|
Name |
Accession |
Description |
Interval |
E-value |
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
24-598 |
9.80e-129 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 391.00 E-value: 9.80e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 24 EMIERSASLYAeenafllkDPVALRELDprseaainfrinpDNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAE 103
Cdd:COG1022 15 DLLRRRAARFP--------DRVALREKE-------------DGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 104 TRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYS-RSQEDKLLGIADNIKQVKNLVSYDLPTENsskl 182
Cdd:COG1022 74 NRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELPSLRHIVVLDPRGLR---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 183 agEDKDLFFLWDLINTGNSIRANGntQYDNLP--IDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKND 260
Cdd:COG1022 150 --DDPRLLSLDELLALGREVADPA--ELEARRaaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 261 TLLSVLPLHHTFEATAGFLLpLSRGGKIAMNDGLRHIAKNLQQSKTSILIAVPLLLETLHKTILRKATGDAKVAKK-YKL 339
Cdd:COG1022 226 RTLSFLPLAHVFERTVSYYA-LAAGATVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKlFRW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 340 GLSLAKA-------------LNKIKLNFNDK-IFAEIHKGLGGHLRLLVCGGAAIEPQILADFNDWGITAIQGYGVTECS 405
Cdd:COG1022 305 ALAVGRRyararlagkspslLLRLKHALADKlVFSKLREALGGRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 406 PIISNNRPKYKEHASAGLPTPHVEVKIineDENGigEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFI 485
Cdd:COG1022 385 PVITVNRPGDNRIGTVGPPLPGVEVKI---AEDG--EILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 486 YITGRKANIIVTKNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYgeqiITAEVFPSVEELAKVLETNAKDIDT--SVLT 563
Cdd:COG1022 460 RITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRPF----LAALIVPDFEALGEWAEENGLPYTSyaELAQ 535
|
570 580 590
....*....|....*....|....*....|....*
gi 1360655949 564 GSVAEGLVKDAISKANKELQNFKKVKDIVLRAEPF 598
Cdd:COG1022 536 DPEVRALIQEEVDRANAGLSRAEQIKRFRLLPKEF 570
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
67-598 |
9.60e-106 |
|
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: 326.86 E-value: 9.60e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 67 EYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTI 146
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 147 FYSrsqedkllgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpiDPRALAVLLFT 226
Cdd:cd05907 82 FVE------------------------------------------------------------------DPDDLATIIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 227 SGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGLRHIAKNLQQSKT 306
Cdd:cd05907 96 SGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 307 SILIAVPLLLETLHKTILRKATGDAKvakkyklglslakalnkiklnfnDKIFAeihKGLGGHLRLLVCGGAAIEPQILA 386
Cdd:cd05907 176 TVFLAVPRVWEKVYAAIKVKAVPGLK-----------------------RKLFD---LAVGGRLRFAASGGAPLPAELLH 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 387 DFNDWGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIiNEDengiGEIIARGPNVMLGYYEDPEKTAEAID 466
Cdd:cd05907 230 FFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRI-ADD----GEILVRGPNVMLGYYKNPEATAEALD 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 467 SEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYgeqiITAEVFPSVEEL 546
Cdd:cd05907 305 ADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRPF----LVALIVPDPEAL 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1360655949 547 AKVLETN--AKDIDTSVLTGSVAEGLVKDAISKANKELQNFKKVKDIVLRAEPF 598
Cdd:cd05907 381 EAWAEEHgiAYTDVAELAANPAVRAEIEAAVEAANARLSRYEQIKKFLLLPEPF 434
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
71-608 |
4.82e-103 |
|
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: 320.16 E-value: 4.82e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSr 150
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 sqedkllgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpiDPRALAVLLFTSGTT 230
Cdd:cd05914 87 -----------------------------------------------------------------DEDDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 231 AKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIA-MNDGLRHIAKNLQQSKTSIL 309
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVfLDKIPSAKIIALAFAQVTPT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 310 IAVPLLLETLHKTIlrKATGDAKVAKKYKLglSLAKALNKIKlnFNDKIFAEIHKGLGGHLRLLVCGGAAIEPQILADFN 389
Cdd:cd05914 182 LGVPVPLVIEKIFK--MDIIPKLTLKKFKF--KLAKKINNRK--IRKLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLR 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 390 DWGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINED-ENGIGEIIARGPNVMLGYYEDPEKTAEAIDSE 468
Cdd:cd05914 256 TIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDpATGEGEIIVRGPNVMKGYYKNPEATAEAFDKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 469 GFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVLLK--ENIIEEVVVygerdEYGEQIITAEVFPsveEL 546
Cdd:cd05914 336 GWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNmpFVLESLVVV-----QEKKLVALAYIDP---DF 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1360655949 547 AKVLETNAKDIdtsvltgsvAEGLVKDAISKANKELQNFKKVKDIVLRAEPFPRNTSKKILR 608
Cdd:cd05914 408 LDVKALKQRNI---------IDAIKWEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGKIKR 460
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
67-610 |
2.37e-92 |
|
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: 292.10 E-value: 2.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 67 EYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTI 146
Cdd:COG0318 21 GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 147 FYsrsqedkllgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpidpralAVLLFT 226
Cdd:COG0318 101 VT------------------------------------------------------------------------ALILYT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 227 SGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGLR--HIAKNLQQS 304
Cdd:COG0318 109 SGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDpeRVLELIERE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 305 KTSILIAVPllleTLHKTILRKATgdakvAKKYKLGlslakalnkiklnfndkifaeihkglggHLRLLVCGGAAIEPQI 384
Cdd:COG0318 189 RVTVLFGVP----TMLARLLRHPE-----FARYDLS----------------------------SLRLVVSGGAPLPPEL 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 385 LADFND-WGITAIQGYGVTECSPIISNNRPKYKEH--ASAGLPTPHVEVKIINED-----ENGIGEIIARGPNVMLGYYE 456
Cdd:COG0318 232 LERFEErFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVDEDgrelpPGEVGEIVVRGPNVMKGYWN 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 457 DPEKTAEAIDsEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIIT 536
Cdd:COG0318 312 DPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVV 389
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1360655949 537 AEVFPSveelakvletnakdiDTSVLTgsvAEGLvkdaISKANKELQNFKKVKDIVLRAEpFPRNTSKKILRNK 610
Cdd:COG0318 390 AFVVLR---------------PGAELD---AEEL----RAFLRERLARYKVPRRVEFVDE-LPRTASGKIDRRA 440
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
65-498 |
7.02e-86 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 274.19 E-value: 7.02e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 65 DNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATV-CGlAIIAPMDKELPANEVENLINRSGA 143
Cdd:pfam00501 16 VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLkAG-AVYVPLNPRLPAEELAYILEDSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 144 NTIFYSRS-QEDKLLGIADNIKQVKNLVSYDLPTENSSKLAGEDKDLFFLWdlintgnsirangntQYDNLPIDPRALAV 222
Cdd:pfam00501 95 KVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVP---------------PPPPPPPDPDDLAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 223 LLFTSGTTAKSKAVMLCHDNL---CVNIYDVCLTV-EFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDG----- 293
Cdd:pfam00501 160 IIYTSGTTGKPKGVMLTHRNLvanVLSIKRVRPRGfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGfpald 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 294 LRHIAKNLQQSKTSILIAVPllleTLHKTILRKAtgdakvakkyklglslakalnkiklnfndkifaEIHKGLGGHLRLL 373
Cdd:pfam00501 240 PAALLELIERYKVTVLYGVP----TLLNMLLEAG---------------------------------APKRALLSSLRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 374 VCGGAAIEPQILADFNDWGITAI-QGYGVTECSPIISNNRPKYKEHA---SAGLPTPHVEVKIINEDENG------IGEI 443
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALvNGYGLTETTGVVTTPLPLDEDLRslgSVGRPLPGTEVKIVDDETGEpvppgePGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1360655949 444 IARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTK 498
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
61-608 |
1.20e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 266.28 E-value: 1.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 61 RINPDNEY-----RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVE 135
Cdd:PRK06187 17 RKHPDKEAvyfdgRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 136 NLINRSGANTIFYSRSQEDKLLGIADNIKQVKN-LVSYDLPTENSSKLAGEDKDLfflwdlintgnsiRANGNTQYDNLP 214
Cdd:PRK06187 97 YILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTvIVEGDGPAAPLAPEVGEYEEL-------------LAAASDTFDFPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 215 IDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLlPLSRGGKIAMNDGL 294
Cdd:PRK06187 164 IDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYL-ALMAGAKQVIPRRF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 295 --RHIAKNLQQSKTSILIAVPllletlhkTILRkatgdakvakkyklglSLAKALNKIKLNFNdkifaeihkglggHLRL 372
Cdd:PRK06187 243 dpENLLDLIETERVTFFFAVP--------TIWQ----------------MLLKAPRAYFVDFS-------------SLRL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 373 LVCGGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRP------KYKEHASAGLPTPHVEVKIINEDEN------- 438
Cdd:PRK06187 286 VIYGGAALPPALLREFKEkFGIDLVQGYGMTETSPVVSVLPPedqlpgQWTKRRSAGRPLPGVEARIVDDDGDelppdgg 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 439 GIGEIIARGPNVMLGYYEDPEKTAEAIDSeGFYHTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFPEEIEFVLLKENII 518
Cdd:PRK06187 366 EVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPAV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 519 EEVVVYGERDEYGEQIITAEVfpsveELAKVLETNAKDIDTSvLTGSVAeglvkdaiskankelqNFKKVKDIVLRAEpF 598
Cdd:PRK06187 444 AEVAVIGVPDEKWGERPVAVV-----VLKPGATLDAKELRAF-LRGRLA----------------KFKLPKRIAFVDE-L 500
|
570
....*....|
gi 1360655949 599 PRNTSKKILR 608
Cdd:PRK06187 501 PRTSVGKILK 510
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
71-608 |
3.82e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 262.15 E-value: 3.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSr 150
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVL- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 sqeDKLLGI----ADNIKQVKNLVSydLPTENSSklagEDKDLFFLWDlintgnSIRANGNTQYDNLPIDPRALAVLLFT 226
Cdd:PRK07656 110 ---GLFLGVdysaTTRLPALEHVVI--CETEEDD----PHTEKMKTFT------DFLAAGDPAERAPEVDPDDVADILFT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 227 SGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAM------NDGLRHIAKN 300
Cdd:PRK07656 175 SGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPlpvfdpDEVFRLIETE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 301 lqqsKTSILIAVPllleTLHKTILrkatgDAKVAKKYKLGlslakalnkiklnfndkifaeihkglggHLRLLVCGGAAI 380
Cdd:PRK07656 255 ----RITVLPGPP----TMYNSLL-----QHPDRSAEDLS----------------------------SLRLAVTGAASM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 381 EPQILADFND-WGI-TAIQGYGVTECSPIISNNRP--KYKEHA-SAGLPTPHVEVKIINEDENGI-----GEIIARGPNV 450
Cdd:PRK07656 294 PVALLERFESeLGVdIVLTGYGLSEASGVTTFNRLddDRKTVAgTIGTAIAGVENKIVNELGEEVpvgevGELLVRGPNV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 451 MLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKAN-IIVtkNGKNIFPEEIEFVLLKENIIEEVVVYGERDE 529
Cdd:PRK07656 374 MKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDmFIV--GGFNVYPAEVEEVLYEHPAVAEAAVIGVPDE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 530 -YGEQIItaevfpsveelAKVLETNAKDIDtsvltgsvAEGLvkdaISKANKELQNFKKVKDIVLRAEpFPRNTSKKILR 608
Cdd:PRK07656 452 rLGEVGK-----------AYVVLKPGAELT--------EEEL----IAYCREHLAKYKVPRSIEFLDE-LPKNATGKVLK 507
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
66-610 |
1.23e-75 |
|
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: 248.81 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 66 NEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANT 145
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 146 IFysrsqedkllgiadnikqvknlvsydlpTENSSKlagedkdlfflwdlintgnsirangntqydnlpidprALAVLLF 225
Cdd:cd17640 81 LV----------------------------VENDSD-------------------------------------DLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 226 TSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLpLSRGGKIAMNDgLRHIAKNLQQSK 305
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFI-FACGCSQAYTS-IRTLKDDLKRVK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 306 TSILIAVPLLLETLHKTIlrkatgDAKVAKKYKLGLSLAKALNkiklnfndkifaeihkgLGGHLRLLVCGGAAIEPQIL 385
Cdd:cd17640 174 PHYIVSVPRLWESLYSGI------QKQVSKSSPIKQFLFLFFL-----------------SGGIFKFGISGGGALPPHVD 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 386 ADFNDWGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDENGI------GEIIARGPNVMLGYYEDPE 459
Cdd:cd17640 231 TFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekGIVWVRGPQVMKGYYKNPE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 460 KTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVLLKENIIEEVVVYGErdeyGEQIITAEV 539
Cdd:cd17640 311 ATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQ----DQKRLGALI 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 540 FPSVEELAKVLETNAKDIDTSVLTGSVAEGL-------VKDAISKANKeLQNFKKVKDIVLRAEPFPRN---TSK-KILR 608
Cdd:cd17640 387 VPNFEELEKWAKESGVKLANDRSQLLASKKVlklykneIKDEISNRPG-FKSFEQIAPFALLEEPFIENgemTQTmKIKR 465
|
..
gi 1360655949 609 NK 610
Cdd:cd17640 466 NV 467
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
22-608 |
1.82e-74 |
|
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: 245.55 E-value: 1.82e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 22 LREMIERSASLYAEENAFLLKDpvalreldprseaainfrinpdneyRGITYRQVNEDRKALGSAMLDLGISKDDKVIIL 101
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMG-------------------------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALM 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 102 AETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSRSQEDKLlgiadnikqvknlvsydlptenssk 181
Cdd:cd05936 56 LPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAVSFTDLL------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 182 lagedkdlfflwdlintgnsirANGNTQYDNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEF--DKN 259
Cdd:cd05936 111 ----------------------AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDllEGD 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 260 DTLLSVLPLHHTFEATAGFLLPLSRGGKIAM--NDGLRHIAKNLQQSKTSILIAVPLLLETLhktilrkatgdAKVAKKY 337
Cdd:cd05936 169 DVVLAALPLFHVFGLTVALLLPLALGATIVLipRFRPIGVLKEIRKHRVTIFPGVPTMYIAL-----------LNAPEFK 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 338 KLGLSlakalnkiklnfndkifaeihkglggHLRLLVCGGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKYK 416
Cdd:cd05936 238 KRDFS--------------------------SLRLCISGGAPLPVEVAERFEElTGVPIVEGYGLTETSPVVAVNPLDGP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 417 EHA-SAGLPTPHVEVKIINEDEN----G-IGEIIARGPNVMLGYYEDPEKTAEAIDsEGFYHTGDYGYIDDRGFIYITGR 490
Cdd:cd05936 292 RKPgSIGIPLPGTEVKIVDDDGEelppGeVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDR 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 491 KANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAEVfpsveelakVLETNAKdidtsvLTgsvAEGL 570
Cdd:cd05936 371 KKDMIIV-GGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFV---------VLKEGAS------LT---EEEI 431
|
570 580 590
....*....|....*....|....*....|....*...
gi 1360655949 571 VKdaisKANKELQNFKKVKDIVLRAEpFPRNTSKKILR 608
Cdd:cd05936 432 IA----FCREQLAGYKVPRQVEFRDE-LPKSAVGKILR 464
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
67-598 |
9.00e-73 |
|
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: 243.28 E-value: 9.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 67 EYRGITYRQVNEDRKALGSAMLDLGI--SKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGAN 144
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 145 TIFysrsqedkllgIADNIKqvknlvsydlptenssklagedkdlFFLW-DLINTGnsiRANgntQYDNLPIDPRALAVL 223
Cdd:cd05927 82 IVF-----------CDAGVK-------------------------VYSLeEFEKLG---KKN---KVPPPPPKPEDLATI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 224 LFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVE----FDKNDTLLSVLPLHHTFEATAGFLLpLSRGGKIAMNDG-LRHIA 298
Cdd:cd05927 120 CYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEilnkINPTDVYISYLPLAHIFERVVEALF-LYHGAKIGFYSGdIRLLL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 299 KNLQQSKTSILIAVPLLLETLHKTILRKATGD-------AKVAKKYKLGlSLAKALNKIKLNFNDKIFAEIHKGLGGHLR 371
Cdd:cd05927 199 DDIKALKPTVFPGVPRVLNRIYDKIFNKVQAKgplkrklFNFALNYKLA-ELRSGVVRASPFWDKLVFNKIKQALGGNVR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 372 LLVCGGAAIEPQIL----ADFndwGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIIN--------EDENG 439
Cdd:cd05927 278 LMLTGSAPLSPEVLeflrVAL---GCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpemnydaKDPNP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 IGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVLLKENIIE 519
Cdd:cd05927 355 RGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 520 EVVVYGERDeygEQIITAEVFPSVEELAKVLETNAKDidtsvlTGSVAEGL----VKDAI-------SKANKeLQNFKKV 588
Cdd:cd05927 435 QIFVYGDSL---KSFLVAIVVPDPDVLKEWAASKGGG------TGSFEELCknpeVKKAIledlvrlGKENG-LKGFEQV 504
|
570
....*....|
gi 1360655949 589 KDIVLRAEPF 598
Cdd:cd05927 505 KAIHLEPEPF 514
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
220-607 |
1.80e-72 |
|
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: 236.41 E-value: 1.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 220 LAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEAtAGFLLPLSRGGKIAMNDGLR--HI 297
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGL-FGLLGALLAGGTVVLLPKFDpeAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 298 AKNLQQSKTSILIAVPLLLETLhktilrkatgdAKVAKKYKLGLSlakalnkiklnfndkifaeihkglggHLRLLVCGG 377
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARL-----------LKAPESAGYDLS--------------------------SLRALVSGG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 378 AAIEPQILADFNDW-GITAIQGYGVTECSPIISNNRPKYKEHA--SAGLPTPHVEVKIINED-----ENGIGEIIARGPN 449
Cdd:cd04433 124 APLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPDDDARKpgSVGRPVPGVEVRIVDPDggelpPGEIGELVVRGPS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 450 VMLGYYEDPEKTAEAiDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDE 529
Cdd:cd04433 204 VMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAVLLGHPGVAEAAVVGVPDP 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1360655949 530 YGEQIITAEVfpsveelakVLETNAkdidtsvltgSVAEGLVKDAISkanKELQNFKKVKDIVlRAEPFPRNTSKKIL 607
Cdd:cd04433 282 EWGERVVAVV---------VLRPGA----------DLDAEELRAHVR---ERLAPYKVPRRVV-FVDALPRTASGKID 336
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
71-531 |
5.18e-68 |
|
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: 229.02 E-value: 5.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATV-CGlAIIAPMDKELPANEVENLINRSGANTIF-- 147
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLfAG-GIFSAANPIYTADELAHQLKISKPKVIFtd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 148 ---YSRSQED-KLLGIADNIKQVKNLVSYDLPTENSSKLAGEDKDLFFLWDLINTGNSIrangntqydnlpidpralAVL 223
Cdd:cd05911 90 pdgLEKVKEAaKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDT------------------AAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 224 LFTSGTTAKSKAVMLCHDNLCVNIYDVCLTV--EFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDG-----LRH 296
Cdd:cd05911 152 LYSSGTTGLPKGVCLSHRNLIANLSQVQTFLygNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFdselfLDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 297 IAKNlqqsKTSILIAVPLLLETLHKTilrkatgdaKVAKKYKLGlslakalnkiklnfndkifaeihkglggHLRLLVCG 376
Cdd:cd05911 232 IEKY----KITFLYLVPPIAAALAKS---------PLLDKYDLS----------------------------SLRVILSG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 377 GAAIEPQILA----DFNDWGITaiQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINED------ENGIGEIIAR 446
Cdd:cd05911 271 GAPLSKELQEllakRFPNATIK--QGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDgkdslgPNEPGEICVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 447 GPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIvtK-NGKNIFPEEIEFVLLKENIIEEVVVYG 525
Cdd:cd05911 349 GPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELI--KyKGFQVAPAELEAVLLEHPGVADAAVIG 426
|
....*.
gi 1360655949 526 ERDEYG 531
Cdd:cd05911 427 IPDEVS 432
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
66-601 |
1.54e-63 |
|
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: 217.85 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 66 NEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANT 145
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 146 IFYSRSQEDkllgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpidpraLAVLLF 225
Cdd:cd17639 81 IFTDGKPDD-----------------------------------------------------------------LACIMY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 226 TSGTTAKSKAVMLCHDNLCVNIYDVCLTV--EFDKNDTLLSVLPLHHTFEATAGFLLpLSRGGKIA-------MNDGLRH 296
Cdd:cd17639 96 TSGSTGNPKGVMLTHGNLVAGIAGLGDRVpeLLGPDDRYLAYLPLAHIFELAAENVC-LYRGGTIGygsprtlTDKSKRG 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 297 IAKNLQQSKTSILIAVPLLLETLHKTILRKATGDAKVAKK-YKLGLSL-AKALNKIKLN--FNDKIFAEIHKGLGGHLRL 372
Cdd:cd17639 175 CKGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTlFWTAYQSkLKALKEGPGTplLDELVFKKVRAALGGRLRY 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 373 LVCGGAAIEPQILADFNDWGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDENGI--------GEII 444
Cdd:cd17639 255 MLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYstdkppprGEIL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 445 ARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVLLKENIIEEVVVY 524
Cdd:cd17639 335 IRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVY 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 525 GERDEYgeqIITAEVFPSVEELAKVLETNAKDIDT--SVLTGSVAEGLVKDAISKANKE--LQNFKKVKDIVLRAEPF-P 599
Cdd:cd17639 415 ADPDKS---YPVAIVVPNEKHLTKLAEKHGVINSEweELCEDKKLQKAVLKSLAETARAagLEKFEIPQGVVLLDEEWtP 491
|
..
gi 1360655949 600 RN 601
Cdd:cd17639 492 EN 493
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
69-608 |
1.72e-63 |
|
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: 215.55 E-value: 1.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFy 148
Cdd:cd17631 19 RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 149 srsqedkllgiadnikqvknlvsydlptenssklagEDkdlfflwdlintgnsirangntqydnlpidpraLAVLLFTSG 228
Cdd:cd17631 98 ------------------------------------DD---------------------------------LALLMYTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 229 TTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGLR--HIAKNLQQSKT 306
Cdd:cd17631 109 TTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDpeTVLDLIERHRV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 307 SILIAVPllleTLHKTILRKATgdakvAKKYKLGlslakalnkiklnfndkifaeihkglggHLRLLVCGGAAIEPQILA 386
Cdd:cd17631 189 TSFFLVP----TMIQALLQHPR-----FATTDLS----------------------------SLRAVIYGGAPMPERLLR 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 387 DFNDWGITAIQGYGVTECSPIISNNRPKykEH----ASAGLPTPHVEVKIINEDEN-----GIGEIIARGPNVMLGYYED 457
Cdd:cd17631 232 ALQARGVKFVQGYGMTETSPGVTFLSPE--DHrrklGSAGRPVFFVEVRIVDPDGRevppgEVGEIVVRGPHVMAGYWNR 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 458 PEKTAEAIDsEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEY-GEQIIT 536
Cdd:cd17631 310 PEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwGEAVVA 387
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1360655949 537 AEVfpsVEELAKVLETnakdidtsvltgsvaeglvkDAISKANKELQNFKKVKDIVLRAEpFPRNTSKKILR 608
Cdd:cd17631 388 VVV---PRPGAELDED--------------------ELIAHCRERLARYKIPKSVEFVDA-LPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
71-610 |
1.31e-60 |
|
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: 209.48 E-value: 1.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIfysr 150
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 sqedkLLGIADNIKQVKNLVSYDLPTENsskLAGEDKDLFFLWDLINTGNSIRANGNTQYDNLPiDPRALAVLLFTSGTT 230
Cdd:cd05926 91 -----LTPKGELGPASRAASKLGLAILE---LALDVGVLIRAPSAESLSNLLADKKNAKSEGVP-LPDDLALILHTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 231 AKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGLRHIA--KNLQQSKTSI 308
Cdd:cd05926 162 GRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTfwPDVRDYNATW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 309 LIAVPllleTLHKTILRKATGDAKVAKkyklglslakalnkiklnfndkifaeihkglgGHLRLLVCGGAAIEPQILADF 388
Cdd:cd05926 242 YTAVP----TIHQILLNRPEPNPESPP--------------------------------PKLRFIRSCSASLPPAVLEAL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 389 ND-WGITAIQGYGVTE-CSPIISNNRPKYKEHA-SAGLPTpHVEVKIINED----ENG-IGEIIARGPNVMLGYYEDPEK 460
Cdd:cd05926 286 EAtFGAPVLEAYGMTEaAHQMTSNPLPPGPRKPgSVGKPV-GVEVRILDEDgeilPPGvVGEICLRGPNVTRGYLNNPEA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 461 TAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIvTKNGKNIFPEEIEFVLLKENIIEEVVVYGERDE-YGEQiITAEV 539
Cdd:cd05926 365 NAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI-NRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEkYGEE-VAAAV 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1360655949 540 FPsvEELAKVLEtnakdidtsvltgsvaeglvKDAISKANKELQNFKKVKDIVLRAEpFPRNTSKKILRNK 610
Cdd:cd05926 443 VL--REGASVTE--------------------EELRAFCRKHLAAFKVPKKVYFVDE-LPKTATGKIQRRK 490
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
65-536 |
2.60e-59 |
|
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: 208.37 E-value: 2.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 65 DNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGAN 144
Cdd:cd05933 3 GDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 145 TIFY-SRSQEDKLLGIADNIKQVKNLVSYDLPTEnssklagEDKDLFFLWD-LINTGNSIranGNTQYDNL--PIDPRAL 220
Cdd:cd05933 83 ILVVeNQKQLQKILQIQDKLPHLKAIIQYKEPLK-------EKEPNLYSWDeFMELGRSI---PDEQLDAIisSQKPNQC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 221 AVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEF----DKNDTLLSVLPLHHTFEATAGFLLPLSRGGKI--AMNDGL 294
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLrpatVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVyfAQPDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 295 R-HIAKNLQQSKTSILIAVPLLLETLH---KTILRKATGDAKV----AKKYKLGLSLAKALNKIK--LNF---NDKIFAE 361
Cdd:cd05933 233 KgTLVKTLREVRPTAFMGVPRVWEKIQekmKAVGAKSGTLKRKiaswAKGVGLETNLKLMGGESPspLFYrlaKKLVFKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 362 IHKGLG-GHLRLLVCGGAAIEPQILADFNDWGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDENGI 440
Cdd:cd05933 313 VRKALGlDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 441 GEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVLLKE-NIIE 519
Cdd:cd05933 393 GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKElPIIS 472
|
490
....*....|....*..
