLSvLGSG-----------ATAFVFNGRFSPETYLELLQKYQINV 271
Cdd:PRK07470 194 NH-LA----DLMPGTTeqdaslvvAP----------LS-HGAGihqlcqvargaATVLLPSERFDPAEVWALVERHRVTN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 272 LCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNRE-----------VVEQFkkyfnltvrdgYGQTESTLLIGFL-- 338
Cdd:PRK07470 258 LFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRAdqkralaklgkVLVQY-----------FGLGEVTGNITVLpp 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 339 -----KDTPQ-RIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLdlPALFKGYYKEPERTAKAQTGKYYITGDLAHV 412
Cdd:PRK07470 327 alhdaEDGPDaRIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIG--PAVFAGYYNNPEANAKAFRDGWFRTGDLGHL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 413 DDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDtlvKELQQFVK 492
Cdd:PRK07470 405 DARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE---AELLAWLD 481
|
490 500 510
....*....|....*....|....*....|....
gi 1441463764 493 NEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDA 526
Cdd:PRK07470 482 GKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
32-526 |
1.89e-56 |
|
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: 197.68 E-value: 1.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILyhnteGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:COG1021 39 PDRIAVV-----DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALPAHRRAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIA--------LEPFTVEFekIKEYDALTKFVIAGQKDGWISLeAEKENASNKLEMADTTRDDMAILS 183
Cdd:COG1021 114 ISHFAEQSEAVAYIIpdrhrgfdYRALAREL--QAEVPSLRHVLVVGDAGEFTSL-DALLAAPADLSEPRPDPDDVAFFQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 184 YTSGTTGNPKAV--THcHGWGFAHLQMAPkhwLC-INEDD--LVWATAA-------PGwqkwvwspFLSVLGSGATAfVF 251
Cdd:COG1021 191 LSGGTTGLPKLIprTH-DDYLYSVRASAE---ICgLDADTvyLAALPAAhnfplssPG--------VLGVLYAGGTV-VL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 252 NGRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTES 331
Cdd:COG1021 258 APDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 332 TLLIGFLKDTPQRI-GSMGKGI-PGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQT--GkYYITG 407
Cdd:COG1021 338 LVNYTRLDDPEEVIlTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLT--RGPYTIRGYYRAPEHNARAFTpdG-FYRTG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 408 DLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGddtlVKEL 487
Cdd:COG1021 415 DLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLT----LAEL 490
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1441463764 488 QQFVKN-EVAPYKYPREIEFVDDLPKTNSGKIRRVELRDA 526
Cdd:COG1021 491 RRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
32-525 |
1.03e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 194.72 E-value: 1.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTEgedisVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK06145 16 PDRAALVYRDQE-----ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEpftvEFEkikeydaltkfVIAGQKDGWISLEAEKENASNKL--------EMADTTRDDMAILS 183
Cdd:PRK06145 91 VAYILGDAGAKLLLVDE----EFD-----------AIVALETPKIVIDAAAQADSRRLaqggleipPQAAVAPTDLVRLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 184 YTSGTTGNPKAVTHCHG---WGFAHLQMApkhwLCINEDDL---------VWATAAPGwqkwvwspfLSVLGSGATAFVF 251
Cdd:PRK06145 156 YTSGTTDRPKGVMHSYGnlhWKSIDHVIA----LGLTASERllvvgplyhVGAFDLPG---------IAVLWVGGTLRIH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 252 NgRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYF-NLTVRDGYGQTE 330
Cdd:PRK06145 223 R-EFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFtRARYIDAYGLTE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 331 STLLIGFLKDTPQ--RIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAKAQTGKYYITGD 408
Cdd:PRK06145 302 TCSGDTLMEAGREieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEIC--MRGPKVTKGYWKDPEKTAEAFYGDWFRSGD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 409 LAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtAGDDTLVKELQ 488
Cdd:PRK06145 380 VGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLN---PGATLTLEALD 456
|
490 500 510
....*....|....*....|....*....|....*..
gi 1441463764 489 QFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK06145 457 RHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
50-530 |
1.61e-55 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 195.66 E-value: 1.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASH-GLSKGDKVLIMMPR----SIATYelyiAALKLGVAIIPCSEMLRTKDLQYRITHGEINAV 124
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNllqyPIALF----GILRAGMIVVNVNPLYTPRELEHQLNDSGAKAI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 125 IALEPFTVEFEKIKEYDALTKFVIAGQKDgwiSLEAEKENASN-------------KLEMA------------------D 173
Cdd:PRK08974 126 VIVSNFAHTLEKVVFKTPVKHVILTRMGD---QLSTAKGTLVNfvvkyikrlvpkyHLPDAisfrsalhkgrrmqyvkpE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 174 TTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMApkhwlcineddlvwataapgwqKWVWSPFLSV------------ 241
Cdd:PRK08974 203 LVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQA----------------------KAAYGPLLHPgkelvvtalply 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 242 ------------LGSGATA-FVFNGRFSPETYLELlQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNR 308
Cdd:PRK08974 261 hifaltvncllfIELGGQNlLITNPRDIPGFVKEL-KKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 309 EVVEQFKKYFNLTVRDGYGQTE-STLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKG 387
Cdd:PRK08974 340 AVAERWVKLTGQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWV--KGPQVMLG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 388 YYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIV 467
Cdd:PRK08974 418 YWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAV 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441463764 468 KAFVILQDHTAGDDtlvkELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAEIEK 530
Cdd:PRK08974 498 KIFVVKKDPSLTEE----ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
32-520 |
4.93e-54 |
|
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: 189.00 E-value: 4.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPcsemlrtkd 111
Cdd:cd05945 5 PDRPAVVE-----GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 lqyrithgeINAVIALEpftvEFEKIKEYDALTKFVIAGqkdgwisleaekenasnklemadttrDDMAILSYTSGTTGN 191
Cdd:cd05945 71 ---------LDASSPAE----RIREILDAAKPALLIADG--------------------------DDNAYIIFTSGSTGR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHG-------WGFAHLQMapkhwlciNEDDLVWATAapgwqkwvwsPF---LSV------LGSGATAFVfNGRF 255
Cdd:cd05945 112 PKGVQISHDnlvsftnWMLSDFPL--------GPGDVFLNQA----------PFsfdLSVmdlypaLASGATLVP-VPRD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 256 SPETYLEL---LQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYF-NLTVRDGYGQTES 331
Cdd:cd05945 173 ATADPKQLfrfLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 332 TLLIGFLKDTPQRIGSM-----GKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKA--QTGKY- 403
Cdd:cd05945 253 TVAVTYIEVTPEVLDGYdrlpiGYAKPGAKLVILDEDGRPVPPGEKGELVI--SGPSVSKGYLNNPEKTAAAffPDEGQr 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 404 -YITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTagDDT 482
Cdd:cd05945 331 aYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGA--EAG 408
|
490 500 510
....*....|....*....|....*....|....*...
gi 1441463764 483 LVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:cd05945 409 LTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDR 446
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
31-517 |
1.27e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 189.71 E-value: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 31 IPDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTK 110
Cdd:PRK07798 16 VPDRVALVC-----GDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 111 DLQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFVI-------AGQKDGWISLEAEKENASNKLEMADTTRDDMAILs 183
Cdd:PRK07798 91 ELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVvvedgsgNDLLPGAVDYEDALAAGSPERDFGERSPDDLYLL- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 184 YTSGTTGNPKAVTHCHG--W-----GFAHLQMAPKHwlciNEDDLVWATAAPGWQKWV-----------WSPFLSVLGSG 245
Cdd:PRK07798 170 YTGGTTGMPKGVMWRQEdiFrvllgGRDFATGEPIE----DEEELAKRAAAGPGMRRFpapplmhgagqWAAFAALFSGQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 246 ATAFVFNGRFSPETYLELLQKYQINVLCCT------PteyrMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYF- 318
Cdd:PRK07798 246 TVVLLPDVRFDADEVWRTIEREKVNVITIVgdamarP----LLDALEARGPYDLSSLFAIASGGALFSPSVKEALLELLp 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 319 NLTVRDGYGQTEStlliGFLKDTPQRIGSMGKGIP----GSSVTVVDDEGNSVPANT--KGNIA----VPLdlpalfkGY 388
Cdd:PRK07798 322 NVVLTDSIGSSET----GFGGSGTVAKGAVHTGGPrftiGPRTVVLDEDGNPVEPGSgeIGWIArrghIPL-------GY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 389 YKEPERTAKaqTGK------YYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDI 462
Cdd:PRK07798 391 YKDPEKTAE--TFPtidgvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDER 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1441463764 463 RGNIVKAFVILQDHTAGDDTlvkELQQFVKNEVAPYKYPREIEFVDDLPKTNSGK 517
Cdd:PRK07798 469 WGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
68-524 |
3.50e-53 |
|
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: 186.88 E-value: 3.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 68 HGLSKGDKVLIMMPRSIATYELYI----AALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIALEPFTVEFEKIkeydal 143
Cdd:cd05922 13 AGGVRGERVVLILPNRFTYIELSFavayAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDA------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 144 tkFVIAGQKDGWISLEAEKENASNkLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQmAPKHWLCINEDDLVw 223
Cdd:cd05922 87 --LPASPDPGTVLDADGIRAARAS-APAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANAR-SIAEYLGITADDRA- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 224 ATAAPgwqkWVWSPFLSVLGS----GATAFVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMAKLqNLNDYDLTHLHSA 299
Cdd:cd05922 162 LTVLP----LSYDYGLSVLNThllrGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRL-GFDPAKLPSLRYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 300 VSAGEPLNREVVEQFKKYFNLT-VRDGYGQTESTLLIGFLKdtPQRI----GSMGKGIPGSSVTVVDDEGNSVPANTKGN 374
Cdd:cd05922 237 TQAGGRLPQETIARLRELLPGAqVYVMYGQTEATRRMTYLP--PERIlekpGSIGLAIPGGEFEILDDDGTPTPPGEPGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 375 IAVplDLPALFKGYYK-EPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKEC 453
Cdd:cd05922 315 IVH--RGPNVMKGYWNdPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1441463764 454 AVVAKPhDIRGNIVKAFVilqdhTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:cd05922 393 AAVGLP-DPLGEKLALFV-----TAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
32-534 |
1.97e-52 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 186.88 E-value: 1.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILyhntEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK06087 37 PDKIAVV----DNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPF-TVEFEK-----IKEYDALTKFVI---AGQKDGWISLEAEKENASNKLEMADTTRDDMAIL 182
Cdd:PRK06087 113 LVWVLNKCQAKMFFAPTLFkQTRPVDlilplQNQLPQLQQIVGvdkLAPATSSLSLSQIIADYEPLTTAITTHGDELAAV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 183 SYTSGTTGNPKAVTHCHGwgfaHLQMAPKHW---LCINEDDLVWATA----APGWQKWVWSPFLSvlgsGATAfVFNGRF 255
Cdd:PRK06087 193 LFTSGTEGLPKGVMLTHN----NILASERAYcarLNLTWQDVFMMPAplghATGFLHGVTAPFLI----GARS-VLLDIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 256 SPETYLELLQKYQIN-VLCCTPTEYRMMAKLQNlNDYDLTHLHSAVSAGEPLNREVVEQFKKYfNLTVRDGYGQTEST-- 332
Cdd:PRK06087 264 TPDACLALLEQQRCTcMLGATPFIYDLLNLLEK-QPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSph 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 333 LLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKA--QTGKYYiTGDLA 410
Cdd:PRK06087 342 AVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEAS--RGPNVFMGYLDEPELTARAldEEGWYY-SGDLC 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 411 HVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAgDDTLVKELQQF 490
Cdd:PRK06087 419 RMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHH-SLTLEEVVAFF 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1441463764 491 VKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAEIEKWQQQ 534
Cdd:PRK06087 498 SRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLTQD 541
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
33-524 |
1.07e-51 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 187.03 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 33 DKKAILYH-NTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPrsiatyelyiAALKLGVAIIPCSEM----- 106
Cdd:PLN02654 104 DKIAIYWEgNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLP----------MLMELPIAMLACARIgavhs 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 107 -----LRTKDLQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFVIAGQKDGW---ISLEAEKENASNK---------- 168
Cdd:PLN02654 174 vvfagFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVsvgICLTYENQLAMKRedtkwqegrd 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 169 ---------------LEMADTtrDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMAPKHWLCINEDDLVWATAAPGW--- 230
Cdd:PLN02654 254 vwwqdvvpnyptkceVEWVDA--EDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWitg 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 231 QKWV-WSPFLSvlgsGATAFVFNGRFS---PETYLELLQKYQINVLCCTPTEYR--MMAKLQNLNDYDLTHLHSAVSAGE 304
Cdd:PLN02654 332 HSYVtYGPMLN----GATVLVFEGAPNypdSGRCWDIVDKYKVTIFYTAPTLVRslMRDGDEYVTRHSRKSLRVLGSVGE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 305 PLNREVveqFKKYFNLT------VRDGYGQTESTlliGFLKDT-----PQRIGSMGKGIPGSSVTVVDDEGNSVPANTKG 373
Cdd:PLN02654 408 PINPSA---WRWFFNVVgdsrcpISDTWWQTETG---GFMITPlpgawPQKPGSATFPFFGVQPVIVDEKGKEIEGECSG 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 374 NIAVPLDLPALFKGYYKEPER---TAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAV 450
Cdd:PLN02654 482 YLCVKKSWPGAFRTLYGDHERyetTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQC 561
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441463764 451 KECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PLN02654 562 AEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
23-526 |
2.11e-50 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 181.61 E-value: 2.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 23 SEIEKYSHIPdkkaiLYHNTeGEDIsvTYQ---QLIEQSnkVGNVLASHGLSKGDKVLIMMPR----SIATYelyiAALK 95
Cdd:PRK08751 33 TSVAKFADRP-----AYHSF-GKTI--TYReadQLVEQF--AAYLLGELQLKKGDRVALMMPNclqyPIATF----GVLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 96 LGVAIIPCSEMLRTKDLQYRITHGEINAVIALEPFTVEFEK------IKEY-------------DALTKFVIAGQK---- 152
Cdd:PRK08751 99 AGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQviadtpVKQVittglgdmlgfpkAALVNFVVKYVKklvp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 153 ----DGWISL-EAEKENASNKLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMApKHWLC----INEDDLVW 223
Cdd:PRK08751 179 eyriNGAIRFrEALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQA-HQWLAgtgkLEEGCEVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 224 ATAAPGWQKWVWSP----FLSVlgSGATAFVFNGRFSPeTYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSA 299
Cdd:PRK08751 258 ITALPLYHIFALTAnglvFMKI--GGCNHLISNPRDMP-GFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 300 VSAGEPLNREVVEQFKKYFNLTVRDGYGQTEST--LLIGFLkDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAV 377
Cdd:PRK08751 335 LGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpaACINPL-TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 378 plDLPALFKGYYKEPERTAKAQTGKYYI-TGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVV 456
Cdd:PRK08751 414 --KGPQVMKGYWKRPEETAKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAV 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441463764 457 AKPHDIRGNIVKAFVILQDH--TAgddtlvKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDA 526
Cdd:PRK08751 492 GVPDEKSGEIVKVVIVKKDPalTA------EDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDA 557
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
182-525 |
4.64e-50 |
|
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: 178.73 E-value: 4.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 182 LSYTSGTTGNPKAVTHCHGWGFAH--LQMAPKHWLCINEDDlVWATAAPGWQKWVWSPFLSVLGSGATAFVFNgRFSPET 259
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDndTLMAAALGFGPGADS-VYLSPAPLYHAAPFRWSMTALFMGGTLVLME-KFDPEE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 260 YLELLQKYQINVLCCTPTEYRMMAKLQN--LNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTE---STLL 334
Cdd:cd05929 208 FLRLIERYRVTFAQFVPTMFVRLLKLPEavRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEgqgLTII 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 335 IG--FLKDTpqriGSMGKGIpGSSVTVVDDEGNSVPANTKGNIAVpldLPALFKGYYKEPERTAKAQTGKYYIT-GDLAH 411
Cdd:cd05929 288 NGeeWLTHP----GSVGRAV-LGKVHILDEDGNEVPPGEIGEVYF---ANGPGFEYTNDPEKTAAARNEGGWSTlGDVGY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 412 VDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFV 491
Cdd:cd05929 360 LDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFL 439
|
330 340 350
....*....|....*....|....*....|....
gi 1441463764 492 KNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:cd05929 440 RDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
32-525 |
4.77e-50 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 180.34 E-value: 4.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILyhnteGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK13382 57 PDRPGLI-----DELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFTVEFEK-IKEYDALTKFVIAGQKDGWISLEAEKENASNKLEMADTTRDDMAILsyTSGTTG 190
Cdd:PRK13382 132 LAEVVTREGVDTVIYDEEFSATVDRaLADCPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILL--TSGTTG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 191 NPKAVTHCHGWGFAHLQ--MAPKHWLCinEDDLVwaTAAPGWQKWVWSPfLSVLGSGATAFVFNGRFSPETYLELLQKYQ 268
Cdd:PRK13382 210 TPKGARRSGPGGIGTLKaiLDRTPWRA--EEPTV--IVAPMFHAWGFSQ-LVLAASLACTIVTRRRFDPEATLDLIDRHR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 269 INVLCCTPTEYRMMAKL--QNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLL-IGFLKDTPQRI 345
Cdd:PRK13382 285 ATGLAVVPVMFDRIMDLpaEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIaTATPADLRAAP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 346 GSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLpaLFKGYykEPERTAKAQTGkYYITGDLAHVDDDGYFWFEGRRD 425
Cdd:PRK13382 365 DTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDT--QFDGY--TSGSTKDFHDG-FMASGDVGYLDENGRLFVVGRDD 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 426 DIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILqdhTAGDDTLVKELQQFVKNEVAPYKYPREIE 505
Cdd:PRK13382 440 EMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL---KPGASATPETLKQHVRDNLANYKVPRDIV 516
|
490 500
....*....|....*....|
gi 1441463764 506 FVDDLPKTNSGKIRRVELRD 525
Cdd:PRK13382 517 VLDELPRGATGKILRRELQA 536
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
32-523 |
5.87e-50 |
|
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: 178.68 E-value: 5.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILyhnteGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd05920 29 PDRIAVV-----DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIalepftvefekikeydaltkfvIAGQKDGWISLEAEKENASNKlemadttrDDMAILSYTSGTTGN 191
Cdd:cd05920 104 LSAFCAHAEAVAYI----------------------VPDRHAGFDHRALARELAESI--------PEVALFLLSGGTTGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGwGFAHLQMAPKHWLCINEDDlVWATAAPGWQKWVWS-P-FLSVLGSGATAfVFNGRFSPETYLELLQKYQI 269
Cdd:cd05920 154 PKLIPRTHN-DYAYNVRASAEVCGLDQDT-VYLAVLPAAHNFPLAcPgVLGTLLAGGRV-VLAPDPSPDAAFPLIEREGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 270 NVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIGFLKDTPQRI-GSM 348
Cdd:cd05920 231 TVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLDDPDEVIiHTQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 349 GKGI-PGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGK-YYITGDLAHVDDDGYFWFEGRRDD 426
Cdd:cd05920 311 GRPMsPDDEIRVVDEEGNPVPPGEEGELLT--RGPYTIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGRIKD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 427 IIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGddtlVKELQQFVKN-EVAPYKYPREIE 505
Cdd:cd05920 389 QINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPS----AAQLRRFLRErGLAAYKLPDRIE 464
|
490
....*....|....*...
gi 1441463764 506 FVDDLPKTNSGKIRRVEL 523
Cdd:cd05920 465 FVDSLPLTAVGKIDKKAL 482
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
50-526 |
1.54e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 177.69 E-value: 1.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPcsemlrtkdLQYRITHGEINAVIA-LE 128
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVP---------LNWRLSASELDALLQdAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 129 PftvefeKIKEYDALtkfVIAGQKDGwISLEAEKENAsNKLEMADTT---RDDMAILSYTSGTTGNPKAVTHCHgwgfAH 205
Cdd:PRK09088 95 P------RLLLGDDA---VAAGRTDV-EDLAAFIASA-DALEPADTPsipPERVSLILFTSGTSGQPKGVMLSE----RN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 206 LQMApkhwlCINEDDLVWATAApgwqkwvwSPFL----------------SVLGSGATAFVFNGrFSPETYLELLQKYQI 269
Cdd:PRK09088 160 LQQT-----AHNFGVLGRVDAH--------SSFLcdapmfhiiglitsvrPVLAVGGSILVSNG-FEPKRTLGRLGDPAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 270 NV--LCCTPteyRMMAKLQNLNDYD---LTHLHSAVSAGEPlnrEVVEQFKKYFNLTVR--DGYGQTESTLLIGFLKDTP 342
Cdd:PRK09088 226 GIthYFCVP---QMAQAFRAQPGFDaaaLRHLTALFTGGAP---HAAEDILGWLDDGIPmvDGFGMSEAGTVFGMSVDCD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 343 ---QRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAKAQTGK-YYITGDLAHVDDDGYF 418
Cdd:PRK09088 300 virAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELL--LRGPNLSPGYWRRPQATARAFTGDgWFRTGDIARRDADGFF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 419 WFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVIlqdHTAGDDTLVKELQQFVKNEVAPY 498
Cdd:PRK09088 378 WVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIV---PADGAPLDLERIRSHLSTRLAKY 454
|
490 500
....*....|....*....|....*...
gi 1441463764 499 KYPREIEFVDDLPKTNSGKIRRVELRDA 526
Cdd:PRK09088 455 KVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
32-526 |
2.15e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 178.60 E-value: 2.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK08162 32 PDRPAVIH-----GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAAS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFT-VEFEKIKEYDALTKFVI--------AGQKDGwiSLEAEKENASNKLEMADTTRDDM--A 180
Cdd:PRK08162 107 IAFMLRHGEAKVLIVDTEFAeVAREALALLPGPKPLVIdvddpeypGGRFIG--ALDYEAFLASGDPDFAWTLPADEwdA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 181 I-LSYTSGTTGNPKAVT--------------------------------HCHGWGFAhlqmapkhwlcineddlvWATAA 227
Cdd:PRK08162 185 IaLNYTSGTTGNPKGVVyhhrgaylnalsnilawgmpkhpvylwtlpmfHCNGWCFP------------------WTVAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 228 pgwqkwvwspflsvlgSGATAfVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLN 307
Cdd:PRK08162 247 ----------------RAGTN-VCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 308 REVVEQFKKY-FNLT-VrdgYGQTE--------------STLLIgflkdtPQRIGSMGK-GIP---GSSVTVVD-DEGNS 366
Cdd:PRK08162 310 AAVIAKMEEIgFDLThV---YGLTEtygpatvcawqpewDALPL------DERAQLKARqGVRyplQEGVTVLDpDTMQP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 367 VPAN--TKGNIAVPLDLpaLFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDAL 444
Cdd:PRK08162 381 VPADgeTIGEIMFRGNI--VMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 445 TNHPAVKECAVVAKPHDIRGNIVKAFVILQD-HTAGDDtlvkELQQFVKNEVAPYKYPREIEFvDDLPKTNSGKIRRVEL 523
Cdd:PRK08162 459 YRHPAVLVAAVVAKPDPKWGEVPCAFVELKDgASATEE----EIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVL 533
|
...
gi 1441463764 524 RDA 526
Cdd:PRK08162 534 REQ 536
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
32-536 |
9.69e-49 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 176.93 E-value: 9.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTegeDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK08315 30 PDREALVYRDQ---GLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPF----------TVEFE-KIKEYDALT-------KFVI-AGQK-----DGWISLEAEKENASN 167
Cdd:PRK08315 107 LEYALNQSGCKALIAADGFkdsdyvamlyELAPElATCEPGQLQsarlpelRRVIfLGDEkhpgmLNFDELLALGRAVDD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 168 -KLE--MADTTRDDMAILSYTSGTTGNPKAVTHCH------GWGFA-HLQMAPKHWLCIneddlvwataaPgwqkwVwsP 237
Cdd:PRK08315 187 aELAarQATLDPDDPINIQYTSGTTGFPKGATLTHrnilnnGYFIGeAMKLTEEDRLCI-----------P-----V--P 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 238 F-------LSVLG---SGATAFVFNGRFSPETYLELLQKYQinvlcCT-----PTeyrM-MAKLQ--NLNDYDLTHLHSA 299
Cdd:PRK08315 249 LyhcfgmvLGNLAcvtHGATMVYPGEGFDPLATLAAVEEER-----CTalygvPT---MfIAELDhpDFARFDLSSLRTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 300 VSAGEPLNREVVEQFKKYFNLT-VRDGYGQTES------TLLigflkDTP--QRIGSMGKGIPGSSVTVVDDE-GNSVPA 369
Cdd:PRK08315 321 IMAGSPCPIEVMKRVIDKMHMSeVTIAYGMTETspvstqTRT-----DDPleKRVTTVGRALPHLEVKIVDPEtGETVPR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 370 NTKGNI-----AVpldlpalFKGYYKEPERTAKAqtgkyyI-------TGDLAHVDDDGYFWFEGRRDDIIISSGYTIGP 437
Cdd:PRK08315 396 GEQGELctrgySV-------MKGYWNDPEKTAEA------IdadgwmhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 438 FEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQ-DHTAGDDtlvkELQQFVKNEVAPYKYPREIEFVDDLPKTNSG 516
Cdd:PRK08315 463 REIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRpGATLTEE----DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTG 538
|
570 580
....*....|....*....|
gi 1441463764 517 KIRRVELRDAEIEKWQQQKD 536
Cdd:PRK08315 539 KIQKFKMREMMIEELGLQAA 558
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
32-523 |
1.27e-48 |
|
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: 174.42 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCsemlrtkD 111
Cdd:cd17643 1 PEAVAVVD-----EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPI-------D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQY---RITHgeinavialepfTVEfekikeyDALTKFVIagqkdgwisleaekenasnklemadTTRDDMAILSYTSGT 188
Cdd:cd17643 69 PAYpveRIAF------------ILA-------DSGPSLLL-------------------------TDPDDLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 189 TGNPKAVTHCHGwGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLGSGATAFVFNG-RFSPETYLELLQKY 267
Cdd:cd17643 105 TGRPKGVVVSHA-NVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEvARSPEDFARLLRDE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 268 QINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNL---TVRDGYGQTESTLLIGFLK----D 340
Cdd:cd17643 184 GVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRPldaaD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 341 TPQRIGS-MGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAK--------AQTGKYYITGDLAH 411
Cdd:cd17643 264 LPAAAASpIGRPLPGLRVYVLDADGRPVPPGVVGELYV--SGAGVARGYLGRPELTAErfvanpfgGPGSRMYRTGDLAR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 412 VDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDdtlVKELQQFV 491
Cdd:cd17643 342 RLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAAD---IAELRALL 418
|
490 500 510
....*....|....*....|....*....|..