gi 1360655949 520 EVVVYGERDEYGEQIIT 536
Cdd:cd05933 473 NAMLIGDKRKFLSMLLT 489
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
65-598 |
1.17e-57 |
|
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: 201.93 E-value: 1.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 65 DNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGAN 144
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 145 TIFysrsqedklLGIADNIKQVKNLVSYDLPTENSSKL-AGEDkdlFFLWDlintgnSIRANGNTQYDNLPIDPRALAVL 223
Cdd:cd05932 81 ALF---------VGKLDDWKAMAPGVPEGLISISLPPPsAANC---QYQWD------DLIAQHPPLEERPTRFPEQLATL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 224 LFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGLRHIAKNLQQ 303
Cdd:cd05932 143 IYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 304 SKTSILIAVPLLLETLHKTILRKAtgdakvaKKYKLGLSLakalnKIKLnFNDKIFAEIHKGLG-GHLRLLVCGGAAIEP 382
Cdd:cd05932 223 ARPTLFFSVPRLWTKFQQGVQDKI-------PQQKLNLLL-----KIPV-VNSLVKRKVLKGLGlDQCRLAGCGSAPVPP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 383 QILADFNDWGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEdengiGEIIARGPNVMLGYYEDPEKTA 462
Cdd:cd05932 290 ALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSPALMMGYYKDPEATA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 463 EAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVLLKENIIEEVVVYGErdeyGEQIITAEVFPS 542
Cdd:cd05932 365 EAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGS----GLPAPLALVVLS 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1360655949 543 VEELAKVLETNAKDIDTSvltgsvaeglVKDAISKANKELQNFKKVKDIVLRAEPF 598
Cdd:cd05932 441 EEARLRADAFARAELEAS----------LRAHLARVNSTLDSHEQLAGIVVVKDPW 486
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
65-552 |
9.23e-53 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 189.57 E-value: 9.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 65 DNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGAN 144
Cdd:PRK06087 44 DNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 145 -----TIFYSRSQEDKLLGIADNIKQVKNLVSYDlptenssKLAGEDKDLfflwdlinTGNSIRANGNTQYDNLPIDPRA 219
Cdd:PRK06087 124 mffapTLFKQTRPVDLILPLQNQLPQLQQIVGVD-------KLAPATSSL--------SLSQIIADYEPLTTAITTHGDE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 220 LAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHtfeATaGFL----LPLSRGGKIAMNDGLR 295
Cdd:PRK06087 189 LAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGH---AT-GFLhgvtAPFLIGARSVLLDIFT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 296 --HIAKNLQQSK-TSILIAVPLLLETLhkTILRKATGDakvakkyklgLSlakalnkiklnfndkifaeihkglggHLRL 372
Cdd:PRK06087 265 pdACLALLEQQRcTCMLGATPFIYDLL--NLLEKQPAD----------LS--------------------------ALRF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 373 LVCGGAAIEPQILADFNDWGITAIQGYGVTECSP--IISNNRPKYKEHASAGLPTPHVEVKIINEDENGI-----GEIIA 445
Cdd:PRK06087 307 FLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPhaVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLppgceGEEAS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 446 RGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVtKNGKNIFPEEIEFVLLKENIIEEVVVYG 525
Cdd:PRK06087 387 RGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIV-RGGENISSREVEDILLQHPKIHDACVVA 465
|
490 500 510
....*....|....*....|....*....|....
gi 1360655949 526 ERDE-YGEQIITAEVF------PSVEELAKVLET 552
Cdd:PRK06087 466 MPDErLGERSCAYVVLkaphhsLTLEEVVAFFSR 499
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
61-598 |
1.48e-51 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 188.38 E-value: 1.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 61 RINPDN---EYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENL 137
Cdd:PLN02736 66 RIRVDGtvgEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 138 INRSGANTIFYSRSQEDKLLGIADNIKQVKNLVSYDLPTENSSKL-AGEDKDLFFLWDLINTGNSirangnTQYDNLPID 216
Cdd:PLN02736 146 VNHAEVAAIFCVPQTLNTLLSCLSEIPSVRLIVVVGGADEPLPSLpSGTGVEIVTYSKLLAQGRS------SPQPFRPPK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 217 PRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEaTAGFLLPLSRGGKIAMNDG-LR 295
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYE-RVNQIVMLHYGVAVGFYQGdNL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 296 HIAKNLQQSKTSILIAVPLLLETLHKTILR--KATGD--------AKVAKKYKL--GLSLAKALNKIklnfndkIFAEIH 363
Cdd:PLN02736 299 KLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGlkerlfnaAYNAKKQALenGKNPSPMWDRL-------VFNKIK 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 364 KGLGGHLRLLVCGGAAIEPQILaDFND--WGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDENGI- 440
Cdd:PLN02736 372 AKLGGRVRFMSSGASPLSPDVM-EFLRicFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYt 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 441 --------GEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVL 512
Cdd:PLN02736 451 sedqpyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVY 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 513 LKENIIEEVVVYGerDEYGEQIItAEVFPSVEEL---AKVLETNAKDI-----DTSVLTGSVAEglvKDAISKANKeLQN 584
Cdd:PLN02736 531 AKCKFVAQCFVYG--DSLNSSLV-AVVVVDPEVLkawAASEGIKYEDLkqlcnDPRVRAAVLAD---MDAVGREAQ-LRG 603
|
570
....*....|....
gi 1360655949 585 FKKVKDIVLRAEPF 598
Cdd:PLN02736 604 FEFAKAVTLVPEPF 617
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
225-534 |
2.25e-51 |
|
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: 180.55 E-value: 2.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 225 FTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGLRHIAKNL--- 301
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSFDPLAVLeai 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 302 QQSKTSILIAVPLLLETLhktilrkatgdakvakkyklglslakaLNKIKLNFNDKifaeihkglgGHLRLLVCGGAAIE 381
Cdd:cd05917 89 EKEKCTALHGVPTMFIAE---------------------------LEHPDFDKFDL----------SSLRTGIMAGAPCP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 382 PQILAD-FNDWGITAIQ-GYGVTECSPIISNNRPK---YKEHASAGLPTPHVEVKIINEdENGI-------GEIIARGPN 449
Cdd:cd05917 132 PELMKRvIEVMNMKDVTiAYGMTETSPVSTQTRTDdsiEKRVNTVGRIMPHTEAKIVDP-EGGIvppvgvpGELCIRGYS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 450 VMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVtKNGKNIFPEEIEFVLLKENIIEEVVVYGERDE 529
Cdd:cd05917 211 VMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMII-RGGENIYPREIEEFLHTHPKVSDVQVVGVPDE 289
|
....*.
gi 1360655949 530 -YGEQI 534
Cdd:cd05917 290 rYGEEV 295
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
68-530 |
2.30e-50 |
|
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: 183.39 E-value: 2.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 68 YRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLAT-VCGlAIIAPMDKELPANEVENLINRSGANTI 146
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAqAIG-ALSLGIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 147 FYS-RSQEDKLLGIADNIKQVKNLVSYDlpTENSSKLagEDKDLFFLWDLINTGNSIRANGNTQYDNL--PIDPRALAVL 223
Cdd:cd17641 88 IAEdEEQVDKLLEIADRIPSVRYVIYCD--PRGMRKY--DDPRLISFEDVVALGRALDRRDPGLYEREvaAGKGEDVAVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 224 LFTSGTTAKSKAVMLCHDNL---CVNIydvcltVEFD---KNDTLLSVLPLHHTFEATAGFLLPLSRGGKI--------A 289
Cdd:cd17641 164 CTTSGTTGKPKLAMLSHGNFlghCAAY------LAADplgPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVnfpeepetM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 290 MNDgLRHIAKNlqqsktsILIAVPLLLETLHKTILRKATgDAKVAKK--YKLGLSLA-KALNKIKLNFNDKIFAEIHKGL 366
Cdd:cd17641 238 MED-LREIGPT-------FVLLPPRVWEGIAADVRARMM-DATPFKRfmFELGMKLGlRALDRGKRGRPVSLWLRLASWL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 367 G--------------GHLRLLVCGGAAIEPQILADFNDWGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKI 432
Cdd:cd17641 309 AdallfrplrdrlgfSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 433 INEdengiGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVL 512
Cdd:cd17641 389 DEV-----GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKL 463
|
490
....*....|....*...
gi 1360655949 513 LKENIIEEVVVYGERDEY 530
Cdd:cd17641 464 KFSPYIAEAVVLGAGRPY 481
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
220-609 |
5.80e-50 |
|
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: 179.41 E-value: 5.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 220 LAVLLFTSGTTAKSKAVMLCHDNLCVNIydVCLTV--EFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMN---DGL 294
Cdd:cd05941 91 PALILYTSGTTGRPKGVVLTHANLAANV--RALVDawRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLpkfDPK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 295 RHIAKNLQQSKTsILIAVPllletlhkTILrkatgdAKVAKKYklglslakalnkiklNFNDKIFAEIHKGLGGHLRLLV 374
Cdd:cd05941 169 EVAISRLMPSIT-VFMGVP--------TIY------TRLLQYY---------------EAHFTDPQFARAAAAERLRLMV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 375 CGGAAIEPQILADFndwgiTAIQG------YGVTECSPIISNnRPKYKEHA-SAGLPTPHVEVKIINE------DENGIG 441
Cdd:cd05941 219 SGSAALPVPTLEEW-----EAITGhtllerYGMTEIGMALSN-PLDGERRPgTVGMPLPGVQARIVDEetgeplPRGEVG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 442 EIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVLLKENIIEEV 521
Cdd:cd05941 293 EIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSEC 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 522 VVYGERD-EYGEqIITAEVFPSVEELAKVLEtnakdidtsvltgsvaeglvkDAISKANKELQNFKKVKDIVLrAEPFPR 600
Cdd:cd05941 373 AVIGVPDpDWGE-RVVAVVVLRAGAAALSLE---------------------ELKEWAKQRLAPYKRPRRLIL-VDELPR 429
|
....*....
gi 1360655949 601 NTSKKILRN 609
Cdd:cd05941 430 NAMGKVNKK 438
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
69-608 |
1.15e-49 |
|
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: 180.12 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFY 148
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 149 SRSQEDKLLGIADNIkqvknLVSYDLPTEnsskLAGEDKDLFflwdlintgnsirANGNTQYDNLPIDPRALAVLLFTSG 228
Cdd:cd05904 111 TAELAEKLASLALPV-----VLLDSAEFD----SLSFSDLLF-------------EADEAEPPVVVIKQDDVAALLYSSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 229 TTAKSKAVMLCHDNLcvnIYDVCLTV-----EFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKI-AMND-GLRHIAKNL 301
Cdd:cd05904 169 TTGRSKGVMLTHRNL---IAMVAQFVagegsNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVvVMPRfDLEELLAAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 302 QQSKTSILIAVPLLLetlhktilrkatgdakvakkyklgLSLAKALNKIKLNFndkifaeihkglgGHLRLLVCGGAAIE 381
Cdd:cd05904 246 ERYKVTHLPVVPPIV------------------------LALVKSPIVDKYDL-------------SSLRQIMSGAAPLG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 382 PQILADF--NDWGITAIQGYGVTECSPIIS------NNRPKYkehASAGLPTPHVEVKIINEDENGI------GEIIARG 447
Cdd:cd05904 289 KELIEAFraKFPNVDLGQGYGMTESTGVVAmcfapeKDRAKY---GSVGRLVPNVEAKIVDPETGESlppnqtGELWIRG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 448 PNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFPEEIEFVLLKENIIEEVVVYGER 527
Cdd:cd05904 366 PSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYK-GFQVAPAELEALLLSHPEILDAAVIPYP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 528 DEYGEQIITAEVFPSVEelakvletnakdidtSVLTgsvaEGLVKDAISkanKELQNFKKVKDIVLrAEPFPRNTSKKIL 607
Cdd:cd05904 445 DEEAGEVPMAFVVRKPG---------------SSLT----EDEIMDFVA---KQVAPYKKVRKVAF-VDAIPKSPSGKIL 501
|
.
gi 1360655949 608 R 608
Cdd:cd05904 502 R 502
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
214-490 |
1.27e-49 |
|
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: 179.45 E-value: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 214 PIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMN-D 292
Cdd:cd05909 143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 293 GL--RHIAKNLQQSKTSILIAVPLLLetlhktilrkaTGDAKVAKKYKLGlslakalnkiklnfndkifaeihkglggHL 370
Cdd:cd05909 223 PLdyKKIPELIYDKKATILLGTPTFL-----------RGYARAAHPEDFS----------------------------SL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 371 RLLVCGGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKY-KEHASAGLPTPHVEVKIINED---ENGIGE--- 442
Cdd:cd05909 264 RLVVAGAEKLKDTLRQEFQEkFGIRILEGYGTTECSPVISVNTPQSpNKEGTVGRPLPGMEVKIVSVEtheEVPIGEggl 343
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1360655949 443 IIARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGR 490
Cdd:cd05909 344 LLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGR 390
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
72-535 |
4.80e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 176.89 E-value: 4.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFY--- 148
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICada 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 149 --SRSQEDKLLGIADNIK--QVKNLVSYDLPT-ENSSKLAGEDKDLFFLW-DLINTGNSI-RANGNTQYDNL-PIDPRAL 220
Cdd:PRK12583 127 fkTSDYHAMLQELLPGLAegQPGALACERLPElRGVVSLAPAPPPGFLAWhELQARGETVsREALAERQASLdRDDPINI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 221 avlLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAM-NDGLRHIA- 298
Cdd:PRK12583 207 ---QYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYpNEAFDPLAt 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 299 -KNLQQSKTSILIAVPLL--------------LETLHKTILRKATGDAKVAKKyklglslakalnkiklnfndkIFAEIH 363
Cdd:PRK12583 284 lQAVEEERCTALYGVPTMfiaeldhpqrgnfdLSSLRTGIMAGAPCPIEVMRR---------------------VMDEMH 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 364 KGlgghlrllvcggaaiEPQIladfndwgitaiqGYGVTECSPII---SNNRPKYKEHASAGLPTPHVEVKIINEDEN-- 438
Cdd:PRK12583 343 MA---------------EVQI-------------AYGMTETSPVSlqtTAADDLERRVETVGRTQPHLEVKVVDPDGAtv 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 439 ---GIGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVtKNGKNIFPEEIEFVLLKE 515
Cdd:PRK12583 395 prgEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMII-RGGENIYPREIEEFLFTH 473
|
490 500
....*....|....*....|.
gi 1360655949 516 NIIEEVVVYGERDE-YGEQII 535
Cdd:PRK12583 474 PAVADVQVFGVPDEkYGEEIV 494
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
72-608 |
4.84e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 167.80 E-value: 4.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYsrs 151
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 152 qEDKLLGIADnikqvknlvsydlptenssKLAGEDKDLFFLWDLINTG----------NSIRANGNTQYDNLPIDPRALA 221
Cdd:PRK08316 115 -DPALAPTAE-------------------AALALLPVDTLILSLVLGGreapggwldfADWAEAGSVAEPDVELADDDLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 222 VLLFTSGTTAKSKAVMLCHDNLcVNIYDVCL-TVEFDKNDTLLSVLPLHHTfeatAG---FLLP-LSRGGkiamndglrh 296
Cdd:PRK08316 175 QILYTSGTESLPKGAMLTHRAL-IAEYVSCIvAGDMSADDIPLHALPLYHC----AQldvFLGPyLYVGA---------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 297 iaknlqqskTSILIAVP---LLLETLHK--------------TILRKATGDakvakKYKLGlSLAKAlnkiklnfndkif 359
Cdd:PRK08316 240 ---------TNVILDAPdpeLILRTIEAeritsffapptvwiSLLRHPDFD-----TRDLS-SLRKG------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 360 aeihkglgghlrllvCGGAAIEP-QILADFNDW--GITAIQGYGVTECSPIISNNRPKykEH----ASAGLPTPHVEVKI 432
Cdd:PRK08316 292 ---------------YYGASIMPvEVLKELRERlpGLRFYNCYGQTEIAPLATVLGPE--EHlrrpGSAGRPVLNVETRV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 433 INEDENGI-----GEIIARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEE 507
Cdd:PRK08316 355 VDDDGNDVapgevGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKT-GGENVASRE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 508 IEFVLLKENIIEEVVVYGERDEYGEQIITAEVFPSVEElakvletnakdidtsvltgSVAEglvKDAISKANKELQNFKK 587
Cdd:PRK08316 433 VEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGA-------------------TVTE---DELIAHCRARLAGFKV 490
|
570 580
....*....|....*....|.
gi 1360655949 588 VKDIVLrAEPFPRNTSKKILR 608
Cdd:PRK08316 491 PKRVIF-VDELPRNPSGKILK 510
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
64-534 |
7.20e-45 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 167.68 E-value: 7.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 64 PDNEY-----RGI--TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLAT-------VCglaiIAPMDKel 129
Cdd:PRK08315 30 PDREAlvyrdQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATakigailVT----INPAYR-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 130 pANEVENLINRSGANTIFYSRSQEDK-----LLGIADNIK--QVKNLVSYDLPT-ENSSKLAGEDKDLFFLWDlintgnS 201
Cdd:PRK08315 104 -LSELEYALNQSGCKALIAADGFKDSdyvamLYELAPELAtcEPGQLQSARLPElRRVIFLGDEKHPGMLNFD------E 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 202 IRANGnTQYDNLPIDPRALAV-------LLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEA 274
Cdd:PRK08315 177 LLALG-RAVDDAELAARQATLdpddpinIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 275 TAGFLLPLSRGGK-IAMNDG------LRHIaknlQQSKTSILIAVPllleTLHKTILrkatgdakvakkyklglslakal 347
Cdd:PRK08315 256 VLGNLACVTHGATmVYPGEGfdplatLAAV----EEERCTALYGVP----TMFIAEL----------------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 348 nkiklnfNDKIFAEIHkgLGgHLRLLVCGGAA--IE--PQILADFNDWGITaIqGYGVTECSPIISNNR---PKYKEHAS 420
Cdd:PRK08315 305 -------DHPDFARFD--LS-SLRTGIMAGSPcpIEvmKRVIDKMHMSEVT-I-AYGMTETSPVSTQTRtddPLEKRVTT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 421 AGLPTPHVEVKIINEDENGI------GEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGR-KAN 493
Cdd:PRK08315 373 VGRALPHLEVKIVDPETGETvprgeqGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRiKDM 452
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1360655949 494 IIvtKNGKNIFPEEIEFVLLKENIIEEVVVYGERDE-YGEQI 534
Cdd:PRK08315 453 II--RGGENIYPREIEEFLYTHPKIQDVQVVGVPDEkYGEEV 492
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
71-553 |
2.46e-44 |
|
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: 163.23 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFysr 150
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 sqedkllgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpIDPralAVLLFTSGTT 230
Cdd:cd05934 81 ----------------------------------------------------------------VDP---ASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 231 AKSKAVMLCHDNLC-VNIYDVCLTVeFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDglRHIAKN----LQQSK 305
Cdd:cd05934 94 GPPKGVVITHANLTfAGYYSARRFG-LGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP--RFSASRfwsdVRRYG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 306 TSILIAVPLLLETLHKTILRKatgdakvakkyklglslakalnkiklnfNDKifaeihkglggHLRLLVCGGAAIEPQIL 385
Cdd:cd05934 171 ATVTNYLGAMLSYLLAQPPSP----------------------------DDR-----------AHRLRAAYGAPNPPELH 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 386 ADFND-WGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINED----ENG-IGEII---ARGPNVMLGYYE 456
Cdd:cd05934 212 EEFEErFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDgqelPAGePGELVirgLRGWGFFKGYYN 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 457 DPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIvTKNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIIT 536
Cdd:cd05934 292 MPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMI-RRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVK 369
|
490 500
....*....|....*....|...
gi 1360655949 537 AEVF------PSVEELAKVLETN 553
Cdd:cd05934 370 AVVVlrpgetLDPEELFAFCEGQ 392
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
163-614 |
3.24e-44 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 166.00 E-value: 3.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 163 IKQVKNLV-SYDLPtenssklagedkdlfflwDLINTGNSIRANGNTQYDNLPIDPRALAVLLFTSGTTAKSKAVMLCHD 241
Cdd:PRK08974 168 VKYIKRLVpKYHLP------------------DAISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 242 NLCVN------IYDVCLTvefDKNDTLLSVLPLHHTFEATAGFLLPLSRGGkiamndglrhiaknlqqskTSILIAVPll 315
Cdd:PRK08974 230 NMLANleqakaAYGPLLH---PGKELVVTALPLYHIFALTVNCLLFIELGG-------------------QNLLITNP-- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 316 letlhktilRKATGDAKVAKKYKLglslaKALNKIKLNFNDKIFAEIHKGLG-GHLRLLVCGGAAIEpQILADfnDW--- 391
Cdd:PRK08974 286 ---------RDIPGFVKELKKYPF-----TAITGVNTLFNALLNNEEFQELDfSSLKLSVGGGMAVQ-QAVAE--RWvkl 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 392 -GITAIQGYGVTECSPIISNNRPKYKEH-ASAGLPTPHVEVKIINEDENGI-----GEIIARGPNVMLGYYEDPEKTAEA 464
Cdd:PRK08974 349 tGQYLLEGYGLTECSPLVSVNPYDLDYYsGSIGLPVPSTEIKLVDDDGNEVppgepGELWVKGPQVMLGYWQRPEATDEV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 465 IdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEygeqiitaevfpSVE 544
Cdd:PRK08974 429 I-KDGWLATGDIAVMDEEGFLRIVDRKKDMILV-SGFNVYPNEIEDVVMLHPKVLEVAAVGVPSE------------VSG 494
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1360655949 545 ELAKVLETnAKDidtsvltgsvaEGLVKDAISK-ANKELQNFKKVKDIVLRAEpFPRNTSKKILRnKEQRN 614
Cdd:PRK08974 495 EAVKIFVV-KKD-----------PSLTEEELIThCRRHLTGYKVPKLVEFRDE-LPKSNVGKILR-RELRD 551
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
214-490 |
1.75e-43 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 167.79 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 214 PIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMN-- 291
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHpd 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 292 --DGLRhIAKNLQQSKTSILIAVPllletlhkTILRKATGDAKVAKkyklglslakalnkikLNFNDkifaeihkglggh 369
Cdd:PRK08633 858 ptDALG-IAKLVAKHRATILLGTP--------TFLRLYLRNKKLHP----------------LMFAS------------- 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKYKE----------HASAGLPTPHVEVKIINED-- 436
Cdd:PRK08633 900 LRLVVAGAEKLKPEVADAFEEkFGIRILEGYGATETSPVASVNLPDVLAadfkrqtgskEGSVGMPLPGVAVRIVDPEtf 979
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1360655949 437 -ENGIGE---IIARGPNVMLGYYEDPEKTAEAI---DSEGFYHTGDYGYIDDRGFIYITGR 490
Cdd:PRK08633 980 eELPPGEdglILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
67-598 |
3.19e-43 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 164.90 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 67 EYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLA------TVcgLAIIAPMDKELPANEvenlINR 140
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGcfrqniTV--VTIYASLGEEALCHS----LNE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 141 SGANTIFYSRSQEDKLLGIADNIKQVKNLVSYDLPTENSSKLAGEDKDlfflWDLINTGNSIRANGNTQYD-NLPIdPRA 219
Cdd:PLN02387 177 TEVTTVICDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSN----WTVSSFSEVEKLGKENPVDpDLPS-PND 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 220 LAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTV-EFDKNDTLLSVLPLHHTFEATAGFLLpLSRGGKIA------MND 292
Cdd:PLN02387 252 IAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHILELAAESVM-AAVGAAIGygspltLTD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 293 GLRHIAK----NLQQSKTSILIAVPLLLETLHKTILRKATGDAKVAKK-----YKLGLSL-------AKALNKIKLNFnd 356
Cdd:PLN02387 331 TSNKIKKgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKlfdiaYKRRLAAiegswfgAWGLEKLLWDA-- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 357 KIFAEIHKGLGGHLRLLVCGGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINE 435
Cdd:PLN02387 409 LVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINIcLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSW 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 436 DENGI---------GEIIARGPNVMLGYYEDPEKTAEA--IDSEG---FYhTGDYGYIDDRGFIYITGRKANIIVTKNGK 501
Cdd:PLN02387 489 EEGGYlisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrwFY-TGDIGQFHPDGCLEIIDRKKDIVKLQHGE 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 502 NIFPEEIEFVLLKENIIEEVVVYGerDEYGEQIItAEVFPS---VEELAKvlETNAKDIDTSVL-TGSVAEGLVKDAISK 577
Cdd:PLN02387 568 YVSLGKVEAALSVSPYVDNIMVHA--DPFHSYCV-ALVVPSqqaLEKWAK--KAGIDYSNFAELcEKEEAVKEVQQSLSK 642
|
570 580
....*....|....*....|...
gi 1360655949 578 ANKE--LQNFKKVKDIVLRAEPF 598
Cdd:PLN02387 643 AAKAarLEKFEIPAKIKLLPEPW 665
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
61-529 |
1.08e-42 |
|
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: 160.87 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 61 RINPDNE--YRGI-------TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPA 131
Cdd:cd12119 7 RLHGDREivSRTHegevhryTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 132 NEVENLINRSGANTIFYSRSQEDKLLGIADNIKQVKNLVsydLPTENSSKLAGEDKDLFFLWDLIntgnsirANGNTQYD 211
Cdd:cd12119 87 EQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVV---VMTDDAAMPEPAGVGVLAYEELL-------AAESPEYD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 212 NLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLT--VEFDKNDTLLSVLPLHHT------FEAT---AGFLL 280
Cdd:cd12119 157 WPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTdgLGLSESDVVLPVVPMFHVnawglpYAAAmvgAKLVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 281 PlsrgGKiamNDGLRHIAKNLQQSKTSILIAVP----LLLETLHktilrkatgdakvAKKYKLGlslakalnkiklnfnd 356
Cdd:cd12119 237 P----GP---YLDPASLAELIEREGVTFAAGVPtvwqGLLDHLE-------------ANGRDLS---------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 357 kifaeihkglggHLRLLVCGGAAIEPQILADFNDWGITAIQGYGVTECSPIISNNRPKYKEH-----------ASAGLPT 425
Cdd:cd12119 281 ------------SLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARPPSEHSnlsedeqlalrAKQGRPV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 426 PHVEVKIINE-------DENGIGEIIARGPNVMLGYYEDPEkTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIvtK 498
Cdd:cd12119 349 PGVELRIVDDdgrelpwDGKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVI--K 425
|
490 500 510
....*....|....*....|....*....|....*..
gi 1360655949 499 NGKnifpEEIEFVLLkENII------EEVVVYGERDE 529
Cdd:cd12119 426 SGG----EWISSVEL-ENAImahpavAEAAVIGVPHP 457
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
16-613 |
1.18e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 161.74 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 16 SYRSRDLREMIERSASLYAEENA--FLLKDpvalreldprseaainfrinpdneyrgITYRQVNEDRKALGSAMLDLGIS 93
Cdd:PRK06710 20 SYDIQPLHKYVEQMASRYPEKKAlhFLGKD---------------------------ITFSVFHDKVKRFANYLQKLGVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 94 KDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIF--------------YSRSQEDKLLGI 159
Cdd:PRK06710 73 KGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnvqsATKIEHVIVTRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 160 ADNIKQVKNLVsYDLPTENSSKLAG--EDKDLFFLWdlintgNSIRANGNTQYDnLPIDPRA-LAVLLFTSGTTAKSKAV 236
Cdd:PRK06710 153 ADFLPFPKNLL-YPFVQKKQSNLVVkvSESETIHLW------NSVEKEVNTGVE-VPCDPENdLALLQYTGGTTGFPKGV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 237 MLCHDNLCVN-------IYDvCLTVEfdknDTLLSVLPLHHTFEATAGFLLPLSRGGKIAM--NDGLRHIAKNLQQSKTS 307
Cdd:PRK06710 225 MLTHKNLVSNtlmgvqwLYN-CKEGE----EVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLipKFDMKMVFEAIKKHKVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 308 ILIAVPllleTLHKTILrkatgDAKVAKKYKLGlslakalnkiklnfndkifaeihkglggHLRLLVCGGAAIEPQILAD 387
Cdd:PRK06710 300 LFPGAP----TIYIALL-----NSPLLKEYDIS----------------------------SIRACISGSAPLPVEVQEK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 388 FND-WGITAIQGYGVTECSPII-SNNRPKYKEHASAGLPTPHVEVKIINEdENG-------IGEIIARGPNVMLGYYEDP 458
Cdd:PRK06710 343 FETvTGGKLVEGYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSL-ETGealppgeIGEIVVKGPQIMKGYWNKP 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 459 EKTAeAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAE 538
Cdd:PRK06710 422 EETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVA-SGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAF 499
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1360655949 539 VFPSVEELAKVLETNakdidtsvltgsvaeglvkdaiSKANKELQNFKKVKDIVLRAEpFPRNTSKKILR----NKEQR 613
Cdd:PRK06710 500 VVLKEGTECSEEELN----------------------QFARKYLAAYKVPKVYEFRDE-LPKTTVGKILRrvliEEEKR 555
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
209-610 |
1.82e-42 |
|
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: 157.89 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 209 QYDNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTfeataGFLLPLSRGGKI 288
Cdd:cd05912 68 QLKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHI-----SGLSILMRSVIY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 289 AMNDGL------RHIAKNLQQSKTSILIAVPLLLEtlhktilrkatgdakvakkyklglslakalnkiklnfndKIFAEI 362
Cdd:cd05912 143 GMTVYLvdkfdaEQVLHLINSGKVTIISVVPTMLQ---------------------------------------RLLEIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 363 HKGLGGHLRLLVCGGAAIEPQILADFNDWGITAIQGYGVTE-CSPIISNNrPKY--KEHASAGLPTPHVEVKIINED--E 437
Cdd:cd05912 184 GEGYPNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTEtCSQIVTLS-PEDalNKIGSAGKPLFPVELKIEDDGqpP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 438 NGIGEIIARGPNVMLGYYEDPEKTAEAIDSeGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENI 517
Cdd:cd05912 263 YEVGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEIEEVLLSHPA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 518 IEEVVVYGERDEYGEQI----ITAEVFPSVEELAKVLETNakdidtsvltgsvaeglvkdaiskankeLQNFKKVKDIVL 593
Cdd:cd05912 341 IKEAGVVGIPDDKWGQVpvafVVSERPISEEELIAYCSEK----------------------------LAKYKVPKKIYF 392
|
410
....*....|....*..
gi 1360655949 594 rAEPFPRNTSKKILRNK 610
Cdd:cd05912 393 -VDELPRTASGKLLRHE 408
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
216-551 |
4.41e-42 |
|
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: 157.54 E-value: 4.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 216 DPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGL- 294
Cdd:cd05903 91 MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 295 -RHIAKNLQQSKTSILIAVPLLLETLHKTILRKATGDAkvakkyklglslakalnkiklnfndkifaeihkglggHLRLL 373
Cdd:cd05903 171 pDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLS-------------------------------------RLRTF 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 374 VCGGAAIEPQILADFNDWGITAIQG-YGVTECSPIISNNRPKYKEHA--SAGLPTPHVEVKIINED-----ENGIGEIIA 445
Cdd:cd05903 214 VCGGATVPRSLARRAAELLGAKVCSaYGSTECPGAVTSITPAPEDRRlyTDGRPLPGVEIKVVDDTgatlaPGVEGELLS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 446 RGPNVMLGYYEDPEKTAEAiDSEGFYHTGDYGYIDDRGFIYITGRKANIIVtKNGKNIFPEEIEFVLLKENIIEEVVVYG 525
Cdd:cd05903 294 RGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIII-RGGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
330 340 350
....*....|....*....|....*....|..
gi 1360655949 526 ERDE-YGEQIITAEVF-----PSVEELAKVLE 551
Cdd:cd05903 372 LPDErLGERACAVVVTksgalLTFDELVAYLD 403
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
61-610 |
2.52e-41 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 156.56 E-value: 2.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 61 RINPDN-----EYRGITYRQVNEDRKALGSAML-DLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEV 134
Cdd:PRK06839 13 YLHPDRiaiitEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 135 ENLINRSGANTIFYSRSQEDKLLGIADNIkQVKNLVSYDLPTENSSKlagedkdlfflwdliNTGNSIRANGNTQYdnlp 214
Cdd:PRK06839 93 IFQLKDSGTTVLFVEKTFQNMALSMQKVS-YVQRVISITSLKEIEDR---------------KIDNFVEKNESASF---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 215 idpralaVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHtFEATAGFLLP-LSRGGKIAMNDG 293
Cdd:PRK06839 153 -------IICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFH-IGGIGLFAFPtLFAGGVIIVPRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 294 LR--HIAKNLQQSKTSILIAVPLLLETLHKTILRKATgdakvakkyklglslakalnkiklNFNdkifaeihkglggHLR 371
Cdd:PRK06839 225 FEptKALSMIEKHKVTVVMGVPTIHQALINCSKFETT------------------------NLQ-------------SVR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 372 LLVCGGAAIEPQILADFNDWGITAIQGYGVTECSP---IISNNRPKYKEhASAGLPTPHVEVKIINEDEN-----GIGEI 443
Cdd:PRK06839 268 WFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPtvfMLSEEDARRKV-GSIGKPVLFCDYELIDENKNkvevgEVGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 444 IARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVV 523
Cdd:PRK06839 347 LIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQVINKLSDVYEVAV 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 524 YGERD-EYGEqiitaevfpsVEELAKVLETNAkdidtsvltgSVAEglvKDAISKANKELQNFKKVKDIVLRAEpFPRNT 602
Cdd:PRK06839 425 VGRQHvKWGE----------IPIAFIVKKSSS----------VLIE---KDVIEHCRLFLAKYKIPKEIVFLKE-LPKNA 480
|
....*...
gi 1360655949 603 SKKILRNK 610
Cdd:PRK06839 481 TGKIQKAQ 488
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
17-614 |
7.83e-40 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 153.64 E-value: 7.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 17 YRSrdLREMIERSASLYAEENAFLLKDpvalreldprseaainfrinpdneyRGITYRQVNEDRKALGSAMLDLGISKDD 96
Cdd:PRK07059 22 YPS--LADLLEESFRQYADRPAFICMG-------------------------KAITYGELDELSRALAAWLQSRGLAKGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 97 KVIILAETRYEWYITYLATV-CGLAIIAPMDKELPaNEVENLINRSGANTIF----YSRSQED----------------K 155
Cdd:PRK07059 75 RVAIMMPNVLQYPVAIAAVLrAGYVVVNVNPLYTP-RELEHQLKDSGAEAIVvlenFATTVQQvlaktavkhvvvasmgD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 156 LLGIADNI-----KQVKNLV-SYDLPTENSSKLAgedkdlfflwdlintgnsIRANGNTQYDNLPIDPRALAVLLFTSGT 229
Cdd:PRK07059 154 LLGFKGHIvnfvvRRVKKMVpAWSLPGHVRFNDA------------------LAEGARQTFKPVKLGPDDVAFLQYTGGT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 230 TAKSKAVMLCHDNLCVNIY--DVCLTVEFDKN---DTLLSV--LPLHHTFEATAGFLLPLSRGGkiamndglrhiaknlq 302
Cdd:PRK07059 216 TGVSKGATLLHRNIVANVLqmEAWLQPAFEKKprpDQLNFVcaLPLYHIFALTVCGLLGMRTGG---------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 303 qskTSILIAVPllletlhktilRKATGDAKVAKKYKLglSLAKALNKIklnFNDKI-FAEIHKGLGGHLRLLVCGGAAIE 381
Cdd:PRK07059 280 ---RNILIPNP-----------RDIPGFIKELKKYQV--HIFPAVNTL---YNALLnNPDFDKLDFSKLIVANGGGMAVQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 382 PQILadfNDW----GITAIQGYGVTECSPIISNNRPKYKEHA-SAGLPTPHVEVKIINEDENG-----IGEIIARGPNVM 451
Cdd:PRK07059 341 RPVA---ERWlemtGCPITEGYGLSETSPVATCNPVDATEFSgTIGLPLPSTEVSIRDDDGNDlplgePGEICIRGPQVM 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 452 LGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYG 531
Cdd:PRK07059 418 AGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILV-SGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHS 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 532 EQIITAEVFpsveelakvletnAKDIDtsvLTgsvaeglVKDAISKANKELQNFKKVKDIVLRAEpFPRNTSKKILRnKE 611
Cdd:PRK07059 497 GEAVKLFVV-------------KKDPA---LT-------EEDVKAFCKERLTNYKRPKFVEFRTE-LPKTNVGKILR-RE 551
|
...
gi 1360655949 612 QRN 614
Cdd:PRK07059 552 LRD 554
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
71-610 |
8.44e-40 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 152.04 E-value: 8.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSR 150
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 SQEDKLLGIadniKQVKnlVSyDLPtenssKLAGEDKDLFFLWDLINTgnsirangntqydnlpidpralAVLLFTSGTT 230
Cdd:PRK03640 108 DFEAKLIPG----ISVK--FA-ELM-----NGPKEEAEIQEEFDLDEV----------------------ATIMYTSGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 231 AKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTfeatAGFllplsrggKIAMND---GLR----------HI 297
Cdd:PRK03640 154 GKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHI----SGL--------SILMRSviyGMRvvlvekfdaeKI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 298 AKNLQQSKTSILIAVPLLLETLhktilrkatgdakvakkyklglslakalnkiklnfndkiFAEIHKG-LGGHLRLLVCG 376
Cdd:PRK03640 222 NKLLQTGGVTIISVVSTMLQRL---------------------------------------LERLGEGtYPSSFRCMLLG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 377 GAAIEPQILADFNDWGITAIQGYGVTE-CSPIISNNrPKY--KEHASAGLPTPHVEVKIINED----ENGIGEIIARGPN 449
Cdd:PRK03640 263 GGPAPKPLLEQCKEKGIPVYQSYGMTEtASQIVTLS-PEDalTKLGSAGKPLFPCELKIEKDGvvvpPFEEGEIVVKGPN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 450 VMLGYYEDPEKTAEAIDSeGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDE 529
Cdd:PRK03640 342 VTKGYLNREDATRETFQD-GWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEIEEVLLSHPGVAEAGVVGVPDD 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 530 YGEQI----ITAEVFPSVEELAKVLETNakdidtsvltgsvaeglvkdaiskankeLQNFKKVKDIVLrAEPFPRNTSKK 605
Cdd:PRK03640 420 KWGQVpvafVVKSGEVTEEELRHFCEEK----------------------------LAKYKVPKRFYF-VEELPRNASGK 470
|
....*
gi 1360655949 606 ILRNK 610
Cdd:PRK03640 471 LLRHE 475
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
66-492 |
1.33e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 154.36 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 66 NEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMdkelpaneVENLinrsGANT 145
Cdd:PTZ00216 117 NETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATV--------YANL----GEDA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 146 IFYSRSqEDKLLGIADNIKQVKNLVS-------------Y--DLPTENSSklagEDKDLFFLWDLINTGNSIRANGNTqy 210
Cdd:PTZ00216 185 LAYALR-ETECKAIVCNGKNVPNLLRlmksggmpnttiiYldSLPASVDT----EGCRLVAWTDVVAKGHSAGSHHPL-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 211 dNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNI-------YDVCltVEFDKNDTLLSVLPLHHTFEATAGFLLpLS 283
Cdd:PTZ00216 258 -NIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGIlaledrlNDLI--GPPEEDETYCSYLPLAHIMEFGVTNIF-LA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 284 RGGKIAMndG-----LRHIAK---NLQQSKTSILIAVPLLLETLHKTILRK--ATGDAK---VAKKYKLGLslaKALNKI 350
Cdd:PTZ00216 334 RGALIGF--GsprtlTDTFARphgDLTEFRPVFLIGVPRIFDTIKKAVEAKlpPVGSLKrrvFDHAYQSRL---RALKEG 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 351 KLN--FNDKIFAEIHKGLGGHLRLLVCGGAAIEPQIlADFND--WGITaIQGYGVTE---CSPIisnNRPKYKEHASAGL 423
Cdd:PTZ00216 409 KDTpyWNEKVFSAPRAVLGGRVRAMLSGGGPLSAAT-QEFVNvvFGMV-IQGWGLTEtvcCGGI---QRTGDLEPNAVGQ 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1360655949 424 PTPHVEVKIINEDE-------NGIGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGR-KA 492
Cdd:PTZ00216 484 LLKGVEMKLLDTEEykhtdtpEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRvKA 560
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
223-608 |
1.74e-39 |
|
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: 147.65 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 223 LLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKI---AMNDgLRHIAK 299
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVvpvAVFD-VDAILE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 300 NLQQSKTSILIAVPllleTLHKTILrkatgDAKVAKKYKLGlslakalnkiklnfndkifaeihkglggHLRLLVCGGAA 379
Cdd:cd17638 84 AIERERITVLPGPP----TLFQSLL-----DHPGRKKFDLS----------------------------SLRAAVTGAAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 380 IEPQILADF-NDWGITAI-QGYGVTECSpIISNNRPKYKEHASA---GLPTPHVEVKIINEdengiGEIIARGPNVMLGY 454
Cdd:cd17638 127 VPVELVRRMrSELGFETVlTAYGLTEAG-VATMCRPGDDAETVAttcGRACPGFEVRIADD-----GEVLVRGYNVMQGY 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 455 YEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQI 534
Cdd:cd17638 201 LDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYIV-GGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEV 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1360655949 535 ITAEVfpsveelakvletnakdidtsvlTGSVAEGLVKDAISKANKE-LQNFkKVKDIVLRAEPFPRNTSKKILR 608
Cdd:cd17638 280 GKAFV-----------------------VARPGVTLTEEDVIAWCRErLANY-KVPRFVRFLDELPRNASGKVMK 330
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
72-598 |
9.93e-39 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 151.51 E-value: 9.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYsrs 151
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFV--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 152 QEDKLLGIAD----NIKQVKNLVSYDLPTENSSKLAGEDKDLFFLW-DLINTGNSIRANGNtqydnlPIDPRALAVLLFT 226
Cdd:PLN02430 155 QDKKIKELLEpdckSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWiDFLHMGKENPSETN------PPKPLDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 227 SGTTAKSKAVMLCHDNL--CVNIYDVCLTVEFDK---NDTLLSVLPLHHTFE-ATAGFLLplSRGGKIAMNDG-LRHIAK 299
Cdd:PLN02430 229 SGTSGDPKGVVLTHEAVatFVRGVDLFMEQFEDKmthDDVYLSFLPLAHILDrMIEEYFF--RKGASVGYYHGdLNALRD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 300 NLQQSKTSILIAVPLLLETLHKTI---------LRKATGDAkvAKKYKLGLSLAKALNKIKLNFNDKI-FAEIHKGLGGH 369
Cdd:PLN02430 307 DLMELKPTLLAGVPRVFERIHEGIqkalqelnpRRRLIFNA--LYKYKLAWMNRGYSHKKASPMADFLaFRKVKAKLGGR 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQIlADFndWGITA----IQGYGVTE-CSPIISNNRPKYKEHASAGLPTPHVEVKIINEDENGI---- 440
Cdd:PLN02430 385 LRLLISGGAPLSTEI-EEF--LRVTScafvVQGYGLTEtLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVPEMGYdplg 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 441 ----GEIIARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVLLKEN 516
Cdd:PLN02430 462 epprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNP 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 517 IIEEVVVYGerDEYgEQIITAEVFPSVEELAKVLETNAkdidtsvLTGSVAE-----GLVKDAISK-----ANKELQNFK 586
Cdd:PLN02430 541 IVEDIWVYG--DSF-KSMLVAVVVPNEENTNKWAKDNG-------FTGSFEElcslpELKEHILSElkstaEKNKLRGFE 610
|
570
....*....|..
gi 1360655949 587 KVKDIVLRAEPF 598
Cdd:PLN02430 611 YIKGVILETKPF 622
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
67-598 |
2.25e-38 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 150.38 E-value: 2.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 67 EYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTI 146
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 147 FYsrsQEDKLLGIADNIKQ----VKNLVSYDlptENSSKLAGEDKDL---FFLWdlintgNSIRANGNTQYDNLPIDPRA 219
Cdd:PLN02861 154 FV---QESKISSILSCLPKcssnLKTIVSFG---DVSSEQKEEAEELgvsCFSW------EEFSLMGSLDCELPPKQKTD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 220 LAVLLFTSGTTAKSKAVMLCHDNLCVNIYDV-CLTVEFDK----NDTLLSVLPLHHTFEATAGFLLpLSRGGKIAMNDG- 293
Cdd:PLN02861 222 ICTIMYTSGTTGEPKGVILTNRAIIAEVLSTdHLLKVTDRvateEDSYFSYLPLAHVYDQVIETYC-ISKGASIGFWQGd 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 294 LRHIAKNLQQSKTSILIAVPLLLETLHKTILRKATGDAKVAKK-------YKLGlSLAKALNKIKLN-FNDKI-FAEIHK 364
Cdd:PLN02861 301 IRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKlfdfaynYKLG-NLRKGLKQEEASpRLDRLvFDKIKE 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 365 GLGGHLRLLVCGGAAIePQILADFndWGITA----IQGYGVTE-CSPIISNNRPKYKEHASAGLPTPHVEVKIINEDENG 439
Cdd:PLN02861 380 GLGGRVRLLLSGAAPL-PRHVEEF--LRVTScsvlSQGYGLTEsCGGCFTSIANVFSMVGTVGVPMTTIEARLESVPEMG 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 I--------GEIIARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFV 511
Cdd:PLN02861 457 YdalsdvprGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENT 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 512 LLKENIIEEVVVYGERdeyGEQIITAEVFPSVEELAKVLETNAKDIDTSVLTGSV-AEGLVKDAISKANKELQ--NFKKV 588
Cdd:PLN02861 536 YSRCPLIASIWVYGNS---FESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLkARKYILDELNSTGKKLQlrGFEML 612
|
570
....*....|
gi 1360655949 589 KDIVLRAEPF 598
Cdd:PLN02861 613 KAIHLEPNPF 622
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
71-610 |
2.34e-38 |
|
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: 148.83 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSR 150
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 SQEDKLLGIADNIKQVKNLVSYDLPTEnsskLAGEDKDLFFLwdlinTGNSirANGNTQYDNLPID---PRALAVLLFTS 227
Cdd:cd17642 125 KGLQKVLNVQKKLKIIKTIIILDSKED----YKGYQCLYTFI-----TQNL--PPGFNEYDFKPPSfdrDEQVALIMNSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 228 GTTAKSKAVMLCHDNLCVNiYDVCLTVEF----DKNDTLLSVLPLHHTFE--ATAGFLLPlsrGGKIAMNDGLRH--IAK 299
Cdd:cd17642 194 GSTGLPKGVQLTHKNIVAR-FSHARDPIFgnqiIPDTAILTVIPFHHGFGmfTTLGYLIC---GFRVVLMYKFEEelFLR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 300 NLQQSKTSILIAVPLLLETLHKTILrkatgdakvAKKYKLGlslakalnkiklnfndkifaeihkglggHLRLLVCGGAA 379
Cdd:cd17642 270 SLQDYKVQSALLVPTLFAFFAKSTL---------VDKYDLS----------------------------NLHEIASGGAP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 380 ----IEPQILADFNDWGITaiQGYGVTEC-SPIISNNRPKYKEhASAGLPTPHVEVKIINEDE------NGIGEIIARGP 448
Cdd:cd17642 313 lskeVGEAVAKRFKLPGIR--QGYGLTETtSAILITPEGDDKP-GAVGKVVPFFYAKVVDLDTgktlgpNERGELCVKGP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 449 NVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFPEEIEFVLLKENIIEEVVVYGERD 528
Cdd:cd17642 390 MIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYK-GYQVPPAELESILLQHPKIFDAGVAGIPD 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 529 EYGEQIITAEVfpsveelakVLETNAKdidtsvLTGSVAEGLVKDAISKAnkelqnfKKVKDIVLRAEPFPRNTSKKILR 608
Cdd:cd17642 469 EDAGELPAAVV---------VLEAGKT------MTEKEVMDYVASQVSTA-------KRLRGGVKFVDEVPKGLTGKIDR 526
|
..