gi 1441463764 492 KNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd17643 419 KELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
32-529 |
2.25e-48 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 177.45 E-value: 2.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTEGED---ISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPrsiATYELYIAALKLGVAIIPC----- 103
Cdd:PRK07529 39 PDAPALSFLLDADPLdrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLP---NLPETHFALWGGEAAGIANpinpl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 104 ------SEMLRTKDLQyrithgeinAVIALEPF--TVEFEKIKEY-DAL----TKFVIAGQKD-----GWISLEAEKE-- 163
Cdd:PRK07529 116 lepeqiAELLRAAGAK---------VLVTLGPFpgTDIWQKVAEVlAALpelrTVVEVDLARYlpgpkRLAVPLIRRKah 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 164 ------NASNKLEMADTTR-------DDMAILSYTSGTTGNPKAVTHCHGwgfahlQMAPKHW-----LCINEDDLVWAt 225
Cdd:PRK07529 187 arildfDAELARQPGDRLFsgrpigpDDVAAYFHTGGTTGMPKLAQHTHG------NEVANAWlgallLGLGPGDTVFC- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 226 AAP-----GWQKWVWSPFLS----VLGSGA----TAFVFNgrfspetYLELLQKYQINVLCCTPTEYRMMAKLQnLNDYD 292
Cdd:PRK07529 260 GLPlfhvnALLVTGLAPLARgahvVLATPQgyrgPGVIAN-------FWKIVERYRINFLSGVPTVYAALLQVP-VDGHD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 293 LTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLL--IGFLkDTPQRIGSMGKGIPGSSVTVV--DDEGNSV- 367
Cdd:PRK07529 332 ISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVssVNPP-DGERRIGSVGLRLPYQRVRVVilDDAGRYLr 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 368 --PANTKGNIAVplDLPALFKGYYkEPERTAKAQT-GKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDAL 444
Cdd:PRK07529 411 dcAVDEVGVLCI--AGPNVFSGYL-EAAHNKGLWLeDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEAL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 445 TNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtAGDDTLVKELQQFVKNEVA-PYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:PRK07529 488 LRHPAVALAAAVGRPDAHAGELPVAYVQLK---PGASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPAL 564
|
....*.
gi 1441463764 524 RDAEIE 529
Cdd:PRK07529 565 RRDAIR 570
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
29-526 |
3.15e-48 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 174.68 E-value: 3.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 29 SHIPDKKAILYHNTEGEDIsvTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLR 108
Cdd:PRK07514 11 AAFADRDAPFIETPDGLRY--TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 109 TKDLQYRITHGEiNAVIALEPftvefekiKEYDALTKfvIAGQK----------DGWISLEAEKENASNKLEMADTTRDD 178
Cdd:PRK07514 89 LAELDYFIGDAE-PALVVCDP--------ANFAWLSK--IAAAAgaphvetldaDGTGSLLEAAAAAPDDFETVPRGADD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 179 MAILSYTSGTTGNPKAVTHCHG------------WGFahlqmapkhwlciNEDDlVWATAAPGWQkwVWSPFLS---VLG 243
Cdd:PRK07514 158 LAAILYTSGTTGRSKGAMLSHGnllsnaltlvdyWRF-------------TPDD-VLIHALPIFH--THGLFVAtnvALL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 244 SGAtAFVFNGRFSPETYLELLQkyQINVLCCTPTEY-RMMAKlQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTV 322
Cdd:PRK07514 222 AGA-SMIFLPKFDPDAVLALMP--RATVMMGVPTFYtRLLQE-PRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 323 RDGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVD-DEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTG 401
Cdd:PRK07514 298 LERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEV--KGPNVFKGYWRMPEKTAEEFRA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 402 K-YYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGD 480
Cdd:PRK07514 376 DgFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALD 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1441463764 481 -DTLVKELqqfvKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDA 526
Cdd:PRK07514 456 eAAILAAL----KGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
177-524 |
5.46e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 173.25 E-value: 5.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 DDMAILSYTSGTTGNPKAVthchgwgfahlqMAPKHWLCINEDDLVWAtaapgwqkWVWSP----------------FLS 240
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGV------------VLSRRAIAADLDALAEA--------WQWTAddvlvhglplfhvhglVLG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 241 VLGS---GATaFVFNGRFSPETYLELLQKyQINVLCCTPTEYRMMAklqnlNDYDLTH-LHSA---VSAGEPLNREVVEQ 313
Cdd:PRK07787 188 VLGPlriGNR-FVHTGRPTPEAYAQALSE-GGTLYFGVPTVWSRIA-----ADPEAARaLRGArllVSGSAALPVPVFDR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 314 FKKYFNLTVRDGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPAN--TKGNIAVplDLPALFKGYYKE 391
Cdd:PRK07787 261 LAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDgeTVGELQV--RGPTLFDGYLNR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 392 PERTAKAQTGK-YYITGDLAHVDDDGYFWFEGRRD-DIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKA 469
Cdd:PRK07787 339 PDATAAAFTADgWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVA 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1441463764 470 FVIlqdhtAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PRK07787 419 YVV-----GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
29-523 |
5.96e-48 |
|
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: 173.46 E-value: 5.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 29 SHIPDKKAILyhnTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLR 108
Cdd:cd05923 12 SRAPDACAIA---DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 109 TKDLQYRITHGEINAVIalepFTVEFEKIKE-YDALTKFVIAGQKDGwislEAEKENASNKLEMADTTRDDMAILSYTSG 187
Cdd:cd05923 89 AAELAELIERGEMTAAV----IAVDAQVMDAiFQSGVRVLALSDLVG----LGEPESAGPLIEDPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 188 TTGNPKAVthchgwGFAHLQMAPKHwlcineddLVWATAAP---GWQKWVWS--PFLSVLGSGAT---AFVFNGR----- 254
Cdd:cd05923 161 TTGLPKGA------VIPQRAAESRV--------LFMSTQAGlrhGRHNVVLGlmPLYHVIGFFAVlvaALALDGTyvvve 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 255 -FSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTEStl 333
Cdd:cd05923 227 eFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 334 lIGFLKDTPQRIGSMGKgiPG--SSVTVVDDEGNSV---PANTKGNIAVPLDLPALFKGYYKEPERTAKAQTGKYYITGD 408
Cdd:cd05923 305 -MNSLYMRDARTGTEMR--PGffSEVRIVRIGGSPDealANGEEGELIVAAAADAAFTGYLNQPEATAKKLQDGWYRTGD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 409 LAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDtlvkELQ 488
Cdd:cd05923 382 VGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAD----ELD 457
|
490 500 510
....*....|....*....|....*....|....*.
gi 1441463764 489 QFVK-NEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd05923 458 QFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
168-534 |
7.20e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 174.95 E-value: 7.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 168 KLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAH-LQMAPKHWLCINEDDLVWATAAPGWQKWVWS---PFLSVLG 243
Cdd:PRK05677 198 PVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmLQCRALMGSNLNEGCEILIAPLPLYHIYAFTfhcMAMMLIG 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 244 sGATAFVFNGRFSPeTYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVR 323
Cdd:PRK05677 278 -NHNILISNPRDLP-AMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAIC 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 324 DGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKY 403
Cdd:PRK05677 356 EGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCV--KGPQVMKGYWQRPEATDEILDSDG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 404 YI-TGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtagDDT 482
Cdd:PRK05677 434 WLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKP----GET 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1441463764 483 LVKE-LQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAEIEKWQQQ 534
Cdd:PRK05677 510 LTKEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAGLK 562
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
32-520 |
1.19e-47 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 175.14 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTE-GEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRsIATyelyiAALklgvAIIPCSemlrtk 110
Cdd:PRK10524 67 PEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPM-IAE-----AAF----AMLACA------ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 111 dlqyRIthGEINAVI----ALEPFTVEFEkikeyDALTKFVI---AGQKDGWIS-----LEAEKENASNK---------- 168
Cdd:PRK10524 131 ----RI--GAIHSVVfggfASHSLAARID-----DAKPVLIVsadAGSRGGKVVpykplLDEAIALAQHKprhvllvdrg 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 169 -LEMADTT-RD-DMAILS----------------------YTSGTTGNPKAVTHCHGwGFA-HLQMAPKHWLCINEDDLV 222
Cdd:PRK10524 200 lAPMARVAgRDvDYATLRaqhlgarvpvewlesnepsyilYTSGTTGKPKGVQRDTG-GYAvALATSMDTIFGGKAGETF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 223 WATAAPGW----QKWVWSPFLSvlgsGATAFVFNG---RFSPETYLELLQKYQINVLCCTPTEYRMMAKlQN---LNDYD 292
Cdd:PRK10524 279 FCASDIGWvvghSYIVYAPLLA----GMATIMYEGlptRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKK-QDpalLRKHD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 293 LTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTES-----TLLIGfLKDTPQRIGSMGKGIPGSSVTVVDDE-GNS 366
Cdd:PRK10524 354 LSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETgwpilAIARG-VEDRPTRLGSPGVPMYGYNVKLLNEVtGEP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 367 VPANTKGNIAVPLDLP-----------ALF-KGYYKEPERTAkaqtgkyYITGDLAHVDDDGYFWFEGRRDDIIISSGYT 434
Cdd:PRK10524 433 CGPNEKGVLVIEGPLPpgcmqtvwgddDRFvKTYWSLFGRQV-------YSTFDWGIRDADGYYFILGRTDDVINVAGHR 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 435 IGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDT-----LVKELQQFVKNEVAPYKYPREIEFVDD 509
Cdd:PRK10524 506 LGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRearlaLEKEIMALVDSQLGAVARPARVWFVSA 585
|
570
....*....|.
gi 1441463764 510 LPKTNSGKIRR 520
Cdd:PRK10524 586 LPKTRSGKLLR 596
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
50-530 |
1.90e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 173.65 E-value: 1.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRS----IATYelyiAALKLGVAIIPCSEMLRTKDLQYRIT-HG----- 119
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCpqhiVAFY----AVLRLGAVVVEHNPLYTAHELEHPFEdHGarvai 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 120 ---EINAVIALEPFTVEFEKI-------------------------KEYDALTKFviAGQKDGWISLEAEKENASNKL-E 170
Cdd:PRK05605 135 vwdKVAPTVERLRRTTPLETIvsvnmiaampllqrlalrlpipalrKARAALTGP--APGTVPWETLVDAAIGGDGSDvS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 171 MADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMApKHWL-CINEDDLVWATAAPGWQKW------VWSPFLsvlg 243
Cdd:PRK05605 213 HPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQG-KAWVpGLGDGPERVLAALPMFHAYgltlclTLAVSI---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 244 sGATAFVFNgRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVR 323
Cdd:PRK05605 288 -GGELVLLP-APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLV 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 324 DGYGQTE-STLLIGFLKDTPQRIGSMGKGIPGSSVTVVD--DEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQT 400
Cdd:PRK05605 366 EGYGLTEtSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLV--RGPQVFKGYWNRPEETAKSFL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 401 GKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGD 480
Cdd:PRK05605 444 DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALD 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1441463764 481 DTLVKElqqFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAEIEK 530
Cdd:PRK05605 524 PEGLRA---YCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEK 570
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
47-525 |
7.43e-47 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 171.93 E-value: 7.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 47 ISVTYQQLIEQSNKVGNVLASH-GLSKGDKVLIMMPrSIATYELYI-AALKLGVAIIPCSEMLRTKDLQYRITHGEINAV 124
Cdd:PRK12492 48 VTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMP-NVLQYPIAVfGALRAGLIVVNTNPLYTAREMRHQFKDSGARAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 125 IALEPFTVEFEKIKEYDALTKFVIAGQKD------GWI---------------SL-------EAEKENASNKLEMADTTR 176
Cdd:PRK12492 127 VYLNMFGKLVQEVLPDTGIEYLIEAKMGDllpaakGWLvntvvdkvkkmvpayHLpqavpfkQALRQGRGLSLKPVPVGL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 DDMAILSYTSGTTGNPKAVTHCHGWGFAHL--------QMAPKHWLCINEDDLVWATAAPGWQKWVWSP-FLSVLGSGA- 246
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANMlqvraclsQLGPDGQPLMKEGQEVMIAPLPLYHIYAFTAnCMCMMVSGNh 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 247 TAFVFNGRFSPeTYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGY 326
Cdd:PRK12492 287 NVLITNPRDIP-GFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 327 GQTE-STLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGK-YY 404
Cdd:PRK12492 366 GLTEtSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCI--KGPQVMKGYWQQPEATAEALDAEgWF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 405 ITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGddtlV 484
Cdd:PRK12492 444 KTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLS----V 519
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1441463764 485 KELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK12492 520 EELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
47-525 |
2.14e-46 |
|
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: 169.43 E-value: 2.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 47 ISVTYQQLIEQSNKVGNVLASHGLSkGDKVLIMMPRSIATYELYIAALKLG--VAIIPCSEMLRTkdLQYRITHGEINAV 124
Cdd:cd05909 6 TSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGkvPVMLNYTAGLRE--LRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 125 IALEPFtveFEKIKeydaLTKFVIAGQKDGWISLEAEKENASNK------LEM-------------ADTTRDDMAILSYT 185
Cdd:cd05909 83 LTSKQF---IEKLK----LHHLFDVEYDARIVYLEDLRAKISKAdkckafLAGkfppkwllrifgvAPVQPDDPAVILFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 186 SGTTGNPKAVTHCHGWGFAHLQMAPKHWLCINEDdlVWATAAP-----GWQKWVWSPFLSvlgsGATAFVFNGRFSPETY 260
Cdd:cd05909 156 SGSEGLPKGVVLSHKNLLANVEQITAIFDPNPED--VVFGALPffhsfGLTGCLWLPLLS----GIKVVFHPNPLDYKKI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 261 LELLQKYQINVLCCTPTEYRMMAKlqNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIGF-LK 339
Cdd:cd05909 230 PELIYDKKATILLGTPTFLRGYAR--AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVnTP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 340 DTPQRIGSMGKGIPGSSVTVVDDEGNS-VPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYF 418
Cdd:cd05909 308 QSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLV--RGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 419 WFEGRRDDIIISSGYTIGPFEVEDALTNH-PAVKECAVVAKPHDIRGNIVkafVILQDHTAGDdtlVKELQQFVKNEVAP 497
Cdd:cd05909 386 TITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKI---VLLTTTTDTD---PSSLNDILKNAGIS 459
|
490 500
....*....|....*....|....*....
gi 1441463764 498 YKY-PREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:cd05909 460 NLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
51-533 |
5.24e-45 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 166.03 E-value: 5.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 51 YQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQY---------RITHGE- 120
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYiledsgarvLIAHADl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 121 INAVIALEPFTVEF-------EKIKEY--DALTKFVIAGQKD--GWisLEAEKENASNKLEMADTtrddmaiLSYTSGTT 189
Cdd:PRK12406 94 LHGLASALPAGVTVlsvptppEIAAAYriSPALLTPPAGAIDweGW--LAQQEPYDGPPVPQPQS-------MIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 190 GNPKAVThchgwgfahlQMAPKHWLCINEDDLVwATA---APGWQKWVWSP--------FLSVLGSGATAFVFNGRFSPE 258
Cdd:PRK12406 165 GHPKGVR----------RAAPTPEQAAAAEQMR-ALIyglKPGIRALLTGPlyhsapnaYGLRAGRLGGVLVLQPRFDPE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 259 TYLELLQKYQINVLCCTPTeyrMMAKLQNLND-----YDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTL 333
Cdd:PRK12406 234 ELLQLIERHRITHMHMVPT---MFIRLLKLPEevrakYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 334 LIGFL-KDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLPALFKgYYKEPERTAKAQTGKYYITGDLAHV 412
Cdd:PRK12406 311 VTFATsEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFT-YHNKPEKRAEIDRGGFITSGDVGYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 413 DDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtAGDDTLVKELQQFVK 492
Cdd:PRK12406 390 DADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQ---PGATLDEADIRAQLK 466
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1441463764 493 NEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAeieKWQQ 533
Cdd:PRK12406 467 ARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP---YWAN 504
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
50-455 |
6.09e-45 |
|
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: 163.59 E-value: 6.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVL-ASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIALE 128
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 129 PFTVEFekikeyDALTKFVIAgqkdgwISLEAEKENASNKLEMADTTR---DDMAILSYTSGTTGNPKAVTHCHGwGFAH 205
Cdd:TIGR01733 81 ALASRL------AGLVLPVIL------LDPLELAALDDAPAPPPPDAPsgpDDLAYVIYTSGSTGRPKGVVVTHR-SLVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 206 LQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLGSGATAFVFNG--RFSPETYLELLQKYQINVLCCTPTEYRMMA 283
Cdd:TIGR01733 148 LLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDeeRDDAALLAALIAEHPVTVLNLTPSLLALLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 284 KLQnlnDYDLTHLHSAVSAGEPLNREVVEQFK-KYFNLTVRDGYGQTESTL-----LIGFLKDTPQRIGSMGKGIPGSSV 357
Cdd:TIGR01733 228 AAL---PPALASLRLVILGGEALTPALVDRWRaRGPGARLINLYGPTETTVwstatLVDPDDAPRESPVPIGRPLANTRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 358 TVVDDEGNSVPantkgnIAVPLDL----PALFKGYYKEPERTAKA---------QTGKYYITGDLAHVDDDGYFWFEGRR 424
Cdd:TIGR01733 305 YVLDDDLRPVP------VGVVGELyiggPGVARGYLNRPELTAERfvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRI 378
|
410 420 430
....*....|....*....|....*....|.
gi 1441463764 425 DDIIISSGYTIGPFEVEDALTNHPAVKECAV 455
Cdd:TIGR01733 379 DDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
32-527 |
8.75e-45 |
|
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: 170.04 E-value: 8.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIatyELYIA---ALKLGVAIIPcsemLr 108
Cdd:COG1020 490 PDAVAVVF-----GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSL---EMVVAllaVLKAGAAYVP----L- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 109 tkDLQY---RITH----GEINAVIALEPFTVEFekikeydaltkfviAGQKDGWISLEAEK-ENASNKLEMADTTRDDMA 180
Cdd:COG1020 557 --DPAYpaeRLAYmledAGARLVLTQSALAARL--------------PELGVPVLALDALAlAAEPATNPPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 181 ILSYTSGTTGNPKAVTHCHGwGFAHLQMAPKHWLCINEDDLVWATAAPG-----WQkwVWSPflsvLGSGATAFVFN--G 253
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHR-ALVNLLAWMQRRYGLGPGDRVLQFASLSfdasvWE--IFGA----LLSGATLVLAPpeA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 254 RFSPETYLELLQKYQINVLCCTPTEYRMMakLQNLNDyDLTHLHSAVSAGEPLNREVVEQFKKYF-NLTVRDGYGQTEST 332
Cdd:COG1020 694 RRDPAALAELLARHRVTVLNLTPSLLRAL--LDAAPE-ALPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETT 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 333 L--LIGFLKDTPQRIGSM--GKGIPGSSVTVVDDEGNSVPantkgnIAVPLDL----PALFKGYYKEPERTA-------- 396
Cdd:COG1020 771 VdsTYYEVTPPDADGGSVpiGRPIANTRVYVLDAHLQPVP------VGVPGELyiggAGLARGYLNRPELTAerfvadpf 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 397 KAQTGKYYITGDLAHVDDDGYFWFEGRRDD---IiisSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVIL 473
Cdd:COG1020 845 GFPGARLYRTGDLARWLPDGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVP 921
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1441463764 474 QDhtaGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAE 527
Cdd:COG1020 922 EA---GAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPA 972
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
26-523 |
3.31e-44 |
|
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: 163.27 E-value: 3.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 26 EKYSHIPDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIatyELYI---AALKLGVAIIP 102
Cdd:cd17655 5 EQAEKTPDHTAVVF-----EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSL---EMIVgilGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 103 CSEMLRTKDLQYRITHGEINAVIALEPFtvefekiKEYDALTKFVIAgqkdgwISLEAEKENASNKLEmADTTRDDMAIL 182
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILLTQSHL-------QPPIAFIGLIDL------LDEDTIYHEESENLE-PVSKSDDLAYV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 183 SYTSGTTGNPKAVTHCHGwGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLgSGATAFVFNG--RFSPETY 260
Cdd:cd17655 143 IYTSGSTGKPKGVMIEHR-GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLL-SGNTLYIVRKetVLDGQAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 261 LELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLhsaVSAGEPLNREVVEQFKKYFNLTVR--DGYGQTESTL----- 333
Cdd:cd17655 221 TQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHL---IVGGEALSTELAKKIIELFGTNPTitNAYGPTETTVdasiy 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 334 LIGFLKDTPQRIgSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDlpALFKGYYKEPERTAK-------AQTGKYYIT 406
Cdd:cd17655 298 QYEPETDQQVSV-PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGE--GVARGYLNRPELTAEkfvddpfVPGERMYRT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 407 GDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAgddtlVKE 486
Cdd:cd17655 375 GDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP-----VAQ 449
|
490 500 510
....*....|....*....|....*....|....*..
gi 1441463764 487 LQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd17655 450 LREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
32-523 |
3.43e-44 |
|
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: 163.14 E-value: 3.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCsemlrtkD 111
Cdd:cd12117 11 PDAVAVVY-----GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL-------D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQY---RITH----GEINAVIALEPFTVEfekikeydaltkfVIAGQKDGWISLEAEKENASNKLEMADTtrDDMAILSY 184
Cdd:cd12117 79 PELpaeRLAFmladAGAKVLLTDRSLAGR-------------AGGLEVAVVIDEALDAGPAGNPAVPVSP--DDLAYVMY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 185 TSGTTGNPK--AVTH------CHGWGFAHLqmapkhwlciNEDDLVWATAAPGWQKW---VWSPFLsvlgSGATAFVFNG 253
Cdd:cd12117 144 TSGSTGRPKgvAVTHrgvvrlVKNTNYVTL----------GPDDRVLQTSPLAFDAStfeIWGALL----NGARLVLAPK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 254 RF--SPETYLELLQKYQINVLCCTPTEYRMMAklqnlnDYD---LTHLHSAVSAGEPLNREVVEQF-KKYFNLTVRDGYG 327
Cdd:cd12117 210 GTllDPDALGALIAEEGVTVLWLTAALFNQLA------DEDpecFAGLRELLTGGEVVSPPHVRRVlAACPGLRLVNGYG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 328 QTESTLligF-----LKDTPQRIGS--MGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDlpALFKGYYKEPERTAK--- 397
Cdd:cd12117 284 PTENTT---FttshvVTELDEVAGSipIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGD--GLALGYLNRPALTAErfv 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 398 ----AQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVIL 473
Cdd:cd12117 359 adpfGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVA 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1441463764 474 qDHTAGDDtlvkELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd12117 439 -EGALDAA----ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
184-520 |
2.98e-43 |
|
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: 156.41 E-value: 2.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 184 YTSGTTGNPKAVTHCHgwgfahlqmapKHWLC---INEDDLVW----ATAAPGwqKWVWSPFL----SVLGSGATaFVFN 252
Cdd:cd17633 7 FTSGTTGLPKAYYRSE-----------RSWIEsfvCNEDLFNIsgedAILAPG--PLSHSLFLygaiSALYLGGT-FIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 253 GRFSPETYLELLQKYQINVLCCTPTeyrMMAKLQNLNDYDlTHLHSAVSAGEPLNREVVEQFKKYFNLTVR-DGYGQTES 331
Cdd:cd17633 73 RKFNPKSWIRKINQYNATVIYLVPT---MLQALARTLEPE-SKIKSIFSSGQKLFESTKKKLKNIFPKANLiEFYGTSEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 332 TLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVpantkGNIAVplDLPALFKGYYKEPErtakAQTGKYYITGDLAH 411
Cdd:cd17633 149 SFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFV--KSEMVFSGYVRGGF----SNPDGWMSVGDIGY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 412 VDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVilqdhtAGDDTLVKELQQFV 491
Cdd:cd17633 218 VDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY------SGDKLTYKQLKRFL 291
|
330 340
....*....|....*....|....*....
gi 1441463764 492 KNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:cd17633 292 KQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
44-524 |
4.93e-43 |
|
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: 160.20 E-value: 4.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 44 GEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPC---------SEMLRTKDLQY 114
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLdpaypaerlAFMLADAGPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 115 RITHGEINAVIALEPftvefekikeydaltkfvIAGQKDGWISLEAEKENASNklemADTTRDDMAILSYTSGTTGNPKA 194
Cdd:cd17651 96 VLTHPALAGELAVEL------------------VAVTLLDQPGAAAGADAEPD----PALDADDLAYVIYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 195 VTHCHGwGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFlSVLGSGATAFVFNG--RFSPETYLELLQKYQINVL 272
Cdd:cd17651 154 VVMPHR-SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIF-STLCAGATLVLPPEevRTDPPALAAWLDEQRISRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 273 CCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLnrEVVEQFKKYFN----LTVRDGYGQTESTLLIGF----LKDTPQR 344
Cdd:cd17651 232 FLPTVALRALAEHGRPLGVRLAALRYLLTGGEQL--VLTEDLREFCAglpgLRLHNHYGPTETHVVTALslpgDPAAWPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 345 IGSMGKGIPGSSVTVVDDEGNSVPantkgnIAVPLDL----PALFKGYYKEPERTAK-------AQTGKYYITGDLAHVD 413
Cdd:cd17651 310 PPPIGRPIDNTRVYVLDAALRPVP------PGVPGELyiggAGLARGYLNRPELTAErfvpdpfVPGARMYRTGDLARWL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 414 DDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtAGDDTLVKELQQFVKN 493
Cdd:cd17651 384 PDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGD---PEAPVDAAELRAALAT 460
|
490 500 510
....*....|....*....|....*....|.
gi 1441463764 494 EVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:cd17651 461 HLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
26-524 |
7.63e-43 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 160.53 E-value: 7.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 26 EKYSHIPDKKAILYHNTeGEdiSVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSE 105
Cdd:PLN02246 31 ERLSEFSDRPCLIDGAT-GR--VYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 106 MLRTKDLQYRITHGEINAVIALEPFTvefEKIKEY---DALTKFVIAGQKDGWISLEAEKENASNKLEMADTTRDDMAIL 182
Cdd:PLN02246 108 FYTPAEIAKQAKASGAKLIITQSCYV---DKLKGLaedDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 183 SYTSGTTGNPKAVTHCHG---WGFAHLQMAPKHWLCINEDDLVWAtAAPGWQKW-VWSPFLSVLGSGAtAFVFNGRFSPE 258
Cdd:PLN02246 185 PYSSGTTGLPKGVMLTHKglvTSVAQQVDGENPNLYFHSDDVILC-VLPMFHIYsLNSVLLCGLRVGA-AILIMPKFEIG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 259 TYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFK-KYFNLTVRDGYGQTES----TL 333
Cdd:PLN02246 263 ALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRaKLPNAVLGQGYGMTEAgpvlAM 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 334 LIGFLKD-TPQRIGSMGKGIPGSSVTVVD-DEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKA-QTGKYYITGDLA 410
Cdd:PLN02246 343 CLAFAKEpFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICI--RGPQIMKGYLNDPEATANTiDKDGWLHTGDIG 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 411 HVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVIlqdHTAGDDTLVKELQQF 490
Cdd:PLN02246 421 YIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV---RSNGSEITEDEIKQF 497
|
490 500 510
....*....|....*....|....*....|....