gi 1360655949 609 NK 610
Cdd:cd17642 527 RK 528
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
82-608 |
2.52e-38 |
|
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: 147.20 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 82 ALGSAMLDLGISKDDKVIILAETRYEWYITYLATV---CGLAIIA-PMDKELPANEVENLINRSGANTIFYSRSQEDKLl 157
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFAVAyagGRLGLVFvPLNPTLKESVLRYLVADAGGRIVLADAGAADRL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 158 giadnikQVKNLVSYDLptenssklagedkdlfflwDLINTGNSIRANGnTQYDNLPIDPRALAVLLFTSGTTAKSKAVM 237
Cdd:cd05922 84 -------RDALPASPDP-------------------GTVLDADGIRAAR-ASAPAHEVSHEDLALLLYTSGSTGSPKLVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 238 LCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFeATAGFLLPLSRGGKIAMNDGL---RHIAKNLQQSKTSILIAVPL 314
Cdd:cd05922 137 LSHQNLLANARSIAEYLGITADDRALTVLPLSYDY-GLSVLNTHLLRGATLVLTNDGvldDAFWEDLREHGATGLAGVPS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 315 LLETLhktiLRKATGDAKVAkkyklglslakalnkiklnfndkifaeihkglggHLRLLVCGGAAIEPQILADFNDwgit 394
Cdd:cd05922 216 TYAML----TRLGFDPAKLP----------------------------------SLRYLTQAGGRLPQETIARLRE---- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 395 AIQG------YGVTECSPIIS-------NNRPkykehASAGLPTPHVEVKIINEDEN-----GIGEIIARGPNVMLGYYE 456
Cdd:cd05922 254 LLPGaqvyvmYGQTEATRRMTylpperiLEKP-----GSIGLAIPGGEFEILDDDGTptppgEPGEIVHRGPNVMKGYWN 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 457 DPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIIT 536
Cdd:cd05922 329 DPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLAL 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1360655949 537 AEVFPSVEElakvletnakdidtsvltgsvaeglVKDAISKANKELQNFKKVKDIVLrAEPFPRNTSKKILR 608
Cdd:cd05922 408 FVTAPDKID-------------------------PKDVLRSLAERLPPYKVPATVRV-VDELPLTASGKVDY 453
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
56-608 |
3.69e-38 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 148.72 E-value: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 56 AAINFRiNPDNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATV-CGlAIIAPMDKELPANEV 134
Cdd:COG0365 26 VALIWE-GEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACArIG-AVHSPVFPGFGAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 135 ENLINRSGANTIF----YSR-----SQEDKLLGIADNIKQVKNLVSYDlPTENSSKLAGedkDLFFlWDLIntgnsirAN 205
Cdd:COG0365 104 ADRIEDAEAKVLItadgGLRggkviDLKEKVDEALEELPSLEHVIVVG-RTGADVPMEG---DLDW-DELL-------AA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 206 GNTQYDNLPIDPRALAVLLFTSGTTAKSKAV-------MLCHDNLCVNIYDVcltvefDKNDTLLSVlplhhtfeATAGF 278
Cdd:COG0365 172 ASAEFEPEPTDADDPLFILYTSGTTGKPKGVvhthggyLVHAATTAKYVLDL------KPGDVFWCT--------ADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 279 --------LLPLSRGGKIAMNDG----------LRHIAKNlqqsKTSILIAVPllletlhkTILR--KATGDaKVAKKYK 338
Cdd:COG0365 238 atghsyivYGPLLNGATVVLYEGrpdfpdpgrlWELIEKY----GVTVFFTAP--------TAIRalMKAGD-EPLKKYD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 339 LGlslakalnkiklnfndkifaeihkglggHLRLLVCGGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKYKE 417
Cdd:COG0365 305 LS----------------------------SLRLLGSAGEPLNPEVWEWWYEaVGVPIVDGWGQTETGGIFISNLPGLPV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 418 HA-SAGLPTPHVEVKIINED-----ENGIGEIIARG--PNVMLGYYEDPEKTAEAI--DSEGFYHTGDYGYIDDRGFIYI 487
Cdd:COG0365 357 KPgSMGKPVPGYDVAVVDEDgnpvpPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 488 TGRKANIIVTkNGKNIFPEEIEFVLLK-ENIIEEVVVyGERDEYGEQIITAEVfpsveelakVLETNAKDIDTsvLTGSV 566
Cdd:COG0365 437 LGRSDDVINV-SGHRIGTAEIESALVShPAVAEAAVV-GVPDEIRGQVVKAFV---------VLKPGVEPSDE--LAKEL 503
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1360655949 567 AEgLVKDAISKankelqnFKKVKDIVLRAEpFPRNTSKKILR 608
Cdd:COG0365 504 QA-HVREELGP-------YAYPREIEFVDE-LPKTRSGKIMR 536
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
72-607 |
2.58e-36 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 144.39 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSRS 151
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 152 QEDKLLGIADN-IKQVKNLVSYDLPTENSSKLAGEDKDLFFLWDlintgNSIRANGNTQYDnLPID-PRALAVLLFTSGT 229
Cdd:PLN02614 161 KISELFKTCPNsTEYMKTVVSFGGVSREQKEEAETFGLVIYAWD-----EFLKLGEGKQYD-LPIKkKSDICTIMYTSGT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 230 TAKSKAVMLCHDNLCVNIYDVC-----LTVEFDKNDTLLSVLPLHHTFEATAGFLLpLSRGGKIAMNDG-LRHIAKNLQQ 303
Cdd:PLN02614 235 TGDPKGVMISNESIVTLIAGVIrllksANAALTVKDVYLSYLPLAHIFDRVIEECF-IQHGAAIGFWRGdVKLLIEDLGE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 304 SKTSILIAVPLLLETLHKTILRKATGDAKVAKK-------YKLGlSLAKALNKIKLN-FNDK-IFAEIHKGLGGHLRLLV 374
Cdd:PLN02614 314 LKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFvfdsafsYKFG-NMKKGQSHVEASpLCDKlVFNKVKQGLGGNVRIIL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 375 CGGAAIEPQILADFNDWG-ITAIQGYGVTE-CSPIISNNRPKYKEHASAGLPTPHVEVKI-----INEDENGI---GEII 444
Cdd:PLN02614 393 SGAAPLASHVESFLRVVAcCHVLQGYGLTEsCAGTFVSLPDELDMLGTVGPPVPNVDIRLesvpeMEYDALAStprGEIC 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 445 ARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVLLKENIIEEVVVY 524
Cdd:PLN02614 473 IRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVY 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 525 GERdeyGEQIITAEVFPSVEELAKVLETNAKDID-TSVLTGSVAEGLVKDAISKANKE--LQNFKKVKDIVLraEPFPRN 601
Cdd:PLN02614 552 GNS---FESFLVAIANPNQQILERWAAENGVSGDyNALCQNEKAKEFILGELVKMAKEkkMKGFEIIKAIHL--DPVPFD 626
|
....*.
gi 1360655949 602 TSKKIL 607
Cdd:PLN02614 627 MERDLL 632
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
220-615 |
3.73e-36 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 143.04 E-value: 3.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 220 LAVLLFTSGTTAKSKAVMLCHDNLCVNIYDV--CL--------TVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIA 289
Cdd:PRK12492 209 IAVLQYTGGTTGLAKGAMLTHGNLVANMLQVraCLsqlgpdgqPLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNV 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 290 MNDGLRHIA---KNLQQSKTSILIAvpllLETLHKTILRKAtgdakvakKYKlglslakalnkiKLNFNdkifaeihkgl 366
Cdd:PRK12492 289 LITNPRDIPgfiKELGKWRFSALLG----LNTLFVALMDHP--------GFK------------DLDFS----------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 367 ggHLRLLVCGGAAIepqILADFNDW----GITAIQGYGVTECSPIISNNrpKYKEHA---SAGLPTPHVEVKIINEDENG 439
Cdd:PRK12492 334 --ALKLTNSGGTAL---VKATAERWeqltGCTIVEGYGLTETSPVASTN--PYGELArlgTVGIPVPGTALKVIDDDGNE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 I-----GEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLK 514
Cdd:PRK12492 407 LplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIV-SGFNVYPNEIEDVVMA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 515 ENIIEEVVVYGERDEYGEQIITAEVFP-----SVEELakvletnakdidtsvltgsvaeglvkDAISKANkeLQNFKKVK 589
Cdd:PRK12492 486 HPKVANCAAIGVPDERSGEAVKLFVVArdpglSVEEL--------------------------KAYCKEN--FTGYKVPK 537
|
410 420
....*....|....*....|....*.
gi 1360655949 590 DIVLRaEPFPRNTSKKILRnKEQRNV 615
Cdd:PRK12492 538 HIVLR-DSLPMTPVGKILR-RELRDI 561
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
12-532 |
6.70e-36 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 142.79 E-value: 6.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 12 PLHESYRSRDLREMIERSASlyaeenafllKDPvalreldprSEAAINFRINPDNEYRG--ITYRQVNEDRKALGSAMLD 89
Cdd:PRK07529 17 PLAARDLPASTYELLSRAAA----------RHP---------DAPALSFLLDADPLDRPetWTYAELLADVTRTANLLHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 90 LGISKDDKVIILAETRYEWYITYL-ATVCGlaIIAPMDKELPANEVENLINRSGANTIFYSRSQED-----KLLGIADNI 163
Cdd:PRK07529 78 LGVGPGDVVAFLLPNLPETHFALWgGEAAG--IANPINPLLEPEQIAELLRAAGAKVLVTLGPFPGtdiwqKVAEVLAAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 164 KQVKNLVSYDLptensSKLAGEDKDLFFLWDLINTGNSIRANGNT---QYDNLPIDPRA-----LAVLLFTSGTTAKSKA 235
Cdd:PRK07529 156 PELRTVVEVDL-----ARYLPGPKRLAVPLIRRKAHARILDFDAElarQPGDRLFSGRPigpddVAAYFHTGGTTGMPKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 236 VMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAM-------NDGL-RHIAKNLQQSKTS 307
Cdd:PRK07529 231 AQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLatpqgyrGPGViANFWKIVERYRIN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 308 ILIAVPllleTLHKTILRKATGDAKVAkkyklglSLAKALnkiklnfndkifaeihkglgghlrllvCGGAAIEPQILAD 387
Cdd:PRK07529 311 FLSGVP----TVYAALLQVPVDGHDIS-------SLRYAL---------------------------CGAAPLPVEVFRR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 388 FND-WGITAIQGYGVTECSPIISNNrPKYKEH--ASAGLPTPHVEVKIINEDENG----------IGEIIARGPNVMLGY 454
Cdd:PRK07529 353 FEAaTGVRIVEGYGLTEATCVSSVN-PPDGERriGSVGLRLPYQRVRVVILDDAGrylrdcavdeVGVLCIAGPNVFSGY 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1360655949 455 YEdPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVtKNGKNIFPEEIEFVLLKENIIEEVVVYGERDEY-GE 532
Cdd:PRK07529 432 LE-AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLII-RGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHaGE 508
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
213-614 |
7.80e-36 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 141.94 E-value: 7.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 213 LPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEF-----DKNDTLLSVLPLHHTFEATAGFLLPLSRGGk 287
Cdd:PRK08751 203 LQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGtgkleEGCEVVITALPLYHIFALTANGLVFMKIGG- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 288 iamndgLRHIAKNLQQsktsiliaVPLLLETLHKTILRKATGdakvakkyklglsLAKALNKIkLN---FNDKIFAEIHK 364
Cdd:PRK08751 282 ------CNHLISNPRD--------MPGFVKELKKTRFTAFTG-------------VNTLFNGL-LNtpgFDQIDFSSLKM 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 365 GLGGhlrllvcgGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKYKEH-ASAGLPTPHVEVKIinEDENG--- 439
Cdd:PRK08751 334 TLGG--------GMAVQRSVAERWKQvTGLTLVEAYGLTETSPAACINPLTLKEYnGSIGLPIPSTDACI--KDDAGtvl 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 ----IGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKE 515
Cdd:PRK08751 404 aigeIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILV-SGFNVYPNEIEDVIAMM 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 516 NIIEEVVVYGERDEYGEQIITAEVFpsveelakvletnAKDidtSVLTGsvaeglvKDAISKANKELQNFKKVKDIVLRA 595
Cdd:PRK08751 483 PGVLEVAAVGVPDEKSGEIVKVVIV-------------KKD---PALTA-------EDVKAHARANLTGYKQPRIIEFRK 539
|
410
....*....|....*....
gi 1360655949 596 EpFPRNTSKKILRnKEQRN 614
Cdd:PRK08751 540 E-LPKTNVGKILR-RELRD 556
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
22-608 |
9.31e-36 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 141.66 E-value: 9.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 22 LREMIERSASLYAEENAFLlkdpvalreldprsEAAINfrinpdneyRGITYRQVNEDRKALGSAMLDLGISKDDKVIIL 101
Cdd:PLN02330 30 LPDFVLQDAELYADKVAFV--------------EAVTG---------KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 102 AETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSrsqedkllgiADNIKQVKNLvsyDLPTenssK 181
Cdd:PLN02330 87 LPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN----------DTNYGKVKGL---GLPV----I 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 182 LAGEDKDLFFL-W-DLINTGNsiRAnGNTQyDNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTV--EFD 257
Cdd:PLN02330 150 VLGEEKIEGAVnWkELLEAAD--RA-GDTS-DNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVgpEMI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 258 KNDTLLSVLPLHHTFEATAGFLLPLSRGGKI-AMND-GLRHIAKNLQQSKTSILIAVPLLLETLHKTilrkatgdaKVAK 335
Cdd:PLN02330 226 GQVVTLGLIPFFHIYGITGICCATLRNKGKVvVMSRfELRTFLNALITQEVSFAPIVPPIILNLVKN---------PIVE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 336 KYKLglslakalNKIKLnfndkifaeihkglgghlRLLVCGGAAIEPQILADFNDW--GITAIQGYGVTECSPIISNNRP 413
Cdd:PLN02330 297 EFDL--------SKLKL------------------QAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHSCITLTHGD 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 414 KYKEHA-----SAGLPTPHVEVKIINED------ENGIGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDR 482
Cdd:PLN02330 351 PEKGHGiakknSVGFILPNLEVKFIDPDtgrslpKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 483 GFIYITGRKANIIVTKnGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAEVfpsveelakVLETNAKDIDTSVL 562
Cdd:PLN02330 431 GDIFIVDRIKELIKYK-GFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACV---------VINPKAKESEEDIL 500
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1360655949 563 TgsvaegLVKDAISkankelqNFKKVKdIVLRAEPFPRNTSKKILR 608
Cdd:PLN02330 501 N------FVAANVA-------HYKKVR-VVQFVDSIPKSLSGKIMR 532
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
71-608 |
2.56e-35 |
|
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: 138.38 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSR 150
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 SQEDkllgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpidpraLAVLLFTSGTT 230
Cdd:cd05935 82 ELDD-----------------------------------------------------------------LALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 231 AKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAM-----NDGLRhiaKNLQQSK 305
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLmarwdRETAL---ELIEKYK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 306 TSILIAVPLLLETLHKTilrkatgdakvakkyklglslakalnkikLNFNDKIFAeihkglggHLRLLVCGGAAIEPQIL 385
Cdd:cd05935 174 VTFWTNIPTMLVDLLAT-----------------------------PEFKTRDLS--------SLKVLTGGGAPMPPAVA 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 386 ADFND-WGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINE------DENGIGEIIARGPNVMLGYYEDP 458
Cdd:cd05935 217 EKLLKlTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIetgrelPPNEVGEIVVRGPQIFKGYWNRP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 459 EKTAEA---IDSEGFYHTGDYGYIDDRGFIYITGRKANIIvTKNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQII 535
Cdd:cd05935 297 EETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMI-NVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEV 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1360655949 536 TAEVFPSVEELAKVLEtnakdidtsvltgsvaeglvKDAISKANKELQNFKKVKDIVLrAEPFPRNTSKKILR 608
Cdd:cd05935 376 KAFIVLRPEYRGKVTE--------------------EDIIEWAREQMAAYKYPREVEF-VDELPRSASGKILW 427
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
35-608 |
5.43e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 139.14 E-value: 5.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 35 EENAFLLKDPVALRELDprseaainfrinpdneyRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLA 114
Cdd:PRK07786 24 ARHALMQPDAPALRFLG-----------------NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 115 TVCGLAIIAPMDKELPANEVENLINRSGANTIFysrsQEDKLLGIADNIKQvknlvsyDLPTENSSKLAGEDKDLfflwD 194
Cdd:PRK07786 87 ANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV----TEAALAPVATAVRD-------IVPLLSTVVVAGGSSDD----S 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 195 LINTGNSIRANGNT-QYDNLPIDPRALavLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDT--LLSVlPLHHt 271
Cdd:PRK07786 152 VLGYEDLLAEAGPAhAPVDIPNDSPAL--IMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDvgFVGV-PLFH- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 272 featagfllplsrggkIAmndGLRHIAKNLQQSKTSILiaVPL-------LLETLHKtilRKATGDAKVAKKYKLGLSLA 344
Cdd:PRK07786 228 ----------------IA---GIGSMLPGLLLGAPTVI--YPLgafdpgqLLDVLEA---EKVTGIFLVPAQWQAVCAEQ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 345 KAlnkiklnfndkifaeihKGLGGHLRLLVCGGAAIEPQIL----ADFNDWGITAIqgYGVTECSPI--ISNNRPKYKEH 418
Cdd:PRK07786 284 QA-----------------RPRDLALRVLSWGAAPASDTLLrqmaATFPEAQILAA--FGQTEMSPVtcMLLGEDAIRKL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 419 ASAGLPTPHVEVKIINEDENG-----IGEIIARGPNVMLGYYEDPEKTAEAIDSeGFYHTGDYGYIDDRGFIYITGRKAN 493
Cdd:PRK07786 345 GSVGKVIPTVAARVVDENMNDvpvgeVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKD 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 494 IIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDE-YGEqiitaevFPsveelakvletnakdIDTSVLTGSVAEGLVK 572
Cdd:PRK07786 424 MIIS-GGENIYCAEVENVLASHPDIVEVAVIGRADEkWGE-------VP---------------VAVAAVRNDDAALTLE 480
|
570 580 590
....*....|....*....|....*....|....*.
gi 1360655949 573 DAISKANKELQNFKKVKDIVLrAEPFPRNTSKKILR 608
Cdd:PRK07786 481 DLAEFLTDRLARYKHPKALEI-VDALPRNPAGKVLK 515
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
71-541 |
1.27e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 137.81 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYE-WYITYLATVCGLAIIA--PMDKE------LPANEVENLINRS 141
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLMAIGAAQLAGLRRTAlhPLGSLddhayvLEDAGISTLIVDP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 142 GAntiFYSRSQEdkLLGIADNIKQVKNLVSYDlptenssklAGEDkdlffLWDLIntgnsirangnTQYDNLPIDPRAL- 220
Cdd:PRK06188 118 AP---FVERALA--LLARVPSLKHVLTLGPVP---------DGVD-----LLAAA-----------AKFGPAPLVAAALp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 221 ---AVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHtfeATAGFLLP-LSRGGKIAMNDG--- 293
Cdd:PRK06188 168 pdiAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH---AGGAFFLPtLLRGGTVIVLAKfdp 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 294 ---LRHIAKnlqQSKTSILIaVPLLLETL--HKtilRKATGDakvakkyklgLSlakalnkiklnfndkifaeihkglgg 368
Cdd:PRK06188 245 aevLRAIEE---QRITATFL-VPTMIYALldHP---DLRTRD----------LS-------------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 369 HLRLLVCGGAAIEPQILADfndwGITAI-----QGYGVTECSPIISNNRPKykEH--------ASAGLPTPHVEVKIINE 435
Cdd:PRK06188 282 SLETVYYGASPMSPVRLAE----AIERFgpifaQYYGQTEAPMVITYLRKR--DHdpddpkrlTSCGRPTPGLRVALLDE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 436 DENGI-----GEIIARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEF 510
Cdd:PRK06188 356 DGREVaqgevGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVT-GGFNVFPREVED 433
|
490 500 510
....*....|....*....|....*....|..
gi 1360655949 511 VLLKENIIEEVVVYGERDE-YGEQiITAEVFP 541
Cdd:PRK06188 434 VLAEHPAVAQVAVIGVPDEkWGEA-VTAVVVL 464
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
69-608 |
2.54e-34 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 136.54 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFY 148
Cdd:PRK07514 27 LRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 149 SRSQEDKLLGIAD--NIKQVKNLvsydlptenssklaGEDKdlfflwdlinTGNSI-RANG-NTQYDNLPIDPRALAVLL 224
Cdd:PRK07514 107 DPANFAWLSKIAAaaGAPHVETL--------------DADG----------TGSLLeAAAAaPDDFETVPRGADDLAAIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 225 FTSGTTAKSKAVMLCHDNLCVNiydvCLTV----EFDKNDTLLSVLPLHHT---FEATAGFLLplSRGGKIAMN--DgLR 295
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGNLLSN----ALTLvdywRFTPDDVLIHALPIFHThglFVATNVALL--AGASMIFLPkfD-PD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 296 HIAKNLQQSktSILIAVPllleTLHKTILRKATGDAKVAKkyklglslakalnkiklnfndkifaeihkglggHLRLLVC 375
Cdd:PRK07514 236 AVLALMPRA--TVMMGVP----TFYTRLLQEPRLTREAAA---------------------------------HMRLFIS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 376 GGAaiePqILAD-FNDW----GITAIQGYGVTECSPIISN-----NRPkykehASAGLPTPHVEVKIINEDEN------G 439
Cdd:PRK07514 277 GSA---P-LLAEtHREFqertGHAILERYGMTETNMNTSNpydgeRRA-----GTVGFPLPGVSLRVTDPETGaelppgE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 IGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLlkeNIIE 519
Cdd:PRK07514 348 IGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIIS-GGYNVYPKEVEGEI---DELP 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 520 EVV---VYG--ERDeYGEQiITAEVfpsveelakVLETNAkDIDTSVLTGSVAEglvkdaiskankELQNFKKVKDIVLR 594
Cdd:PRK07514 424 GVVesaVIGvpHPD-FGEG-VTAVV---------VPKPGA-ALDEAAILAALKG------------RLARFKQPKRVFFV 479
|
570
....*....|....*...
gi 1360655949 595 AEpFPRNT----SKKILR 608
Cdd:PRK07514 480 DE-LPRNTmgkvQKNLLR 496
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
204-539 |
2.64e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 137.44 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 204 ANGNTQYDNLP-IDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEF--DKNDTLLSVLPLHHTFEATAGFLL 280
Cdd:PRK05605 204 IGGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGlgDGPERVLAALPMFHAYGLTLCLTL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 281 PLSRGGKIAMNDGLR--HIAKNLQQSKTSILIAVPllleTLHKTILRKATgdakvakkyKLGLSLAKalnkiklnfndki 358
Cdd:PRK05605 284 AVSIGGELVLLPAPDidLILDAMKKHPPTWLPGVP----PLYEKIAEAAE---------ERGVDLSG------------- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 359 faeihkglgghLRLLVCGGAAIEPQILADfndW----GITAIQGYGVTECSPIISNN------RPKYkehasAGLPTPHV 428
Cdd:PRK05605 338 -----------VRNAFSGAMALPVSTVEL---WekltGGLLVEGYGLTETSPIIVGNpmsddrRPGY-----VGVPFPDT 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 429 EVKIINEDENGI-------GEIIARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGK 501
Cdd:PRK05605 399 EVRIVDPEDPDEtmpdgeeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGF 476
|
330 340 350
....*....|....*....|....*....|....*....
gi 1360655949 502 NIFPEEIEFVLLKENIIEEVVVYG-ERDEYGEQIITAEV 539
Cdd:PRK05605 477 NVYPAEVEEVLREHPGVEDAAVVGlPREDGSEEVVAAVV 515
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
57-608 |
3.35e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 136.17 E-value: 3.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 57 AINFRINPDN---EYRG--ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPA 131
Cdd:PRK06145 9 AFHARRTPDRaalVYRDqeISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 132 NEVENLINRSGANTIFYSRSQEdkllgiADNIKQVKNLVSYDLPTENSSKLAgedkdlfflwdlintgnsirANGNTQYD 211
Cdd:PRK06145 89 DEVAYILGDAGAKLLLVDEEFD------AIVALETPKIVIDAAAQADSRRLA--------------------QGGLEIPP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 212 NLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTfeatAGFLLPlsrGGKIAMN 291
Cdd:PRK06145 143 QAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHV----GAFDLP---GIAVLWV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 292 DGLRHIAKNLQQsktsiliavpllletlhKTILrkatgdAKVAKKYKLGLSLAKALNKIKLNFNDKIFAEIhkglgGHLR 371
Cdd:PRK06145 216 GGTLRIHREFDP-----------------EAVL------AAIERHRLTCAWMAPVMLSRVLTVPDRDRFDL-----DSLA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 372 LLVCGGAAIEPQILADFNDWGITA--IQGYGVTE-CS--PIISNNRpKYKEHASAGLPTPHVEVKIINED-----ENGIG 441
Cdd:PRK06145 268 WCIGGGEKTPESRIRDFTRVFTRAryIDAYGLTEtCSgdTLMEAGR-EIEKIGSTGRALAHVEIRIADGAgrwlpPNMKG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 442 EIIARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEV 521
Cdd:PRK06145 347 EICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEVERVIYELPEVAEA 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 522 VVYGERD-EYGEQIitaevfpsveelakvletnakdidTSVLTGSVAEGLVKDAISK-ANKELQNFKKVKDIVLRAEpFP 599
Cdd:PRK06145 425 AVIGVHDdRWGERI------------------------TAVVVLNPGATLTLEALDRhCRQRLASFKVPRQLKVRDE-LP 479
|
....*....
gi 1360655949 600 RNTSKKILR 608
Cdd:PRK06145 480 RNPSGKVLK 488
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
69-608 |
4.83e-34 |
|
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: 136.60 E-value: 4.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGiSKDDKVIILAETRYEWYITYLATVCGLAIIAPMDkeLPANevenlinrsgantify 148
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP--PPTP---------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 149 sRSQEDKLLGIADNIkQVKNLVS----YDLPTENSSKLAGEDKDLFFLWDLINTGnsiranGNTQYDNLPIDPRALAVLL 224
Cdd:cd05931 84 -GRHAERLAAILADA-GPRVVLTtaaaLAAVRAFAASRPAAGTPRLLVVDLLPDT------SAADWPPPSPDPDDIAYLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 225 FTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGkiamndglrhiaknlqqs 304
Cdd:cd05931 156 YTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGG------------------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 305 kTSIL------IAVPLL-LETLHKtilRKATGDA-----------KVAKKYKLGLSLakalnkiklnfndkifaeihkgl 366
Cdd:cd05931 218 -PSVLmspaafLRRPLRwLRLISR---YRATISAapnfaydlcvrRVRDEDLEGLDL----------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 367 gGHLRLLVCGGAAIEPQILADFND----WGI--TAIQ-GYGVTECSPIISNNRP-------------------------- 413
Cdd:cd05931 271 -SSWRVALNGAEPVRPATLRRFAEafapFGFrpEAFRpSYGLAEATLFVSGGPPgtgpvvlrvdrdalagravavaaddp 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 414 KYKEHASAGLPTPHVEVKIINED------ENGIGEIIARGPNVMLGYYEDPEKTAE------AIDSEGFYHTGDYGYIDD 481
Cdd:cd05931 350 AARELVSCGRPLPDQEVRIVDPEtgrelpDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLGFLHD 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 482 rGFIYITGRKANIIVtKNGKNIFPEEIEFVLlkENIIEE-----VVVYGERDEYGEQ-IITAEVFPSVEELAkvletnak 555
Cdd:cd05931 430 -GELYITGRLKDLII-VRGRNHYPQDIEATA--EEAHPAlrpgcVAAFSVPDDGEERlVVVAEVERGADPAD-------- 497
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1360655949 556 didtsvlTGSVAEGLVkDAISKANKElqnfkKVKDIVL-RAEPFPRNTSKKILR 608
Cdd:cd05931 498 -------LAAIAAAIR-AAVAREHGV-----APADVVLvRPGSIPRTSSGKIQR 538
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
219-547 |
4.06e-33 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 129.37 E-value: 4.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 219 ALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTfeataGFLLPLSR----GGKIAMNDGL 294
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHV-----GGLAILVRsllaGAELVLLERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 295 RHIAKNLQQSKTSILIAVPLLLETLhktiLRKATGDAKVAKkyklglslakalnkiklnfndkifaeihkglgghLRLLV 374
Cdd:cd17630 76 QALAEDLAPPGVTHVSLVPTQLQRL----LDSGQGPAALKS----------------------------------LRAVL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 375 CGGAAIEPQILADFNDWGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEdengiGEIIARGPNVMLGY 454
Cdd:cd17630 118 LGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----GEIWVGGASLAMGY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 455 YEDPEKtaEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERD-EYGEQ 533
Cdd:cd17630 193 LRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAALAAHPAVRDAFVVGVPDeELGQR 269
|
330
....*....|....*..
gi 1360655949 534 IITAEVF---PSVEELA 547
Cdd:cd17630 270 PVAVIVGrgpADPAELR 286
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
19-546 |
4.78e-33 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 133.27 E-value: 4.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 19 SRDLREMIERSASLYAEENAFLLKDpvalRELDPRseaainfrinpdnEYrgiTYRQVNEDRKALGSAMLDLGISKDDKV 98
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIFES----SGGVVR-------------RY---SYLELNEEINRTANLFYSLGIRKGDKV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 99 IILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFysrsQEDKLLGIADNIKQ-----VKNLVsyd 173
Cdd:PRK08008 66 ALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLV----TSAQFYPMYRQIQQedatpLRHIC--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 174 LPTENSSKLAGedkdlfflwdlINTGNSIRANGNTQYDNL-PIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCL 252
Cdd:PRK08008 139 LTRVALPADDG-----------VSSFTQLKAQQPATLCYApPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAW 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 253 TVEFDKNDTLLSVLPLHHT-FEATAgfLLP-LSRGGKIAMND--GLRHIAKNLQQSKTSILIAVPLLLETLhktILRKAT 328
Cdd:PRK08008 208 QCALRDDDVYLTVMPAFHIdCQCTA--AMAaFSAGATFVLLEkySARAFWGQVCKYRATITECIPMMIRTL---MVQPPS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 329 GDAKVAK----KYKLGLSLAKalnkiKLNFNDKifaeihkglgghlrllvcggaaiepqiladfndWGITAIQGYGVTEC 404
Cdd:PRK08008 283 ANDRQHClrevMFYLNLSDQE-----KDAFEER---------------------------------FGVRLLTSYGMTET 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 405 SPIISNNRPKYKEH-ASAGLPTPHVEVKIINED-----ENGIGEIIARG---PNVMLGYYEDPEKTAEAIDSEGFYHTGD 475
Cdd:PRK08008 325 IVGIIGDRPGDKRRwPSIGRPGFCYEAEIRDDHnrplpAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGD 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1360655949 476 YGYIDDRGFIYITGRKANIIvTKNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAEVFP------SVEEL 546
Cdd:PRK08008 405 TGYVDEEGFFYFVDRRCNMI-KRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLnegetlSEEEF 480
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
72-614 |
6.95e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 132.80 E-value: 6.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSRS 151
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 152 QEDKLLGIA--DNIKqvknLVSYDLPTENSsklagedkdLFFlWDLINTGNSirangntQYDNLPIDPRALAVLLFTSGT 229
Cdd:PLN02246 132 YVDKLKGLAedDGVT----VVTIDDPPEGC---------LHF-SELTQADEN-------ELPEVEISPDDVVALPYSSGT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 230 TAKSKAVMLCHDNL--CV---------NIYdvcltveFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIA------MND 292
Cdd:PLN02246 191 TGLPKGVMLTHKGLvtSVaqqvdgenpNLY-------FHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILimpkfeIGA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 293 GLRHIaknlQQSKTSILIAVPLLLETLHKTilrkatgdaKVAKKYKLG-----LSLAKALNKiklnfndkifaEIHKGLG 367
Cdd:PLN02246 264 LLELI----QRHKVTIAPFVPPIVLAIAKS---------PVVEKYDLSsirmvLSGAAPLGK-----------ELEDAFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 368 GHLRLLVCGgaaiepqiladfndwgitaiQGYGVTECSPIISNNRPKYKE-----HASAGLPTPHVEVKIINED------ 436
Cdd:PLN02246 320 AKLPNAVLG--------------------QGYGMTEAGPVLAMCLAFAKEpfpvkSGSCGTVVRNAELKIVDPEtgaslp 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 437 ENGIGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFPEEIEFVLLKEN 516
Cdd:PLN02246 380 RNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYK-GFQVAPAELEALLISHP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 517 IIEEVVVYGERDEygeqiITAEVfPsveeLAKVLETNAKDIdtsvltgsvAEGLVKDAISkanKELQNFKKVKDiVLRAE 596
Cdd:PLN02246 459 SIADAAVVPMKDE-----VAGEV-P----VAFVVRSNGSEI---------TEDEIKQFVA---KQVVFYKRIHK-VFFVD 515
|
570
....*....|....*...
gi 1360655949 597 PFPRNTSKKILRnKEQRN 614
Cdd:PLN02246 516 SIPKAPSGKILR-KDLRA 532
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
72-523 |
8.16e-33 |
|
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: 130.46 E-value: 8.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDL-GISKDDKVIILAETRYEWYITYLATV-CGLAIIaPMDKELPANEVENLINRSGANTIFYS 149
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLkAGAAYV-PLDPAYPAERLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 150 RSQEDKLLGIADNIKQVKNLVSYDLPTENSSKLAGEdkdlfflwdlintgnsirangntqydnlPIDPRALAVLLFTSGT 229
Cdd:TIGR01733 80 SALASRLAGLVLPVILLDPLELAALDDAPAPPPPDA----------------------------PSGPDDLAYVIYTSGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 230 TAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHH---TFEatagFLLPLSRGGKIA------MNDGLRHIAKN 300
Cdd:TIGR01733 132 TGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFdasVEE----IFGALLAGATLVvppedeERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 301 LQQSKTSILIAVPLLLETLhktilrkatgdakvakkyklglslakalnkiklnfndkifAEIHKGLGGHLRLLVCGGAAI 380
Cdd:TIGR01733 208 IAEHPVTVLNLTPSLLALL----------------------------------------AAALPPALASLRLVILGGEAL 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 381 EPQ----ILADFNDWGItaIQGYGVTECSPIISNNR-----PKYKEHASAGLPTPHVEVKIINEDEN-----GIGEIIAR 446
Cdd:TIGR01733 248 TPAlvdrWRARGPGARL--INLYGPTETTVWSTATLvdpddAPRESPVPIGRPLANTRLYVLDDDLRpvpvgVVGELYIG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 447 GPNVMLGYYEDPEKTAEAI--------DSEGFYHTGDYGYIDDRGFIYITGRKANIIvtK-NGKNIFPEEIEFVLLKENI 517
Cdd:TIGR01733 326 GPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQV--KiRGYRIELGEIEAALLRHPG 403
|
....*.
gi 1360655949 518 IEEVVV 523
Cdd:TIGR01733 404 VREAVV 409
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
44-610 |
2.09e-32 |
|
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: 131.64 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 44 PVALRELDPRS------EAAINFR------INPDNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYIT 111
Cdd:cd05906 1 PLHRPEGAPRTllelllRAAERGPtkgityIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 112 YLATVCGLAIIAP----MDKELPANEVENLINRS---GANTIFYSRSQEDKLLGIAdnikqvknlvsYDLPTENSSKLAG 184
Cdd:cd05906 81 FWACVLAGFVPAPltvpPTYDEPNARLRKLRHIWqllGSPVVLTDAELVAEFAGLE-----------TLSGLPGIRVLSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 185 EDKDlfflwdlintgnsiraNGNTQYDNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLS 264
Cdd:cd05906 150 EELL----------------DTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 265 VLPLHHTFEATAGFLLPLSRGGkiamndglRHIaknlqQSKTSILIAVPLL-LETLHKtilrkatgdakvakkYKLGLSL 343
Cdd:cd05906 214 WVPLDHVGGLVELHLRAVYLGC--------QQV-----HVPTEEILADPLRwLDLIDR---------------YRVTITW 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 344 AK--ALNKIkLNFNDKIfaEIHKGLGGHLRLLVCGGAAIEPQILADFND----WGI--TAIQ-GYGVTE-CSPIISNNRP 413
Cdd:cd05906 266 APnfAFALL-NDLLEEI--EDGTWDLSSLRYLVNAGEAVVAKTIRRLLRllepYGLppDAIRpAFGMTEtCSGVIYSRSF 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 414 KYKEH------ASAGLPTPHVEVKIINEDENG-----IGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDr 482
Cdd:cd05906 343 PTYDHsqalefVSLGRPIPGVSMRIVDDEGQLlpegeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 483 GFIYITGR-KANIIVtkNGKNIFPEEIEFVLLKENIIEE--VVVYGERDEYGEQIITAEVFPSVEELAKVLETNAKDIdT 559
Cdd:cd05906 422 GNLTITGRtKDTIIV--NGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAI-R 498
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1360655949 560 SVLTGSVaeGLVKDAIskankelqnfkkvkdIVLRAEPFPRNTSKKILRNK 610
Cdd:cd05906 499 SVVSREV--GVSPAYL---------------IPLPKEEIPKTSLGKIQRSK 532
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
61-597 |
2.62e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 132.09 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 61 RINPDNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDkelPAnevenlinr 140
Cdd:PRK12582 71 REPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVS---PA--------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 141 sgantifYSRSQED--KLLGIADNIKQVKNLVSYDLPTENSSKLAGEDKDlfflwDLINTGNSIRANGNTQYDNL----- 213
Cdd:PRK12582 139 -------YSLMSHDhaKLKHLFDLVKPRVVFAQSGAPFARALAALDLLDV-----TVVHVTGPGEGIASIAFADLaatpp 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 214 ---------PIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKND---TLLSVLPLHHTFEATAGFLLP 281
Cdd:PRK12582 207 taavaaaiaAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPpppVSLDWMPWNHTMGGNANFNGL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 282 LSRGGKIAMNDGLrhiaknlqqsktsiliAVPlllETLHKTI--LRK----ATGDAKVAkkYKLglsLAKALNKiklnfN 355
Cdd:PRK12582 287 LWGGGTLYIDDGK----------------PLP---GMFEETIrnLREisptVYGNVPAG--YAM---LAEAMEK-----D 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 356 DKIFAEIHKglggHLRLLVCGGAAIEPQILADFNDWGITAI-------QGYGVTECSPIISNNRPKYKEHASAGLPTPHV 428
Cdd:PRK12582 338 DALRRSFFK----NLRLMAYGGATLSDDLYERMQALAVRTTghripfyTGYGATETAPTTTGTHWDTERVGLIGLPLPGV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 429 EVKIINedengIG---EIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYG-YIDD----RGFIYiTGRkaniiVTKNG 500
Cdd:PRK12582 414 ELKLAP-----VGdkyEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAArFVDPddpeKGLIF-DGR-----VAEDF 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 501 K-------NIFPEEIEFVLLKENIIEEVVVYGERDEYgeqiITAEVFPSVEELAKVLETNAKDIDTSVLTGSVAEGLvKD 573
Cdd:PRK12582 483 KlstgtwvSVGTLRPDAVAACSPVIHDAVVAGQDRAF----IGLLAWPNPAACRQLAGDPDAAPEDVVKHPAVLAIL-RE 557
|
570 580
....*....|....*....|....*
gi 1360655949 574 AISKANKELQNF-KKVKDIVLRAEP 597
Cdd:PRK12582 558 GLSAHNAEAGGSsSRIARALLMTEP 582
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
69-615 |
9.24e-32 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 129.92 E-value: 9.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAeTRYEWYITY-LATVCGLAIIAPMD-----KElpANEVENLINRSG 142
Cdd:PLN02860 31 RRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAA-LNSDLYLEWlLAVACAGGIVAPLNyrwsfEE--AKSAMLLVRPVM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 143 ANTIFYSRSQEDKLLgiADNIKQVKNLVSYDLPTENSSklagedkdlFFLWDLINTGNSIRANGNTQYDNLPIDPRALAV 222
Cdd:PLN02860 108 LVTDETCSSWYEELQ--NDRLPSLMWQVFLESPSSSVF---------IFLNSFLTTEMLKQRALGTTELDYAWAPDDAVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 223 LLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTfeatAGfllpLSRGGKIAMNdGLRHI----- 297
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHI----GG----LSSALAMLMV-GACHVllpkf 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 298 -AKN----LQQSKTSILIAVPLLLETLHKTILRKATGdakvakkyKLGLSLAKALNkiklnfndkifaeihkGLGGHLRL 372
Cdd:PLN02860 248 dAKAalqaIKQHNVTSMITVPAMMADLISLTRKSMTW--------KVFPSVRKILN----------------GGGSLSSR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 373 LVCGGAAIEPQIlADFNDWGIT--------------AIQGYGVTECSPIISNNRPKYKEHAS-AGLPTPHVEVKIINEDE 437
Cdd:PLN02860 304 LLPDAKKLFPNA-KLFSAYGMTeacssltfmtlhdpTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAPHVELKIGLDES 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 438 NGIGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENI 517
Cdd:PLN02860 383 SRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKT-GGENVYPEEVEAVLSQHPG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 518 IEEVVVYGERDEYGEQIITAEVfpSVEELAKVLETNAKDIDTSVLtgsVAEGLVKDAISKanKELQNFKKVKDIVLRAEP 597
Cdd:PLN02860 462 VASVVVVGVPDSRLTEMVVACV--RLRDGWIWSDNEKENAKKNLT---LSSETLRHHCRE--KNLSRFKIPKLFVQWRKP 534
|
570
....*....|....*...
gi 1360655949 598 FPRNTSKKILRNKEQRNV 615
Cdd:PLN02860 535 FPLTTTGKIRRDEVRREV 552
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
216-490 |
1.72e-31 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 130.86 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 216 DPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGLR 295
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSPL 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 296 H---IAKNLQQSKTSILIAVPLLLetlhktilrkaTGDAKVAKKYklglslakalnkiklNFNDkifaeihkglgghLRL 372
Cdd:PRK06814 871 HyriIPELIYDTNATILFGTDTFL-----------NGYARYAHPY---------------DFRS-------------LRY 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 373 LVCGGaaiEPQILADFNDW----GITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIinEDENGI---GEIIA 445
Cdd:PRK06814 912 VFAGA---EKVKEETRQTWmekfGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRL--EPVPGIdegGRLFV 986
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1360655949 446 RGPNVMLGYYeDPEK--TAEAIdSEGFYHTGDYGYIDDRGFIYITGR 490
Cdd:PRK06814 987 RGPNVMLGYL-RAENpgVLEPP-ADGWYDTGDIVTIDEEGFITIKGR 1031
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
214-548 |
4.71e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 127.96 E-value: 4.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 214 PIDPRA--LAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKND---TLLSVLPLHHTFEATAGFLlplsrggki 288
Cdd:PRK05677 201 EANPQAddVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYHIYAFTFHCM--------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 289 AMNDGLRHiaknlqqsktSILIAVPllletlhktilRKATGDAKVAKKYK----LGL-SLAKALnkiklnFNDKIFAEIH 363
Cdd:PRK05677 272 AMMLIGNH----------NILISNP-----------RDLPAMVKELGKWKfsgfVGLnTLFVAL------CNNEAFRKLD 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 364 KGlggHLRLLVCGGAAIEpqiLADFNDW----GITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDEN- 438
Cdd:PRK05677 325 FS---ALKLTLSGGMALQ---LATAERWkevtGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNe 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 439 ----GIGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLK 514
Cdd:PRK05677 399 lplgEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILV-SGFNVYPNELEDVLAA 477
|
330 340 350
....*....|....*....|....*....|....*
gi 1360655949 515 ENIIEEVVVYGERDE-YGEQIITAEVFPSVEELAK 548
Cdd:PRK05677 478 LPGVLQCAAIGVPDEkSGEAIKVFVVVKPGETLTK 512
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
72-532 |
8.95e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 126.07 E-value: 8.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSgantifysrs 151
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDA---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 152 qEDKLLgIADNIKQvknlvsydlptenSSKLAGEDKDLFflwdlintgnSIRANGNTQYDNLPIDPRALAVLLFTSGTTA 231
Cdd:PRK09088 94 -EPRLL-LGDDAVA-------------AGRTDVEDLAAF----------IASADALEPADTPSIPPERVSLILFTSGTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 232 KSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGLRHIAKNLQQSKTSILIA 311
Cdd:PRK09088 149 QPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPALGIT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 312 ----VPLLLEtlhktILRKATGDAkvakkyklglslAKALnkiklnfndkifaeihkglgGHLRLLVCGGAaiePQILAD 387
Cdd:PRK09088 229 hyfcVPQMAQ-----AFRAQPGFD------------AAAL--------------------RHLTALFTGGA---PHAAED 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 388 FNDW---GITAIQGYGVTECSPI--ISNNRPKYKEHA-SAGLPTPHVEVKIINEDENGI-----GEIIARGPNVMLGYYE 456
Cdd:PRK09088 269 ILGWlddGIPMVDGFGMSEAGTVfgMSVDCDVIRAKAgAAGIPTPTVQTRVVDDQGNDCpagvpGELLLRGPNLSPGYWR 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1360655949 457 DPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERD-EYGE 532
Cdd:PRK09088 349 RPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFIS-GGENVYPAEIEAVLADHPGIRECAVVGMADaQWGE 424
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
64-581 |
3.72e-30 |
|
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: 125.24 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 64 PDNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYE-WYITYLATVCGLAIiAPMDkelPAnevenlinrsg 142
Cdd:cd05921 19 GNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEhALMALAAMYAGVPA-APVS---PA----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 143 antifYSRSQED--KLLGIADNIK--------------QVKNLVSYDLPTEnSSKLAGEDKDLFFLWDLINT---GNSIR 203
Cdd:cd05921 84 -----YSLMSQDlaKLKHLFELLKpglvfaqdaapfarALAAIFPLGTPLV-VSRNAVAGRGAISFAELAATpptAAVDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 204 ANGNTQydnlpidPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDV--CLTVEFDKNDTLLSVLPLHHTFEATAGFLLP 281
Cdd:cd05921 158 AFAAVG-------PDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLeqTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 282 LSRGGKIAMNDG------LRHIAKNLQQSKTSILIAVPLLLETLHKTiLRKatgDAKVAKKYklglslakalnkiklnfn 355
Cdd:cd05921 231 LYNGGTLYIDDGkpmpggFEETLRNLREISPTVYFNVPAGWEMLVAA-LEK---DEALRRRF------------------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 356 dkiFAEihkglgghLRLLVCGGAAIEPQILADFNDWG-------ITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHV 428
Cdd:cd05921 289 ---FKR--------LKLMFYAGAGLSQDVWDRLQALAvatvgerIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 429 EVKIINEDenGIGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDD-----RGFIYiTGRkaniiVTKNGK-- 501
Cdd:cd05921 358 ELKLVPSG--GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADpddpaKGLVF-DGR-----VAEDFKla 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 502 -----NIFPEEIEFVLLKENIIEEVVVYGE-RDEYGeqiitAEVFPSVEELAKVLETNAKDiDTSVLTGSVAEGLVKDAI 575
Cdd:cd05921 430 sgtwvSVGPLRARAVAACAPLVHDAVVAGEdRAEVG-----ALVFPDLLACRRLVGLQEAS-DAEVLRHAKVRAAFRDRL 503
|
....*.
gi 1360655949 576 SKANKE 581
Cdd:cd05921 504 AALNGE 509
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
72-610 |
4.76e-30 |
|
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: 123.95 E-value: 4.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLAT-VCGlAIIAPMDKELPANEVENLINRSGANTIFysr 150
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVpMAG-AVLNALNTRLDAEEIAFILRHSEAKVLF--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 sqedkllgiadnikqvknlVSYDLPTEnsSKLAGEDKDlfFLWdlintgnsIRangntqydnlPIDPRALAVLLFTSGTT 230
Cdd:cd12118 107 -------------------VDREFEYE--DLLAEGDPD--FEW--------IP----------PADEWDPIALNYTSGTT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 231 AKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTfeatAGFLLPLSRGGKIAMNDGLRH-----IAKNLQQSK 305
Cdd:cd12118 146 GRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHC----NGWCFPWTVAAVGGTNVCLRKvdakaIYDLIEKHK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 306 TSILIAVPLLLETLhktilrkatgdakvakkyklglslAKALNKIKLNFNDKIFAEIhkglgghlrllvcGGAAIEPQIL 385
Cdd:cd12118 222 VTHFCGAPTVLNML------------------------ANAPPSDARPLPHRVHVMT-------------AGAPPPAAVL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 386 ADFNDWGITAIQGYGVTECSPIIS--------NNRP---KYKEHASAGLPTPHVE-VKIIN--------EDENGIGEIIA 445
Cdd:cd12118 265 AKMEELGFDVTHVYGLTETYGPATvcawkpewDELPteeRARLKARQGVRYVGLEeVDVLDpetmkpvpRDGKTIGEIVF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 446 RGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFPEEIEFVLLKENIIEEVVVYG 525
Cdd:cd12118 345 RGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISG-GENISSVEVEGVLYKHPAVLEAAVVA 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 526 ERDEY-GEqiiTAEVFPSVEELAKVLEtnakdidtsvltgsvaeglvKDAISKANKELQNFKKVKDIVLRaePFPRNTSK 604
Cdd:cd12118 423 RPDEKwGE---VPCAFVELKEGAKVTE--------------------EEIIAFCREHLAGFMVPKTVVFG--ELPKTSTG 477
|
....*.