gi 1441463764 491 VKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PLN02246 498 VAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
21-533 |
1.26e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 158.79 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 21 IISEIEKY-SHIPDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGlSKGDKVLIMMPRSIATYELYIAALKLGVA 99
Cdd:PRK07638 3 ITKEYKKHaSLQPNKIAIKE-----NDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 100 IIPCSEMLRTKDLQYRITHGEINAVIALEPFTVEFEkikeyDALTKFVIAGQKDGWISLEAEKENASNKLEmadttrDDM 179
Cdd:PRK07638 77 CVPLDIKWKQDELKERLAISNADMIVTERYKLNDLP-----DEEGRVIEIDEWKRMIEKYLPTYAPIENVQ------NAP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 180 AILSYTSGTTGNPKAVTHCH-GWgfAHLQMAPKHWLCINEDDLVwatAAPGwqKWVWSPFL----SVLGSGATAFVFNgR 254
Cdd:PRK07638 146 FYMGFTSGSTGKPKAFLRAQqSW--LHSFDCNVHDFHMKREDSV---LIAG--TLVHSLFLygaiSTLYVGQTVHLMR-K 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 255 FSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLThlhsAVSAGEPLNREVVEQFKKYF-NLTVRDGYGQTESTL 333
Cdd:PRK07638 218 FIPNQVLDKLETENISVMYTVPTMLESLYKENRVIENKMK----IISSGAKWEAEAKEKIKNIFpYAKLYEFYGASELSF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 334 lIGFL--KDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAH 411
Cdd:PRK07638 294 -VTALvdEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYV--KSPQFFMGYIIGGVLARELNADGWMTVRDVGY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 412 VDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHtagddtlVKELQQFV 491
Cdd:PRK07638 371 EDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSAT-------KQQLKSFC 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1441463764 492 KNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD--AEIEKWQQ 533
Cdd:PRK07638 444 LQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSwiENQEKIYE 487
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
32-520 |
1.64e-42 |
|
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: 158.22 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd12116 1 PDATAVRD-----DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIAlepftvefekikeyDALTKFVIAGQKDGWISLEAEKENASNKLEmADTTRDDMAILSYTSGTTGN 191
Cdd:cd12116 76 LRYILEDAEPALVLT--------------DDALPDRLPAGLPVLLLALAAAAAAPAAPR-TPVSPDDLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGwGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLgSGATAFVFNG--RFSPETYLELLQKYQI 269
Cdd:cd12116 141 PKGVVVSHR-NLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLL-AGARVVIAPRetQRDPEALARLIEAHSI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 270 NVLCCTPTEYRMMAKLQNLNDYDLThlhsAVSAGEPLNREVVEQfkkyfnLTVRDG-----YGQTESTL--LIGFLKDTP 342
Cdd:cd12116 219 TVMQATPATWRMLLDAGWQGRAGLT----ALCGGEALPPDLAAR------LLSRVGslwnlYGPTETTIwsTAARVTAAA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 343 QRIgSMGKGIPGSSVTVVDDEGNSVPAntkgniAVPLDL----PALFKGYYKEPERTAKA--------QTGKYYITGDLA 410
Cdd:cd12116 289 GPI-PIGRPLANTQVYVLDAALRPVPP------GVPGELyiggDGVAQGYLGRPALTAERfvpdpfagPGSRLYRTGDLV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 411 HVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVkAFVILQDHTAGDDTlvkELQQF 490
Cdd:cd12116 362 RRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAGAAPDAA---ALRAH 437
|
490 500 510
....*....|....*....|....*....|
gi 1441463764 491 VKNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:cd12116 438 LRATLPAYMVPSAFVRLDALPLTANGKLDR 467
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
44-520 |
4.24e-42 |
|
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: 156.60 E-value: 4.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 44 GEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINA 123
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 124 VIALEPftvefekikeydaltkfviagqkdgwisleaekenasnklemadttrDDMAILSYTSGTTGNPKAVTHCHGwgf 203
Cdd:cd05907 81 LFVEDP-----------------------------------------------DDLATIIYTSGTTGRPKGVMLSHR--- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 204 aHLqmapkHWLCINEDDLVwaTAAPGWQKWVWSPFLSVLGSGATAFVF-------NGRFSPETYLELLQKYQINVLCCTP 276
Cdd:cd05907 111 -NI-----LSNALALAERL--PATEGDRHLSFLPLAHVFERRAGLYVPllagariYFASSAETLLDDLSEVRPTVFLAVP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 277 TEYRMMAKLQNLND--------YDLTHLHS---AVSAGEPLNREVVEQFKKyFNLTVRDGYGQTESTLLIGFLKDTPQRI 345
Cdd:cd05907 183 RVWEKVYAAIKVKAvpglkrklFDLAVGGRlrfAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 346 GSMGKGIPGSSVTVVDDegnsvpantkGNIAVplDLPALFKGYYKEPERTAKAQTGK-YYITGDLAHVDDDGYFWFEGRR 424
Cdd:cd05907 262 GTVGKPLPGVEVRIADD----------GEILV--RGPNVMLGYYKNPEATAEALDADgWLHTGDLGEIDEDGFLHITGRK 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 425 DDIII-SSGYTIGPFEVEDALTNHPAVKECAVVA--KPH-----DIRGNIVKAFVILQDHTAGDDT-------LVKELQQ 489
Cdd:cd05907 330 KDLIItSGGKNISPEPIENALKASPLISQAVVIGdgRPFlvaliVPDPEALEAWAEEHGIAYTDVAelaanpaVRAEIEA 409
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1441463764 490 FVKN---EVAPYKYPREIEFVDDLP------KTNSGKIRR 520
Cdd:cd05907 410 AVEAanaRLSRYEQIKKFLLLPEPFtiengeLTPTLKLKR 449
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
239-520 |
2.37e-41 |
|
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: 151.65 E-value: 2.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 239 LSVLGSGATAFVFNgRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLhSAVSAGEplNREVVEQFKKYF 318
Cdd:cd17637 60 LATFHAGGANVVME-KFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSL-RHVLGLD--APETIQRFEETT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 319 NLTVRDGYGQTESTLLIGFlKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKA 398
Cdd:cd17637 136 GATFWSLYGQTETSGLVTL-SPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV--RGPLVFQGYWNLPELTAYT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 399 QTGKYYITGDLAHVDDDGYFWFEGRR--DDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdh 476
Cdd:cd17637 213 FRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLK-- 290
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1441463764 477 tAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:cd17637 291 -PGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
178-520 |
4.30e-41 |
|
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: 151.26 E-value: 4.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 178 DMAILSYTSGTTGNPKAVTHCHGWGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLGSGATAfVFNGRFSP 257
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCV-TGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 258 ETYLELLQKYQINVLCCTPTEY-RMMAKLQNLNDYDLTHLHSAVSAGEPLNREVveQFKKYFNLT-VRDGYGQTEST--L 333
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLsKLVSELKSANATVPSLRLIGYGGSRAIAADV--RFIEATGLTnTAQVYGLSETGtaL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 334 LIGFLKDTPQrIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVD 413
Cdd:cd17635 159 CLPTDDDSIE-INAVGRPYPGVDVYLAATDGIAGPSASFGTIWI--KSPANMLGYWNNPERTAEVLIDGWVNTGDLGERR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 414 DDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTagDDTLVKELQQFVKN 493
Cdd:cd17635 236 EDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAEL--DENAIRALKHTIRR 313
|
330 340
....*....|....*....|....*..
gi 1441463764 494 EVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:cd17635 314 ELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-517 |
4.71e-41 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 151.77 E-value: 4.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 DDMAILsYTSGTTGNPKAVTHCH---------GWGFAHLQMAPKHWL---CINEDDLVWATAAP---GWQKWVWspfLSV 241
Cdd:cd05924 4 DDLYIL-YTGGTTGMPKGVMWRQedifrmlmgGADFGTGEFTPSEDAhkaAAAAAGTVMFPAPPlmhGTGSWTA---FGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 242 LGSGATAFVFNGRFSPETYLELLQKYQINVLCCTPTeyrMMAK-----LQNLNDYDLTHLHSAVSAGEPLNREVVEQFKK 316
Cdd:cd05924 80 LLGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGD---AMARplidaLRDAGPYDLSSLFAISSGGALLSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 317 YF-NLTVRDGYGQTESTLLiGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVP--ANTKGNIA----VPLdlpalfkGYY 389
Cdd:cd05924 157 LVpNITLVDAFGSSETGFT-GSGHSAGSGPETGPFTRANPDTVVLDDDGRVVPpgSGGVGWIArrghIPL-------GYY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 390 KEPERTAK----AQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGN 465
Cdd:cd05924 229 GDEAKTAEtfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1441463764 466 IVKAfvILQDHTAGDDTLvKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGK 517
Cdd:cd05924 309 EVVA--VVQLREGAGVDL-EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-530 |
5.35e-41 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 151.48 E-value: 5.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 DDMAILSYTSGTTGNPKAVTHCHG------WGFAHLQMapkhwlcINEDDLVWAtAAPGWQKW-VWSPFLSVLGSGATAF 249
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSnevynaWMLALNSL-------FDPDDVLLC-GLPLFHVNgSVVTLLTPLASGAHVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 250 VFN--GRFSPETYLE---LLQKYQINVLCCTPTEYrmMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRD 324
Cdd:cd05944 74 LAGpaGYRNPGLFDNfwkLVERYRITSLSTVPTVY--AALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 325 GYGQTESTLLIGF-LKDTPQRIGSMGKGIPGSSVTVV--DDEGNSV---PANTKGNIAVPLdlPALFKGY-YKEPERTAK 397
Cdd:cd05944 152 GYGLTEATCLVAVnPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLrdcAPDEVGEICVAG--PGVFGGYlYTEGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 398 AQTGkYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHT 477
Cdd:cd05944 230 VADG-WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGA 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1441463764 478 AGDDTlvkELQQFVKNEVAPY-KYPREIEFVDDLPKTNSGKIRRVELRDAEIEK 530
Cdd:cd05944 309 VVEEE---ELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
49-524 |
1.53e-40 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 155.96 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 49 VTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIALE 128
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 129 PFTVEFEKIKEYDAltkfviagqkdgwisleAEKENASNKLEMAD---TTRDDMAILSYTSGTTGNPKAVTHCHGWGFAH 205
Cdd:PRK06060 111 ALRDRFQPSRVAEA-----------------AELMSEAARVAPGGyepMGGDALAYATYTSGTTGPPKAAIHRHADPLTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 206 LQMAPKHWLCINEDDLVWATA----APGWQKWVWSPflsvLGSGATAFVFNGRFSPETYLELLQKYQINVLCCTPTeyrM 281
Cdd:PRK06060 174 VDAMCRKALRLTPEDTGLCSArmyfAYGLGNSVWFP----LATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPN---F 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 282 MAKLQNLNDYD-LTHLHSAVSAGEPLNREVVEQFKKYFN-LTVRDGYGQTEstllIG--FLKDTPQ--RIGSMGKGIPGS 355
Cdd:PRK06060 247 FARVIDSCSPDsFRSLRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE----VGqtFVSNRVDewRLGTLGRVLPPY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 356 SVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPErtAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTI 435
Cdd:PRK06060 323 EIRVVAPDGTTAGPGVEGDLWV--RGPAIAKGYWNRPD--SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 436 GPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNS 515
Cdd:PRK06060 399 DPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPN 478
|
....*....
gi 1441463764 516 GKIRRVELR 524
Cdd:PRK06060 479 GKLVRGALR 487
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
32-456 |
3.62e-40 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 153.72 E-value: 3.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAiLYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSiatYELYI---AALKLGVAIIPCSEMLR 108
Cdd:COG1022 25 PDRVA-LREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNR---PEWVIadlAILAAGAVTVPIYPTSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 109 TKDLQYRITHGEINAVIALEPFTVEfeKIKEY-DALT--KFVIA------GQKDGWISLEA-----EKENASNKLE--MA 172
Cdd:COG1022 101 AEEVAYILNDSGAKVLFVEDQEQLD--KLLEVrDELPslRHIVVldprglRDDPRLLSLDEllalgREVADPAELEarRA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 173 DTTRDDMAILSYTSGTTGNPKAVTHCHGwGFAHLQMAPKHWLCINEDDLV-----WAtaapgwqkWV----WSpfLSVLG 243
Cdd:COG1022 179 AVKPDDLATIIYTSGTTGRPKGVMLTHR-NLLSNARALLERLPLGPGDRTlsflpLA--------HVfertVS--YYALA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 244 SGAT-AFVFngrfSPETYLELLQKYQINVLCCTPTEY-----RMMAKLQNL------------------NDYDLT----- 294
Cdd:COG1022 248 AGATvAFAE----SPDTLAEDLREVKPTFMLAVPRVWekvyaGIQAKAEEAgglkrklfrwalavgrryARARLAgksps 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 295 ------------------------HLHSAVSAGEPLNREVVEqfkkYFN---LTVRDGYGQTESTLLIGFLKDTPQRIGS 347
Cdd:COG1022 324 lllrlkhaladklvfsklrealggRLRFAVSGGAALGPELAR----FFRalgIPVLEGYGLTETSPVITVNRPGDNRIGT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 348 MGKGIPGSSVTVVDDegnsvpaN---TKGniavpldlPALFKGYYKEPERTAKA-QTGKYYITGDLAHVDDDGYFWFEGR 423
Cdd:COG1022 400 VGPPLPGVEVKIAED-------GeilVRG--------PNVMKGYYKNPEATAEAfDADGWLHTGDIGELDEDGFLRITGR 464
|
490 500 510
....*....|....*....|....*....|....
gi 1441463764 424 RDDIII-SSGYTIGPFEVEDALTNHPAVKECAVV 456
Cdd:COG1022 465 KKDLIVtSGGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
32-523 |
8.24e-40 |
|
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: 150.10 E-value: 8.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAIlyhntEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIatyELYIAAL---KLGVAIIPCsemlr 108
Cdd:cd17652 1 PDAPAV-----VFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSA---ELVVAILavlKAGAAYLPL----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 109 tkDLQY---RITH--GEINAVIALepftvefekikeydaltkfviagqkdgwisleaekenasnklemadTTRDDMAILS 183
Cdd:cd17652 68 --DPAYpaeRIAYmlADARPALLL----------------------------------------------TTPDNLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 184 YTSGTTGNPK--AVTHChgwGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSpFLSVLGSGATAFVF--NGRFSPET 259
Cdd:cd17652 100 YTSGSTGRPKgvVVTHR---GLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATLVLApaEELLPGEP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 260 YLELLQKYQINVLCCTPteyrmmAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQF---KKYFNltvrdGYGQTESTLLIG 336
Cdd:cd17652 176 LADLLREHRITHVTLPP------AALAALPPDDLPDLRTLVVAGEACPAELVDRWapgRRMIN-----AYGPTETTVCAT 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 337 FLK-DTPQRIGSMGKGIPGSSVTVVDDEGNSVPantkgnIAVPLDL----PALFKGYYKEPERTAK--------AQTGKY 403
Cdd:cd17652 245 MAGpLPGGGVPPIGRPVPGTRVYVLDARLRPVP------PGVPGELyiagAGLARGYLNRPGLTAErfvadpfgAPGSRM 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 404 YITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDdtl 483
Cdd:cd17652 319 YRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPT--- 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1441463764 484 VKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd17652 396 AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
32-525 |
2.06e-39 |
|
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: 148.61 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAIlyhntEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPcsemLRTKD 111
Cdd:cd17653 11 PDAVAV-----ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP----LDAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHgeinavialepftvefekikeydaltkfVIagqkdgwisleaekENASNKLEMADTTRDDMAILSYTSGTTGN 191
Cdd:cd17653 82 PSARIQA----------------------------IL--------------RTSGATLLLTTDSPDDLAYIIFTSGSTGI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGwGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFlSVLGSGATaFVFngRFSPETYLELLQKyqINV 271
Cdd:cd17653 120 PKGVMVPHR-GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIF-STLCNGGT-LVL--ADPSDPFAHVART--VDA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 272 LCCTPTeyrmmaKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKkyFNLTVRDGYGQTESTLLIGFLKDTPQRIGSMGKG 351
Cdd:cd17653 193 LMSTPS------ILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWS--PGRRLYNAYGPTECTISSTMTELLPGQPVTIGKP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 352 IPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKA------QTG-KYYITGDLAHVDDDGYFWFEGRR 424
Cdd:cd17653 265 IPNSTCYILDADLQPVPEGVVGEICI--SGVQVARGYLGNPALTASKfvpdpfWPGsRMYRTGDYGRWTEDGGLEFLGRE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 425 DDIIISSGYTIGPFEVED-ALTNHPAVKECAVVAkphdIRGNIVkAFVilqdhtAGDDTLVKELQQFVKNEVAPYKYPRE 503
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIV----VNGRLV-AFV------TPETVDVDGLRSELAKHLPSYAVPDR 411
|
490 500
....*....|....*....|..
gi 1441463764 504 IEFVDDLPKTNSGKIRRVELRD 525
Cdd:cd17653 412 IIALDSFPLTANGKVDRKALRE 433
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
32-525 |
6.65e-39 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 149.78 E-value: 6.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTEgedisVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PLN03102 28 PNRTSIIYGKTR-----FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVI---ALEPFTVEFEK---------------IKEYDALTK-FVIAGQKDGWISLEAEKENASNKLEMA 172
Cdd:PLN03102 103 IAAILRHAKPKILFvdrSFEPLAREVLHllssedsnlnlpvifIHEIDFPKRpSSEELDYECLIQRGEPTPSLVARMFRI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 173 DTTRDDMAiLSYTSGTTGNPKAVTHCHGWGFAHLQMAPKHWLCINEDDLVWATaaPGWQKWVWSPFLSVLGSGATAFVFN 252
Cdd:PLN03102 183 QDEHDPIS-LNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTL--PMFHCNGWTFTWGTAARGGTSVCMR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 253 GRFSPETYlELLQKYQINVLCCTPTEYRMMAKLQNLndyDLTHLHSAV---SAGEPLNREVVEQFKKyFNLTVRDGYGQT 329
Cdd:PLN03102 260 HVTAPEIY-KNIEMHNVTHMCCVPTVFNILLKGNSL---DLSPRSGPVhvlTGGSPPPAALVKKVQR-LGFQVMHAYGLT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 330 ESTLLIGF---------LKDTPQRIGSMGKGIPGSSVTVVD----DEGNSVPANTKGNIAVPLDLPALFKGYYKEPERTA 396
Cdd:PLN03102 335 EATGPVLFcewqdewnrLPENQQMELKARQGVSILGLADVDvknkETQESVPRDGKTMGEIVIKGSSIMKGYLKNPKATS 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 397 KAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDh 476
Cdd:PLN03102 415 EAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEK- 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1441463764 477 taGDDTLVKELQQFVKNEVAPYKY----------PREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PLN03102 494 --GETTKEDRVDKLVTRERDLIEYcrenlphfmcPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
178-520 |
1.05e-38 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 144.18 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 178 DMAILSYTSGTTGNPKAVTHCH--------GWGFAHLQMAPKHWLCINeddlvwataapgwqkwvwsPFLSVLG--SGAT 247
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrqtlraaaAWADCADLTEDDRYLIIN-------------------PFFHTFGykAGIV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 248 AFVFNGR-------FSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNL 320
Cdd:cd17638 62 ACLLTGAtvvpvavFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 321 -TVRDGYGQTES-TLLIGFLKDTPQRIGSM-GKGIPGSSVTVVDDegnsvpantkGNIAVplDLPALFKGYYKEPERTAK 397
Cdd:cd17638 142 eTVLTAYGLTEAgVATMCRPGDDAETVATTcGRACPGFEVRIADD----------GEVLV--RGYNVMQGYLDDPEATAE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 398 AQTGKYYI-TGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDH 476
Cdd:cd17638 210 AIDADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1441463764 477 TAGDDtlvKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:cd17638 290 VTLTE---EDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
32-520 |
5.14e-38 |
|
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: 145.88 E-value: 5.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPC-------- 103
Cdd:cd17646 12 PDAPAVVD-----EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLdpgypadr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 104 -SEMLRTKDLQYRITHGEINAVIA--LEPFTVEFEKIKEYDALtkfviagqkdgwisleaekenasnkLEMADTTRDDMA 180
Cdd:cd17646 87 lAYMLADAGPAVVLTTADLAARLPagGDVALLGDEALAAPPAT-------------------------PPLVPPRPDNLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 181 ILSYTSGTTGNPKAVTHCHGwGFAHlQMApkhWLC----INEDDLVWATAAPGWQKWVWSPFLSvLGSGATAFVF--NGR 254
Cdd:cd17646 142 YVIYTSGSTGRPKGVMVTHA-GIVN-RLL---WMQdeypLGPGDRVLQKTPLSFDVSVWELFWP-LVAGARLVVArpGGH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 255 FSPETYLELLQKYQINVLCCTPTeyrMMAK-LQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTL 333
Cdd:cd17646 216 RDPAYLAALIREHGVTTCHFVPS---MLRVfLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 334 LIGFLK---DTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAK-------AQTGKY 403
Cdd:cd17646 293 DVTHWPvrgPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELY--LGGVQLARGYLGRPALTAErfvpdpfGPGSRM 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 404 YITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTl 483
Cdd:cd17646 371 YRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDT- 449
|
490 500 510
....*....|....*....|....*....|....*..
gi 1441463764 484 vKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:cd17646 450 -AALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDR 485
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
48-530 |
5.24e-38 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 147.05 E-value: 5.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 48 SVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPrSIATYELY-IAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIA 126
Cdd:PLN02330 55 AVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLP-NVAEYGIVaLGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 127 LEpftVEFEKIKEYD----ALTKFVIAGQKDgWISLEAEKENASNKLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGWG 202
Cdd:PLN02330 134 ND---TNYGKVKGLGlpviVLGEEKIEGAVN-WKELLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 203 FAHLQMApkhwLCINEDDLVWATAAPGWqkwvwSPFLSVLGSGATAF---------VFNGRFSPETYLELLQKYQINVLC 273
Cdd:PLN02330 210 VANLCSS----LFSVGPEMIGQVVTLGL-----IPFFHIYGITGICCatlrnkgkvVVMSRFELRTFLNALITQEVSFAP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 274 CTPTEYRMMAKLQNLNDYDLTHL--HSAVSAGEPLNREVVEQFKKYF-NLTVRDGYGQTESTLLIGFLKDTPQRIG---- 346
Cdd:PLN02330 281 IVPPIILNLVKNPIVEEFDLSKLklQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHSCITLTHGDPEKGHGiakk 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 347 -SMGKGIPGSSVTVVD-DEGNSVPANTKGNIAVPLDlpALFKGYYKEPERTAKAQTGKYYI-TGDLAHVDDDGYFWFEGR 423
Cdd:PLN02330 361 nSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ--CVMQGYYNNKEETDRTIDEDGWLhTGDIGYIDDDGDIFIVDR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 424 RDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDtlvKELQQFVKNEVAPYKYPRE 503
Cdd:PLN02330 439 IKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE---EDILNFVAANVAHYKKVRV 515
|
490 500
....*....|....*....|....*..
gi 1441463764 504 IEFVDDLPKTNSGKIRRVELRDAEIEK 530
Cdd:PLN02330 516 VQFVDSIPKSLSGKIMRRLLKEKMLSI 542
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
25-525 |
5.11e-37 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 144.12 E-value: 5.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 25 IEKYSHIPDKKAILYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCS 104
Cdd:PRK06018 16 IDHAARIHGNREVVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 105 EMLRTKDLQYRITHGEINAVIALEPFTVEFEKIKEY-DALTKFVIAGQKD--------GWISLEAEKENASNKLEMADTT 175
Cdd:PRK06018 96 PRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKlPSVERYVVLTDAAhmpqttlkNAVAYEEWIAEADGDFAWKTFD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 176 RDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMApkhwlciNEDDLVWATAA-------PGWQKWVWSPFLSVLGSGATA 248
Cdd:PRK06018 176 ENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMA-------NNGDALGTSAAdtmlpvvPLFHANSWGIAFSAPSMGTKL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 249 FVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYfNLTVRDGYGQ 328
Cdd:PRK06018 249 VMPGAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGM 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 329 TE-------STLLIGFLKDTP-QRIGSMGK-GIP--GSSVTVVDDEGNSVP--ANTKGNIAVplDLPALFKGYYKEPERT 395
Cdd:PRK06018 328 TEmsplgtlAALKPPFSKLPGdARLDVLQKqGYPpfGVEMKITDDAGKELPwdGKTFGRLKV--RGPAVAAAYYRVDGEI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 396 AKAQtgKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNivKAFVILQd 475
Cdd:PRK06018 406 LDDD--GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDE--RPLLIVQ- 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1441463764 476 HTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK06018 481 LKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
32-523 |
6.17e-37 |
|
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: 142.07 E-value: 6.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAIlyhntEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd12115 13 PDAIAL-----VCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIalepftvefekikeydaltkfviagqkdgwisleaekenasnklemadTTRDDMAILSYTSGTTGN 191
Cdd:cd12115 88 LRFILEDAQARLVL------------------------------------------------TDPDDLAYVIYTSGSTGR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGWGFAHLQMAPKHWlciNEDDL--VWATAAPGWQKWVWSPFLSvLGSGATAFVFNGRFSPETYLELLQKYQI 269
Cdd:cd12115 120 PKGVAIEHRNAAAFLQWAAAAF---SAEELagVLASTSICFDLSVFELFGP-LATGGKVVLADNVLALPDLPAAAEVTLI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 270 NVLcctPTeyrMMAKLQNLNDydlthLHSAVS----AGEPLNREVVE------QFKKYFNLtvrdgYGQTESTLLIGFLK 339
Cdd:cd12115 196 NTV---PS---AAAELLRHDA-----LPASVRvvnlAGEPLPRDLVQrlyarlQVERVVNL-----YGPSEDTTYSTVAP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 340 DTPQRIG--SMGKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAK-------AQTGKYYITGDLA 410
Cdd:cd12115 260 VPPGASGevSIGRPLANTQAYVLDRALQPVPLGVPGELY--IGGAGVARGYLGRPGLTAErflpdpfGPGARLYRTGDLV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 411 HVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGddtLVKELQQF 490
Cdd:cd12115 338 RWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG---LVEDLRRH 414
|
490 500 510
....*....|....*....|....*....|...
gi 1441463764 491 VKNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd12115 415 LGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
32-518 |
8.52e-36 |
|
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: 139.07 E-value: 8.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDK-VLIMMPRSIATYELYIAALKLGVAIIPCsemlrtk 110
Cdd:cd17648 1 PDRVAVVY-----GDKRLTYRELNERANRLAHYLLSVAEIRPDDlVGLVLDKSELMIIAILAVWKAGAAYVPI------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 111 DLQYrithgeinavialePftvefekikeyDALTKFVIagqkdgwisleaekENASNKLEMADTTrdDMAILSYTSGTTG 190
Cdd:cd17648 69 DPSY--------------P-----------DERIQFIL--------------EDTGARVVITNST--DLAYAIYTSGTTG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 191 NPKAVTHCHGwGFAHL--QMAPKHWLCINEDDLVWATAApgwqkWVWSPF-----LSVLGsGATAFVFN--GRFSPETYL 261
Cdd:cd17648 108 KPKGVLVEHG-SVVNLrtSLSERYFGRDNGDEAVLFFSN-----YVFDFFveqmtLALLN-GQKLVVPPdeMRFDPDRFY 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 262 ELLQKYQINVLCCTPTEyrmmaklqnLNDYDL---THLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTL--LIG 336
Cdd:cd17648 181 AYINREKVTYLSGTPSV---------LQQYDLarlPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVtnHKR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 337 FLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLPAlfKGYYKEPERTA------------KAQTGKY- 403
Cdd:cd17648 252 FFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVA--RGYLNRPELTAerflpnpfqteqERARGRNa 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 404 --YITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAK--PHDIRGNIVKAFV--ILQDHT 477
Cdd:cd17648 330 rlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKedASQAQSRIQKYLVgyYLPEPG 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1441463764 478 AGDDTlvkELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKI 518
Cdd:cd17648 410 HVPES---DLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
178-525 |
1.02e-35 |
|
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: 135.92 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 178 DMAILSYTSGTTGNPKAVTHCHGwgfAHL-----------QMAPKHWLCINEddLV-WATAAPGWqKWVWSPFLSVLGSG 245
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAA---NLLasaaglhsrlgFGGGDSWLLSLP--LYhVGGLAILV-RSLLAGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 246 ATAFVFNGRFSPETYLELlqkyqinvlccTPTEYRMMakLQNLNDYD-LTHLHSAVSAGEPLNREVVEQFKKYfNLTVRD 324
Cdd:cd17630 75 NQALAEDLAPPGVTHVSL-----------VPTQLQRL--LDSGQGPAaLKSLRAVLLGGAPIPPELLERAADR-GIPLYT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 325 GYGQTE--STLLIGFLKDTPQriGSMGKGIPGSSVTVVDDegnsvpantkGNIAVplDLPALFKGYYKEPERTAKAQTGK 402
Cdd:cd17630 141 TYGMTEtaSQVATKRPDGFGR--GGVGVLLPGRELRIVED----------GEIWV--GGASLAMGYLRGQLVPEFNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 403 YYiTGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVilqdhTAGDDT 482
Cdd:cd17630 207 FT-TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI-----VGRGPA 280
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1441463764 483 LVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:cd17630 281 DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
20-520 |
1.48e-35 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 139.26 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 20 NIISEIEKYSHI-PDKKAILYHNTEgedisVTYQQLIEQSNKVGNVLASHGLSKGDKVLI---MMPRSIATYelyIAALK 95
Cdd:PRK04813 3 DIIETIEEFAQTqPDFPAYDYLGEK-----LTYGQLKEDSDALAAFIDSLKLPDKSPIIVfghMSPEMLATF---LGAVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 96 LGVAIIPC---SEMLRTKDLqyrITHGEINAVIALEPFTVEFEKIKEYDAltkfviAGQKDGWISLEAEKENASNKLema 172
Cdd:PRK04813 75 AGHAYIPVdvsSPAERIEMI---IEVAKPSLIIATEELPLEILGIPVITL------DELKDIFATGNPYDFDHAVKG--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 173 dttrDDMAILSYTSGTTGNPKAVThchgwgfahlqmapkhwlcINEDDLV----WAT---AAPGWQKWV-WSPF---LSV 241
Cdd:PRK04813 143 ----DDNYYIIFTSGTTGKPKGVQ-------------------ISHDNLVsftnWMLedfALPEGPQFLnQAPYsfdLSV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 242 ------LGSGATAFVF------NgrfsPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNRE 309
Cdd:PRK04813 200 mdlyptLASGGTLVALpkdmtaN----FKQLFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 310 VVEQFKKYF-NLTVRDGYGQTESTLLIGFLKDTPQRIGSM-----GKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPA 383
Cdd:PRK04813 276 TAKKLLERFpSATIYNTYGPTEATVAVTSIEITDEMLDQYkrlpiGYAKPDSPLLIIDEEGTKLPDGEQGEIVI--SGPS 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 384 LFKGYYKEPERTAKA--QTGKY--YITGDLAHVdDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVA-- 457
Cdd:PRK04813 354 VSKGYLNNPEKTAEAffTFDGQpaYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPyn 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441463764 458 KPHDIRgNIVkAFVILQDHTAGDD-TLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:PRK04813 433 KDHKVQ-YLI-AYVVPKEEDFEREfELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
42-520 |
1.60e-35 |
|
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: 138.34 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 42 TEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEI 121
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 122 NAVialepftvefekikeydaltkFViagqkdgwisleaekenasnklemadTTRDDMAILSYTSGTTGNPKAV--THCH 199
Cdd:cd05914 81 KAI---------------------FV--------------------------SDEDDVALINYTSGTTGNSKGVmlTYRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 200 GWGFAHlqmAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLGSGATaFVFNGRFSPETyLELLQKYQI--NVLCCTPT 277
Cdd:cd05914 114 IVSNVD---GVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAH-VVFLDKIPSAK-IIALAFAQVtpTLGVPVPL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 278 E-------------------YRMMAKLQNLNDYDLT----------HLHSAVSAGEPLNREVVEQFKKyFNLTVRDGYGQ 328
Cdd:cd05914 189 ViekifkmdiipkltlkkfkFKLAKKINNRKIRKLAfkkvheafggNIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 329 TESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEgnsvPANTKGNIAVplDLPALFKGYYKEPERTAKAQT--GKYYiT 406
Cdd:cd05914 268 TETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIV--RGPNVMKGYYKNPEATAEAFDkdGWFH-T 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 407 GDLAHVDDDGYFWFEGRRDDIII-SSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIV----KAFVILQDHTAGDD 481
Cdd:cd05914 341 GDLGKIDAEGYLYIRGRKKEMIVlSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYidpdFLDVKALKQRNIID 420
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1441463764 482 TLVKELQQFVKNEVAPYKYPREIEFV-DDLPKTNSGKIRR 520
Cdd:cd05914 421 AIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
172-532 |
1.79e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 139.43 E-value: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 172 ADTTRDDMAILSYTSGTTGNPKAVTHCHG-WGFAHLQMAPKHWLCinEDDLVWAT----------AApgwqkwvWSPFLS 240
Cdd:PRK07867 147 RVADPDDLFMLIFTSGTSGDPKAVRCTHRkVASAGVMLAQRFGLG--PDDVCYVSmplfhsnavmAG-------WAVALA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 241 vlgSGAtAFVFNGRFSPETYLELLQKYQINVL--CCTPTEYrMMAKLQNLNDYDLTHlhSAVSAGEPLNREVvEQFKKYF 318
Cdd:PRK07867 218 ---AGA-SIALRRKFSASGFLPDVRRYGATYAnyVGKPLSY-VLATPERPDDADNPL--RIVYGNEGAPGDI-ARFARRF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 319 NLTVRDGYGQTESTLLIGFLKDTPQriGSMGKGIPGssVTVVD-DEGNSVP-----ANTKGNIA------VPLDLPALFK 386
Cdd:PRK07867 290 GCVVVDGFGSTEGGVAITRTPDTPP--GALGPLPPG--VAIVDpDTGTECPpaedaDGRLLNADeaigelVNTAGPGGFE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 387 GYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNI 466
Cdd:PRK07867 366 GYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQ 445
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441463764 467 VKAFVILQDHTAGDDTlvkELQQFV--KNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRdaeIEKWQ 532
Cdd:PRK07867 446 VMAALVLAPGAKFDPD---AFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLS---AEGVD 507
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
32-524 |
1.86e-35 |
|
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: 137.88 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd17649 1 PDAVALVF-----GDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPftvefekikeydaltkfviagqkdgwisleaekenasnklemadttrDDMAILSYTSGTTGN 191
Cdd:cd17649 76 LRYMLEDSGAGLLLTHHP-----------------------------------------------RQLAYVIYTSGSTGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGWGFAHLQ-------MAPK----HWLCINEDdlvwaTAAPGWqkwvwspfLSVLGSGATAFVFNGR--FSPE 258
Cdd:cd17649 109 PKGVAVSHGPLAAHCQataerygLTPGdrelQFASFNFD-----GAHEQL--------LPPLICGACVVLRPDElwASAD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 259 TYLELLQKYQINVLCCTPTEYRMMAK-LQNLNDYDLTHLHSAVSAGEPLNREVVEQFKK----YFNltvrdGYGQTEST- 332
Cdd:cd17649 176 ELAEMVRELGVTVLDLPPAYLQQLAEeADRTGDGRPPSLRLYIFGGEALSPELLRRWLKapvrLFN-----AYGPTEATv 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 333 --LLIGFLKDTPQRIGSM--GKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAK--------AQT 400
Cdd:cd17649 251 tpLVWKCEAGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGELY--IGGEGLARGYLGRPELTAErfvpdpfgAPG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 401 GKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVkAFVILQDHTAGD 480
Cdd:cd17649 329 SRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLRAAAAQP 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1441463764 481 DtLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:cd17649 408 E-LRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
32-523 |
3.34e-35 |
|
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: 137.79 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHntegeDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd12114 1 PDATAVICG-----DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPftvefekikeYDALTKFVIAGQKDGWISLEAEKENASnklemADTTRDDMAILSYTSGTTGN 191
Cdd:cd12114 76 REAILADAGARLVLTDGP----------DAQLDVAVFDVLILDLDALAAPAPPPP-----VDVAPDDLAYVIFTSGSTGT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAV--THchgwgfahlQMAPKHWLCINE------DDLVWATAAPGWQKWVWSPFlSVLGSGATaFVF---NGRFSPETY 260
Cdd:cd12114 141 PKGVmiSH---------RAALNTILDINRrfavgpDDRVLALSSLSFDLSVYDIF-GALSAGAT-LVLpdeARRRDPAHW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 261 LELLQKYQINVLCCTPteyrmmAKLQNLndydLTHLHSAVSAGEPLnREVV-----------EQFKKYF-NLTVRDGYGQ 328
Cdd:cd12114 210 AELIERHGVTLWNSVP------ALLEML----LDVLEAAQALLPSL-RLVLlsgdwipldlpARLRALApDARLISLGGA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 329 TE----STLL-IGflkDTPQRIGSM--GKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLPALfkGYYKEPERTAK---- 397
Cdd:cd12114 279 TEasiwSIYHpID---EVPPDWRSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVAL--GYLGDPELTAArfvt 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 398 -AQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVkAFVILQDH 476
Cdd:cd12114 354 hPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLA-AFVVPDND 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1441463764 477 TAGDDTLvkELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd12114 433 GTPIAPD--ALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
239-516 |
1.71e-34 |
|
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: 132.81 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 239 LSVLGSGATAFVFNG------RFSPETYLELLQKYQinvlcCT------PTeyrmMAKLQNLND---YDLTHLHSAVSAG 303
Cdd:cd17636 53 IGTLMFTLATFHAGGtnvfvrRVDAEEVLELIEAER-----CThafllpPT----IDQIVELNAdglYDLSSLRSSPAAP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 304 E--PLNREVVEQFKKYFNltvrdGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDL 381
Cdd:cd17636 124 EwnDMATVDTSPWGRKPG-----GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVA--RG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 382 PALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHD 461
Cdd:cd17636 197 PTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDP 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441463764 462 IRGNIVKAFVILQ-DHTAGDDtlvkELQQFVKNEVAPYKYPREIEFVDDLPKTNSG 516
Cdd:cd17636 277 RWAQSVKAIVVLKpGASVTEA----ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
32-523 |
2.32e-34 |
|
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: 135.29 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd17656 2 PDAVAVVF-----ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFVIAGQKDGWISLEAEKenasnklemadttrDDMAILSYTSGTTGN 191
Cdd:cd17656 77 RIYIMLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNS--------------DDLLYIIYTSGTTGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGwGFAHLQMAPKHWLCINEDDLVWATAAPGWQKwVWSPFLSVLGSGATAFVFN--GRFSPETYLELLQKYQI 269
Cdd:cd17656 143 PKGVQLEHK-NMVNLLHFEREKTNINFSDKVLQFATCSFDV-CYQEIFSTLLSGGTLYIIReeTKRDVEQLFDLVKRHNI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 270 NVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPL--NREVVEQFKKYfNLTVRDGYGQTESTLLIGFL---KDTPQR 344
Cdd:cd17656 221 EVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLviTNEFKEMLHEH-NVHLHNHYGPSETHVVTTYTinpEAEIPE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 345 IGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAKA-------QTGKYYITGDLAHVDDDGY 417
Cdd:cd17656 300 LPPIGKPISNTWIYILDQEQQLQPQGIVGELYI--SGASVARGYLNRQELTAEKffpdpfdPNERMYRTGDLARYLPDGN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 418 FWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKA-FVILQDHTagddtlVKELQQFVKNEVA 496
Cdd:cd17656 378 IEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAyFVMEQELN------ISQLREYLAKQLP 451
|
490 500
....*....|....*....|....*..
gi 1441463764 497 PYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd17656 452 EYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
32-523 |
3.17e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 138.76 E-value: 3.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhnteGEDIsVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSE------ 105
Cdd:PRK12467 526 PERPALVF----GEQV-LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPeypqdr 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 106 ---MLRTKDLQYRITHGEINAVIALEpftvefekikeyDALTKFVIAgQKDGWISLEAEkENASNKLEmadttRDDMAIL 182
Cdd:PRK12467 601 layMLDDSGVRLLLTQSHLLAQLPVP------------AGLRSLCLD-EPADLLCGYSG-HNPEVALD-----PDNLAYV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 183 SYTSGTTGNPKAVTHCHGwGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSvLGSGATAFV--FNGRFSPETY 260
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHG-ALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGA-LASGATLHLlpPDCARDAEAF 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 261 LELLQKYQINVLCCTPTEYRMMakLQNLNDYDLTHLHSAVSAGEPLNREVVEQ-FKKYFNLTVRDGYGQTESTL--LIGF 337
Cdd:PRK12467 740 AALMADQGVTVLKIVPSHLQAL--LQASRVALPRPQRALVCGGEALQVDLLARvRALGPGARLINHYGPTETTVgvSTYE 817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 338 LKDTPQRIGS--MGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDlpALFKGYYKEPERTAK--------AQTGKYYITG 407
Cdd:PRK12467 818 LSDEERDFGNvpIGQPLANLGLYILDHYLNPVPVGVVGELYIGGA--GLARGYHRRPALTAErfvpdpfgADGGRLYRTG 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 408 DLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDiRGNIVKAFVIL------QDHTAGDD 481
Cdd:PRK12467 896 DLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD-AGLQLVAYLVPaavadgAEHQATRD 974
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1441463764 482 TLVKELQQfvkneVAP-YKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:PRK12467 975 ELKAQLRQ-----VLPdYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
20-525 |
3.64e-34 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 136.12 E-value: 3.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 20 NIISEIEKYSHIPDKKAILYHNTeGEDISVTYQQLIEQSNKVG--NVLashGLSKGDKVLIMMPRSIATYELYIAALKLG 97
Cdd:PLN02574 41 DAVSFIFSHHNHNGDTALIDSST-GFSISYSELQPLVKSMAAGlyHVM---GVRQGDVVLLLLPNSVYFPVIFLAVLSLG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 98 VAIIPCSEMLRTKDLQYRIThgEINAVIALepftVEFEKIKEYDALTKFVIaGQKDGWISLEAEKENASNKLEMADTT-- 175
Cdd:PLN02574 117 GIVTTMNPSSSLGEIKKRVV--DCSVGLAF----TSPENVEKLSPLGVPVI-GVPENYDFDSKRIEFPKFYELIKEDFdf 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 176 -------RDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMAPKHWLCINED---DLVWATAAPGWQKWVWSPFLSVLGSG 245
Cdd:PLN02574 190 vpkpvikQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYpgsDNVYLAALPMFHIYGLSLFVVGLLSL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 246 ATAFVFNGRFSPETYLELLQKYQINVLCCTPTeyRMMAklqnlndydLTHLHSAVSAG------------EPLNREVVEQ 313
Cdd:PLN02574 270 GSTIVVMRRFDASDMVKVIDRFKVTHFPVVPP--ILMA---------LTKKAKGVCGEvlkslkqvscgaAPLSGKFIQD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 314 FKKYF-NLTVRDGYGQTESTLL--IGFLKDTPQRIGSMGKGIPGSSVTVVD-DEGNSVPANTKGNIAvpLDLPALFKGYY 389
Cdd:PLN02574 339 FVQTLpHVDFIQGYGMTESTAVgtRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELW--IQGPGVMKGYL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 390 KEPERTA-KAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVK 468
Cdd:PLN02574 417 NNPKATQsTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1441463764 469 AFVILQDHTAGDDTLVKElqqFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PLN02574 497 AFVVRRQGSTLSQEAVIN---YVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
42-536 |
2.09e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 133.72 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 42 TEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEI 121
Cdd:PRK06164 29 LIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 122 nAVIALEPftvEFEKIK--------EYDALTK----FVIAGQKD--------GWISLEAEKENASNKLEMADTTRDDMAI 181
Cdd:PRK06164 109 -RWLVVWP---GFKGIDfaailaavPPDALPPlraiAVVDDAADatpapapgARVQLFALPDPAPPAAAGERAADPDAGA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 182 LSYT-SGTTGNPKAVTH------CHGWGFAHLqmapkhwLCINEDDLVWAtAAPGWQKWVWSPFLSVLGSGATAF---VF 251
Cdd:PRK06164 185 LLFTtSGTTSGPKLVLHrqatllRHARAIARA-------YGYDPGAVLLA-ALPFCGVFGFSTLLGALAGGAPLVcepVF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 252 NGrfsPETyLELLQKYQINVLCCTPTEYRMMAKLQNlNDYDLTHLHS-AVSAGEPLNREVVEQFKKYfNLTVRDGYGQTE 330
Cdd:PRK06164 257 DA---ART-ARALRRHRVTHTFGNDEMLRRILDTAG-ERADFPSARLfGFASFAPALGELAALARAR-GVPLTGLYGSSE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 331 -STLLIGFLKDTPQRIGSMGKGIPGSS---VTVVDDEGNSV-PANTKGNIAVplDLPALFKGYYKEPERTAKAQTGK-YY 404
Cdd:PRK06164 331 vQALVALQPATDPVSVRIEGGGRPASPearVRARDPQDGALlPDGESGEIEI--RAPSLMRGYLDNPDATARALTDDgYF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 405 ITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDirGNIVK-AFVILQDHTAGDDtl 483
Cdd:PRK06164 409 RTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKTVPvAFVIPTDGASPDE-- 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441463764 484 vKELQQFVKNEVAPYKYPREIEFVDDLPKT---NSGKIRRVELRDAEIEKWQQQKD 536
Cdd:PRK06164 485 -AGLMAACREALAGFKVPARVQVVEAFPVTesaNGAKIQKHRLREMAQARLAAERA 539
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
32-526 |
2.39e-33 |
|
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: 133.56 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTEGEDIsVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMmprsIATYELYIAAL---KLGvAIIPCsemLR 108
Cdd:cd05906 24 PTKGITYIDADGSEEF-QSYQDLLEDARRLAAGLRQLGLRPGDSVILQ----FDDNEDFIPAFwacVLA-GFVPA---PL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 109 TKDLQYRITHGEIN------------AVIALEPFTVEFEKIKEYDALTKFVIagqkdgwISLEAEKENASNKlEMADTTR 176
Cdd:cd05906 95 TVPPTYDEPNARLRklrhiwqllgspVVLTDAELVAEFAGLETLSGLPGIRV-------LSIEELLDTAADH-DLPQSRP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 DDMAILSYTSGTTGNPKAVTHCHGwgfahlQM----APKHWLC-INEDDLVWataapgwqkwVWSPFLSVLGSG------ 245
Cdd:cd05906 167 DDLALLMLTSGSTGFPKAVPLTHR------NIlarsAGKIQHNgLTPQDVFL----------NWVPLDHVGGLVelhlra 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 246 ----------ATAFVFNgrfSPETYLELLQKYQINVlccTPTEYRMMAKLQNL------NDYDLTHLHSAVSAGEPLNRE 309
Cdd:cd05906 231 vylgcqqvhvPTEEILA---DPLRWLDLIDRYRVTI---TWAPNFAFALLNDLleeiedGTWDLSSLRYLVNAGEAVVAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 310 VVEQF----KKY-FNLTV-RDGYGQTESTLLIGFLKDTPQ-------RIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIA 376
Cdd:cd05906 305 TIRRLlrllEPYgLPPDAiRPAFGMTETCSGVIYSRSFPTydhsqalEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 377 VplDLPALFKGYYKEPERTAKAQT-GKYYITGDLAHVdDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAV 455
Cdd:cd05906 385 V--RGPVVTKGYYNNPEANAEAFTeDGWFRTGDLGFL-DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFT 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441463764 456 VAKPHDIRGNIVKAFVIL----QDHTAGDDTLVKELQQFVKNEV---APYKYPREIEfvdDLPKTNSGKIRRVELRDA 526
Cdd:cd05906 462 AAFAVRDPGAETEELAIFfvpeYDLQDALSETLRAIRSVVSREVgvsPAYLIPLPKE---EIPKTSLGKIQRSKLKAA 536
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
172-525 |
3.32e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 132.84 E-value: 3.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 172 ADTTRDDMAILSYTSGTTGNPKAVTHCHGW-GFAHLQMAPKHWLciNEDDLVW---------ATAApgwqkwVWSPflsV 241
Cdd:PRK13388 145 REVDAMDPFMLIFTSGTTGAPKAVRCSHGRlAFAGRALTERFGL--TRDDVCYvsmplfhsnAVMA------GWAP---A 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 242 LGSGATaFVFNGRFSPETYLELLQKYQINVL--CCTPTEYrMMAKLQNLNDYDLThlhSAVSAGEPLNREVVEQFKKYFN 319
Cdd:PRK13388 214 VASGAA-VALPAKFSASGFLDDVRRYGATYFnyVGKPLAY-ILATPERPDDADNP---LRVAFGNEASPRDIAEFSRRFG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 320 LTVRDGYGQTESTLLIGFLKDTPQriGSMGKGIPGssVTVVDDEGNSVPA---------------------NTKGniavp 378
Cdd:PRK13388 289 CQVEDGYGSSEGAVIVVREPGTPP--GSIGRGAPG--VAIYNPETLTECAvarfdahgallnadeaigelvNTAG----- 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 379 ldlPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAK 458
Cdd:PRK13388 360 ---AGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAV 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1441463764 459 PHDIRGNIVKAFVILQDhtaGDDTLVKELQQFVKN--EVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK13388 437 PDERVGDQVMAALVLRD---GATFDPDAFAAFLAAqpDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
32-526 |
3.67e-33 |
|
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: 131.90 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAIlyhntEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd05918 13 PDAPAV-----CAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRIThgEINAVIALepftvefekikeydaltkfviagqkdgwisleaekenASNKlemadttrDDMAILSYTSGTTGN 191
Cdd:cd05918 88 LQEILQ--DTGAKVVL-------------------------------------TSSP--------SDAAYVIFTSGSTGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAV------------THCHGWGFAH----LQMAPKHW-LCINEddlvwataapgwqkwvwspFLSVLGSGATAFVfngr 254
Cdd:cd05918 121 PKGVviehralstsalAHGRALGLTSesrvLQFASYTFdVSILE-------------------IFTTLAAGGCLCI---- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 255 fSPETYL-----ELLQKYQINVLCCTPTeyrmMAKLqnLNDYDLTHLHSAVSAGEPLNREVVEQFKKyfNLTVRDGYGQT 329
Cdd:cd05918 178 -PSEEDRlndlaGFINRLRVTWAFLTPS----VARL--LDPEDVPSLRTLVLGGEALTQSDVDTWAD--RVRLINAYGPA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 330 ESTLL-IGFLKDTPQRIGSMGKGIPGSS-VTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAKA--------- 398
Cdd:cd05918 249 ECTIAaTVSPVVPSTDPRNIGRPLGATCwVVDPDNHDRLVPIGAVGELL--IEGPILARGYLNDPEKTAAAfiedpawlk 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 399 -----QTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNH-PAVKECAV-VAKPHD--IRGNIVkA 469
Cdd:cd05918 327 qegsgRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVeVVKPKDgsSSPQLV-A 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1441463764 470 FVILQDHTAGDD--------------TLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDA 526
Cdd:cd05918 406 FVVLDGSSSGSGdgdslflepsdefrALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
32-520 |
2.13e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 133.16 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK12316 4565 PDAVAVVF-----DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRIthgEINAVIALEPFTVEFEKIKEYDALTKFVIaGQKDGWISLEAEkeNASNKLEmadttRDDMAILSYTSGTTGN 191
Cdd:PRK12316 4640 LAYMM---EDSGAALLLTQSHLLQRLPIPDGLASLAL-DRDEDWEGFPAH--DPAVRLH-----PDNLAYVIYTSGSTGR 4708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGWGFAHLQMAPKHWLCINEDDLVWATA----APGWQkWVWspflsVLGSGATAFVFN-GRFSPETYLELLQK 266
Cdd:PRK12316 4709 PKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSfsfdGSHEG-LYH-----PLINGASVVIRDdSLWDPERLYAEIHE 4782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 267 YQINVLCCTPTEYRMMAKlQNLNDYDLTHLHSAVSAGEPLNREVVEQ-FKKYFNLTVRDGYGQTEST---LLIGFLKDTP 342
Cdd:PRK12316 4783 HRVTVLVFPPVYLQQLAE-HAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTvtvLLWKARDGDA 4861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 343 QRIGSM--GKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLPAlfKGYYKEPERTAK--------AQTGKYYITGDLAHV 412
Cdd:PRK12316 4862 CGAAYMpiGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVA--RGYLERPALTAErfvpdpfgAPGGRLYRTGDLARY 4939
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 413 DDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVkAFVILQDHTAGDDT-----LVKEL 487
Cdd:PRK12316 4940 RADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLV-GYVVPQDPALADADeaqaeLRDEL 5018
|
490 500 510
....*....|....*....|....*....|...