gi 1360655949 605 KILRNK 610
Cdd:cd12118 478 KIQKFV 483
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
72-611 |
7.67e-30 |
|
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: 122.45 E-value: 7.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSrs 151
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 152 QEDkllgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpidpraLAVLLFTSGTTA 231
Cdd:cd05972 80 AED-----------------------------------------------------------------PALIYFTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 232 KSKAVMLCHDNLCVNIYDVCLTVEFDKNDtllsvlpLHHTFEATA-------GFLLPLSRGGKIAMNDGLRHIAKN---- 300
Cdd:cd05972 95 LPKGVLHTHSYPLGHIPTAAYWLGLRPDD-------IHWNIADPGwakgawsSFFGPWLLGATVFVYEGPRFDAERilel 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 301 LQQSKTSILIAVPllletlhkTILRKatgdakvakkyklglsLAKALnkiklnfndkifaeIHKGLGGHLRLLVCGGAAI 380
Cdd:cd05972 168 LERYGVTSFCGPP--------TAYRM----------------LIKQD--------------LSSYKFSHLRLVVSAGEPL 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 381 EPQILADFND-WGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDENGI-----GEI-IARGPNVM-L 452
Cdd:cd05972 210 NPEVIEWWRAaTGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELppgeeGDIaIKLPPPGLfL 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 453 GYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGE 532
Cdd:cd05972 290 GYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKS-SGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRG 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1360655949 533 QIITAEVfpsveelakVLETNAKDIDTsvltgsvaegLVKDAISKANKELQNFKKVKDIVLRAEpFPRNTSKKILRNKE 611
Cdd:cd05972 368 EVVKAFV---------VLTSGYEPSEE----------LAEELQGHVKKVLAPYKYPREIEFVEE-LPKTISGKIRRVEL 426
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
69-610 |
1.58e-29 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 122.48 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFY 148
Cdd:cd05959 28 GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 149 SrsQEdkllgIADNIKQVKNLVSYDLPTENSSKLAGEDKDLFFLWDLINTGNSIRANGNTQYDnlpiDPralAVLLFTSG 228
Cdd:cd05959 108 S--GE-----LAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAATHAD----DP---AFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 229 TTAKSKAVMLCHDNLCV--NIY--DVCLTVEfdkNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGL---RHIAKNL 301
Cdd:cd05959 174 STGRPKGVVHLHADIYWtaELYarNVLGIRE---DDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERptpAAVFKRI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 302 QQSKTSILIAVPllleTLHKTILRkatgdAKVAKKYklGLSlakalnkiklnfndkifaeihkglggHLRLLVCGGAAIE 381
Cdd:cd05959 251 RRYRPTVFFGVP----TLYAAMLA-----APNLPSR--DLS--------------------------SLRLCVSAGEALP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 382 PQIladFNDW----GITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDEN-----GIGEIIARGPNVML 452
Cdd:cd05959 294 AEV---GERWkarfGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGdvadgEPGELYVRGPSSAT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 453 GYYEDPEKTAEAIDSEGFYhTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGE 532
Cdd:cd05959 371 MYWNNRDKTRDTFQGEWTR-TGDKYVRDDDGFYTYAGRADDMLKV-SGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 533 QIITAEVfpsveelakVLETNAKDidtsvlTGSVAEGL---VKDAiskankeLQNFKKVKDIVLRAEpFPRNTSKKILRN 609
Cdd:cd05959 449 TKPKAFV---------VLRPGYED------SEALEEELkefVKDR-------LAPYKYPRWIVFVDE-LPKTATGKIQRF 505
|
.
gi 1360655949 610 K 610
Cdd:cd05959 506 K 506
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
69-532 |
1.97e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 122.76 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALgSAML--DLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTI 146
Cdd:PRK08314 34 RAISYRELLEEAERL-AGYLqqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 147 FYSRSQEDKLLGiADNIKQVKNLVSYD----LPTENSSKL-----------AGEDKDLFFLWDLINTGNSIRAngntqyd 211
Cdd:PRK08314 113 IVGSELAPKVAP-AVGNLRLRHVIVAQysdyLPAEPEIAVpawlraepplqALAPGGVVAWKEALAAGLAPPP------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 212 nLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAM- 290
Cdd:PRK08314 185 -HTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLm 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 291 -----NDGLRHIAKNLQQSKTSI------LIAVPllletlhktilrkatgdakvakkyklglslakalnkiklNFNDKIF 359
Cdd:PRK08314 264 prwdrEAAARLIERYRVTHWTNIptmvvdFLASP---------------------------------------GLAERDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 360 AEihkglgghLRLLVCGGAAIePQILAD--FNDWGITAIQGYGVTEC-SPIISN--NRPKYKehaSAGLPTPHVEVKIIN 434
Cdd:PRK08314 305 SS--------LRYIGGGGAAM-PEAVAErlKELTGLDYVEGYGLTETmAQTHSNppDRPKLQ---CLGIPTFGVDARVID 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 435 ED------ENGIGEIIARGPNVMLGYYEDPEKTAEA---IDSEGFYHTGDYGYIDDRGFIYITGRKANIIvTKNGKNIFP 505
Cdd:PRK08314 373 PEtleelpPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMI-NASGFKVWP 451
|
490 500
....*....|....*....|....*...
gi 1360655949 506 EEIEFVLLKENIIEEVVVYGERDEY-GE 532
Cdd:PRK08314 452 AEVENLLYKHPAIQEACVIATPDPRrGE 479
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-532 |
2.06e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 119.89 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 220 LAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAM-------ND 292
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyrNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 293 GL-RHIAKNLQQSKTSILIAVPLLLetlhkTILRKATGDAKVakkyklglslakalnkiklnfndkifaeihkglgGHLR 371
Cdd:cd05944 84 GLfDNFWKLVERYRITSLSTVPTVY-----AALLQVPVNADI----------------------------------SSLR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 372 LLVCGGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKY-KEHASAGLPTPHVEVKIINEDENG---------- 439
Cdd:cd05944 125 FAMSGAAPLPVELRARFEDaTGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGLRLPYARVRIKVLDGVGrllrdcapde 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 IGEIIARGPNVMLGYYEDpEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVtKNGKNIFPEEIEFVLLKENIIE 519
Cdd:cd05944 205 VGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLII-RGGHNIDPALIEEALLRHPAVA 282
|
330
....*....|....
gi 1360655949 520 EVVVYGERDEY-GE 532
Cdd:cd05944 283 FAGAVGQPDAHaGE 296
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
71-551 |
7.27e-29 |
|
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: 119.55 E-value: 7.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATV-CGLAIIaPMDKELPANEVENLINRSGANTIFYs 149
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLkAGAAYV-PLDPSYPAERLAYILEDSGAKLVLT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 150 rsqedkllgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpiDPRALAVLLFTSGT 229
Cdd:cd05930 91 ------------------------------------------------------------------DPDDLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 230 TAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLhhTFEATAG-FLLPLSRGGKI------AMNDGlRHIAKNLQ 302
Cdd:cd05930 105 TGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSF--SFDVSVWeIFGALLAGATLvvlpeeVRKDP-EALADLLA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 303 QSKTSILIAVPllletlhktilrkatgdakvakkyklglSLAKALnkiklnfndkiFAEIHKGLGGHLRLLVCGGAAIEP 382
Cdd:cd05930 182 EEGITVLHLTP----------------------------SLLRLL-----------LQELELAALPSLRLVLVGGEALPP 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 383 QILADFND--WGITAIQGYGVTECSPIISNNRPKYKEHASA----GLPTPHVEVKIINEDEN-----GIGEIIARGPNVM 451
Cdd:cd05930 223 DLVRRWREllPGARLVNLYGPTEATVDATYYRVPPDDEEDGrvpiGRPIPNTRVYVLDENLRpvppgVPGELYIGGAGLA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 452 LGYYEDPEKTAEAI------DSEGFYHTGDYGYIDDRG-FIYItGRKANIIvtK-NGKNIFPEEIEFVLLKENIIEEVVV 523
Cdd:cd05930 303 RGYLNRPELTAERFvpnpfgPGERMYRTGDLVRWLPDGnLEFL-GRIDDQV--KiRGYRIELGEIEAALLAHPGVREAAV 379
|
490 500 510
....*....|....*....|....*....|....
gi 1360655949 524 YGERDEYGEQIITA------EVFPSVEELAKVLE 551
Cdd:cd05930 380 VAREDGDGEKRLVAyvvpdeGGELDEEELRAHLA 413
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
225-608 |
7.85e-29 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 117.12 E-value: 7.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 225 FTSGTTAKSKAVMLCHDN----LCVNIYDVCLTVEfdknDTLLSVLPLHHTFeATAGFLLPLSRGGKI---AMNDGLRHI 297
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSwiesFVCNEDLFNISGE----DAILAPGPLSHSL-FLYGAISALYLGGTFigqRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 298 AKnLQQSKTSILIAVPLLLETLhktiLRKATGDAKVakkyklglslakalnKIKLNFNDKIFAEIHKGLgghlrllvcgg 377
Cdd:cd17633 82 RK-INQYNATVIYLVPTMLQAL----ARTLEPESKI---------------KSIFSSGQKLFESTKKKL----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 378 AAIEPQI-LADFndwgitaiqgYGVTECSPIISN-NRPKYKEHaSAGLPTPHVEVKIINEDENGIGEIIARGPNVMLGYY 455
Cdd:cd17633 131 KNIFPKAnLIEF----------YGTSELSFITYNfNQESRPPN-SVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 456 edpekTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQII 535
Cdd:cd17633 200 -----RGGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1360655949 536 TAevfpsveelakvletnakdidtsVLTGsvaEGLV-KDAISKANKELQNFKKVKDIVlRAEPFPRNTSKKILR 608
Cdd:cd17633 274 VA-----------------------LYSG---DKLTyKQLKRFLKQKLSRYEIPKKII-FVDSLPYTSSGKIAR 320
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
71-608 |
4.34e-28 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 118.79 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLD-LGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYS 149
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 150 RSQEDKLLGIADNIKQVKNLVSYDLPTENSSKlagedkdlfFLWDLINTGNSIRANGNTQYDnlpidpraLAVLLFTSGT 229
Cdd:PLN02574 147 PENVEKLSPLGVPVIGVPENYDFDSKRIEFPK---------FYELIKEDFDFVPKPVIKQDD--------VAAIMYSSGT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 230 TAKSKAVMLCHDNLcvnIYDVCLTVEFDK--------NDTLLSVLPLHHTFeatagfllplsrggkiamndGLRhiaknl 301
Cdd:PLN02574 210 TGASKGVVLTHRNL---IAMVELFVRFEAsqyeypgsDNVYLAALPMFHIY--------------------GLS------ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 302 qqsktsiLIAVPLLleTLHKTILrkatgdakVAKKYKLGlSLAKALNKIKLN----FNDKIFAEIH--KGLGGH----LR 371
Cdd:PLN02574 261 -------LFVVGLL--SLGSTIV--------VMRRFDAS-DMVKVIDRFKVThfpvVPPILMALTKkaKGVCGEvlksLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 372 LLVCGGAAIEPQILADFNDW--GITAIQGYGVTECSPIISN--NRPKYKEHASAGLPTPHVEVKIINEDE------NGIG 441
Cdd:PLN02574 323 QVSCGAAPLSGKFIQDFVQTlpHVDFIQGYGMTESTAVGTRgfNTEKLSKYSSVGLLAPNMQAKVVDWSTgcllppGNCG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 442 EIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFPEEIEFVLLKENIIEEV 521
Cdd:PLN02574 403 ELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYK-GFQIAPADLEAVLISHPEIIDA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 522 VVYGERDEYGEQIITAEVFPSVEelakvletnakdidtSVLTGSvaeglvkDAISKANKELQNFKKVKDIVLrAEPFPRN 601
Cdd:PLN02574 482 AVTAVPDKECGEIPVAFVVRRQG---------------STLSQE-------AVINYVAKQVAPYKKVRKVVF-VQSIPKS 538
|
....*..
gi 1360655949 602 TSKKILR 608
Cdd:PLN02574 539 PAGKILR 545
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
211-509 |
8.40e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 117.79 E-value: 8.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 211 DNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFD-KNDTLLSVLPLHHTFEATAGFLLPLSRGG--- 286
Cdd:PRK07768 145 DPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAelv 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 287 KIAMNDGLRHiaknlqqsktsiliavPLL-LETLHKtilRKATGDAKVAKKYKLglsLAKALNKiklnfndkifAEIHKG 365
Cdd:PRK07768 225 KVTPMDFLRD----------------PLLwAELISK---YRGTMTAAPNFAYAL---LARRLRR----------QAKPGA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 366 LG-GHLRLLVCGGAAIEPQILADFNDWGI------TAI-QGYGVTECSPIIS--------------------------NN 411
Cdd:PRK07768 273 FDlSSLRFALNGAEPIDPADVEDLLDAGArfglrpEAIlPAYGMAEATLAVSfspcgaglvvdevdadllaalrravpAT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 412 RPKYKEHASAGLPTPHVEVKIINED-----ENGIGEIIARGPNVMLGYYeDPEKTAEAIDSEGFYHTGDYGYIDDRGFIY 486
Cdd:PRK07768 353 KGNTRRLATLGPPLPGLEVRVVDEDgqvlpPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVV 431
|
330 340
....*....|....*....|...
gi 1360655949 487 ITGRKANIIVTkNGKNIFPEEIE 509
Cdd:PRK07768 432 VCGRVKDVIIM-AGRNIYPTDIE 453
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
216-608 |
8.91e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 117.01 E-value: 8.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 216 DPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKiamndgLR 295
Cdd:PRK07787 126 DPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNR------FV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 296 HIAK-------NLQQSKTSILIAVPllletlhkTILRKATGDAKVAKkyklglSLAKAlnkiklnfndkifaeihkglgg 368
Cdd:PRK07787 200 HTGRptpeayaQALSEGGTLYFGVP--------TVWSRIAADPEAAR------ALRGA---------------------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 369 hlRLLVCGGAAIEPQILADFNDW-GITAIQGYGVTECSPIIS-----NNRPKYkehasAGLPTPHVEVKIINE------- 435
Cdd:PRK07787 244 --RLLVSGSAALPVPVFDRLAALtGHRPVERYGMTETLITLStradgERRPGW-----VGLPLAGVETRLVDEdggpvph 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 436 DENGIGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKNIFPEEIEFVLLKE 515
Cdd:PRK07787 317 DGETVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGH 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 516 NIIEEVVVYGERDEYGEQIITAEVFPsveelakvletnAKDIDTSVLTGSVAEGLvkdAISKANKElqnfkkvkdiVLRA 595
Cdd:PRK07787 397 PGVREAAVVGVPDDDLGQRIVAYVVG------------ADDVAADELIDFVAQQL---SVHKRPRE----------VRFV 451
|
410
....*....|...
gi 1360655949 596 EPFPRNTSKKILR 608
Cdd:PRK07787 452 DALPRNAMGKVLK 464
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
64-608 |
1.18e-27 |
|
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: 116.84 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 64 PDNEYRgITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGA 143
Cdd:cd05923 23 PARGLR-LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 144 NTIFYSrsqedkllgiadNIKQvknlvsydlPTENSSKLAGEdkdLFFLWDLINTGNsirangNTQYDNLPID----PRA 219
Cdd:cd05923 102 TAAVIA------------VDAQ---------VMDAIFQSGVR---VLALSDLVGLGE------PESAGPLIEDpprePEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 220 LAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVE--FDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAM--NDGLR 295
Cdd:cd05923 152 PAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGlrHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVveEFDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 296 HIAKNLQQSKTSILIAVPLLLetlhktilrkatgDAKVAKKYKLGLSLaKALNKIklnfndkIFAeihkglgghlrllvc 375
Cdd:cd05923 232 DALKLIEQERVTSLFATPTHL-------------DALAAAAEFAGLKL-SSLRHV-------TFA--------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 376 gGAAIEPQILADFNDwgitAIQG-----YGVTEC--SPIISNNRPkykehASAGLPTPHVEVKII-----------NEDE 437
Cdd:cd05923 276 -GATMPDAVLERVNQ----HLPGekvniYGTTEAmnSLYMRDART-----GTEMRPGFFSEVRIVriggspdealaNGEE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 438 ngiGEII--ARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKE 515
Cdd:cd05923 346 ---GELIvaAAADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHPSEIERVLSRH 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 516 NIIEEVVVYGERDEYGEQIITAEVFPSVEELAkvletnAKDIDTSVLTgsvaeglvkdaiskanKELQNFKKVKDIVLRA 595
Cdd:cd05923 421 PGVTEVVVIGVADERWGQSVTACVVPREGTLS------ADELDQFCRA----------------SELADFKRPRRYFFLD 478
|
570
....*....|...
gi 1360655949 596 EpFPRNTSKKILR 608
Cdd:cd05923 479 E-LPKNAMNKVLR 490
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
222-534 |
2.82e-27 |
|
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: 112.75 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 222 VLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTfeatAGFLLPLS---RGGK-IAMN-----D 292
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHI----AGLNLALAtfhAGGAnVVMEkfdpaE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 293 GLRHIaknlQQSKTSILIAVPLLLetlhKTILRKATgdakvakkyKLGLSLAKALNKIKLNFNDKIfaeihkglgghLRL 372
Cdd:cd17637 80 ALELI----EEEKVTLMGSFPPIL----SNLLDAAE---------KSGVDLSSLRHVLGLDAPETI-----------QRF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 373 LVCGGAAIepqiladfndWgitaiQGYGVTECSPIIS----NNRPKykehaSAGLPTPHVEVKIINEDENGI-----GEI 443
Cdd:cd17637 132 EETTGATF----------W-----SLYGQTETSGLVTlspyRERPG-----SAGRPGPLVRVRIVDDNDRPVpagetGEI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 444 IARGPNVMLGYYEDPEKTAEAIDsEGFYHTGDYGYIDDRGFIYITGRKANIIVTK-NGKNIFPEEIEFVLLKENIIEEVV 522
Cdd:cd17637 192 VVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKPEKELIKpGGENVYPAEVEKVILEHPAIAEVC 270
|
330
....*....|...
gi 1360655949 523 VYGERD-EYGEQI 534
Cdd:cd17637 271 VIGVPDpKWGEGI 283
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
218-608 |
8.72e-27 |
|
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: 111.58 E-value: 8.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 218 RALAVLLFTSGTTAKSKAVMLCHDNL-CVNIYDVCLTVEFDKNDTLLSVLPLHHTFeATAGFLLPLSRGGKIAM---NDG 293
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIG-GLWWILTCLIHGGLCVTggeNTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 294 LRHIAKNLQQSKTSILIAVPllletlhktilrkatgdakvakkyklglslaKALNKIKLNFNDKIfAEIHKglgghLRLL 373
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVP-------------------------------TLLSKLVSELKSAN-ATVPS-----LRLI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 374 VCGGAAIEPQILADFNDWGITAI-QGYGVTECSPI--ISNNRpKYKEHASAGLPTPHVEVKIINED-----ENGIGEIIA 445
Cdd:cd17635 123 GYGGSRAIAADVRFIEATGLTNTaQVYGLSETGTAlcLPTDD-DSIEINAVGRPYPGVDVYLAATDgiagpSASFGTIWI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 446 RGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVtKNGKNIFPEEIEFVLLKENIIEEVVVYG 525
Cdd:cd17635 202 KSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESIN-CGGVKIAPDEVERIAEGVSGVQECACYE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 526 ERDE-YGEQIItAEVFPSVEElakvletnakdiDTSVLTGsvaeglvkdAISKANKELQNFKKVKDIVLrAEPFPRNTSK 604
Cdd:cd17635 280 ISDEeFGELVG-LAVVASAEL------------DENAIRA---------LKHTIRRELEPYARPSTIVI-VTDIPRTQSG 336
|
....
gi 1360655949 605 KILR 608
Cdd:cd17635 337 KVKR 340
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
52-529 |
6.38e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 112.07 E-value: 6.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 52 PRSEAAINFRINpDNEYRGITYRQVNE--DRKALGsaMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKEL 129
Cdd:PRK13295 38 PDKTAVTAVRLG-TGAPRRFTYRELAAlvDRVAVG--LARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 130 PANEVENLINRSGANTI-----FYSRSQEDKLLGIADNIKQVKNLVSYDlptenssklaGEDKDLF--FL----WDLint 198
Cdd:PRK13295 115 RERELSFMLKHAESKVLvvpktFRGFDHAAMARRLRPELPALRHVVVVG----------GDGADSFeaLLitpaWEQ--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 199 gnsiRANGNTQYDNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGF 278
Cdd:PRK13295 182 ----EPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 279 LLPLSRGGKIAMND---GLRHIAKNLQQSKTSILIAVPLLLETlhktilrkatgdAKVAKKYKLGLSlakalnkiklnfn 355
Cdd:PRK13295 258 MMPVMLGATAVLQDiwdPARAAELIRTEGVTFTMASTPFLTDL------------TRAVKESGRPVS------------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 356 dkifaeihkglggHLRLLVCGGAAIEPQILADFND-WGITAIQGYGVTECS--PIISNNRPKYKEHASAGLPTPHVEVKI 432
Cdd:PRK13295 313 -------------SLRTFLCAGAPIPGALVERARAaLGAKIVSAWGMTENGavTLTKLDDPDERASTTDGCPLPGVEVRV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 433 INED-----ENGIGEIIARGPNVMLGYYEDPEKTAEaiDSEGFYHTGDYGYIDDRGFIYITGRKANIIVtKNGKNIFPEE 507
Cdd:PRK13295 380 VDADgaplpAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVII-RGGENIPVVE 456
|
490 500
....*....|....*....|..
gi 1360655949 508 IEFVLLKENIIEEVVVYGERDE 529
Cdd:PRK13295 457 IEALLYRHPAIAQVAIVAYPDE 478
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
217-561 |
2.09e-25 |
|
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: 110.27 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 217 PRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGgkiaMNDGLRH 296
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAG----MNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 297 iaknlqqskTSILIAVPLLLetLHKTILRKATGDAKVAKKYKLglsLAKALNKIKLNFNDKifaeihkglgGHLRLLVCG 376
Cdd:cd05908 181 ---------TRLFIRRPILW--LKKASEHKATIVSSPNFGYKY---FLKTLKPEKANDWDL----------SSIRMILNG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 377 GAAIEPQILADFND----WGI--TAIQG-YGVTECS------PIISNNRPKY--KEHASAGLPTPHV------------- 428
Cdd:cd05908 237 AEPIDYELCHEFLDhmskYGLkrNAILPvYGLAEASvgaslpKAQSPFKTITlgRRHVTHGEPEPEVdkkdsecltfvev 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 429 -------EVKIINEDENG-----IGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDrGFIYITGRKANIIV 496
Cdd:cd05908 317 gkpidetDIRICDEDNKIlpdgyIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRN-GRLVITGREKDIIF 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 497 TkNGKNIFPEEIEFVLLKENIIE--EVVVYGERDEYGEQ---IITAEVFPSVEELAKVletnAKDIDTSV 561
Cdd:cd05908 396 V-NGQNVYPHDIERIAEELEGVElgRVVACGVNNSNTRNeeiFCFIEHRKSEDDFYPL----GKKIKKHL 460
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
63-547 |
2.76e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 110.74 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 63 NPDNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYE-WYITYLATVCGLAIiAPMDkelPAnevenlinrs 141
Cdd:PRK08180 62 GADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEhALLALAAMYAGVPY-APVS---PA---------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 142 gantifYSRSQED--KLLGIADNIK--------------QVKNLVSYDLPTENSSKLAGEDKDLFFLwDLINTGNSIRAN 205
Cdd:PRK08180 128 ------YSLVSQDfgKLRHVLELLTpglvfaddgaafarALAAVVPADVEVVAVRGAVPGRAATPFA-ALLATPPTAAVD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 206 GNTQydnlPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKND--TLLSVLPLHHTFEATAGFLLPLS 283
Cdd:PRK08180 201 AAHA----AVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGGNHNLGIVLY 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 284 RGGKIAMNDG----------LRhiakNLQQSKTSILIAVPLLLETLhKTILRKatgDAKVAKKYklglslakalnkikln 353
Cdd:PRK08180 277 NGGTLYIDDGkptpggfdetLR----NLREISPTVYFNVPKGWEML-VPALER---DAALRRRF---------------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 354 fndkiFAEihkglgghLRLLVCGGAAIEPQILADFNDWGITAI-------QGYGVTECSPIISN-----NRPKYkehasA 421
Cdd:PRK08180 333 -----FSR--------LKLLFYAGAALSQDVWDRLDRVAEATCgerirmmTGLGMTETAPSATFttgplSRAGN-----I 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 422 GLPTPHVEVKIINEDenGIGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYG-YID----DRGFIYiTGRkaniiV 496
Cdd:PRK08180 395 GLPAPGCEVKLVPVG--GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVrFVDpadpERGLMF-DGR-----I 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1360655949 497 TKNGK-------NIFPEEIEFVLLKENIIEEVVVYGE-RDEygeqiITAEVFPSVEELA 547
Cdd:PRK08180 467 AEDFKlssgtwvSVGPLRARAVSAGAPLVQDVVITGHdRDE-----IGLLVFPNLDACR 520
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
69-532 |
6.18e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 108.98 E-value: 6.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFY 148
Cdd:PRK07470 31 RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 149 SRSQEDKLLGIADNIKQVKNLVSYDLPTenssklAGEDKDlfflwDLI--NTGNSIrANGNTQYDnlpiDPralAVLLFT 226
Cdd:PRK07470 111 HADFPEHAAAVRAASPDLTHVVAIGGAR------AGLDYE-----ALVarHLGARV-ANAAVDHD----DP---CWFFFT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 227 SGTTAKSKAVMLCHDNLCVNIYD-VC-LTVEFDKNDTLLSVLPLHHTfeatAGF--LLPLSRGGKIAMNDGLR----HIA 298
Cdd:PRK07470 172 SGTTGRPKAAVLTHGQMAFVITNhLAdLMPGTTEQDASLVVAPLSHG----AGIhqLCQVARGAATVLLPSERfdpaEVW 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 299 KNLQQSKTSILIAVPllletlhkTILRKATGDAKVAKkYKlglslakalnkiklnfndkifaeiHkglgGHLRLLVCGGA 378
Cdd:PRK07470 248 ALVERHRVTNLFTVP--------TILKMLVEHPAVDR-YD------------------------H----SSLRYVIYAGA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 379 AI--EPQILAdFNDWGITAIQGYGVTECSPIISNNRPKYkeHA----------SAGLPTPHVEVKIINEDENGI-----G 441
Cdd:PRK07470 291 PMyrADQKRA-LAKLGKVLVQYFGLGEVTGNITVLPPAL--HDaedgpdarigTCGFERTGMEVQIQDDEGRELppgetG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 442 EIIARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEV 521
Cdd:PRK07470 368 EICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYIS-GGSNVYPREIEEKLLTHPAVSEV 445
|
490
....*....|..