gi 1441463764 488 QQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:PRK12316 5019 KAALRERLPEYMVPAHLVFLARMPLTPNGKLDR 5051
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
29-456 |
8.74e-32 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 128.86 E-value: 8.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 29 SHIPDKKAILYHNTEGEDISVTYQ-----QLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPC 103
Cdd:PRK09274 17 QERPDQLAVAVPGGRGADGKLAYDelsfaELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 104 SEMLRTKDLQYRITHGEINAVIALEPFTVE---FEKIKeyDALTKFVIAGQKDGW--ISLE-AEKENASNKLEMADTTRD 177
Cdd:PRK09274 97 DPGMGIKNLKQCLAEAQPDAFIGIPKAHLArrlFGWGK--PSVRRLVTVGGRLLWggTTLAtLLRDGAAAPFPMADLAPD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 178 DMAILSYTSGTTGNPKAVTHCHGWGFAHLQMAPKHW-LCINEDDLvwATAapgwqkwvwsPFLSVLGS--GATAFVFNGR 254
Cdd:PRK09274 175 DMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYgIEPGEIDL--PTF----------PLFALFGPalGMTSVIPDMD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 255 FS------PETYLELLQKYQINVLCCTPteyrmmAKLQNLNDYDLTHLHS------AVSAGEPLNREVVEQFKKYFNLTV 322
Cdd:PRK09274 243 PTrpatvdPAKLFAAIERYGVTNLFGSP------ALLERLGRYGEANGIKlpslrrVISAGAPVPIAVIERFRAMLPPDA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 323 R--DGYGQTESTLL--IG---FLKDTPQRIGSM-----GKGIPGSSVTVVD---------DEGNSVPANTKGNIAVplDL 381
Cdd:PRK09274 317 EilTPYGATEALPIssIEsreILFATRAATDNGagicvGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVV--AG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 382 PALFKGYYKEPERTAKA-----QTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVV 456
Cdd:PRK09274 395 PMVTRSYYNRPEATRLAkipdgQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALV 474
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
32-526 |
1.16e-31 |
|
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: 128.51 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILY-HNTEGEDISVTYQQLIEQSNKVGNVLASHGLsKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTK 110
Cdd:cd05931 7 PDRPAYTFlDDEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 111 DlQYRITH----GEINAVIALEPFTVEFEKIKEYDAltkfviAGQKDGWISLEAEKENASNKLEMADTTRDDMAILSYTS 186
Cdd:cd05931 86 H-AERLAAiladAGPRVVLTTAAALAAVRAFAASRP------AAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 187 GTTGNPKAVTHCHGWGFAHLQMAPKHWLCinEDDLVWATaapgwqkwvWSPF----------LSVLGSGATAfVFngrFS 256
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIRRAYGL--DPGDVVVS---------WLPLyhdmgligglLTPLYSGGPS-VL---MS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 257 PETY-------LELLQKYQINV---------LCCTpteyrmMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYF-- 318
Cdd:cd05931 224 PAAFlrrplrwLRLISRYRATIsaapnfaydLCVR------RVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFap 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 319 -NL---TVRDGYGQTESTLLI----------------------GFLKDTP----QRIGSMGKGIPGSSVTVVDDEGNS-V 367
Cdd:cd05931 298 fGFrpeAFRPSYGLAEATLFVsggppgtgpvvlrvdrdalagrAVAVAADdpaaRELVSCGRPLPDQEVRIVDPETGReL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 368 PANTKGNIAVplDLPALFKGYYKEPERTAKAQT-------GKYYITGDLAHVDDdGYFWFEGRRDDIIISSGYTIGPFEV 440
Cdd:cd05931 378 PDGEVGEIWV--RGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 441 EDALTN-HPAVKE--CAVVAKPHDIRGnivkAFVILQDHTAG-----DDTLVKELQQFVKNE--VAPykypREIEFV--D 508
Cdd:cd05931 455 EATAEEaHPALRPgcVAAFSVPDDGEE----RLVVVAEVERGadpadLAAIAAAIRAAVAREhgVAP----ADVVLVrpG 526
|
570
....*....|....*...
gi 1441463764 509 DLPKTNSGKIRRVELRDA 526
Cdd:cd05931 527 SIPRTSSGKIQRRACRAA 544
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
172-518 |
2.51e-31 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 129.27 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 172 ADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQmAPKHWLCINEDDLVWATAapgwqkwvwsPFLSVLGSGATAFV- 250
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDVFNLRNDDVILSSL----------PFFHSFGLTVTLWLp 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 251 ----FNGRFSP-----ETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLT 321
Cdd:PRK08633 846 llegIKVVYHPdptdaLGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIR 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 322 VRDGYGQTESTLLI----------GFLKDTPQRIGSMGKGIPGSSVTVVD-DEGNSVPANTKGNIAVplDLPALFKGYYK 390
Cdd:PRK08633 926 ILEGYGATETSPVAsvnlpdvlaaDFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILI--GGPQVMKGYLG 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 391 EPERTAKA----QTGKYYITGDLAHVDDDGYFWFEGR--RDDII----ISSGytigpfEVEDALtnHPAVK----ECAVV 456
Cdd:PRK08633 1004 DPEKTAEVikdiDGIGWYVTGDKGHLDEDGFLTITDRysRFAKIggemVPLG------AVEEEL--AKALGgeevVFAVT 1075
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441463764 457 AKPHDIRGnivKAFVILQDHTAGDdtlVKELQQFVKN-EVAPYKYPREIEFVDDLPKTNSGKI 518
Cdd:PRK08633 1076 AVPDEKKG---EKLVVLHTCGAED---VEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
44-533 |
2.83e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 129.69 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 44 GEdISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPC---------SEMLRTKDLQY 114
Cdd:PRK12316 533 GE-ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLdpeypaerlAYMLEDSGVQL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 115 RITHgeiNAVIALEPFTVEFEKIkEYDALTKFViAGQKDGWISLEAEKENasnklemadttrddMAILSYTSGTTGNPKA 194
Cdd:PRK12316 612 LLSQ---SHLGRKLPLAAGVQVL-DLDRPAAWL-EGYSEENPGTELNPEN--------------LAYVIYTSGSTGKPKG 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 195 VTHCHGWGFAHLQMApKHWLCINEDDLVWATAAPGWQKWVWSPFLSvLGSGATAFVF--NGRFSPETYLELLQKYQINVL 272
Cdd:PRK12316 673 AGNRHRALSNRLCWM-QQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAapGDHRDPAKLVELINREGVDTL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 273 CCTPTeyRMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQ-FKKYFNLTVRDGYGQTESTllIGFLKDTPQRIG----S 347
Cdd:PRK12316 751 HFVPS--MLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAA--IDVTHWTCVEEGgdsvP 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 348 MGKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAK-------AQTGKYYITGDLAHVDDDGYFWF 420
Cdd:PRK12316 827 IGRPIANLACYILDANLEPVPVGVLGELY--LAGRGLARGYHGRPGLTAErfvpspfVAGERMYRTGDLARYRADGVIEY 904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 421 EGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAkphdIRGNIVKAFVILQDhTAGDdtLVKELQQFVKNEVAPYKY 500
Cdd:PRK12316 905 AGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLES-EGGD--WREALKAHLAASLPEYMV 977
|
490 500 510
....*....|....*....|....*....|...
gi 1441463764 501 PREIEFVDDLPKTNSGKIRRVELRDAEIEKWQQ 533
Cdd:PRK12316 978 PAQWLALERLPLTPNGKLDRKALPAPEASVAQQ 1010
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
45-529 |
3.58e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 129.13 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 45 EDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPC---------SEMLRTKDLQYR 115
Cdd:PRK12467 3117 GDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLdpeyprerlAYMIEDSGVKLL 3196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 116 ITHGEInavialepftveFEKIKEYDALTKFVIAGqkdgwISLEAEKENASNKLEMADttrdDMAILSYTSGTTGNPKAV 195
Cdd:PRK12467 3197 LTQAHL------------LEQLPAPAGDTALTLDR-----LDLNGYSENNPSTRVMGE----NLAYVIYTSGSTGKPKGV 3255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 196 THCHGWGFAHLQ-MAPKHWLCINEDDLVWATAApgWQKWVWSpFLSVLGSGATAFVFNGR-FSPETYLELLQKYQINVLC 273
Cdd:PRK12467 3256 GVRHGALANHLCwIAEAYELDANDRVLLFMSFS--FDGAQER-FLWTLICGGCLVVRDNDlWDPEELWQAIHAHRISIAC 3332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 274 CTPteyrmmAKLQNLNDY----DLTHLHSAVSAGEPLNREVVEQ-FKKYFNLTVRDGYGQTESTLLIGFLK-DTPQRIGS 347
Cdd:PRK12467 3333 FPP------AYLQQFAEDaggaDCASLDIYVFGGEAVPPAAFEQvKRKLKPRGLTNGYGPTEAVVTVTLWKcGGDAVCEA 3406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 348 ----MGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLpaLFKGYYKEPERTAK--------AQTGKYYITGDLAHVDDD 415
Cdd:PRK12467 3407 pyapIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVG--LARGYHQRPSLTAErfvadpfsGSGGRLYRTGDLARYRAD 3484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 416 GYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDiRGNIVKAFVILQDHTAGddtLVKELQQFVKNEV 495
Cdd:PRK12467 3485 GVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPADPQGD---WRETLRDHLAASL 3560
|
490 500 510
....*....|....*....|....*....|....
gi 1441463764 496 APYKYPREIEFVDDLPKTNSGKIRRVELRDAEIE 529
Cdd:PRK12467 3561 PDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAK 3594
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
32-523 |
6.46e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 125.88 E-value: 6.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILyhnteGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK13383 49 PGRTAII-----DDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFTVEfekikeydaltkfvIAGQKDGWISLE---AEKENASNKLEMADTTRddmaILSYTSGT 188
Cdd:PRK13383 124 LAAALRAHHISTVVADNEFAER--------------IAGADDAVAVIDpatAGAEESGGRPAVAAPGR----IVLLTSGT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 189 TGNPKAVTHchgwgfahlqmAPKHWLCINeddlVWATAAP------GWQKWVWSPFLSVLGSGATAF-------VFNGR- 254
Cdd:PRK13383 186 TGKPKGVPR-----------APQLRSAVG----VWVTILDrtrlrtGSRISVAMPMFHGLGLGMLMLtialggtVLTHRh 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 255 FSPETYLELLQKYQINVLCCTPTeyrMMAKLQNLNDY-----DLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQT 329
Cdd:PRK13383 251 FDAEAALAQASLHRADAFTAVPV---VLARILELPPRvrarnPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGST 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 330 EstLLIGFL------KDTPQrigSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLPAlfKGYykePERTAKAQTGKY 403
Cdd:PRK13383 328 E--VGIGALatpadlRDAPE---TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAG--TRY---TDGGGKAVVDGM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 404 YITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhtAGDDTL 483
Cdd:PRK13383 398 TSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLH---PGSGVD 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1441463764 484 VKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:PRK13383 475 AAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
46-534 |
5.35e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.84 E-value: 5.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 46 DISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVI 125
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL 3159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 126 ALEPFTVEfekikeydaltkfviAGQKDGWISLEAEKENASNKLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAH 205
Cdd:PRK12316 3160 SQSHLRLP---------------LAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNH 3224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 206 LQmAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSvLGSGATAFVFNGRF--SPETYLELLQKYQINVLCCTPTEYRMMa 283
Cdd:PRK12316 3225 LC-WMQQAYGLGVGDRVLQFTTFSFDVFVEELFWP-LMSGARVVLAGPEDwrDPALLVELINSEGVDVLHAYPSMLQAF- 3301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 284 kLQNLNDYDLTHLHSAVSAGEPLNREVVEQFkkYFNLTVRDGYGQTESTLLIGFLKDTPQRIGS--MGKGIPGSSVTVVD 361
Cdd:PRK12316 3302 -LEEEDAHRCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD 3378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 362 DEGNSVPANTKGNIAVPLDLPAlfKGYYKEPERTAK-------AQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYT 434
Cdd:PRK12316 3379 GSLEPVPVGALGELYLGGEGLA--RGYHNRPGLTAErfvpdpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFR 3456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 435 IGPFEVEDALTNHPAVKECAVVAkphdIRGNIVKAFVILQDHTAgddTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTN 514
Cdd:PRK12316 3457 IELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDEAG---DLREALKAHLKASLPEYMVPAHLLFLERMPLTP 3529
|
490 500
....*....|....*....|
gi 1441463764 515 SGKIRRVELRDAEIEKWQQQ 534
Cdd:PRK12316 3530 NGKLDRKALPRPDAALLQQD 3549
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
32-523 |
1.65e-29 |
|
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: 121.39 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd17644 14 PDAVAVVF-----EDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIalepftvefekikeydaltkfviagqkdgwisleaekenasnklemadTTRDDMAILSYTSGTTGN 191
Cdd:cd17644 89 LTYILEDAQISVLL------------------------------------------------TQPENLAYVIYTSGSTGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGWGFAHLQMAPKHWLCINEDDlVWATAAPGWQKWVWSPFLSVLgSGATAFVFNG--RFSPETYLELLQKYQI 269
Cdd:cd17644 121 PKGVMIEHQSLVNLSHGLIKEYGITSSDR-VLQFASIAFDVAAEEIYVTLL-SGATLVLRPEemRSSLEDFVQYIQQWQL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 270 NVLCCTPTEYRMMAKLQNLNDYDL-THLHSAVSAGEPLNREVVEQFKKYF--NLTVRDGYGQTESTL---LIGFLKDTPQ 343
Cdd:cd17644 199 TVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVgnFIQLINVYGPTEATIaatVCRLTQLTER 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 344 RIGS--MGKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAK---------AQTGKYYITGDLAHV 412
Cdd:cd17644 279 NITSvpIGRPIANTQVYILDENLQPVPVGVPGELH--IGGVGLARGYLNRPELTAEkfishpfnsSESERLYKTGDLARY 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 413 DDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDdtlVKELQQFVK 492
Cdd:cd17644 357 LPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPS---TVELRQFLK 433
|
490 500 510
....*....|....*....|....*....|.
gi 1441463764 493 NEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd17644 434 AKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
33-524 |
3.89e-29 |
|
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: 120.61 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 33 DKKAILYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDL 112
Cdd:cd05915 9 GRKEVVSRLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 113 qyrithgeinaVIALEPftvefEKIKEYDALTKFV-IAGQKDGWISLEAEKENASNKLEMAD---------------TTR 176
Cdd:cd05915 89 -----------AYILNH-----AEDKVLLFDPNLLpLVEAIRGELKTVQHFVVMDEKAPEGYlayeealgeeadpvrVPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 DDMAILSYTSGTTGNPKAVTHCHGWGFAHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLGSGATAFVFNGRFS 256
Cdd:cd05915 153 RAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 257 PETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPlNREVVEQFKKYFNLTVRDGYGQTE------ 330
Cdd:cd05915 233 PASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTEtspvvv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 331 STLLIGFLKDTPQRIGSMGKGIPG-----SSVTVVDDEGNSVPANTKGNIAVPLDLPALFKGYYKEPERT-AKAQTGKYY 404
Cdd:cd05915 312 QNFVKSHLESLSEEEKLTLKAKTGlpiplVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATrSALTPDGFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 405 ITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDDtlv 484
Cdd:cd05915 392 RTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPE--- 468
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1441463764 485 kELQQFVKNEVAPYKY-PREIEFVDDLPKTNSGKIRRVELR 524
Cdd:cd05915 469 -ELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
439-517 |
8.71e-29 |
|
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: 108.79 E-value: 8.71e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1441463764 439 EVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtaGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGK 517
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP---GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
184-520 |
1.10e-28 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 120.62 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 184 YTSGTTGNPKAVTHCHGwgfAHLQMAPKHWLCINEDDL---VWATAAPGWQKWvWSPFLSVLGSGATAFVFNGRFSP--- 257
Cdd:PTZ00237 261 YTSGTTGNSKAVVRSNG---PHLVGLKYYWRSIIEKDIptvVFSHSSIGWVSF-HGFLYGSLSLGNTFVMFEGGIIKnkh 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 258 -ETYL-ELLQKYQINVLCCTPTEYRMMAKL----QNLND-YDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTE 330
Cdd:PTZ00237 337 iEDDLwNTIEKHKVTHTLTLPKTIRYLIKTdpeaTIIRSkYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 331 S--TLLIGFLKDTPQRIGSmgkGIPGSSV--TVVDDEGNSVPANTKGNIAVPLDLPALFKG-YYKEPERTAKAQTG--KY 403
Cdd:PTZ00237 417 IgiTYLYCYGHINIPYNAT---GVPSIFIkpSILSEDGKELNVNEIGEVAFKLPMPPSFATtFYKNDEKFKQLFSKfpGY 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 404 YITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVIL----QDHTAG 479
Cdd:PTZ00237 494 YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLkqdqSNQSID 573
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1441463764 480 DDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:PTZ00237 574 LNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
32-520 |
1.45e-28 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 119.22 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK05852 30 PEAPALVV---TADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRIthGEINAVIALEPFTVEFEKIKE---YDALTKFVIAGQKDGWISLEAEKENASNKLEMADTT---RDDMAILSYT 185
Cdd:PRK05852 107 QRVRS--QAAGARVVLIDADGPHDRAEPttrWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPeglRPDDAMIMFT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 186 SGTTGNPKAVThchgWGFAHLQmAPKHWLC----INEDDlvwATAA--PGWQ-KWVWSPFLSVLGSGATAFV-FNGRFSP 257
Cdd:PRK05852 185 GGTTGLPKMVP----WTHANIA-SSVRAIItgyrLSPRD---ATVAvmPLYHgHGLIAALLATLASGGAVLLpARGRFSA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 258 ETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTH--LHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTEST--- 332
Cdd:PRK05852 257 HTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPaaLRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAThqv 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 333 -----LLIGFLKDTPQRIGSMGKGIpGSSVTVVDDEGNSVPANTKGNiaVPLDLPALFKGYYKEPERTAKAQTGKYYITG 407
Cdd:PRK05852 337 tttqiEGIGQTENPVVSTGLVGRST-GAQIRIVGSDGLPLPAGAVGE--VWLRGTTVVRGYLGDPTITAANFTDGWLRTG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 408 DLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAgddTLVKEL 487
Cdd:PRK05852 414 DLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAP---PTAEEL 490
|
490 500 510
....*....|....*....|....*....|...
gi 1441463764 488 QQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:PRK05852 491 VQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
26-523 |
5.23e-28 |
|
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: 116.50 E-value: 5.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 26 EKYSHIPDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPcse 105
Cdd:cd17645 6 EQVERTPDHVAVVD-----RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 106 mlrtkdlqyrithgeinaviaLEPftvefekikEYdaltkfviAGQKDGWISLEAEKenasnKLEMADTtrDDMAILSYT 185
Cdd:cd17645 78 ---------------------IDP---------DY--------PGERIAYMLADSSA-----KILLTNP--DDLAYVIYT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 186 SGTTGNPKAVTHCH-------GWGFAHLQMAPkhwlciNEDDLVWATAapGWQKWVWSPFLSVLgSGATAFVFNgrfsPE 258
Cdd:cd17645 113 SGSTGLPKGVMIEHhnlvnlcEWHRPYFGVTP------ADKSLVYASF--SFDASAWEIFPHLT-AGAALHVVP----SE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 259 TYLEL--LQKY------QINVLCcTPTEYRMMAkLQNlndydlTHLHSAVSAGEPLNREVVEQFKKYfnltvrDGYGQTE 330
Cdd:cd17645 180 RRLDLdaLNDYfnqegiTISFLP-TGAAEQFMQ-LDN------QSLRVLLTGGDKLKKIERKGYKLV------NNYGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 331 STLLI-GFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDlpALFKGYYKEPERTAKAQTG-------K 402
Cdd:cd17645 246 NTVVAtSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE--GLARGYLNRPELTAEKFIVhpfvpgeR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 403 YYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVilqdhTAGDDT 482
Cdd:cd17645 324 MYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYV-----TAPEEI 398
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1441463764 483 LVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd17645 399 PHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
49-522 |
4.41e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 115.09 E-value: 4.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 49 VTYQQLIEQSNKVGNVLASHGLSKGDKVLIM--MPRSIATyeLYIAALKLGVAIIpcseML----RTKDLQY-------R 115
Cdd:PRK07768 30 HTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPVEIAP--TAQGLWMRGASLT----MLhqptPRTDLAVwaedtlrV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 116 ITHGEINAVIALEPFTVEFEKIKEydaltkfviagqkDGWISLEAEKENASNKLEMADTTRDDMAILSYTSGTTGNPKAV 195
Cdd:PRK07768 104 IGMIGAKAVVVGEPFLAAAPVLEE-------------KGIRVLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 196 --THCHGWGFAHLQMAPKHwlcINEDDLVWATaapgwqkwvWSP---------FLSV-LGSGATA-FVFNGRF--SPETY 260
Cdd:PRK07768 171 qiTHGNLYANAEAMFVAAE---FDVETDVMVS---------WLPlfhdmgmvgFLTVpMYFGAELvKVTPMDFlrDPLLW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 261 LELLQKYQINVLCCTPTEY----RMMAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQF---KKYFNL---TVRDGYGQTE 330
Cdd:PRK07768 239 AELISKYRGTMTAAPNFAYallaRRLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLldaGARFGLrpeAILPAYGMAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 331 STLLIGF--------------------------LKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDlpAL 384
Cdd:PRK07768 319 ATLAVSFspcgaglvvdevdadllaalrravpaTKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGE--SV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 385 FKGyYKEPERTAKAQ-TGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDiR 463
Cdd:PRK07768 397 TPG-YLTMDGFIPAQdADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-A 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441463764 464 GNIVKAF-VILQDHTAGDDTLVKELQQFVKNEV--APYKYPREIEFVD--DLPKTNSGKIRRVE 522
Cdd:PRK07768 475 GHSREGFaVAVESNAFEDPAEVRRIRHQVAHEVvaEVGVRPRNVVVLGpgSIPKTPSGKLRRAN 538
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
32-524 |
6.52e-27 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 114.97 E-value: 6.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVaiipCSEMLRT-- 109
Cdd:PRK08279 51 PDRPALLF-----EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGA----VVALLNTqq 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 110 --KDLQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFV-IAGQK-----DGWISLEAEKENAS--NKLEMADTTRDDM 179
Cdd:PRK08279 122 rgAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLwVAGGDtlddpEGYEDLAAAAAGAPttNPASRSGVTAKDT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 180 AILSYTSGTTGNPKA--VTHcHGW-----GFAHLqmapkhwLCINEDDLVW----------ATAAPGwqkwvwspflSVL 242
Cdd:PRK08279 202 AFYIYTSGTTGLPKAavMSH-MRWlkamgGFGGL-------LRLTPDDVLYcclplyhntgGTVAWS----------SVL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 243 GSGATaFVFNGRFSPETYLELLQKYQINV------LCctpteyRMMAKlQNLNDYDLTH-LHSAVSAGepLNREVVEQFK 315
Cdd:PRK08279 264 AAGAT-LALRRKFSASRFWDDVRRYRATAfqyigeLC------RYLLN-QPPKPTDRDHrLRLMIGNG--LRPDIWDEFQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 316 KYFNLT-VRDGYGQTESTL-LIGFLkdtpQRIGSMGKgIPGSSVT---VVD-DEGNSVPA-NTKGN-IAVPLDLPAL--- 384
Cdd:PRK08279 334 QRFGIPrILEFYAASEGNVgFINVF----NFDGTVGR-VPLWLAHpyaIVKyDVDTGEPVrDADGRcIKVKPGEVGLlig 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 385 -------FKGyYKEPERTAK-------AQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAV 450
Cdd:PRK08279 409 ritdrgpFDG-YTDPEASEKkilrdvfKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGV 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1441463764 451 KECAV--VAKP-HDirGNIVKAFVILQDHTAGDdtlVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PRK08279 488 EEAVVygVEVPgTD--GRAGMAAIVLADGAEFD---LAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLR 559
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
32-523 |
9.20e-27 |
|
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: 112.95 E-value: 9.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTEgedisVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd17650 1 PDAIAVSDATRQ-----LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIaLEPftvefekikeydaltkfviagqkdgwisleaekenasnklemadttrDDMAILSYTSGTTGN 191
Cdd:cd17650 76 LQYMLEDSGAKLLL-TQP-----------------------------------------------EDLAYVIYTSGTTGK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAV--TH------CHGW---------GFAHLQMAPkhwlcINEDdlVWAtaapgwqkwvwSPFLSVLGSGATAFVF--N 252
Cdd:cd17650 108 PKGVmvEHrnvahaAHAWrreyeldsfPVRLLQMAS-----FSFD--VFA-----------GDFARSLLNGGTLVICpdE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 253 GRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAV--SAGEPLN--REVVEQFKKYFNLTvrDGYGQ 328
Cdd:cd17650 170 VKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIvgSDGCKAQdfKTLAARFGQGMRII--NSYGV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 329 TESTLLIGFLKDTPQRIGS-----MGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDlpALFKGYYKEPERTAK------ 397
Cdd:cd17650 248 TEATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGA--GVARGYLNRPELTAErfvenp 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 398 -AQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKEcAVVAKPHDIRGNIVKAFVILQDH 476
Cdd:cd17650 326 fAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDKGGEARLCAYVVAAA 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1441463764 477 TAgdDTlvKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd17650 405 TL--NT--AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
32-525 |
1.80e-26 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 113.40 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGvAIIPCSEM-LRTK 110
Cdd:PLN02479 34 PTRKSVVH-----GSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAG-AVVNCVNIrLNAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 111 DLQYRITHGEINAVIA-LEPFTVEFE--KIKEYDALTKF-----VIAGQKD------------GWISLEAEKENASNKLE 170
Cdd:PLN02479 108 TIAFLLEHSKSEVVMVdQEFFTLAEEalKILAEKKKSSFkppllIVIGDPTcdpkslqyalgkGAIEYEKFLETGDPEFA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 171 MADTTRDDMAI-LSYTSGTTGNPKAVT--------------------------------HCHGWGFAHLQMApkhwLCIN 217
Cdd:PLN02479 188 WKPPADEWQSIaLGYTSGTTASPKGVVlhhrgaylmalsnaliwgmnegavylwtlpmfHCNGWCFTWTLAA----LCGT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 218 EDDLVWATAapgwqKWVWSpflSVLGSGATAF-----VFNGRF-SP--ETYLELLQKYQINVLCCTPTEYRMMAklQNLN 289
Cdd:PLN02479 264 NICLRQVTA-----KAIYS---AIANYGVTHFcaapvVLNTIVnAPksETILPLPRVVHVMTAGAAPPPSVLFA--MSEK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 290 DYDLTHLH--------SAVSAGEPLNRE--VVEQFKkyfnLTVRDGYgqtestlligflkdtpQRIGSMGkgipgssVTV 359
Cdd:PLN02479 334 GFRVTHTYglsetygpSTVCAWKPEWDSlpPEEQAR----LNARQGV----------------RYIGLEG-------LDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 360 VDDEGNS-VPANTKGNIAVPLDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPF 438
Cdd:PLN02479 387 VDTKTMKpVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 439 EVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAGDD--TLVKELQQFVKNEVAPYKYPREIEFvDDLPKTNSG 516
Cdd:PLN02479 467 EVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDeaALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATG 545
|
....*....
gi 1441463764 517 KIRRVELRD 525
Cdd:PLN02479 546 KIQKHVLRA 554
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
32-524 |
2.87e-26 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 112.39 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTegediSVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPrSIAtyELYI---AALKLGVAIIPC----- 103
Cdd:PRK10946 37 SDAIAVICGER-----QFSYRELNQASDNLACSLRRQGIKPGDTALVQLG-NVA--EFYItffALLKLGVAPVNAlfshq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 104 -SEM----------LRTKDLQYRITHGE--INAVIALEPftvefekikeydALTKFVIAGQkDGWISLEAEKENASNKLE 170
Cdd:PRK10946 109 rSELnayasqiepaLLIADRQHALFSDDdfLNTLVAEHS------------SLRVVLLLND-DGEHSLDDAINHPAEDFT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 171 MADTTRDDMAILSYTSGTTGNPKAV--TH-------------ChgwGFAhlqmAPKHWLCINEDDLVWATAAPGwqkwvw 235
Cdd:PRK10946 176 ATPSPADEVAFFQLSGGSTGTPKLIprTHndyyysvrrsveiC---GFT----PQTRYLCALPAAHNYPMSSPG------ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 236 spFLSVLGSGATAfVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMakLQNLND----YDLTHLHSAVSAGEPLNREVV 311
Cdd:PRK10946 243 --ALGVFLAGGTV-VLAPDPSATLCFPLIEKHQVNVTALVPPAVSLW--LQAIAEggsrAQLASLKLLQVGGARLSETLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 312 EQFKKYFNLTVRDGYGQTEStlLIGF--LKDTPQRI-GSMGKGI-PGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKG 387
Cdd:PRK10946 318 RRIPAELGCQLQQVFGMAEG--LVNYtrLDDSDERIfTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMT--RGPYTFRG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 388 YYKEPERTAKA-QTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNI 466
Cdd:PRK10946 394 YYKSPQHNASAfDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEK 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1441463764 467 VKAFVILQDHtagddtlVK--ELQQFVKNE-VAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PRK10946 474 SCAFLVVKEP-------LKavQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
50-533 |
3.04e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 114.10 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIALEP 129
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSH 1680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 130 FTVEFEKIKEYDALtkfvIAGQKDGWISLEAEKENASNklemadTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLQmA 209
Cdd:PRK12467 1681 LQARLPLPDGLRSL----VLDQEDDWLEGYSDSNPAVN------LAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLC-A 1749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 210 PKHWLCINEDDLVWATAAPGWQKWVWSPFLSVLGSGATAFV-FNGRFSPETYLELLQKYQINVLCCTPTEYRMMAKL--Q 286
Cdd:PRK12467 1750 TQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIApPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMdeQ 1829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 287 NLNDYDLTHLhsaVSAGEPLNREVVEQ-FKKYFNLTVRDGYGQTESTLLIGF----LKDTPQRIGS-MGKGIPGSSVTVV 360
Cdd:PRK12467 1830 VEHPLSLRRV---VCGGEALEVEALRPwLERLPDTGLFNLYGPTETAVDVTHwtcrRKDLEGRDSVpIGQPIANLSTYIL 1906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 361 DDEGNSVPANTKGNIAVPLDlpALFKGYYKEPERTAK-------AQTG-KYYITGDLAHVDDDGYFWFEGRRDDIIISSG 432
Cdd:PRK12467 1907 DASLNPVPIGVAGELYLGGV--GLARGYLNRPALTAErfvadpfGTVGsRLYRTGDLARYRADGVIEYLGRIDHQVKIRG 1984
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 433 YTIGPFEVEDALTNHPAVKECAVVAkpHDIR-GNIVKAFVILQDHTAGDD-----TLVKELQQFVKNEVAPYKYPREIEF 506
Cdd:PRK12467 1985 FRIELGEIEARLREQGGVREAVVIA--QDGAnGKQLVAYVVPTDPGLVDDdeaqvALRAILKNHLKASLPEYMVPAHLVF 2062
|
490 500
....*....|....*....|....*..
gi 1441463764 507 VDDLPKTNSGKIRRVELRDAEIEKWQQ 533
Cdd:PRK12467 2063 LARMPLTPNGKLDRKALPAPDASELQQ 2089
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
45-523 |
4.53e-24 |
|
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: 105.84 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 45 EDISVTYQQLIEQSNKVGNVLASH-GLSKGDKVLIMMPRSIATYELYIAALKLG--VAIIPCSemLRTKDLQYRITHGEI 121
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNTN--IRSKSLLHCFRCCGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 122 NAVI-------ALEPFTVEFEKikeyDALTKFVIAGQK--DGWISLEAEKENASNKLEMAD----TTRDDMAILSYTSGT 188
Cdd:cd05938 80 KVLVvapelqeAVEEVLPALRA----DGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASlrahVTIKSPALYIYTSGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 189 TGNPKA--VTHCHGWgfahlQMAPKHWLC-INEDDLVWATAapgwqkwvwsP----------FLSVLGSGATaFVFNGRF 255
Cdd:cd05938 156 TGLPKAarISHLRVL-----QCSGFLSLCgVTADDVIYITL----------PlyhssgfllgIGGCIELGAT-CVLKPKF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 256 SPETYLELLQKYQINV----------LCCTPteyrmmaklQNLNDYDlthlHSA-VSAGEPLNREVVEQFKKYF-NLTVR 323
Cdd:cd05938 220 SASQFWDDCRKHNVTViqyigellryLCNQP---------QSPNDRD----HKVrLAIGNGLRADVWREFLRRFgPIRIR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 324 DGYGQTESTllIGFLKDTpQRIGSMGKG-------IPGSSVTVVDDEGNSVPANTKGNIAVPLDLPAL----------FK 386
Cdd:cd05938 287 EFYGSTEGN--IGFFNYT-GKIGAVGRVsylykllFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLlvakitqqspFL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 387 GYYKEPERTAKA------QTGK-YYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAV--VA 457
Cdd:cd05938 364 GYAGDKEQTEKKllrdvfKKGDvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVT 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1441463764 458 KP-HDirGNIVKAFVILQDHTAGDdtlVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd05938 444 VPgHE--GRIGMAAVKLKPGHEFD---GKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
182-525 |
9.46e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 104.79 E-value: 9.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 182 LSYTSGTTGNPKAVTHCHGWGFAHLQMA--PKHwLCINEDDLVWATAaPGWQKWVWSPFLSVLGSGATaFVFNG-RFSPE 258
Cdd:PRK07008 181 LCYTSGTTGNPKGALYSHRSTVLHAYGAalPDA-MGLSARDAVLPVV-PMFHVNAWGLPYSAPLTGAK-LVLPGpDLDGK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 259 TYLELLQKYQINVLCCTPTEYRMMaklqnlndydLTHLHSAVSAGEPLNREVV----------EQFKKYFNLTVRDGYGQ 328
Cdd:PRK07008 258 SLYELIEAERVTFSAGVPTVWLGL----------LNHMREAGLRFSTLRRTVIggsacppamiRTFEDEYGVEVIHAWGM 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 329 TE-------STLLIGFLKDTP----QRIGSMGKGIPGSSVTVVDDEGNSVPANTK--GNIAVplDLPALFKGYYKepeRT 395
Cdd:PRK07008 328 TEmsplgtlCKLKWKHSQLPLdeqrKLLEKQGRVIYGVDMKIVGDDGRELPWDGKafGDLQV--RGPWVIDRYFR---GD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 396 AKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPH---DIRGNIVkafVI 472
Cdd:PRK07008 403 ASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHpkwDERPLLV---VV 479
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1441463764 473 LQdhtAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK07008 480 KR---PGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
326-525 |
1.26e-23 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 103.54 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 326 YGQTESTLLIGFLKdtPQRI----GSMGKGIPGSSVTVVddegnsvpANTKGNIAVplDLPALFKGYYkePERTAKAqtg 401
Cdd:PRK07445 261 YGMTETASQIATLK--PDDFlagnNSSGQVLPHAQITIP--------ANQTGNITI--QAQSLALGYY--PQILDSQ--- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 402 KYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDhtagDD 481
Cdd:PRK07445 324 GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKD----PS 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1441463764 482 TLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PRK07445 400 ISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
50-524 |
1.27e-23 |
|
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: 103.59 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIipcsemlrtkdlqyrithgeinavialep 129
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVA----------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 130 ftvefekikeydALTKFVIAGQkdgwiSLEAEKENASNKLEMADTtrddmAILSYTSGTTGNPKA--VTHCHGWGFAHLQ 207
Cdd:cd05940 56 ------------ALINYNLRGE-----SLAHCLNVSSAKHLVVDA-----ALYIYTSGTTGLPKAaiISHRRAWRGGAFF 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 208 MapkHWLCINEDDLVWAT-----AAPGWQKWVwspflSVLGSGATaFVFNGRFSPETYLELLQKYQinvlcCTPTEY--- 279
Cdd:cd05940 114 A---GSGGALPSDVLYTClplyhSTALIVGWS-----ACLASGAT-LVIRKKFSASNFWDDIRKYQ-----ATIFQYige 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 280 --RMMAKlQNLNDYDLTHLHSAVSaGEPLNREVVEQFKKYFNL-TVRDGYGQTESTllIGFLkDTPQRIGSMGKgIPGSS 356
Cdd:cd05940 180 lcRYLLN-QPPKPTERKHKVRMIF-GNGLRPDIWEEFKERFGVpRIAEFYAATEGN--SGFI-NFFGKPGAIGR-NPSLL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 357 VTV-------VDDEGNSVPANTKGN-IAVPLDLPAL----------FKGYYKEPERTAK------AQTGKYYITGDLAHV 412
Cdd:cd05940 254 RKVaplalvkYDLESGEPIRDAEGRcIKVPRGEPGLlisrinplepFDGYTDPAATEKKilrdvfKKGDAWFNTGDLMRL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 413 DDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAV--VAKP-HDirGNIVKAFVILQDHTAGDdtlVKELQQ 489
Cdd:cd05940 334 DGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPgTD--GRAGMAAIVLQPNEEFD---LSALAA 408
|
490 500 510
....*....|....*....|....*....|....*
gi 1441463764 490 FVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:cd05940 409 HLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
32-523 |
1.53e-23 |
|
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: 104.66 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCS-EMlrtk 110
Cdd:cd05943 82 ADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSpDF---- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 111 dlqyrithGeINAVIA----LEP---FTVE--FEKIKEYDALTK-------------------FVIAGQKDG-----WIS 157
Cdd:cd05943 158 --------G-VPGVLDrfgqIEPkvlFAVDayTYNGKRHDVREKvaelvkglpsllavvvvpyTVAAGQPDLskiakALT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 158 LEAEK-ENASNKLEMADTTRDD-MAILsYTSGTTGNPKAVTHCHGWGFahLQMAPKHWLCIN---EDDLVWATaAPGWQK 232
Cdd:cd05943 229 LEDFLaTGAAGELEFEPLPFDHpLYIL-YSSGTTGLPKCIVHGAGGTL--LQHLKEHILHCDlrpGDRLFYYT-TCGWMM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 233 WVWspFLSVLGSGATAFVFNG---RFSPETYLELLQKYQINVLCCTPTeYRMM---AKLQNLNDYDLTHLHSAVSAGEPL 306
Cdd:cd05943 305 WNW--LVSGLAVGATIVLYDGspfYPDTNALWDLADEEGITVFGTSAK-YLDAlekAGLKPAETHDLSSLRTILSTGSPL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 307 NRE----VVEQFKKyfNLTVRDGYGQTE-STLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSVPANtKGNIAVPLDL 381
Cdd:cd05943 382 KPEsfdyVYDHIKP--DVLLASISGGTDiISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVWGE-KGELVCTKPF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 382 PALFKGYYKEPE--RTAKAQTGKY---YITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVV 456
Cdd:cd05943 459 PSMPVGFWNDPDgsRYRAAYFAKYpgvWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVV 538
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1441463764 457 AKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKirRVEL 523
Cdd:cd05943 539 GQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK--KVEV 603
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
35-526 |
1.65e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 103.93 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 35 KAILYHNTEGEDiSVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEML--RTKDL 112
Cdd:PRK05857 29 EAIALRRCDGTS-ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLpiAAIER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 113 QYRIThgEINAVIALEPFTVEFEKIKE----YDALTKFVIAGQKDGWISLEAEKENASnklemADTTRDDMAILSYTSGT 188
Cdd:PRK05857 108 FCQIT--DPAAALVAPGSKMASSAVPEalhsIPVIAVDIAAVTRESEHSLDAASLAGN-----ADQGSEDPLAMIFTSGT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 189 TGNPKAVTHCHGWGFAhlqmAPKhwlCINEDDLVWATAAPGwqKWVWSPfLSVLGSGATAFVFNGRF----------SPE 258
Cdd:PRK05857 181 TGEPKAVLLANRTFFA----VPD---ILQKEGLNWVTWVVG--ETTYSP-LPATHIGGLWWILTCLMhgglcvtggeNTT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 259 TYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGeplNREVVEQFKKYFNLTVRDG--YGQTES---TL 333
Cdd:PRK05857 251 SLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAADVRFIEATGVRTAqvYGLSETgctAL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 334 LIGFLKDTPQRI--GSMGKGIPGSSVTVVDDEGNSVPANTKGNIA----VPLDLPALFKGYYKEPERTAKAQTGKYYITG 407
Cdd:PRK05857 328 CLPTDDGSIVKIeaGAVGRPYPGVDVYLAATDGIGPTAPGAGPSAsfgtLWIKSPANMLGYWNNPERTAEVLIDGWVNTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 408 DLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQdhTAGDDTLVKEL 487
Cdd:PRK05857 408 DLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVAS--AELDESAARAL 485
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1441463764 488 QQFV----KNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDA 526
Cdd:PRK05857 486 KHTIaarfRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAA 528
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
48-534 |
6.26e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.55 E-value: 6.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 48 SVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRIthgEINAVIAL 127
Cdd:PRK05691 2213 TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMI---EDSGIGLL 2289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 128 EPFTVEFEKIKEYDA-LTKFVIagqKDGWISLEAEKENASNKLEMADttrdDMAILSYTSGTTGNPKAVTHCHGWGFAHL 206
Cdd:PRK05691 2290 LSDRALFEALGELPAgVARWCL---EDDAAALAAYSDAPLPFLSLPQ----HQAYLIYTSGSTGKPKGVVVSHGEIAMHC 2362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 207 Q-------MAPK----HWLCINEDdlvwatAApgwQKWVWSPFLSvlgsGATAFV-FNGRFSPETYLELLQKYQINVLCC 274
Cdd:PRK05691 2363 QavierfgMRADdcelHFYSINFD------AA---SERLLVPLLC----GARVVLrAQGQWGAEEICQLIREQQVSILGF 2429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 275 TPTEYRMMAklQNL-NDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVR-DGYGQTESTL--LIGFLKDT-PQRIGS-- 347
Cdd:PRK05691 2430 TPSYGSQLA--QWLaGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFfNAYGPTETVVmpLACLAPEQlEEGAASvp 2507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 348 MGKGIPGSSVTVVDDEGNSVPANTKGNIAVplDLPALFKGYYKEPERTAK--------AQTGKYYITGDLAHVDDDGYFW 419
Cdd:PRK05691 2508 IGRVVGARVAYILDADLALVPQGATGELYV--GGAGLAQGYHDRPGLTAErfvadpfaADGGRLYRTGDLVRLRADGLVE 2585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 420 FEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAkpHDI-RGNIVKAFVILQDHTAGDD---TLVKELQQFVKNEV 495
Cdd:PRK05691 2586 YVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA--LDTpSGKQLAGYLVSAVAGQDDEaqaALREALKAHLKQQL 2663
|
490 500 510
....*....|....*....|....*....|....*....
gi 1441463764 496 APYKYPREIEFVDDLPKTNSGKIRRVELRDAEIEKWQQQ 534
Cdd:PRK05691 2664 PDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQA 2702
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
32-533 |
1.29e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.56 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK12316 2017 PEAIAVVF-----GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAER 2091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIAlepftvefekikEYDALTKFVIAGqkdGWISL----EAEKENASNKLEMADTTRDDMAILSYTSG 187
Cdd:PRK12316 2092 LAYMLEDSGAALLLT------------QRHLLERLPLPA---GVARLpldrDAEWADYPDTAPAVQLAGENLAYVIYTSG 2156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 188 TTGNPKAVTHCHGWGFAHLQMAPKHWLCINED-DLVWATAAPGWQKWVWSPFLSVlgsGATAFVFNGR-FSPETYLELLQ 265
Cdd:PRK12316 2157 STGLPKGVAVSHGALVAHCQAAGERYELSPADcELQFMSFSFDGAHEQWFHPLLN---GARVLIRDDElWDPEQLYDEME 2233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 266 KYQINVLCCTPTEYRMMAKLQNLNDYDLThLHSAVSAGEPLNREVVEQFKK------YFNltvrdGYGQTESTLLIGFLK 339
Cdd:PRK12316 2234 RHGVTILDFPPVYLQQLAEHAERDGRPPA-VRVYCFGGEAVPAASLRLAWEalrpvyLFN-----GYGPTEAVVTPLLWK 2307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 340 DTPQRIGS-----MGKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAK--------AQTGKYYIT 406
Cdd:PRK12316 2308 CRPQDPCGaayvpIGRALGNRRAYILDADLNLLAPGMAGELY--LGGEGLARGYLNRPGLTAErfvpdpfsASGERLYRT 2385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 407 GDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKpHDIRGNIVKAFVILQDhtaGDDTLVKE 486
Cdd:PRK12316 2386 GDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDD---AAEDLLAE 2461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1441463764 487 LQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAEIEKWQQ 533
Cdd:PRK12316 2462 LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQ 2508
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
49-456 |
1.58e-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: 94.35 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 49 VTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSiatYELYIA---ALKLGVAIIPCSEMLRTKDLQYRITHGEINAVI 125
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNS---PRWLIAdqgIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 126 AlepftvefekikeydaltkfviagqkdgwisleaekENASnklemadttrDDMAILSYTSGTTGNPKAVTHCHGwGFAH 205
Cdd:cd17640 83 V------------------------------------ENDS----------DDLATIIYTSGTTGNPKGVMLTHA-NLLH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 206 lQMapKHWLCIneddlvwATAAPGwqkwvwSPFLSVLGS------GATAFVFNGRF-----SPETYLELLQKYQINVLCC 274
Cdd:cd17640 116 -QI--RSLSDI-------VPPQPG------DRFLSILPIwhsyerSAEYFIFACGCsqaytSIRTLKDDLKRVKPHYIVS 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 275 TPteyRMMAKLQNlndydltHLHSAVSAGEPLNREVVEQFK--------------------KYFNLT---VRDGYGQTES 331
Cdd:cd17640 180 VP---RLWESLYS-------GIQKQVSKSSPIKQFLFLFFLsggifkfgisgggalpphvdTFFEAIgieVLNGYGLTET 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 332 TLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEGNSV-PANTKGNIAVplDLPALFKGYYKEPERTAKAQTGK-YYITGDL 409
Cdd:cd17640 250 SPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWV--RGPQVMKGYYKNPEATSKVLDSDgWFNTGDL 327
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1441463764 410 AHVDDDGYFWFEGR-RDDIIISSGYTIGPFEVEDALTNHPAVKECAVV 456
Cdd:cd17640 328 GWLTCGGELVLTGRaKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
32-523 |
2.41e-20 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 94.86 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGvAI-IPCS-EMlrt 109
Cdd:PRK03584 98 DDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLG-AIwSSCSpDF--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 110 kdlqyrithGEiNAVIA----LEP---FTVEF-----------EKIKE----YDALTKFVI---------AGQKDGWISL 158
Cdd:PRK03584 174 ---------GV-QGVLDrfgqIEPkvlIAVDGyryggkafdrrAKVAElraaLPSLEHVVVvpylgpaaaAAALPGALLW 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 159 -EAEKENASNKLEMADTTRDD-MAILsYTSGTTGNPKAVTHCHGwG--FAHLQMAPKHWLCINEDDLVWATaAPGWQKWV 234
Cdd:PRK03584 244 eDFLAPAEAAELEFEPVPFDHpLWIL-YSSGTTGLPKCIVHGHG-GilLEHLKELGLHCDLGPGDRFFWYT-TCGWMMWN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 235 WspFLSVLGSGATAFVFNGrfSP-----ETYLELLQKYQINVLCCTPTEYRMMAK--LQNLNDYDLTHLHSAVSAGEPLN 307
Cdd:PRK03584 321 W--LVSGLLVGATLVLYDG--SPfypdpNVLWDLAAEEGVTVFGTSAKYLDACEKagLVPGETHDLSALRTIGSTGSPLP 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 308 RE----VVEQFKKyfNLTVRDGYGQTE-STLLIGFLKDTPQRIGSM-GKGIpGSSVTVVDDEGNSVpANTKGNIAVPLDL 381
Cdd:PRK03584 397 PEgfdwVYEHVKA--DVWLASISGGTDiCSCFVGGNPLLPVYRGEIqCRGL-GMAVEAWDEDGRPV-VGEVGELVCTKPF 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 382 PALFKGYYKEPErtakaqtGKYYIT------------GDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPA 449
Cdd:PRK03584 473 PSMPLGFWNDPD-------GSRYRDayfdtfpgvwrhGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPE 545
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441463764 450 VKECAVVAKPHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIrrVEL 523
Cdd:PRK03584 546 VLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKK--VEL 617
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
147-524 |
2.54e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 92.42 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 147 VIAGQKDGWISLEAEKENASNKLemADTTR------DDMAILSYTSGTTGNPKAV-------------THCH--GWGFAH 205
Cdd:PRK07824 1 ALAGRAPALLPVPAQDERRAALL--RDALRvgepidDDVALVVATSGTTGTPKGAmltaaaltasadaTHDRlgGPGQWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 206 LQMAPKHwlcineddlvwataAPGWQKWVWSpflSVLGSGATAFVFNGRFSPETYLELLQKYQinvlccTPTEYRMMAKL 285
Cdd:PRK07824 79 LALPAHH--------------IAGLQVLVRS---VIAGSEPVELDVSAGFDPTALPRAVAELG------GGRRYTSLVPM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 286 QNLNDYD-------LTHLHSAVSAGEPLNREVVEQFKKyFNLTVRDGYGQTESTLliGFLKDtpqrigsmGKGIPGSSVT 358
Cdd:PRK07824 136 QLAKALDdpaataaLAELDAVLVGGGPAPAPVLDAAAA-AGINVVRTYGMSETSG--GCVYD--------GVPLDGVRVR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 359 VVDdegnsvpantkGNIAvpLDLPALFKGYYKEPERTAKAQTGkYYITGDLAHVDDdGYFWFEGRRDDIIISSGYTIGPF 438
Cdd:PRK07824 205 VED-----------GRIA--LGGPTLAKGYRNPVDPDPFAEPG-WFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 439 EVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVILQDHTAgdDTLvKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKI 518
Cdd:PRK07824 270 VVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPA--PTL-EALRAHVARTLDRTAAPRELHVVDELPRRGIGKV 346
|
....*.
gi 1441463764 519 RRVELR 524
Cdd:PRK07824 347 DRRALV 352
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
181-528 |
9.71e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 91.64 E-value: 9.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 181 ILSYTSGTTGNPKAVTHchGWGFAHLQMAPKHWLCINEDDLVWATAAPGWQKW-VWSPFLSVLGSGATAFVFNGRfSPET 259
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRR--SWTEIDREIEAYNEALNCEQDETPIVACPVTHSYgLICGVLAALTRGSKPVIITNK-NPKF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 260 YLELLQKYQINVLCCTPTEYRMMAKLQNLNDydltHLHSAVSAGEPLNREVVEQFKKYFNLTVRDgYGQTEStlliGFLK 339
Cdd:PRK08308 182 ALNILRNTPQHILYAVPLMLHILGRLLPGTF----QFHAVMTSGTPLPEAWFYKLRERTTYMMQQ-YGCSEA----GCVS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 340 DTPQ--RIGSMGKGIPGSSVTVVDDEGNsvpantkgniavpldlpalfkgyykePERTaKAQTGKYYI-TGDLAHVDDDG 416
Cdd:PRK08308 253 ICPDmkSHLDLGNPLPHVSVSAGSDENA--------------------------PEEI-VVKMGDKEIfTKDLGYKSERG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 417 YFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVIlQDHTAGDDtlvkELQQFVKNEVA 496
Cdd:PRK08308 306 TLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI-SHEEIDPV----QLREWCIQHLA 380
|
330 340 350
....*....|....*....|....*....|..