gi 1360655949 522 VVYGERDE-YGE 532
Cdd:PRK07470 446 AVLGVPDPvWGE 457
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
69-610 |
9.26e-25 |
|
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: 107.55 E-value: 9.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIApmdkelpanevenlinrsGANTify 148
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAV------------------VINP--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 149 sRSQEDKLLGIADNikqvknlvsydlptenssklagedkdlfflwdlintgnsirangnTQYDNLPIDPRALAVLLFTSG 228
Cdd:cd05919 68 -LLHPDDYAYIARD---------------------------------------------CEARLVVTSADDIAYLLYSSG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 229 TTAKSKAVMLCHDN-------LCVNIYDVcltvefDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGLR---HIA 298
Cdd:cd05919 102 TTGPPKGVMHAHRDpllfadaMAREALGL------TPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPtaeRVL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 299 KNLQQSKTSILIAVPllleTLHKTILRKATGDAKVAKKyklglslakalnkiklnfndkifaeihkglgghLRLLVCGGA 378
Cdd:cd05919 176 ATLARFRPTVLYGVP----TFYANLLDSCAGSPDALRS---------------------------------LRLCVSAGE 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 379 AIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDENGI-----GEIIARGPNVML 452
Cdd:cd05919 219 ALPRGLGERWMEhFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIppgeeGDLLVRGPSAAV 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 453 GYYEDPEKTaEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGe 532
Cdd:cd05919 299 GYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLIIQHPAVAEAAVVAVPESTG- 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1360655949 533 qIITAEVFPSVEELAKVLETNAKDIDTSVLtgsvaeglvkdaiskanKELQNFKKVKDIVLrAEPFPRNTSKKILRNK 610
Cdd:cd05919 376 -LSRLTAFVVLKSPAAPQESLARDIHRHLL-----------------ERLSAHKVPRRIAF-VDELPRTATGKLQRFK 434
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
71-547 |
1.12e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 108.05 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSR 150
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 sqedklLGIADNikqvknlvsyDLPTENSSKLA---GEDKDLFFLWDLINTGNSIRANGNTQYDN--LPIDpralAVLLF 225
Cdd:PRK05852 124 ------DGPHDR----------AEPTTRWWPLTvnvGGDSGPSGGTLSVHLDAATEPTPATSTPEglRPDD----AMIMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 226 TSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGLRHIAK----NL 301
Cdd:PRK05852 184 TGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAHtfwdDI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 302 QQSKTSILIAVPllleTLHKTILRKATGDAKVAKKYKLglslakalnkiklnfndkifaeihkglgghlRLLVCGGAAIE 381
Cdd:PRK05852 264 KAVGATWYTAVP----TIHQILLERAATEPSGRKPAAL-------------------------------RFIRSCSAPLT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 382 PQI-LADFNDWGITAIQGYGVTECSPIISNNRPKYKEH-----ASAGL--PTPHVEVKIINED-----ENGIGEIIARGP 448
Cdd:PRK05852 309 AETaQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQtenpvVSTGLvgRSTGAQIRIVGSDglplpAGAVGEVWLRGT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 449 NVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIvTKNGKNIFPEEIEFVLLKENIIEEVVVYGERD 528
Cdd:PRK05852 389 TVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELI-NRGGEKISPERVEGVLASHPNVMEAAVFGVPD 466
|
490 500
....*....|....*....|....*
gi 1360655949 529 E-YGEQ----IITAEV-FPSVEELA 547
Cdd:PRK05852 467 QlYGEAvaavIVPRESaPPTAEELV 491
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
65-532 |
1.36e-24 |
|
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: 107.92 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 65 DNEYRgITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLA-TVCGLA-IIApmdkeLPA---NEVENLIN 139
Cdd:COG1021 46 DGERR-LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFAlFRAGAIpVFA-----LPAhrrAEISHFAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 140 RSGANTIFYSRSQED-KLLGIADNIKQvknlvsyDLPTENSSKLAGEDKDLFFLWDLINTGNSIRANGntqydnlpIDPR 218
Cdd:COG1021 120 QSEAVAYIIPDRHRGfDYRALARELQA-------EVPSLRHVLVVGDAGEFTSLDALLAAPADLSEPR--------PDPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 219 ALAVLLFTSGTTAKSKAVMLCHDNLCVNIY---DVCltvEFDKNDTLLSVLPLHHTFE-ATAGFLLPLSRGGKIAMNDGl 294
Cdd:COG1021 185 DVAFFQLSGGTTGLPKLIPRTHDDYLYSVRasaEIC---GLDADTVYLAALPAAHNFPlSSPGVLGVLYAGGTVVLAPD- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 295 rhiaknlqqskTSILIAVPLlletlhktILR-KATGDAkvakkykLGLSLAKALnkikLNFndkifAEIHKGLGGHLRLL 373
Cdd:COG1021 261 -----------PSPDTAFPL--------IEReRVTVTA-------LVPPLALLW----LDA-----AERSRYDLSSLRVL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 374 VCGGA--------AIEPQiladfndWGITAIQGYGVTE----CSPIisnNRPKYKEHASAGLP-TPHVEVKIINEDEN-- 438
Cdd:COG1021 306 QVGGAklspelarRVRPA-------LGCTLQQVFGMAEglvnYTRL---DDPEEVILTTQGRPiSPDDEVRIVDEDGNpv 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 439 --G-IGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVtKNGKNIFPEEIEFVLLKE 515
Cdd:COG1021 376 ppGeVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQIN-RGGEKIAAEEVENLLLAH 454
|
490
....*....|....*...
gi 1360655949 516 NIIEEVVVYGERDEY-GE 532
Cdd:COG1021 455 PAVHDAAVVAMPDEYlGE 472
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
58-490 |
3.35e-24 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 107.49 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 58 INFRinPDNeYRGITyrqvnedRKALG-SAMLDLGISKDDKVIILAETryewyitylATVCGLAII-APMDKELPA---- 131
Cdd:PRK08043 227 VNFT--PDS-YRKLL-------KKTLFvGRILEKYSVEGERIGLMLPN---------ATISAAVIFgASLRRRIPAmmny 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 132 ----NEVENLINRSGANTIFYSRS--QEDKLLGIADNIKQVKNLVSYDLPTEnsskLAGEDKdLFFLWDLINTGNSIran 205
Cdd:PRK08043 288 tagvKGLTSAITAAEIKTIFTSRQflDKGKLWHLPEQLTQVRWVYLEDLKDD----VTTADK-LWIFAHLLMPRLAQ--- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 206 gntqydnLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRG 285
Cdd:PRK08043 360 -------VKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTG 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 286 GKIAMNDGLRHIAknlqqsktsiliAVPLLLETLHKTILRKAT---GD-AKVAKKYKlglslakalnkiklnfndkiFAE 361
Cdd:PRK08043 433 AEVFLYPSPLHYR------------IVPELVYDRNCTVLFGTStflGNyARFANPYD--------------------FAR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 362 ihkglgghLRLLVCGGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINED--EN 438
Cdd:PRK08043 481 --------LRYVVAGAEKLQESTKQLWQDkFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPgiEQ 552
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1360655949 439 GiGEIIARGPNVMLGYY--EDP-------EKTAEAIDSEGFYHTGDYGYIDDRGFIYITGR 490
Cdd:PRK08043 553 G-GRLQLKGPNIMNGYLrvEKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGR 612
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
64-552 |
1.06e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 104.97 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 64 PDNEY-----RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLI 138
Cdd:PRK07798 17 PDRVAlvcgdRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 139 NRSGANTIFYSRSQEDKLLGIADNIKQVKNLVSYDLPTENSSKLAGEDKDlfflwDLINTGNSIRANGNTQYDNLpidpr 218
Cdd:PRK07798 97 DDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYE-----DALAAGSPERDFGERSPDDL----- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 219 alaVLLFTSGTTAKSKAVMLCHDNlcvnIYDVCL------TVEF--DKND-----------TLLSVLPLHHTFEATAGFL 279
Cdd:PRK07798 167 ---YLLYTGGTTGMPKGVMWRQED----IFRVLLggrdfaTGEPieDEEElakraaagpgmRRFPAPPLMHGAGQWAAFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 280 LPLSrGGKIAMNDGLRHIAKNLqqsktsiliavpllLETLHKtilRKA-----TGDAkVAKkyklglSLAKALnkiklnf 354
Cdd:PRK07798 240 ALFS-GQTVVLLPDVRFDADEV--------------WRTIER---EKVnvitiVGDA-MAR------PLLDAL------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 355 ndkifAEIHKGLGGHLRLLVCGGAAIEPQILADFNDW--GITAIQGYGVTE---CSPIISNNRPkykEHASAGLPTPHVE 429
Cdd:PRK07798 288 -----EARGPYDLSSLFAIASGGALFSPSVKEALLELlpNVVLTDSIGSSEtgfGGSGTVAKGA---VHTGGPRFTIGPR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 430 VKIINEDEN----GIGEI--IARGPNVMLGYYEDPEKTAEA---IDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNG 500
Cdd:PRK07798 360 TVVLDEDGNpvepGSGEIgwIARRGHIPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGRGSVCINT-GG 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1360655949 501 KNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAEVF------PSVEELAKVLET 552
Cdd:PRK07798 439 EKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQlregarPDLAELRAHCRS 496
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
53-535 |
8.20e-23 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 102.78 E-value: 8.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 53 RSEAAINFRINPDNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMdkELPAN 132
Cdd:PRK09192 32 LGEAGMNFYDRRGQLEEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL--PLPMG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 133 ---------EVENLINRSGANTIFYSrsqeDKLLGIADNIKQVKNLVsYDLPTENSSKLAGEDKDLfflwdlintgnsir 203
Cdd:PRK09192 110 fggresyiaQLRGMLASAQPAAIITP----DELLPWVNEATHGNPLL-HVLSHAWFKALPEADVAL-------------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 204 angntqydnLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYD-VCLTVEFDKNDTLLSVLPLHHTFeATAGFLL-P 281
Cdd:PRK09192 171 ---------PRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAiSHDGLKVRPGDRCVSWLPFYHDM-GLVGFLLtP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 282 LS--------RGGKIAMND--GLRHIAKNlqqsKTSILIAVPLLLETlhktILRKATGDAKVAkkykLGLSlakalnkik 351
Cdd:PRK09192 241 VAtqlsvdylPTRDFARRPlqWLDLISRN----RGTISYSPPFGYEL----CARRVNSKDLAE----LDLS--------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 352 lnfndkifaeihkglggHLRLLVCGGAAIEPQIL---------ADFNDWGITAiqGYGVTECSPIIS------------- 409
Cdd:PRK09192 300 -----------------CWRVAGIGADMIRPDVLhqfaeafapAGFDDKAFMP--SYGLAEATLAVSfsplgsgivveev 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 410 --------------NNRP-KYKEHASAGLPTPHVEVKIINED-----ENGIGEIIARGPNVMLGYYEDPEkTAEAIDSEG 469
Cdd:PRK09192 361 drdrleyqgkavapGAETrRVRTFVNCGKALPGHEIEIRNEAgmplpERVVGHICVRGPSLMSGYFRDEE-SQDVLAADG 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1360655949 470 FYHTGDYGYIDDrGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIE--EVVVYGERDEYGEQII 535
Cdd:PRK09192 440 WLDTGDLGYLLD-GYLYITGRAKDLIII-NGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIV 505
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
72-500 |
2.24e-22 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 100.98 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILA--ETRY--EWY-ITYLATVCglaiiAPMDKELPANEVENLINRSGANTI 146
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAwnTWRHleAWYgIMGIGAIC-----HTVNPRLFPEQIAWIINHAEDRVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 147 FYSRSQEDKLLGIADNIKQV-----------------KNLVSYDlptensSKLAGEDKDlfFLWDLIntgnsirangntq 209
Cdd:PRK06018 116 ITDLTFVPILEKIADKLPSVeryvvltdaahmpqttlKNAVAYE------EWIAEADGD--FAWKTF------------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 210 ydnlpiDPRALAVLLFTSGTTAKSKAVMLCHDNlcvNIYDVCLTVEFD-----KNDTLLSVLPLHHTFEATAGFLLPlSR 284
Cdd:PRK06018 175 ------DENTAAGMCYTSGTTGDPKGVLYSHRS---NVLHALMANNGDalgtsAADTMLPVVPLFHANSWGIAFSAP-SM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 285 GGKIAMN----DGlRHIAKNLQQSKTSILIAVP----LLLETLHKTilrkatgdakvakkyklGLSLAkalnkiklnfnd 356
Cdd:PRK06018 245 GTKLVMPgaklDG-ASVYELLDTEKVTFTAGVPtvwlMLLQYMEKE-----------------GLKLP------------ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 357 kifaeihkglggHLRLLVCGGAAIEPQILADFNDWGITAIQGYGVTECSPI--ISNNRPKYKE---------HASAGLPT 425
Cdd:PRK06018 295 ------------HLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLgtLAALKPPFSKlpgdarldvLQKQGYPP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 426 PHVEVKIINEDENGI-------GEIIARGPNVMLGYYedpEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIvtK 498
Cdd:PRK06018 363 FGVEMKITDDAGKELpwdgktfGRLKVRGPAVAAAYY---RVDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVI--K 437
|
..
gi 1360655949 499 NG 500
Cdd:PRK06018 438 SG 439
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
71-490 |
3.99e-22 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 100.28 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVnedRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSR 150
Cdd:PRK06334 46 LSYNQV---RKAVIALATKVSKYPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 SQEDKLLGI-ADNIKQVKNLVSYDlptenssklagEDKDLFFLWDLINTG--NSIRANGNTQYDNLP-IDPRALAVLLFT 226
Cdd:PRK06334 123 QLMQHLAQThGEDAEYPFSLIYME-----------EVRKELSFWEKCRIGiyMSIPFEWLMRWFGVSdKDPEDVAVILFT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 227 SGTTAKSKAVMLCHDNLCVNiYDVCLTVeFD--KNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDG---LRHIAKNL 301
Cdd:PRK06334 192 SGTEKLPKGVPLTHANLLAN-QRACLKF-FSpkEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNplyPKKIVEMI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 302 QQSKTSILIAVPLLLETLHKTilrkatgdakvAKKYKLGLSlakalnkiklnfndkifaeihkglggHLRLLVCGGAAIE 381
Cdd:PRK06334 270 DEAKVTFLGSTPVFFDYILKT-----------AKKQESCLP--------------------------SLRFVVIGGDAFK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 382 ----PQILADFNDwgITAIQGYGVTECSPIIS-NNRPKYKEHASAGLPTPHVEVKIINED------ENGIGEIIARGPNV 450
Cdd:PRK06334 313 dslyQEALKTFPH--IQLRQGYGTTECSPVITiNTVNSPKHESCVGMPIRGMDVLIVSEEtkvpvsSGETGLVLTRGTSL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1360655949 451 MLGYY-EDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGR 490
Cdd:PRK06334 391 FSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGR 431
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
93-526 |
1.33e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 99.41 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 93 SKDDKVIILAETRYEWYITYLATVCGLAIiapMDKELPANE----VENLINRSGANTIFYSRSQEDKL--LGIADNIKQV 166
Cdd:PTZ00342 165 SIDVIVDILNETKLEWLCLDLDLVEGLLE---RKNELPHLKkliiLDTLIKSKEININKEEKNNGSNVnnNGNKNNKEEQ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 167 KNLVSYDLPTENSSKLAGEDKD-LFFLWDLI----NTGNSI------RANGNTQYDNLPIDPRALAVLLFTSGTTAKSKA 235
Cdd:PTZ00342 242 KGNDLSNELEDISLGPLEYDKEkLEKIKDLKekakKLGISIilfddmTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKG 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 236 VMLCHDNLCVNIYDVCLTVEFDKN--DTLLSVLPLHHTFEATAGFLLpLSRGGKIAM-NDGLRHIAKNLQQSKTSILIAV 312
Cdd:PTZ00342 322 VMLSNKNLYNTVVPLCKHSIFKKYnpKTHLSYLPISHIYERVIAYLS-FMLGGTINIwSKDINYFSKDIYNSKGNILAGV 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 313 PLLLETLHKTILRKaTGDAKVAKKY--KLGLSLAKALNKIKL-NFNDKIF---AEIHKGLGGHLRLLVCGGAAIEPQILA 386
Cdd:PTZ00342 401 PKVFNRIYTNIMTE-INNLPPLKRFlvKKILSLRKSNNNGGFsKFLEGIThisSKIKDKVNPNLEVILNGGGKLSPKIAE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 387 DF-NDWGITAIQGYGVTECS-PIISNNRPKYKEHASAGLPTPHVEVKIIN------EDENGIGEIIARGPNVMLGYYEDP 458
Cdd:PTZ00342 480 ELsVLLNVNYYQGYGLTETTgPIFVQHADDNNTESIGGPISPNTKYKVRTwetykaTDTLPKGELLIKSDSIFSGYFLEK 559
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1360655949 459 EKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGknifpEEIEFVLLKeNIIEEV------VVYGE 526
Cdd:PTZ00342 560 EQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQG-----EYIETDMLN-NLYSQIsfinfcVVYGD 627
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
71-548 |
2.28e-21 |
|
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: 97.32 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATV-CGLAIIaPMDKELPANEVENLINRSGANTIFYs 149
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALkAGHAYV-PLDASSPAERIREILDAAKPALLIA- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 150 rsqedkllgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpiDPRALAVLLFTSGT 229
Cdd:cd05945 95 ------------------------------------------------------------------DGDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 230 TAKSKAVMLCHDNLcVNIYDVCLTvEFDKN--DTLLSVLPLH---HTFE-----ATAGFLLPLSRggkiAMNDGLRHIAK 299
Cdd:cd05945 109 TGRPKGVQISHDNL-VSFTNWMLS-DFPLGpgDVFLNQAPFSfdlSVMDlypalASGATLVPVPR----DATADPKQLFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 300 NLQQSKTSILIAVPLLLE--TLHKTILRKAT---------GDAkvakkykLGLSLAKALnkiklnfndkifaeihkglgg 368
Cdd:cd05945 183 FLAEHGITVWVSTPSFAAmcLLSPTFTPESLpslrhflfcGEV-------LPHKTARAL--------------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 369 HLRLlvcGGAAIepqiladFNDWGIT----AIQGYGVTEcsPIISNNRPkykehASAGLPTPHVEVKIINED-----ENG 439
Cdd:cd05945 235 QQRF---PDARI-------YNTYGPTeatvAVTYIEVTP--EVLDGYDR-----LPIGYAKPGAKLVILDEDgrpvpPGE 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 IGEIIARGPNVMLGYYEDPEKTAEA---IDSEGFYHTGDYGYIDDRGFIYITGRKANIIvtK-NGKNIFPEEIEFVLLKE 515
Cdd:cd05945 298 KGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRLEADGLLFYRGRLDFQV--KlNGYRIELEEIEAALRQV 375
|
490 500 510
....*....|....*....|....*....|...
gi 1360655949 516 NIIEEVVVYGERDEYGEQIITAEVFPSVEELAK 548
Cdd:cd05945 376 PGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAG 408
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
370-608 |
3.54e-21 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 96.60 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQILADFNDWGITAIQGYGVTECSPIISNNRPK--YKEHASAGLPTPHVEVKIINedeNGIGEIIARG 447
Cdd:PRK07445 232 FRTILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATLKPDdfLAGNNSSGQVLPHAQITIPA---NQTGNITIQA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 448 PNVMLGYYedPEKtaeaIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGER 527
Cdd:PRK07445 309 QSLALGYY--PQI----LDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAILATGLVQDVCVLGLP 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 528 DEYGEQIITAEVFPsveelakvletnaKDIDTSVLTgsvaeglVKDAISkanKELQNFKKVKDIvLRAEPFPRNTSKKIL 607
Cdd:PRK07445 382 DPHWGEVVTAIYVP-------------KDPSISLEE-------LKTAIK---DQLSPFKQPKHW-IPVPQLPRNPQGKIN 437
|
.
gi 1360655949 608 R 608
Cdd:PRK07445 438 R 438
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
69-533 |
8.22e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 96.00 E-value: 8.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNED----RKALGSAMldlgiSKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGAN 144
Cdd:PRK07638 25 RVLTYKDWFESvckvANWLNEKE-----SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 145 TIFYSRSQEDKLLGIAD---NIKQVKNLVSYDLPTEnssklagedkdlfflwdlintgnsirANGNtqydNLPIDPRALA 221
Cdd:PRK07638 100 MIVTERYKLNDLPDEEGrviEIDEWKRMIEKYLPTY--------------------------APIE----NVQNAPFYMG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 222 vllFTSGTTAKSKAVMLCH----DNLCVNIYDVCLTVEfDK---NDTLLSVLPLHHTFEAT-AGFLLPLSRggKIAMNDG 293
Cdd:PRK07638 150 ---FTSGSTGKPKAFLRAQqswlHSFDCNVHDFHMKRE-DSvliAGTLVHSLFLYGAISTLyVGQTVHLMR--KFIPNQV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 294 LrhiaKNLQQSKTSILIAVPLLLETLHKTilrKATGDAKVakkyKLGLSLAK----ALNKIKLNFNdkifaeihkglggH 369
Cdd:PRK07638 224 L----DKLETENISVMYTVPTMLESLYKE---NRVIENKM----KIISSGAKweaeAKEKIKNIFP-------------Y 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLvcggaaiepqilaDFndwgitaiqgYGVTECSPI--ISNNRPKYKEHaSAGLPTPHVEVKIINED-----ENGIGE 442
Cdd:PRK07638 280 AKLY-------------EF----------YGASELSFVtaLVDEESERRPN-SVGRPFHNVQVRICNEAgeevqKGEIGT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 443 IIARGPNVMLGYYEDPEKTAEaIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVV 522
Cdd:PRK07638 336 VYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIESVLHEHPAVDEIV 413
|
490
....*....|..
gi 1360655949 523 VYGERDEY-GEQ 533
Cdd:PRK07638 414 VIGVPDSYwGEK 425
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
370-557 |
1.08e-20 |
|
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: 96.03 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQIladFNDW----GITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDENGI----- 440
Cdd:cd05970 303 LRYCTTAGEALNPEV---FNTFkektGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCeagee 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 441 GEIIAR---GPNVML--GYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKE 515
Cdd:cd05970 380 GEIVIRtskGKPVGLfgGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKS-SGYRIGPFEVESALIQH 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1360655949 516 NIIEEVVVYGERDEYGEQIITAEV-----FPSVEELAKVLETNAKDI 557
Cdd:cd05970 458 PAVLECAVTGVPDPIRGQVVKATIvlakgYEPSEELKKELQDHVKKV 504
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
71-516 |
1.55e-20 |
|
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: 94.68 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSR 150
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 SQEDkllgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpidpraLAVLLFTSGTT 230
Cdd:cd17653 103 SPDD-----------------------------------------------------------------LAYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 231 AKSKAVMLCHDNLcVNIydvcltVEF----------DKNDTLLSVlplhhTFEATAGFLLP-LSRGGKIA---MNDGLRH 296
Cdd:cd17653 118 GIPKGVMVPHRGV-LNY------VSQpparldvgpgSRVAQVLSI-----AFDACIGEIFStLCNGGTLVladPSDPFAH 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 297 IAKNLqqsktSILIAVPLLLETLHKTILRkatgdakvakkyklglslakalnkiklnfndkifaeihkglggHLRLLVCG 376
Cdd:cd17653 186 VARTV-----DALMSTPSILSTLSPQDFP-------------------------------------------NLKTIFLG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 377 GAAIePQILADfnDW--GITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDEN-----GIGEIIARGPN 449
Cdd:cd17653 218 GEAV-PPSLLD--RWspGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQpvpegVVGEICISGVQ 294
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1360655949 450 VMLGYYEDPEKTAEAIDSEGFYH------TGDYGYIDDRGFIYITGRKANIIvtKN-GKNIFPEEIEFVLLKEN 516
Cdd:cd17653 295 VARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQV--KVrGFRINLEEIEEVVLQSQ 366
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
55-610 |
2.52e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 94.61 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 55 EAAINFRINPD-----NEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAET-RYEWYITYLATVCGlAIIAPMDKE 128
Cdd:PRK07788 54 LVAHAARRAPDraaliDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNhRGFVLALYAAGKVG-ARIILLNTG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 129 LPANEVENLINRSGANTIFYSRSQEDKLLGIADNIKQVKNLVSYdlpTENSSKLAGEDKDLFflwDLINTGNSIRangnt 208
Cdd:PRK07788 133 FSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGN---PDDDEPSGSTDETLD---DLIAGSSTAP----- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 209 qydnLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFeATAGFLLPLSRGGKI 288
Cdd:PRK07788 202 ----LPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHAT-GWAHLTLAMALGSTV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 289 AMN------DGLRHIAKNlqqsKTSILIAVPLLLetlhKTILRKatgDAKVAKKYKLGlslakalnkiklnfndkifaei 362
Cdd:PRK07788 277 VLRrrfdpeATLEDIAKH----KATALVVVPVML----SRILDL---GPEVLAKYDTS---------------------- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 363 hkglggHLRLLVCGGAAIEPQILADFND-WGITAIQGYGVTECSpIISNNRPK--YKEHASAGLPTPHVEVKIINEDENG 439
Cdd:PRK07788 324 ------SLKIIFVSGSALSPELATRALEaFGPVLYNLYGSTEVA-FATIATPEdlAEAPGTVGRPPKGVTVKILDENGNE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 I-----GEIIARGPNVMLGYYEDPEKtaEAIDseGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLK 514
Cdd:PRK07788 397 VprgvvGRIFVGNGFPFEGYTDGRDK--QIID--GLLSSGDVGYFDEDGLLFVDGRDDDMIVS-GGENVFPAEVEDLLAG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 515 ENIIEEVVVYG-ERDEYGEQIitaEVFPSVEELAkvletnAKDIDTsvltgsvaeglVKDAIsKANkeLQNFKKVKDIVL 593
Cdd:PRK07788 472 HPDVVEAAVIGvDDEEFGQRL---RAFVVKAPGA------ALDEDA-----------IKDYV-RDN--LARYKVPRDVVF 528
|
570
....*....|....*..