gi 1441463764 497 PYKYPREIEFVDDLPKTNSGKIRRVELRDAEI 528
Cdd:PRK08308 381 PYQVPHEIESVTEIPKNANGKVSRKLLELGEV 412
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-456 |
1.28e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 91.75 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQyrithgeiNAVIALEP 129
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLK--------QCLQEAEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 130 ftvefekikeydaltkfviagqkDGWISLEaekenasnkleMADttrDDMAILsYTSGTTGNPKAVTHCHGWGFAHLQmA 209
Cdd:cd05910 76 -----------------------DAFIGIP-----------KAD---EPAAIL-FTSGSTGTPKGVVYRHGTFAAQID-A 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 210 PKHWLCINEDDLVWATAAPgwqkwvWSPFLSVLGSGATAFVFN----GRFSPETYLELLQKYQINVLCCTPTEYRMMAKL 285
Cdd:cd05910 117 LRQLYGIRPGEVDLATFPL------FALFGPALGLTSVIPDMDptrpARADPQKLVGAIRQYGVSIVFGSPALLERVARY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 286 QNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFN-----LTVrdgYGQTEStLLIGFLKD-----TPQRIGSMGKG---- 351
Cdd:cd05910 191 CAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSdeaeiLTP---YGATEA-LPVSSIGSrellaTTTAATSGGAGtcvg 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 352 --IPGSSVTVV--DDEG-------NSVPANTKGNIAVplDLPALFKGYYKEPERTAKAQT-----GKYYITGDLAHVDDD 415
Cdd:cd05910 267 rpIPGVRVRIIeiDDEPiaewddtLELPRGEIGEITV--TGPTVTPTYVNRPVATALAKIddnseGFWHRMGDLGYLDDE 344
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1441463764 416 GYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVV 456
Cdd:cd05910 345 GRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
50-524 |
1.61e-19 |
|
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: 91.33 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEINAVIalep 129
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 130 ftvefekikeYDALTKfviagqkdgwisLEAEKENASNKLEMADTTrdDMAILSYTSGTTGNPKA--VTHchgwgFAHLQ 207
Cdd:cd05939 81 ----------FNLLDP------------LLTQSSTEPPSQDDVNFR--DKLFYIYTSGTTGLPKAavIVH-----SRYYR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 208 MAP--KHWLCINEDDLVWA------TAApgwqkwvwspflSVLGSG-----ATAFVFNGRFSPETYLELLQKYQinvlcC 274
Cdd:cd05939 132 IAAgaYYAFGMRPEDVVYDclplyhSAG------------GIMGVGqallhGSTVVIRKKFSASNFWDDCVKYN-----C 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 275 TPTEY-----RMMAKlQNLNDYDLTH-LHSAVSAGepLNREVVEQFKKYFNLT-VRDGYGQTESTLLIGFLKDTPQRIGS 347
Cdd:cd05939 195 TIVQYigeicRYLLA-QPPSEEEQKHnVRLAVGNG--LRPQIWEQFVRRFGIPqIGEFYGATEGNSSLVNIDNHVGACGF 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 348 MGKgIPGS----SVTVVDDE---------GNSVPANTK------GNIaVPLDLPALFKGYYKEPERTAK------AQTGK 402
Cdd:cd05939 272 NSR-ILPSvypiRLIKVDEDtgelirdsdGLCIPCQPGepgllvGKI-IQNDPLRRFDGYVNEGATNKKiardvfKKGDS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 403 YYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAV--VAKPHdIRGNIVKAFVILQDHTAGD 480
Cdd:cd05939 350 AFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAIVDPERKVDL 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1441463764 481 DTLVKELQQfvknEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:cd05939 429 DRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
50-456 |
6.33e-19 |
|
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: 89.84 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGLSKGDKVLIMmPRSIATYELYIAALKLGVAI-IPCSEMLRTKDLQYRITHGEINAVIAle 128
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALI-SKNCAEWFITDLAIWMAGHIsVPLYPTLNPDTIRYVLEHSESKALFV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 129 pftvefEKIKEYDAlTKFVIAGQ--------------KDGWISLEAEkenaSNKLEMADTTRDD-MAILSYTSGTTGNPK 193
Cdd:cd05932 85 ------GKLDDWKA-MAPGVPEGlisislpppsaancQYQWDDLIAQ----HPPLEERPTRFPEqLATLIYTSGTTGQPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 194 AVTHCHG-WGFAhLQMAPKHwLCINEDD--LVWATAAPGWQKwVWSPFLSVLGSGATAFVFngrfSPETYLELLQKYQIN 270
Cdd:cd05932 154 GVMLTFGsFAWA-AQAGIEH-IGTEENDrmLSYLPLAHVTER-VFVEGGSLYGGVLVAFAE----SLDTFVEDVQRARPT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 271 VLCCTP---TEYRM-------MAKLQNL---------------NDYDLTHLHSAVSAGEPLNREVVEQFKKyFNLTVRDG 325
Cdd:cd05932 227 LFFSVPrlwTKFQQgvqdkipQQKLNLLlkipvvnslvkrkvlKGLGLDQCRLAGCGSAPVPPALLEWYRS-LGLNILEA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 326 YGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVDDEgnsvpantkgniAVPLDLPALFKGYYKEPERTAKAQTGKYYI 405
Cdd:cd05932 306 YGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISEDG------------EILVRSPALMMGYYKDPEATAEAFTADGFL 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1441463764 406 -TGDLAHVDDDGYFWFEGRRDDII-ISSGYTIGPFEVEDALTNHPAVKECAVV 456
Cdd:cd05932 374 rTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
177-524 |
7.83e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.86 E-value: 7.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 DDMAILSYTSGTTGNPKAVTHCHGwGFAHLQMAPKHWLCINEDDlVWATAAPGWQKWVWSPFLSVLGSGAtAFVFNGRFS 256
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHS-ALIVQSLAKIAIVGYGEDD-VYLHTAPLCHIGGLSSALAMLMVGA-CHVLLPKFD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 257 PETYLELLQKYQINVLCCTPTeyrMMAKL-----QNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYF-NLTVRDGYGQTE 330
Cdd:PLN02860 249 AKAALQAIKQHNVTSMITVPA---MMADLisltrKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 331 --STLLIGFLKD--------------------TPQRIGS-MGKGIPGSSVTVVDDEGNSVpantkGNIAVplDLPALFKG 387
Cdd:PLN02860 326 acSSLTFMTLHDptlespkqtlqtvnqtksssVHQPQGVcVGKPAPHVELKIGLDESSRV-----GRILT--RGPHVMLG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 388 YYKEPERTAKAQTGKYYI-TGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNI 466
Cdd:PLN02860 399 YWGQNSETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEM 478
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1441463764 467 VKAFVILQDH-TAGDDTLVKELQQFV-----------KNEVAPYKYPREI-EFVDDLPKTNSGKIRRVELR 524
Cdd:PLN02860 479 VVACVRLRDGwIWSDNEKENAKKNLTlssetlrhhcrEKNLSRFKIPKLFvQWRKPFPLTTTGKIRRDEVR 549
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
46-534 |
8.41e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 91.00 E-value: 8.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 46 DISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKDLQYRITHGEInavi 125
Cdd:PRK05691 3743 DQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRT---- 3818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 126 alePFTVEFEKIKE--YDALTKFVIAGQKDGWISLEAEKENASNKLEMADTTRDDMAILSYTSGTTGNPKAVThCHGWGF 203
Cdd:PRK05691 3819 ---PVLVCSAACREqaRALLDELGCANRPRLLVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVM-VEQRGM 3894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 204 AHLQMAPKHWLCINEDDLVWATAAPGWQKWVWSpFLSvlgsgatAFVFNGRFS---------PETYLELLQKYQINVLCC 274
Cdd:PRK05691 3895 LNNQLSKVPYLALSEADVIAQTASQSFDISVWQ-FLA-------APLFGARVEivpnaiahdPQGLLAHVQAQGITVLES 3966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 275 TPTEY-RMMAklqnlNDYD-LTHLHSAVSAGEPLNREVVEQF-KKYFNLTVRDGYGQTESTLLIGFLK-DTPQRIGS--- 347
Cdd:PRK05691 3967 VPSLIqGMLA-----EDRQaLDGLRWMLPTGEAMPPELARQWlQRYPQIGLVNAYGPAECSDDVAFFRvDLASTRGSylp 4041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 348 MGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLdlPALFKGYYKEPERTAKA-------QTG-KYYITGDLAHVDDDGYFW 419
Cdd:PRK05691 4042 IGSPTDNNRLYLLDEALELVPLGAVGELCVAG--TGVGRGYVGDPLRTALAfvphpfgAPGeRLYRTGDLARRRSDGVLE 4119
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 420 FEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKpHDIRGNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYK 499
Cdd:PRK05691 4120 YVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQ-EGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYM 4198
|
490 500 510
....*....|....*....|....*....|....*
gi 1441463764 500 YPREIEFVDDLPKTNSGKIRRVELRDAEIEKWQQQ 534
Cdd:PRK05691 4199 VPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQ 4233
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
32-535 |
9.51e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.53 E-value: 9.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntEGEdiSVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPC-------- 103
Cdd:PRK05691 1145 PERIALVW---DGG--SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLdpdypaer 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 104 -SEMLRTKDLQYRITHGEInavialepftveFEKIKEYDALTKFVIAGQK-DGWISleaekenASNKLEMADttrDDMAI 181
Cdd:PRK05691 1220 lAYMLADSGVELLLTQSHL------------LERLPQAEGVSAIALDSLHlDSWPS-------QAPGLHLHG---DNLAY 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 182 LSYTSGTTGNPKAVthchgwGFAHLQMAPK-HWL----CINEDDLVWATAAPGWQKWVWSPFLSVLGSGATAFVFNGRF- 255
Cdd:PRK05691 1278 VIYTSGSTGQPKGV------GNTHAALAERlQWMqatyALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHr 1351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 256 SPETYLELLQKYQINVLCCTPTEYRMMakLQNLNDYDLTHLHSAVSAGEPLNRE----VVEQFKkyfNLTVRDGYGQTES 331
Cdd:PRK05691 1352 DPQRIAELVQQYGVTTLHFVPPLLQLF--IDEPLAAACTSLRRLFSGGEALPAElrnrVLQRLP---QVQLHNRYGPTET 1426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 332 TLLIGFL---KDTPQRiGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPERTAK-------AQTG 401
Cdd:PRK05691 1427 AINVTHWqcqAEDGER-SPIGRPLGNVLCRVLDAELNLLPPGVAGELC--IGGAGLARGYLGRPALTAErfvpdplGEDG 1503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 402 -KYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFVIlqdhTAGD 480
Cdd:PRK05691 1504 aRLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTG----EAGQ 1579
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1441463764 481 DTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELRDAEiekWQQQK 535
Cdd:PRK05691 1580 EAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPV---WQQRE 1631
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
33-525 |
6.21e-17 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 83.98 E-value: 6.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 33 DKKAILYHNtEGEDIS----VTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLR 108
Cdd:PLN03052 190 DSIAIIWRD-EGSDDLpvnrMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 109 TKDLQYRITHGEINAVialepFTVEF-----------EKIKEYDALTKFVIAGqKDGWISLEAEKENAS--NKLEMADTT 175
Cdd:PLN03052 269 PSEIATRLKISKAKAI-----FTQDVivrggksiplySRVVEAKAPKAIVLPA-DGKSVRVKLREGDMSwdDFLARANGL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 176 RDD-------MAILSYT-----SGTTGNPKAV--TH-------CHGWgfAHLQMAPKHWLCineddlvWATAApGWQKWV 234
Cdd:PLN03052 343 RRPdeykaveQPVEAFTnilfsSGTTGEPKAIpwTQltplraaADAW--AHLDIRKGDIVC-------WPTNL-GWMMGP 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 235 WSPFLSVLgSGATAFVFNGrfSP--ETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLTHLHSAVSAGEPLNREvve 312
Cdd:PLN03052 413 WLVYASLL-NGATLALYNG--SPlgRGFAKFVQDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIRCFGSTGEASSVD--- 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 313 qfkKYFNLTVRDGY-------GQTE--STLLIGFLKDtPQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDlPA 383
Cdd:PLN03052 487 ---DYLWLMSRAGYkpiieycGGTElgGGFVTGSLLQ-PQAFAAFSTPAMGCKLFILDDSGNPYPDDAPCTGELALF-PL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 384 LF------------KGYYK-EPERTAKaQTGKYyitGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDAL-TNHPA 449
Cdd:PLN03052 562 MFgasstllnadhyKVYFKgMPVFNGK-ILRRH---GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADES 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 450 VKECAVVAKPHDIRG--NIVkAFVILQDHTAGDDTLvKELQQFVKNEVA----PYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:PLN03052 638 VLETAAIGVPPPGGGpeQLV-IAAVLKDPPGSNPDL-NELKKIFNSAIQkklnPLFKVSAVVIVPSFPRTASNKVMRRVL 715
|
..
gi 1441463764 524 RD 525
Cdd:PLN03052 716 RQ 717
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
49-459 |
9.89e-17 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 83.25 E-value: 9.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 49 VTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCS--------EMLRTKDLQYRITHGE 120
Cdd:cd05921 26 VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSpayslmsqDLAKLKHLFELLKPGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 121 INAVIAlEPFTVEFEKIKEyDALTKFVIAGQKDGWISLEAEKENASNKLEMAD-----TTRDDMAILSYTSGTTGNPKAV 195
Cdd:cd05921 106 VFAQDA-APFARALAAIFP-LGTPLVVSRNAVAGRGAISFAELAATPPTAAVDaafaaVGPDTVAKFLFTSGSTGLPKAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 196 THCHGWGFAHLQMAPKHWLCINEDDLVWATAAPgwqkwvWS-------PFLSVLGSGATAFVFNGRFSP---ETYLELLQ 265
Cdd:cd05921 184 INTQRMLCANQAMLEQTYPFFGEEPPVLVDWLP------WNhtfggnhNFNLVLYNGGTLYIDDGKPMPggfEETLRNLR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 266 KYQINVLCCTPTEYRM----MAKLQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKyfnLTVRD---------GYGQTEST 332
Cdd:cd05921 258 EISPTVYFNVPAGWEMlvaaLEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQA---LAVATvgeripmmaGLGATETA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 333 LLIGFLKDTPQRIGSMGKGIPGSSVTVvddegnsVPANTKgnIAVPLDLPALFKGYYKEPERTAKA--QTGkYYITGDLA 410
Cdd:cd05921 335 PTATFTHWPTERSGLIGLPAPGTELKL-------VPSGGK--YEVRVKGPNVTPGYWRQPELTAQAfdEEG-FYCLGDAA 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1441463764 411 H-VDDD----GyFWFEGR-RDDIIISSG--YTIGPFEVEDALTNHPAVKEcAVVAKP 459
Cdd:cd05921 405 KlADPDdpakG-LVFDGRvAEDFKLASGtwVSVGPLRARAVAACAPLVHD-AVVAGE 459
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
35-524 |
3.63e-16 |
|
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: 81.00 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 35 KAILYHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPcsemlrtkdlqy 114
Cdd:cd05908 2 EGIIFILGDKKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVP------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 115 rITHGEINAVIalepftveFEKIKEYDALTK-FVIAgqkdgwiSLEAEKENAsnklemadttrDDMAILSYTSGTTGNPK 193
Cdd:cd05908 70 -VSIGSNEEHK--------LKLNKVWNTLKNpYLIT-------EEEVLCELA-----------DELAFIQFSSGSTGDPK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 194 AVTHCHGwGFAHLQMAPKHWLCINEDD--LVWATAAPGWQkwVWSPFLSVLGSGATAFVFNGRF---SPETYLELLQKYQ 268
Cdd:cd05908 123 GVMLTHE-NLVHNMFAILNSTEWKTKDriLSWMPLTHDMG--LIAFHLAPLIAGMNQYLMPTRLfirRPILWLKKASEHK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 269 INVLCCTPTEYRMMAKLQN---LNDYDLTHLHSAVSAGEPLNREVVEQFKKY---FNL---TVRDGYGQTEST------- 332
Cdd:cd05908 200 ATIVSSPNFGYKYFLKTLKpekANDWDLSSIRMILNGAEPIDYELCHEFLDHmskYGLkrnAILPVYGLAEASvgaslpk 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 333 --------------LLIG-----FLKDTPQ--RIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAvpLDLPALFKGYYKE 391
Cdd:cd05908 280 aqspfktitlgrrhVTHGepepeVDKKDSEclTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQ--IRGKNVTPGYYNN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 392 PERTAKAQTGK-YYITGDLAHVDDdGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVA---KPHDIRGNIV 467
Cdd:cd05908 358 PEATAKVFTDDgWLKTGDLGFIRN-GRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEI 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1441463764 468 KAFVIlqdHTAGDDTLVKeLQQFVKNEVAPYKYPR--EIEFVDDLPKTNSGKIRRVELR 524
Cdd:cd05908 437 FCFIE---HRKSEDDFYP-LGKKIKKHLNKRGGWQinEVLPIRRIPKTTSGKVKRYELA 491
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
73-423 |
4.28e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 81.02 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 73 GDKVLIMMPRSIATYELYIAALKLGV--AIIPCSEMLRtkDLQYRITHGEINAVIALEPFTVEFEKIK----EYDALTKF 146
Cdd:PRK06334 67 DQHIGIMMPASAGAYIAYFATLLSGKipVMINWSQGLR--EVTACANLVGVTHVLTSKQLMQHLAQTHgedaEYPFSLIY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 147 V--IAGQKDGW------ISLEAEKENASNKLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHlQMAPKHWLCINE 218
Cdd:PRK06334 145 MeeVRKELSFWekcrigIYMSIPFEWLMRWFGVSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLAN-QRACLKFFSPKE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 219 DDLVWATAAP----GWQKWVWSPFLSVLgsgATAFVFNgRFSPETYLELLQKYQINVLCCTPTEYRMMAKLQNLNDYDLT 294
Cdd:PRK06334 224 DDVMMSFLPPfhayGFNSCTLFPLLSGV---PVVFAYN-PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 295 HLHSAVSAGEPLNREVVEQFKKYF-NLTVRDGYGQTESTLLIGF-LKDTPQRIGSMGKGIPGSSVTVVDDEgNSVPANTK 372
Cdd:PRK06334 300 SLRFVVIGGDAFKDSLYQEALKTFpHIQLRQGYGTTECSPVITInTVNSPKHESCVGMPIRGMDVLIVSEE-TKVPVSSG 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1441463764 373 GNIAVPLDLPALFKGYYKEPERTAKAQTG--KYYITGDLAHVDDDGYFWFEGR 423
Cdd:PRK06334 379 ETGLVLTRGTSLFSGYLGEDFGQGFVELGgeTWYVTGDLGYVDRHGELFLKGR 431
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
177-530 |
5.90e-15 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 77.09 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 DDMAILSYTSGTTGNPKAV------THCHGWGFAH-LQMAP--KHWLCInedDLVWATAApgwqkwvWSPFLSVLGSGAT 247
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAaiswrrTLVTSNLLSHdLNLKNgdRTYTCM---PLYHGTAA-------FLGACNCLMSGGT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 248 aFVFNGRFSPET--------------YLELLQKYQINVlccTPTEYRMMAKLQnlndydlthlhsaVSAGEPLNREVVEQ 313
Cdd:cd05937 157 -LALSRKFSASQfwkdvrdsgatiiqYVGELCRYLLST---PPSPYDRDHKVR-------------VAWGNGLRPDIWER 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 314 FKKYFNL-TVRDGYGQTESTLLIGFLKDTPQRIGSMGKGIP------GSSVTVV--DDEGNSV------------PANTK 372
Cdd:cd05937 220 FRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLirrwkfENQVVLVkmDPETDDPirdpktgfcvraPVGEP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 373 GNI--AVPLDLPALFKGYYKEPERTAKA------QTGK-YYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDA 443
Cdd:cd05937 300 GEMlgRVPFKNREAFQGYLHNEDATESKlvrdvfRKGDiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADV 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 444 LTNHPAVKECAV--VAKP-HDirGNIVKAFVILQDHTAGDDTLVK-ELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIR 519
Cdd:cd05937 380 LGAHPDIAEANVygVKVPgHD--GRAGCAAITLEESSAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQ 457
|
410
....*....|.
gi 1441463764 520 RVELRDAEIEK 530
Cdd:cd05937 458 KGVLRDEGVDP 468
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
32-523 |
6.19e-15 |
|
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: 77.13 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:cd17654 1 PDRPALII-DQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRIThgeinavialepftvefekikeyDALTKFVIAGQKDGwislEAEKENASNKLEMADTTRDDMAILSYTSGTTGN 191
Cdd:cd17654 80 SLTVMK-----------------------KCHVSYLLQNKELD----NAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PK--AVTH-CHGWGFAHLQMAPKhwlcINEDDLVWATAAPGWQKWVWSPFLSVLgSGATAFVfngrfSPETYLELLQKY- 267
Cdd:cd17654 133 PKivAVPHkCILPNIQHFRSLFN----ITSEDILFLTSPLTFDPSVVEIFLSLS-SGATLLI-----VPTSVKVLPSKLa 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 268 -------QINVLCCTPTEYRMMAK--LQNLNDYDLTHLHSAVSAGEPLNREVV-EQFKKYFNLT-VRDGYGQTE----ST 332
Cdd:cd17654 203 dilfkrhRITVLQATPTLFRRFGSqsIKSTVLSATSSLRVLALGGEPFPSLVIlSSWRGKGNRTrIFNIYGITEvscwAL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 333 LLIGFLKDTPQRIGSmgkGIPGSSVTVVDDEGNSVPANtkgniavpLDLPALFKGYY-KEPERTAKAQtgkYYITGDLAH 411
Cdd:cd17654 283 AYKVPEEDSPVQLGS---PLLGTVIEVRDQNGSEGTGQ--------VFLGGLNRVCIlDDEVTVPKGT---MRATGDFVT 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 412 VDDDGYFwFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDirgNIVkAFVILQDHtagDDTLVKELQqfv 491
Cdd:cd17654 349 VKDGELF-FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQ---RLI-AFIVGESS---SSRIHKELQ--- 417
|
490 500 510
....*....|....*....|....*....|..
gi 1441463764 492 KNEVAPYKYPREIEFVDDLPKTNSGKIRRVEL 523
Cdd:cd17654 418 LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
33-524 |
7.30e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 77.52 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 33 DKKAILYHNTEGEDIsvTYQQLIEQSNKVGNVLASH-GLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK05620 25 DTTVTTWGGAEQEQT--TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEiNAVIALEPFTVE--FEKIKEYDALTKFVIAGQKDGWI------------SLEAEKENASNKLEMADTTRD 177
Cdd:PRK05620 103 IVHIINHAE-DEVIVADPRLAEqlGEILKECPCVRAVVFIGPSDADSaaahmpegikvySYEALLDGRSTVYDWPELDET 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 178 DMAILSYTSGTTGNPKAVTHCHGWGFAH-LQMAPKHWLCInEDDLVWATAAPGWQKWVWSPFLSVLGSGaTAFVFNGR-F 255
Cdd:PRK05620 182 TAAAICYSTGTTGAPKGVVYSHRSLYLQsLSLRTTDSLAV-THGESFLCCVPIYHVLSWGVPLAAFMSG-TPLVFPGPdL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 256 SPETYLELLQKYQINVLCCTPTEYrmmakLQNLNDYDLTH-----LHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTE 330
Cdd:PRK05620 260 SAPTLAKIIATAMPRVAHGVPTLW-----IQLMVHYLKNPpermsLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 331 sTLLIGFLKDTPQ----------RIgSMGKGIPGSSVTVVDDeGNSVPANTKGNIAVPLDLPALFKGYYKEP--ERTAKA 398
Cdd:PRK05620 335 -TSPVGTVARPPSgvsgearwayRV-SQGRFPASLEYRIVND-GQVMESTDRNEGEIQVRGNWVTASYYHSPteEGGGAA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 399 QTGK---------------YYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIR 463
Cdd:PRK05620 412 STFRgedvedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKW 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1441463764 464 GNIVKAFVILQDHTAGDDTLVKELQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PRK05620 492 GERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
180-453 |
7.75e-14 |
|
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: 74.32 E-value: 7.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 180 AILSYTSGTTGNPKAVTHCHG---W----GFAHLQMAPK--------------H--------WLCINEDDLVWaTAAPGW 230
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDnitWtakaASQHMDLRPAtvgqesvvsylplsHiaaqildiWLPIKVGGQVY-FAQPDA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 231 QKW-------------------VWSPFLSVLGSGAT--------AFVFNGRFSPETYLELLQKYQINVLCCTPTEYRMMA 283
Cdd:cd05933 232 LKGtlvktlrevrptafmgvprVWEKIQEKMKAVGAksgtlkrkIASWAKGVGLETNLKLMGGESPSPLFYRLAKKLVFK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 284 KLQNLNDYDltHLHSAVSAGEPLNREVveqfKKYF---NLTVRDGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVV 360
Cdd:cd05933 312 KVRKALGLD--RCQKFFTGAAPISRET----LEFFlslNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIH 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 361 --DDEGNsvpantkGNIAVPLDLpaLFKGYYKEPERTAKA-QTGKYYITGDLAHVDDDGYFWFEGRRDDIII-SSGYTIG 436
Cdd:cd05933 386 npDADGI-------GEICFWGRH--VFMGYLNMEDKTEEAiDEDGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENVP 456
|
330
....*....|....*..
gi 1441463764 437 PFEVEDaltnhpAVKEC 453
Cdd:cd05933 457 PVPIED------AVKKE 467
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
39-536 |
2.82e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 72.35 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 39 YHNTEGEDISV-TYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGV--AIIPCSEMLRTKD---- 111
Cdd:PRK09192 39 FYDRRGQLEEAlPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLvpVPLPLPMGFGGREsyia 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 -LQYRITHGEINAVIA---LEPFTVEfekikeydaltkfvIAGQKDGWISLEAEKENAsnkLEMADT-----TRDDMAIL 182
Cdd:PRK09192 119 qLRGMLASAQPAAIITpdeLLPWVNE--------------ATHGNPLLHVLSHAWFKA---LPEADValprpTPDDIAYL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 183 SYTSGTTGNPKAVTHCHGWGFAHLQMAPKHWLCINEDDLVWAtaapgwqkwvWSPF----------LSVLGSGATA-FVF 251
Cdd:PRK09192 182 QYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPGDRCVS----------WLPFyhdmglvgflLTPVATQLSVdYLP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 252 NGRFS--PETYLELLQKYQINVLCCTPTEYRMMAK---LQNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDG- 325
Cdd:PRK09192 252 TRDFArrPLQWLDLISRNRGTISYSPPFGYELCARrvnSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDk 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 326 -----YGQTESTLLIGF-------------------------LKDTPQRIGSM---GKGIPGSSVTVVDDEGNSVPANTK 372
Cdd:PRK09192 332 afmpsYGLAEATLAVSFsplgsgivveevdrdrleyqgkavaPGAETRRVRTFvncGKALPGHEIEIRNEAGMPLPERVV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 373 GNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDdGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVK- 451
Cdd:PRK09192 412 GHICV--RGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLLD-GYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRs 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 452 -ECAVVAKPHDIRGNIVkafVILQDHTAGDDT---LVKELQQFVKN--------EVAPykyPREiefvddLPKTNSGKIR 519
Cdd:PRK09192 489 gDAAAFSIAQENGEKIV---LLVQCRISDEERrgqLIHALAALVRSefgveaavELVP---PHS------LPRTSSGKLS 556
|
570
....*....|....*..
gi 1441463764 520 RVELRDAEIEKWQQQKD 536
Cdd:PRK09192 557 RAKAKKRYLSGAFASLD 573
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
32-520 |
6.96e-13 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 71.61 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYhntegEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCsemlrtkD 111
Cdd:PRK10252 472 PDAPALAD-----ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL-------D 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQY---RIthgeinAVIaLEpftvefekikeyDALTKFVIAGQK------DGWISLEAEKENASNKLEMADTTR---DDM 179
Cdd:PRK10252 540 TGYpddRL------KMM-LE------------DARPSLLITTADqlprfaDVPDLTSLCYNAPLAPQGAAPLQLsqpHHT 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 180 AILSYTSGTTGNPKAVTHCHG-------WGFAHLQMAPkhwlcineDDLVWATAAPGWQKWVWSPFLSVLgSGATAFVF- 251
Cdd:PRK10252 601 AYIIFTSGSTGRPKGVMVGQTaivnrllWMQNHYPLTA--------DDVVLQKTPCSFDVSVWEFFWPFI-AGAKLVMAe 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 252 -NGRFSPETYLELLQKYQINVLCCTPTeyrMMAKL------QNLNDYDLThLHSAVSAGEPLNREVVEQFKKYFNLTVRD 324
Cdd:PRK10252 672 pEAHRDPLAMQQFFAEYGVTTTHFVPS---MLAAFvasltpEGARQSCAS-LRQVFCSGEALPADLCREWQQLTGAPLHN 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 325 GYGQTESTLLIGFLKDTPQRIGSmgkgIPGSSVT-----------VVDDEGNSVPANTKGNIAvpLDLPALFKGYYKEPE 393
Cdd:PRK10252 748 LYGPTEAAVDVSWYPAFGEELAA----VRGSSVPigypvwntglrILDARMRPVPPGVAGDLY--LTGIQLAQGYLGRPD 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 394 RTAK-------AQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKphdirgni 466
Cdd:PRK10252 822 LTASrfiadpfAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHAC-------- 893
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1441463764 467 vkafVILQDHTAGDDT------LVKE---------LQQFVKNEVAPYKYPREIEFVDDLPKTNSGKIRR 520
Cdd:PRK10252 894 ----VINQAAATGGDArqlvgyLVSQsglpldtsaLQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDR 958
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
180-524 |
7.47e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 70.95 E-value: 7.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 180 AILSYTSGTTGNPK-------AVTHCHGWGFAHLQMAPKH-----WLCINED----DLVWA--TAAPGWQkwvwSPflsv 241
Cdd:PRK05851 155 AVLQGTAGSTGTPRtailspgAVLSNLRGLNARVGLDAATdvgcsWLPLYHDmglaFLLTAalAGAPLWL----AP---- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 242 lgsgATAFVFngrfSPETYLELLQKYQINVLCCTPTEYRMMAKL-QNLNDYDLTHLHSAVSAGEPLNrevVEQFKKYFNL 320
Cdd:PRK05851 227 ----TTAFSA----SPFRWLSWLSDSRATLTAAPNFAYNLIGKYaRRVSDVDLGALRVALNGGEPVD---CDGFERFATA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 321 TVRDG---------YGQTESTLLI-------GFLKD--------TPQRIGSMGKGIPGSSVTVVDDEGnSVPANTKGNIA 376
Cdd:PRK05851 296 MAPFGfdagaaapsYGLAESTCAVtvpvpgiGLRVDevttddgsGARRHAVLGNPIPGMEVRISPGDG-AAGVAGREIGE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 377 VPLDLPALFKGYYKEpertAKAQTGKYYITGDLAHVDDDGYFwFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVV 456
Cdd:PRK05851 375 IEIRGASMMSGYLGQ----APIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVV 449
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1441463764 457 AKPHDiRGNIVKAFVILQDHTAGD-DTLVKELQQFVKNEVApyKYPREIEFVD--DLPKTNSGKIRRVELR 524
Cdd:PRK05851 450 AVGTG-EGSARPGLVIAAEFRGPDeAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVK 517
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
45-524 |
3.34e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 68.97 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 45 EDISV---TYQQLIEQSNKVGNVLASHGlSKGDKVLIMMPRSIATyelyiAALKLGVAI---IPCseMLR----TKDLQY 114
Cdd:PRK08043 225 EDVNFtpdSYRKLLKKTLFVGRILEKYS-VEGERIGLMLPNATIS-----AAVIFGASLrrrIPA--MMNytagVKGLTS 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 115 RITHGEINAVIALEPFtveFEKIKeydaLTKFVIAGQKDGWISLEAEKEN--ASNKL-----------EMADTTRDDMAI 181
Cdd:PRK08043 297 AITAAEIKTIFTSRQF---LDKGK----LWHLPEQLTQVRWVYLEDLKDDvtTADKLwifahllmprlAQVKQQPEDAAL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 182 LSYTSGTTGNPKAVTHCHGWGFAHLQ-------MAPKhwlcineDDLVWATA---APGWQKWVWSPFLSvlgsGATAFVF 251
Cdd:PRK08043 370 ILFTSGSEGHPKGVVHSHKSLLANVEqiktiadFTPN-------DRFMSALPlfhSFGLTVGLFTPLLT----GAEVFLY 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 252 NgrfSPETYL---ELLQKYQINVLCCTPTEYRMMAKLQNlnDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQ 328
Cdd:PRK08043 439 P---SPLHYRivpELVYDRNCTVLFGTSTFLGNYARFAN--PYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGV 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 329 TESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVddegnSVPANTKGNiAVPLDLPALFKGYYK-------EPERTAKAQ-- 399
Cdd:PRK08043 514 TECAPVVSINVPMAAKPGTVGRILPGMDARLL-----SVPGIEQGG-RLQLKGPNIMNGYLRvekpgvlEVPTAENARge 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 400 --TGkYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVED-ALTNHPAvKECAVVAKPHDIRGnivKAFVIL-QD 475
Cdd:PRK08043 588 meRG-WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPD-KQHATAIKSDASKG---EALVLFtTD 662
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1441463764 476 HTAGDDTLVKELQQFVKNEVApykYPREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PRK08043 663 SELTREKLQQYAREHGVPELA---VPRDIRYLKQLPLLGSGKPDFVTLK 708
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
180-525 |
4.75e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 68.30 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 180 AILsYTSGTTGNPKAV--TH-------CHGWgfAHLQMAPKHWLCineddlvWATAApgwqKWVWSPFL--SVLGSGATA 248
Cdd:PLN03051 123 NIL-FSSGTTGEPKAIpwTHlsplrcaSDGW--AHMDIQPGDVVC-------WPTNL----GWMMGPWLlySAFLNGATL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 249 FVFNGrfSPET--YLELLQKYQINVLCCTPTEYRMMAK--LQNLNDYDLTHLHSAVSAGEPLNREvveqfkKYFNLTVRD 324
Cdd:PLN03051 189 ALYGG--APLGrgFGKFVQDAGVTVLGLVPSIVKAWRHtgAFAMEGLDWSKLRVFASTGEASAVD------DVLWLSSVR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 325 GY--------GQTEstLLIGFLKDT---PQRIGSMGKGIPGSSVTVVDDEGNSVPANTKGNIAVPLDLPAL--------- 384
Cdd:PLN03051 261 GYykpvieycGGTE--LASGYISSTllqPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVGEVALAPPMLgasdrllna 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 385 --FKGYYK-EPERTAKAQTGKYYitGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTN-HPAVKECAV--VAK 458
Cdd:PLN03051 339 dhDKVYYKgMPMYGSKGMPLRRH--GDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAvgVAP 416
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441463764 459 PH---DIRGNIVKAFVILQDHTAGD-DTLVKELQQFVKNEVAP-YKYPReIEFVDDLPKTNSGKIRRVELRD 525
Cdd:PLN03051 417 PDggpELLVIFLVLGEEKKGFDQARpEALQKKFQEAIQTNLNPlFKVSR-VKIVPELPRNASNKLLRRVLRD 487
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
50-416 |
7.40e-12 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 67.63 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 50 TYQQLIEQSNKVGNVLASHGL--SKGDKVLIMMPRS----IATYELYIAALklgvAIIPCSEMLRTKDLQYRITHGEINA 123
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRpewiISELACYAYSL----VTVPLYDTLGPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 124 VIALEPFTVefekikeydaltkfviagqkdgwISL-EAEKENASNKLEMADTTRDDMAILSYTSGTTGNPKAVTHCHGwG 202
Cdd:cd05927 83 VFCDAGVKV-----------------------YSLeEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHG-N 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 203 FAHLQMA----PKHWLCINEDDlvwataapgwqkwVWSPFL------------SVLGSGATAFVFNGrfSPETYLELLQK 266
Cdd:cd05927 139 IVSNVAGvfkiLEILNKINPTD-------------VYISYLplahifervveaLFLYHGAKIGFYSG--DIRLLLDDIKA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 267 YQINVLCCTPTEY-RMMAKLQN------------LN---DYDLTHLHSA---------------------------VSAG 303
Cdd:cd05927 204 LKPTVFPGVPRVLnRIYDKIFNkvqakgplkrklFNfalNYKLAELRSGvvraspfwdklvfnkikqalggnvrlmLTGS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 304 EPLNREVVEQFKKYFNLTVRDGYGQTESTlLIGFLKDtPQ--RIGSMGKGIPGSSVTVVDdegnsVP--------ANTKG 373
Cdd:cd05927 284 APLSPEVLEFLRVALGCPVLEGYGQTECT-AGATLTL-PGdtSVGHVGGPLPCAEVKLVD-----VPemnydakdPNPRG 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1441463764 374 NIAVplDLPALFKGYYKEPERTAKA--QTGkYYITGDLAHVDDDG 416
Cdd:cd05927 357 EVCI--RGPNVFSGYYKDPEKTAEAldEDG-WLHTGDIGEWLPNG 398
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
30-524 |
2.59e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.73 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 30 HIPDKKAILYHNTEGEDISV-TYQQLIEQSNKVGNVLASHGlSKGDKVLIMMPRSIATYELYIAALKLGVAIIPC--SEM 106
Cdd:PRK05691 21 QTPDRLALRFLADDPGEGVVlSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAypPES 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 107 LRTKDlQYRIThgeinAVIA-LEP---FTVE--FEKIKEYDALTkfviAGQKDGWISLEAEKENASNKLEMADTTRDDMA 180
Cdd:PRK05691 100 ARRHH-QERLL-----SIIAdAEPrllLTVAdlRDSLLQMEELA----AANAPELLCVDTLDPALAEAWQEPALQPDDIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 181 ILSYTSGTTGNPKAVTHCHGWGFAHLQMApKHWLCI--NEDDLVWAtaapgwqkwvWSPFLSVLG----------SGATA 248
Cdd:PRK05691 170 FLQYTSGSTALPKGVQVSHGNLVANEQLI-RHGFGIdlNPDDVIVS----------WLPLYHDMGliggllqpifSGVPC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 249 FVFNGRF---SPETYLELLQKYQINVLCCTPTEYRMMAKL---QNLNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTV 322
Cdd:PRK05691 239 VLMSPAYfleRPLRWLEAISEYGGTISGGPDFAYRLCSERvseSALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 323 RD------GYGQTESTLL---------IGFLK-------------DTPQRIGSMGKGIPGSSVTVVD-DEGNSVPANTKG 373
Cdd:PRK05691 319 FDpdsffaSYGLAEATLFvsggrrgqgIPALEldaealarnraepGTGSVLMSCGRSQPGHAVLIVDpQSLEVLGDNRVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 374 NIAVplDLPALFKGYYKEPERTAKA---QTGKYYI-TGDLAHVDDdGYFWFEGRRDDIIISSGYTIGPFEVEDALTNhpa 449
Cdd:PRK05691 399 EIWA--SGPSIAHGYWRNPEASAKTfveHDGRTWLrTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIEKTVER--- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 450 vkECAVVAKPHdirgniVKAFVILQDHTAG----------------DDTLVKELQQFVKNevAPYKYPREIEFVDD--LP 511
Cdd:PRK05691 473 --EVEVVRKGR------VAAFAVNHQGEEGigiaaeisrsvqkilpPQALIKSIRQAVAE--ACQEAPSVVLLLNPgaLP 542
|
570
....*....|...
gi 1441463764 512 KTNSGKIRRVELR 524
Cdd:PRK05691 543 KTSSGKLQRSACR 555
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
170-456 |
2.99e-11 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 65.91 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 170 EMADTTRDDMAILSYTSGTTGNPKAVTHCHG----WGFAHLQMAPKHwlciNEDDLVWATAAPgwqkWVWSPFLSVLGSG 245
Cdd:cd17641 151 EVAAGKGEDVAVLCTTSGTTGKPKLAMLSHGnflgHCAAYLAADPLG----PGDEYVSVLPLP----WIGEQMYSVGQAL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 246 ATAFVFNGRFSPETYLELLQKYQINVLCCTPTEY---------RMM---------------AKLQNLND----------- 290
Cdd:cd17641 223 VCGFIVNFPEEPETMMEDLREIGPTFVLLPPRVWegiaadvraRMMdatpfkrfmfelgmkLGLRALDRgkrgrpvslwl 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 291 ------------------YDLTHLHSAVSAGEPLNREVveqFKKYFNLTV--RDGYGQTESTLLIGFLKDTPQRIGSMGK 350
Cdd:cd17641 303 rlaswladallfrplrdrLGFSRLRSAATGGAALGPDT---FRFFHAIGVplKQLYGQTELAGAYTVHRDGDVDPDTVGV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 351 GIPGSSVTVvddegnsvpANTkGNIAVplDLPALFKGYYKEPERTAKAQTGKYYI-TGDLAHVDDDGYFWFEGRRDDI-I 428
Cdd:cd17641 380 PFPGTEVRI---------DEV-GEILV--RSPGVFVGYYKNPEATAEDFDEDGWLhTGDAGYFKENGHLVVIDRAKDVgT 447
|
330 340
....*....|....*....|....*...
gi 1441463764 429 ISSGYTIGPFEVEDALTNHPAVKEcAVV 456
Cdd:cd17641 448 TSDGTRFSPQFIENKLKFSPYIAE-AVV 474
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
185-522 |
4.60e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 58.62 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 185 TSGTTGNPKAVTHCH------GWGFAH-LQMAPkhwlcINEDDLVWATAAPGWqkwvWSPFLSV-LG---SGATAFVFNG 253
Cdd:COG1541 91 SSGTTGKPTVVGYTRkdldrwAELFARsLRAAG-----VRPGDRVQNAFGYGL----FTGGLGLhYGaerLGATVIPAGG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 254 rFSPETYLELLQKYQINVLCCTPTeY--RMMAKLQNLN-DYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTE 330
Cdd:COG1541 162 -GNTERQLRLMQDFGPTVLVGTPS-YllYLAEVAEEEGiDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 331 STLLIGFlkDTPQRigsmgKG--IPGSS--VTVVDDE-GNSVPANTKGNI--------AVPLdLpalfkgyykepeRtak 397
Cdd:COG1541 240 VGPGVAY--ECEAQ-----DGlhIWEDHflVEIIDPEtGEPVPEGEEGELvvttltkeAMPL-I------------R--- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 398 aqtgkyYITGDLAHVDDD------GYFWFE---GRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVK 468
Cdd:COG1541 297 ------YRTGDLTRLLPEpcpcgrTHPRIGrilGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELT 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441463764 469 AFVILqDHTAGDDTLVKELQQFVKNEVapyKYPREIEFV--DDLPKTNsGKIRRVE 522
Cdd:COG1541 371 VRVEL-APGASLEALAEAIAAALKAVL---GLRAEVELVepGSLPRSE-GKAKRVI 421
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
173-460 |
1.11e-08 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 57.61 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 173 DTTRDDMAILSYTSGTTGNPKAVTHCHG------WGFAHlqMAPKHwlcINEDDLVWAtaapgwqkwvWSPFLSVLGSGA 246
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGnlvagiAGLGD--RVPEL---LGPDDRYLA----------YLPLAHIFELAA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 247 TAFVF--NGRF---SPETYLEL--------LQKYQINVLCCTP----TEYR-MMAKLQNL-------------------- 288
Cdd:cd17639 149 ENVCLyrGGTIgygSPRTLTDKskrgckgdLTEFKPTLMVGVPaiwdTIRKgVLAKLNPMgglkrtlfwtayqsklkalk 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 289 NDYD--------------LT--HLHSAVSAGEPLNREVVEqFKKYFNLTVRDGYGQTEsTLLIGFLKDTPQ-RIGSMGKG 351
Cdd:cd17639 229 EGPGtplldelvfkkvraALggRLRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTE-TCAGGTVQDPGDlETGRVGPP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 352 IPGSSVTVVD-DEGNSVP--ANTKGNIAvpLDLPALFKGYYKEPERTAKAQTGK-YYITGDLAHVDDDGYFWFEGRRDDI 427
Cdd:cd17639 307 LPCCEIKLVDwEEGGYSTdkPPPRGEIL--IRGPNVFKGYYKNPEKTKEAFDGDgWFHTGDIGEFHPDGTLKIIDRKKDL 384
|
330 340 350
....*....|....*....|....*....|....
gi 1441463764 428 I-ISSGYTIGPFEVEDALTNHPAVKECAVVAKPH 460
Cdd:cd17639 385 VkLQNGEYIALEKLESIYRSNPLVNNICVYADPD 418
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
300-455 |
7.31e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 55.11 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 300 VSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIGFLKDTPQRIGSMGKGIPGSSVTVVD-------DEGNSVPantK 372
Cdd:PLN02736 382 SSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemnytSEDQPYP---R 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 373 GNIAVplDLPALFKGYYKEPERTAKAqtgkyyitgdlahVDDDGYF-------WFEGRRDDII--------ISSGYTIGP 437
Cdd:PLN02736 459 GEICV--RGPIIFKGYYKDEVQTREV-------------IDEDGWLhtgdiglWLPGGRLKIIdrkknifkLAQGEYIAP 523
|
170
....*....|....*...
gi 1441463764 438 FEVEDALTNHPAVKECAV 455
Cdd:PLN02736 524 EKIENVYAKCKFVAQCFV 541
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
32-539 |
1.92e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 53.72 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 32 PDKKAILYHntegeDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIMMPRSIATYELYIAALKLGVAIIPCSEMLRTKD 111
Cdd:PRK09029 17 PQAIALRLN-----DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 112 LQYRITHGEINAVIALEPFtvefekiKEYDALTkfviagqkdgwiSLEAEKENASNKLEMADttrDDMAILSYTSGTTGN 191
Cdd:PRK09029 92 LEELLPSLTLDFALVLEGE-------NTFSALT------------SLHLQLVEGAHAVAWQP---QRLATMTLTSGSTGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 192 PKAVTHCHGwgfAHLQMAPKhwLCinedDLVWATAAPGW-----------QK--WVWspflsvLGSGATaFVFNGrfsPE 258
Cdd:PRK09029 150 PKAAVHTAQ---AHLASAEG--VL----SLMPFTAQDSWllslplfhvsgQGivWRW------LYAGAT-LVVRD---KQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 259 TYLELLQKyqinvlcCT-----PTEyrmmakLQNLNDYDLTHL---H-----SAVSAgeplnrEVVEQFKKYfnlTVRD- 324
Cdd:PRK09029 211 PLEQALAG-------CThaslvPTQ------LWRLLDNRSEPLslkAvllggAAIPV------ELTEQAEQQ---GIRCw 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 325 -GYGQTE--STLligflkdTPQRI-GSMGKG--IPGSSVTVVDDE----GNSVpantkgniavpldlpALfkGYYKEPER 394
Cdd:PRK09029 269 cGYGLTEmaSTV-------CAKRAdGLAGVGspLPGREVKLVDGEiwlrGASL---------------AL--GYWRQGQL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 395 TakaqtgkyyitgDLahVDDDGyfWFE---------------GRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKP 459
Cdd:PRK09029 325 V------------PL--VNDEG--WFAtrdrgewqngeltilGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVA 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 460 HDIRGNIVKAFVILQDHTAgddtlVKELQQFVKNEVAPYKYPreIEFVdDLPKT--NSG-KIRRVELRDaeiekWQQQKD 536
Cdd:PRK09029 389 DAEFGQRPVAVVESDSEAA-----VVNLAEWLQDKLARFQQP--VAYY-LLPPElkNGGiKISRQALKE-----WVAQQL 455
|
...
gi 1441463764 537 SNQ 539
Cdd:PRK09029 456 GNN 458
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
177-524 |
2.08e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.82 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 177 DDMAILSYTSGTTGNPKAVTHCHGWGFAHL-QMAPKhwLCINEDDLVWaTAAPgwqkwVWSPFlsVLGSGATAFVFNG-- 253
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHRNLLANRaQVAAR--IDFSPEDKVF-NALP-----VFHSF--GLTGGLVLPLLSGvk 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 254 RF---SPETYL---ELLqkYQIN--VLCCTPT---EYRMMAklqnlNDYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTV 322
Cdd:PRK06814 863 VFlypSPLHYRiipELI--YDTNatILFGTDTflnGYARYA-----HPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRI 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 323 RDGYGQTESTLLIGFlkDTPQ--RIGSMGKGIPG-----SSVTVVDDEGN-SVpantKGniavpldlPALFKGYYK-EPE 393
Cdd:PRK06814 936 LEGYGVTETAPVIAL--NTPMhnKAGTVGRLLPGieyrlEPVPGIDEGGRlFV----RG--------PNVMLGYLRaENP 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 394 RTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHPAVKECAVVAKPHDIRGNIVKAFvil 473
Cdd:PRK06814 1002 GVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIILL--- 1078
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1441463764 474 qdhTAGDDTLVKELQQFVKNEVAPYKY-PREIEFVDDLPKTNSGKIRRVELR 524
Cdd:PRK06814 1079 ---TTASDATRAAFLAHAKAAGASELMvPAEIITIDEIPLLGTGKIDYVAVT 1127
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
26-523 |
2.91e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 53.02 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 26 EKYSHIPDKKAILY----HNTEGEDISVTYQQLIEQSNKVGNVLASHGlSKGDKVLIMMPRSIATYELYIAALKLGVAII 101
Cdd:PRK05850 9 ERASLQPDDAAFTFidyeQDPAGVAETLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 102 PCSEMlrtkdlQYRITHGEINAVIALEPFTVEFEKIKEYDALTKFVIAGQKDG---WISLEAEKENASNKLEMADTTRDD 178
Cdd:PRK05850 88 PLSVP------QGGAHDERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSappVIEVDLLDLDSPRGSDARPRDLPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 179 MAILSYTSGTTGNPKAVTHCHGWGFAHLQ------MAPKHwlcineddlvwATAAPGWQKWVWSPFLSVLG--SGATAFV 250
Cdd:PRK05850 162 TAYLQYTSGSTRTPAGVMVSHRNVIANFEqlmsdyFGDTG-----------GVPPPDTTVVSWLPFYHDMGlvLGVCAPI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 251 FNGR----FSPETYlelLQKyqinvlcctPTEY-RMMAKLQ---------------------NLNDYDLTHLHSAVSAGE 304
Cdd:PRK05850 231 LGGCpavlTSPVAF---LQR---------PARWmQLLASNPhafsaapnfafelavrktsddDMAGLDLGGVLGIISGSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 305 PLN----REVVEQFKKyFNL---TVRDGYGQTESTLLI---------------------GFLKDTPQRIGS--MGKGIPG 354
Cdd:PRK05850 299 RVHpatlKRFADRFAP-FNLretAIRPSYGLAEATVYVatrepgqppesvrfdyeklsaGHAKRCETGGGTplVSYGSPR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 355 SS-VTVVDDEGN-SVPANTKGNIAVPLDLPALfkGYYKEP---ERTAKAQ---------TGKYYITGDLAHVDDDGYFwF 420
Cdd:PRK05850 378 SPtVRIVDPDTCiECPAGTVGEIWVHGDNVAA--GYWQKPeetERTFGATlvdpspgtpEGPWLRTGDLGFISEGELF-I 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 421 EGRRDDIIISSGYTIGPFEVEdaltnhPAVKE-----CAVVAKPHDIRGNIVkafVILQDHTAGD-DTLVKELQQFVKNE 494
Cdd:PRK05850 455 VGRIKDLLIVDGRNHYPDDIE------ATIQEitggrVAAISVPDDGTEKLV---AIIELKKRGDsDEEAMDRLRTVKRE 525
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1441463764 495 V--APYKYPREIefVDDL--------PKTNSGKIRR---VEL 523
Cdd:PRK05850 526 VtsAISKSHGLS--VADLvlvapgsiPITTSGKIRRaacVEQ 565
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
174-416 |
3.93e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 49.59 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 174 TTRDDMAILSYTSGTTGNPKAVTHCHGWGFAHLqMAPKHWL-----CINEDDLVWAtaapgwqkwvWSPFLSVLGSGATA 248
Cdd:PTZ00216 261 ENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGI-LALEDRLndligPPEEDETYCS----------YLPLAHIMEFGVTN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 249 -FVFNGRF----SPETYLEL-------LQKYQINVLCCTPTEYRMMAK------------------------LQNLNDYD 292
Cdd:PTZ00216 330 iFLARGALigfgSPRTLTDTfarphgdLTEFRPVFLIGVPRIFDTIKKaveaklppvgslkrrvfdhayqsrLRALKEGK 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 293 LT-----------------HLHSAVSAGEPLNREVVEQFKKYFNLTVRdGYGQTEsTLLIGflkdTPQRIGSM-----GK 350
Cdd:PTZ00216 410 DTpywnekvfsapravlggRVRAMLSGGGPLSAATQEFVNVVFGMVIQ-GWGLTE-TVCCG----GIQRTGDLepnavGQ 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 351 GIPGSSVTVVDDEG---NSVPaNTKGNIAvpLDLPALFKGYYKEPERTAKAQT-GKYYITGDLAHVDDDG 416
Cdd:PTZ00216 484 LLKGVEMKLLDTEEykhTDTP-EPRGEIL--LRGPFLFKGYYKQEELTREVLDeDGWFHTGDVGSIAANG 550
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
25-472 |
6.02e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 45.78 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 25 IEKYSHIP--DKKAILyHNTEGEDISVTYQQLIEQSNKVGNVLASHGLSKGDKVLIM---MPRSIATYElyiAALKLGVA 99
Cdd:PLN02614 55 VEKYPNNPmlGRREIV-DGKPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYganSPEWIISME---ACNAHGLY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 100 IIPCSEMLRTKDLQYRITHGEINAVIalepftVEFEKIKEYDAL----TKFVIAGQKDGWISLEaEKENASN-------- 167
Cdd:PLN02614 131 CVPLYDTLGAGAVEFIISHSEVSIVF------VEEKKISELFKTcpnsTEYMKTVVSFGGVSRE-QKEEAETfglviyaw 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 168 ----------KLEMADTTRDDMAILSYTSGTTGNPKAVTHCHG------WGFAHLQMAPKHWLCINEDDLVWATAAPGWQ 231
Cdd:PLN02614 204 deflklgegkQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNEsivtliAGVIRLLKSANAALTVKDVYLSYLPLAHIFD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 232 KWVWSPFLSVlgSGATAFvfnGRFSPETYLELLQKYQINVLCCTPTEY-RMMAKLQN-LND--------------YDLTH 295
Cdd:PLN02614 284 RVIEECFIQH--GAAIGF---WRGDVKLLIEDLGELKPTIFCAVPRVLdRVYSGLQKkLSDggflkkfvfdsafsYKFGN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 296 L---HSAVSAGEPLNREVVEQFKKYFNLTVR--------------------------DGYGQTESTllIGFLKDTPQRIG 346
Cdd:PLN02614 359 MkkgQSHVEASPLCDKLVFNKVKQGLGGNVRiilsgaaplashvesflrvvacchvlQGYGLTESC--AGTFVSLPDELD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 347 SMGKgiPGSSVTVVDDEGNSVP--------ANTKGNIAVplDLPALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYF 418
Cdd:PLN02614 437 MLGT--VGPPVPNVDIRLESVPemeydalaSTPRGEICI--RGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSM 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1441463764 419 WFEGRRDDII-ISSGYTIGPFEVEDALTNHPAVKECAVVakphdirGNIVKAFVI 472
Cdd:PLN02614 513 KIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWVY-------GNSFESFLV 560
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
300-423 |
7.05e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 45.48 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 300 VSAGEPLNREVVEQFKKYFNLTVRDGYGQTESTLLIgFLKD-TPQRIGSMGKGI-PGSSVTVVDDE----GNSVPantKG 373
Cdd:PTZ00342 467 LNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPI-FVQHaDDNNTESIGGPIsPNTKYKVRTWEtykaTDTLP---KG 542
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1441463764 374 NIAVPLDlpALFKGYYKEPERTAKAQT-GKYYITGDLAHVDDDGYFWFEGR 423
Cdd:PTZ00342 543 ELLIKSD--SIFSGYFLEKEQTKNAFTeDGYFKTGDIVQINKNGSLTFLDR 591
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
256-451 |
8.33e-05 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 44.92 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 256 SPETYLELLQKYQINVLCCTPTEYRMMA-KLQNLN-DYDLTHLHSAVSAGEPLNREVVEQFKKYFNLTVRDGYGQTEstl 333
Cdd:cd05913 158 NTERQLQLIKDFGPTVLCCTPSYALYLAeEAEEEGiDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTE--- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 334 ligflkdtpqrIGSMGKGIPGSS------------VTVVDDE-GNSVPANTKGNI--------AVPL------DLPALfk 386
Cdd:cd05913 235 -----------IIGPGVAFECEEkdglhiwedhfiPEIIDPEtGEPVPPGEVGELvfttltkeAMPLiryrtrDITRL-- 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1441463764 387 gyykEPERTAKAQTgkyyitgdlaHVDDDGyfwFEGRRDDIIISSGYTIGPFEVEDALTNHPAVK 451
Cdd:cd05913 302 ----LPGPCPCGRT----------HRRIDR---ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLG 349
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
300-452 |
7.65e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 42.11 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 300 VSAGEPLNREVVEQFKKYFNLTVRDGYGQTEST--LLIGFlkdtPQRIGSMGK-GIPGSSVTV----VDDEG-NSVPANT 371
Cdd:PLN02430 389 ISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLgpTTLGF----PDEMCMLGTvGAPAVYNELrleeVPEMGyDPLGEPP 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441463764 372 KGNIAVPLDlpALFKGYYKEPERTAKAQTGKYYITGDLAHVDDDGYFWFEGRRDDII-ISSGYTIGPFEVEDALTNHPAV 450
Cdd:PLN02430 465 RGEICVRGK--CLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQNPIV 542
|
..
gi 1441463764 451 KE 452
Cdd:PLN02430 543 ED 544
|
|
| |