gi 1360655949 594 RAEpFPRNTSKKILRNK 610
Cdd:PRK07788 529 LDE-LPRNPTGKVLKRE 544
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
71-529 |
2.81e-20 |
|
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: 94.26 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSR 150
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 SQEDKLLGIADnikqvknlvsydLPTENSSKLAGEDkdlfflwdlintgnsirangntqyDNLPI--DPRALAVLLFTSG 228
Cdd:cd12114 93 PDAQLDVAVFD------------VLILDLDALAAPA------------------------PPPPVdvAPDDLAYVIFTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 229 TTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHH---TFEatagFLLPLSRGGKIAMNDGLR-----HIAKN 300
Cdd:cd12114 137 STGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFdlsVYD----IFGALSAGATLVLPDEARrrdpaHWAEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 301 LQQSKTSILIAVPLLLETLhktiLRKATGDAKvakkykLGLSLAKAL---NKIKLNFNDKIfaeihKGLGGHLRLLVCGG 377
Cdd:cd12114 213 IERHGVTLWNSVPALLEML----LDVLEAAQA------LLPSLRLVLlsgDWIPLDLPARL-----RALAPDARLISLGG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 378 AaiepqiladfndwgitaiqgygvTECSpIISNNRPKYKEHAS-----AGLPTPHVEVKIINEDEN-----GIGEIIARG 447
Cdd:cd12114 278 A-----------------------TEAS-IWSIYHPIDEVPPDwrsipYGRPLANQRYRVLDPRGRdcpdwVPGELWIGG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 448 PNVMLGYYEDPEKTAEA----IDSEGFYHTGDYGYIDDRGFIYITGRKaNIIVTKNGKNIFPEEIEFVLLKENIIEE--V 521
Cdd:cd12114 334 RGVALGYLGDPELTAARfvthPDGERLYRTGDLGRYRPDGTLEFLGRR-DGQVKVRGYRIELGEIEAALQAHPGVARavV 412
|
....*...
gi 1360655949 522 VVYGERDE 529
Cdd:cd12114 413 VVLGDPGG 420
|
|
| DHB_AMP_lig |
TIGR02275 |
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme ... |
69-550 |
4.06e-20 |
|
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme family (pfam00501). Members activate 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate; many are involved in synthesis of siderophores such as enterobactin, vibriobactin, vulnibactin, etc. The most closely related proteine believed to differ in function activates salicylate rather than DHB. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 274063 [Multi-domain] Cd Length: 526 Bit Score: 94.09 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVcgLAIIAPMDKeLPAN---EVENLINRSGANT 145
Cdd:TIGR02275 47 RQWSYRELDQRADNLAAGLTKLGIKQGDTAVVQLPNIAEFYIVFFALL--KLGVAPVLA-LFSHrksELTAYASQIEPAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 146 IFYSRSQEdkLLGIADNIKQVKNlvsyDLPTENSSKLAGED-KDLFFLWdlINTGNSirangntQYDNLPIDPRALAVLL 224
Cdd:TIGR02275 124 YIIDRAHS--LFDYDDFARQLQS----KLPTLRNIIVAGQTgEAELFLW--LESPAE-------PVKFPPTKSDEVAFFQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 225 FTSGTTAKSKAVMLCHDNLcvnIYDVCLTVE---FDKNDTLLSVLPLHHTFE-ATAGFLLPLSRGGKIAM--NDGLRHIA 298
Cdd:TIGR02275 189 LSGGSTGTPKLIPRTHNDY---YYSVRRSVEicwLTQQTRYLCALPAAHNYPlSSPGALGVFYAGGCVVLapDPSPTDCF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 299 KNLQQSKTSILIAVPLLLETLHKTilrkatgdakvAKKYKLGLSlakalnkiklnfndkifaeihkglggHLRLLVCGGA 378
Cdd:TIGR02275 266 PLIERHKVTVTALVPPAVALWMQA-----------ASKSRADLS--------------------------SLKLLQVGGA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 379 ----AIEPQILADFndwGITAIQGYGVTEcsPIISNNR---PKYKEHASAGLP-TPHVEVKIINEDENGI-----GEIIA 445
Cdd:TIGR02275 309 kfsaAAARRVPAVF---GCQLQQVFGMAE--GLVNYTRlddPAEIIFTTQGRPmSPDDEVRVVDDHGNPVapgetGMLLT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 446 RGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIvTKNGKNIFPEEIEFVLLKENIIEEVVVYG 525
Cdd:TIGR02275 384 RGPYTFRGYYKAPEHNAAAFDAEGFYYTGDLVRLTPEGYIVVVGRAKDQI-NRGGEKIAAEEIENLLLAHPAVHDAALVS 462
|
490 500 510
....*....|....*....|....*....|
gi 1360655949 526 ERDEY-GEQ----IITAEVFPSVEELAKVL 550
Cdd:TIGR02275 463 MPDELlGEKscafIVVRDPALKAAQLRRFL 492
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
72-541 |
6.06e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 93.67 E-value: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLAtvCGL--AIIAPMDKELPANEVENLINRSGAntifys 149
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLG--CAWlgAIAVPINTALRGPQLEHILRNSGA------ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 150 rsqedKLLGI-ADNIKQVKNLVSYDLPTENssklagedkdlffLWdLINTGNSIRANGNTQYDNLP----------IDPR 218
Cdd:PRK06155 120 -----RLLVVeAALLAALEAADPGDLPLPA-------------VW-LLDAPASVSVPAGWSTAPLPpldapapaaaVQPG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 219 ALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTfEATAGFLLPLSRGGKIAMndGLRHIA 298
Cdd:PRK06155 181 DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHT-NALNAFFQALLAGATYVL--EPRFSA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 299 KNLQQSKTSILIAVPLLLETLHKTILRKATGDAKVAKKYKLGLslakalnkiklnfndkifaeihkglgghlrllvcgGA 378
Cdd:PRK06155 258 SGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVAL-----------------------------------GP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 379 AIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKYKEhASAGLPTPHVEVKIINEDENGI-----GEIIARGPN--- 449
Cdd:PRK06155 303 GVPAALHAAFRErFGVDLLDGYGSTETNFVIAVTHGSQRP-GSMGRLAPGFEARVVDEHDQELpdgepGELLLRADEpfa 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 450 VMLGYYEDPEKTAEAIDSEGFyHTGDYGYIDDRGFIYITGRKANIIvTKNGKNIFPEEIEFVLLKENIIEEVVVYGERDE 529
Cdd:PRK06155 382 FATGYFGMPEKTVEAWRNLWF-HTGDRVVRDADGWFRFVDRIKDAI-RRRGENISSFEVEQVLLSHPAVAAAAVFPVPSE 459
|
490
....*....|..
gi 1360655949 530 YGEQIITAEVFP 541
Cdd:PRK06155 460 LGEDEVMAAVVL 471
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
221-551 |
2.50e-19 |
|
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: 91.23 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 221 AVLLFTSGTTAKSKAVMLCHDNLcvnIYDVCLTVE---FDKNDTLLSVLPLHHTFE-ATAGFLLPLSRGGKIAMNDGLR- 295
Cdd:cd05920 142 ALFLLSGGTTGTPKLIPRTHNDY---AYNVRASAEvcgLDQDTVYLAVLPAAHNFPlACPGVLGTLLAGGRVVLAPDPSp 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 296 -HIAKNLQQSKTSILIAVPLLLETLhktilrkatgdAKVAKKYKLGLSlakalnkiklnfndkifaeihkglggHLRLLV 374
Cdd:cd05920 219 dAAFPLIEREGVTVTALVPALVSLW-----------LDAAASRRADLS--------------------------SLRLLQ 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 375 CGGAAIEP----QILADFndwGITAIQGYGVTEcsPIISNNR---PKYKEHASAGLP-TPHVEVKIINEDENGI-----G 441
Cdd:cd05920 262 VGGARLSPalarRVPPVL---GCTLQQVFGMAE--GLLNYTRlddPDEVIIHTQGRPmSPDDEIRVVDEEGNPVppgeeG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 442 EIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVtKNGKNIFPEEIEFVLLKENIIEEV 521
Cdd:cd05920 337 ELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQIN-RGGEKIAAEEVENLLLRHPAVHDA 415
|
330 340 350
....*....|....*....|....*....|....*
gi 1360655949 522 VVYGERDEY-GEQ----IITAEVFPSVEELAKVLE 551
Cdd:cd05920 416 AVVAMPDELlGERscafVVLRDPPPSAAQLRRFLR 450
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
370-610 |
2.70e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 91.30 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQILADFNDW-GITAIQGYGVTECSPIISNNRPKYKEH-ASAGLPTPHVEVKIINEDEN-----GIGE 442
Cdd:PRK12406 273 LRHVIHAAAPCPADVKRAMIEWwGPVIYEYYGSTESGAVTFATSEDALSHpGTVGKAAPGAELRFVDEDGRplpqgEIGE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 443 IIARGP-NVMLGYYEDPEKTAEaIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEV 521
Cdd:PRK12406 353 IYSRIAgNPDFTYHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEIEAVLHAVPGVHDC 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 522 VVYGERD-EYGEQIITA-EVFPSVEelakvletnakdIDTSVLTGSVAEGLVKdaiskankelqnFKKVKDIVLRAEpFP 599
Cdd:PRK12406 431 AVFGIPDaEFGEALMAVvEPQPGAT------------LDEADIRAQLKARLAG------------YKVPKHIEIMAE-LP 485
|
250
....*....|.
gi 1360655949 600 RNTSKKILRNK 610
Cdd:PRK12406 486 REDSGKIFKRR 496
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
214-539 |
7.80e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 90.09 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 214 PIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDg 293
Cdd:PRK13388 146 EVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPA- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 294 lrhiaknlQQSKTSILIAVpllletlhktilRK--ATGDAKVAKKykLGLSLAK------ALNKIKLNFndkifaeihkg 365
Cdd:PRK13388 225 --------KFSASGFLDDV------------RRygATYFNYVGKP--LAYILATperpddADNPLRVAF----------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 366 lgghlrllvcgGAAIEPQILADF-NDWGITAIQGYGVTECSPIISnnRPKYKEHASAGLPTPHVEV-------------- 430
Cdd:PRK13388 272 -----------GNEASPRDIAEFsRRFGCQVEDGYGSSEGAVIVV--REPGTPPGSIGRGAPGVAIynpetltecavarf 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 431 ----KIINEDEnGIGEIIAR-GPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFP 505
Cdd:PRK13388 339 dahgALLNADE-AIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSA 415
|
330 340 350
....*....|....*....|....*....|....*
gi 1360655949 506 EEIEFVLLKENIIEEVVVYGERDEY-GEQIITAEV 539
Cdd:PRK13388 416 APIERILLRHPAINRVAVYAVPDERvGDQVMAALV 450
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
83-610 |
1.12e-18 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 89.69 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 83 LGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSRSqedkllgIADN 162
Cdd:PLN03102 52 LAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRS-------FEPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 163 IKQVKNLVSYD---------LPTENSSKLAGEDKDLFFLwDLINTG----NSIRANGNTQYDNLPIDpralavLLFTSGT 229
Cdd:PLN03102 125 AREVLHLLSSEdsnlnlpviFIHEIDFPKRPSSEELDYE-CLIQRGeptpSLVARMFRIQDEHDPIS------LNYTSGT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 230 TAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTfeatAGFLLPLSRGGKIAMNDGLRH-----IAKNLQQS 304
Cdd:PLN03102 198 TADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHC----NGWTFTWGTAARGGTSVCMRHvtapeIYKNIEMH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 305 KTSILIAVPLLLETLHKtilrkatGDakvakkyKLGLSlakalnkiklnfndkifaeiHKGLGGHLrllVCGGAAIEPQI 384
Cdd:PLN03102 274 NVTHMCCVPTVFNILLK-------GN-------SLDLS--------------------PRSGPVHV---LTGGSPPPAAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 385 LADFNDWGITAIQGYGVTECS-PIIS-------NNRPKYKE---HASAG---LPTPHVEVK------IINEDENGIGEII 444
Cdd:PLN03102 317 VKKVQRLGFQVMHAYGLTEATgPVLFcewqdewNRLPENQQmelKARQGvsiLGLADVDVKnketqeSVPRDGKTMGEIV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 445 ARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLK-ENIIEEVVV 523
Cdd:PLN03102 397 IKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEVENVLYKyPKVLETAVV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 524 YGERDEYGEQiitaevfPSVEELAKVLETNAKDIDTSVLTGSvaeglvKDAISKANKELQNFKKVKDIVLRAEpFPRNTS 603
Cdd:PLN03102 475 AMPHPTWGET-------PCAFVVLEKGETTKEDRVDKLVTRE------RDLIEYCRENLPHFMCPRKVVFLQE-LPKNGN 540
|
....*..
gi 1360655949 604 KKILRNK 610
Cdd:PLN03102 541 GKILKPK 547
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
367-613 |
1.87e-18 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 89.05 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 367 GGHLRLLVCGGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKYKEHA-SAGLPTPHVEVKIINEDENG----- 439
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMDqFGDVIYNNYNATEAGMIATATPADLRAAPdTAGRPAEGTEIRILDQDFREvptge 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 IGEIIARGPNVMLGYyeDPEKTAEAIDseGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIE 519
Cdd:PRK13382 391 VGTIFVRNDTQFDGY--TSGSTKDFHD--GFMASGDVGYLDENGRLFVVGRDDEMIVS-GGENVYPIEVEKTLATHPDVA 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 520 EVVVYG-ERDEYGeQIITAEVfpsveelakvletnakdidtsVLTGSVAEgLVKDAISKANKELQNFKKVKDIVLRAEpF 598
Cdd:PRK13382 466 EAAVIGvDDEQYG-QRLAAFV---------------------VLKPGASA-TPETLKQHVRDNLANYKVPRDIVVLDE-L 521
|
250
....*....|....*
gi 1360655949 599 PRNTSKKILRNKEQR 613
Cdd:PRK13382 522 PRGATGKILRRELQA 536
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
72-555 |
3.16e-18 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 87.56 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSRS 151
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 152 QEDKLlgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpiDPRALAVLLFTSGTTA 231
Cdd:cd05969 82 LYERT-----------------------------------------------------------DPEDPTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 232 KSKAVMLCHDNLcvniYDVCLTVEFdkndtllsVLPLH------HTFE------ATAGFLLPLSRGGKIAMNDG---LRH 296
Cdd:cd05969 103 TPKGVLHVHDAM----IFYYFTGKY--------VLDLHpddiywCTADpgwvtgTVYGIWAPWLNGVTNVVYEGrfdAES 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 297 IAKNLQQSKTSILIAVPLLLETLHKTilrkatgDAKVAKKYKLGlslakalnkiklnfndkifaeihkglggHLRLLVCG 376
Cdd:cd05969 171 WYGIIERVKVTVWYTAPTAIRMLMKE-------GDELARKYDLS----------------------------SLRFIHSV 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 377 GAAIEPQILAdfndWGITAIQ-----GYGVTECSPIISNNRPKYKEHA-SAGLPTPHVEVKIINEDENGI-----GEIIA 445
Cdd:cd05969 216 GEPLNPEAIR----WGMEVFGvpihdTWWQTETGSIMIANYPCMPIKPgSMGKPLPGVKAAVVDENGNELppgtkGILAL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 446 RG--PNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVV 523
Cdd:cd05969 292 KPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKT-SGHRVGPFEVESALMEHPAVAEAGV 369
|
490 500 510
....*....|....*....|....*....|....*..
gi 1360655949 524 YGERDEYGEQIITA-----EVFPSVEELAKVLETNAK 555
Cdd:cd05969 370 IGKPDPLRGEIIKAfislkEGFEPSDELKEEIINFVR 406
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
422-539 |
3.88e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 88.17 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 422 GLPTPHVEVKIINEDENGI------GEIIARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANII 495
Cdd:PRK06178 390 GLPVPGTEFKICDFETGELlplgaeGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEML 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1360655949 496 VTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAEV 539
Cdd:PRK06178 469 KV-NGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFV 511
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
71-534 |
4.50e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 87.65 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATV-CGLAIIaPMDKELPANEVENLINRSGANTIFYS 149
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARrSGLYYT-PINWHLTAAEIAYIVDDSGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 150 RsqedkllGIADNIKQVKNLVSYDLPTEnssKLAGEDKDLFflwdlintgNSIRANGNTQYDNLPIDPRALAVLLFTSGT 229
Cdd:PRK08276 91 A-------ALADTAAELAAELPAGVPLL---LVVAGPVPGF---------RSYEEALAAQPDTPIADETAGADMLYSSGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 230 TAKSKAV------MLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHT----FEATAGFLlplsrGGKIAMNDG------ 293
Cdd:PRK08276 152 TGRPKGIkrplpgLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTaplrFGMSALAL-----GGTVVVMEKfdaeea 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 294 LRHIaknlQQSKTSILIAVPLLLETLHKTilrkatgDAKVAKKYKLGlslakalnkiklnfndkifaeihkglggHLRLL 373
Cdd:PRK08276 227 LALI----ERYRVTHSQLVPTMFVRMLKL-------PEEVRARYDVS----------------------------SLRVA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 374 VCGGAAIEPQILADFNDW-GITAIQGYGVTECSPIISNNRPKYKEH-ASAGLPTpHVEVKIINEDEN-----GIGEIIAR 446
Cdd:PRK08276 268 IHAAAPCPVEVKRAMIDWwGPIIHEYYASSEGGGVTVITSEDWLAHpGSVGKAV-LGEVRILDEDGNelppgEIGTVYFE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 447 GPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYG- 525
Cdd:PRK08276 347 MDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIIS-GGVNIYPQEIENLLVTHPKVADVAVFGv 425
|
....*....
gi 1360655949 526 ERDEYGEQI 534
Cdd:PRK08276 426 PDEEMGERV 434
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
370-608 |
4.95e-18 |
|
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: 87.05 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQILADFNDWGITAI-QGYGVTECSPIISNNRPKYKEH-ASAGLPTPHvEVKIIneDENG-------I 440
Cdd:cd05929 246 LKRVIHAAAPCPPWVKEQWIDWGGPIIwEYYGGTEGQGLTIINGEEWLTHpGSVGRAVLG-KVHIL--DEDGnevppgeI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 441 GEIIARGPNVMLgYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEE 520
Cdd:cd05929 323 GEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIIS-GGVNIYPQEIENALIAHPKVLD 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 521 VVVYGERDEYGEQIITAEVFPsveelakVLETNAKDIDtsvltgsvAEGLvkdaISKANKELQNFKKVKDIVLRAEPfPR 600
Cdd:cd05929 401 AAVVGVPDEELGQRVHAVVQP-------APGADAGTAL--------AEEL----IAFLRDRLSRYKCPRSIEFVAEL-PR 460
|
....*...
gi 1360655949 601 NTSKKILR 608
Cdd:cd05929 461 DDTGKLYR 468
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
370-609 |
6.56e-18 |
|
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: 86.72 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQILAdfndW-----GITAIQGYGVTECSPIISNN------RPkykehASAGLPTPHVEVKIIneDEN 438
Cdd:cd05971 209 LRAIATGGESLGEELLG----WareqfGVEVNEFYGQTECNLVIGNCsalfpiKP-----GSMGKPIPGHRVAIV--DDN 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 439 G-------IGEIIARGPN--VMLGYYEDPEKTAEAIDSeGFYHTGDYGYIDDRGFIYITGRKANIIvTKNGKNIFPEEIE 509
Cdd:cd05971 278 GtplppgeVGEIAVELPDpvAFLGYWNNPSATEKKMAG-DWLLTGDLGRKDSDGYFWYVGRDDDVI-TSSGYRIGPAEIE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 510 FVLLKENIIEEVVVYGERDEYGEQIITAEVfpsveelakvletnakdidtsVLTGSVaegLVKDAISkanKELQNFKKVK 589
Cdd:cd05971 356 ECLLKHPAVLMAAVVGIPDPIRGEIVKAFV---------------------VLNPGE---TPSDALA---REIQELVKTR 408
|
250 260 270
....*....|....*....|....*....|
gi 1360655949 590 divLRAEPFPR----------NTSKKILRN 609
Cdd:cd05971 409 ---LAAHEYPReiefvnelprTATGKIRRR 435
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
71-550 |
1.62e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYIT-YLATVCGLAIIApMDKELPANEVENLINRSGANTIFYS 149
Cdd:PRK13390 25 VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVlWAALRSGLYITA-INHHLTAPEADYIVGDSGARVLVAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 150 RSqedkLLGIADNikqvknlVSYDLPTEnssklagedkdlfflwdlINTGNSIRANGNTQYDNLPIDPRAL-----AVLL 224
Cdd:PRK13390 104 AA----LDGLAAK-------VGADLPLR------------------LSFGGEIDGFGSFEAALAGAGPRLTeqpcgAVML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 225 FTSGTTAKSKAVMLCHDNLCVN------------IYDVcltvefDKNDTLLSVLPLHHTfeatagflLPL-------SRG 285
Cdd:PRK13390 155 YSSGTTGFPKGIQPDLPGRDVDapgdpivaiaraFYDI------SESDIYYSSAPIYHA--------APLrwcsmvhALG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 286 GKIAM------NDGLRHIAKnlqqSKTSILIAVPLLLETLHKTilrkatgDAKVAKKYKLGlslakalnkiklnfndkif 359
Cdd:PRK13390 221 GTVVLakrfdaQATLGHVER----YRITVTQMVPTMFVRLLKL-------DADVRTRYDVS------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 360 aeihkglggHLRLLVCGGAAIEPQILADFNDW-GITAIQGYGVTECSPIISNNRPKYKEH-ASAG---LPTPHvevkIIN 434
Cdd:PRK13390 271 ---------SLRAVIHAAAPCPVDVKHAMIDWlGPIVYEYYSSTEAHGMTFIDSPDWLAHpGSVGrsvLGDLH----ICD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 435 EDENG-----IGEIIARGPNVMLGYYEDPEKTAEAID-SEGFYHT-GDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEE 507
Cdd:PRK13390 338 DDGNElpagrIGTVYFERDRLPFRYLNDPEKTAAAQHpAHPFWTTvGDLGSVDEDGYLYLADRKSFMIIS-GGVNIYPQE 416
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1360655949 508 IEFVLLKENIIEEVVVYGERD-EYGEQI-----ITAEVFPSvEELAKVL 550
Cdd:PRK13390 417 TENALTMHPAVHDVAVIGVPDpEMGEQVkaviqLVEGIRGS-DELAREL 464
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
202-509 |
1.66e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 86.11 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 202 IRANGNTQYDNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGF--L 279
Cdd:PRK09274 158 LRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPALGMtsV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 280 LP---LSRGGKiaMNDglRHIAKNLQQSKTSILIAVPLLLETLhktilrkatGDAKVAkkyklglslakalNKIKLNfnd 356
Cdd:PRK09274 238 IPdmdPTRPAT--VDP--AKLFAAIERYGVTNLFGSPALLERL---------GRYGEA-------------NGIKLP--- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 357 kifaeihkglggHLRLLVCGGAAIEPQILADFNDW---GITAIQGYGVTECSPIIS--------NNRPKYKEHASA--GL 423
Cdd:PRK09274 289 ------------SLRRVISAGAPVPIAVIERFRAMlppDAEILTPYGATEALPISSiesreilfATRAATDNGAGIcvGR 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 424 PTPHVEVKIINEDEN--------------GIGEIIARGPNVMLGYYEDPEKTAEA--IDSEG-FYH-TGDYGYIDDRGFI 485
Cdd:PRK09274 357 PVDGVEVRIIAISDApipewddalrlatgEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdVWHrMGDLGYLDAQGRL 436
|
330 340
....*....|....*....|....
gi 1360655949 486 YITGRKANIIVTkNGKNIFPEEIE 509
Cdd:PRK09274 437 WFCGRKAHRVET-AGGTLYTIPCE 459
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
63-541 |
2.04e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 85.33 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 63 NPDN---EYRG--ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATV-CGLAIIaPMDKELPANEVEN 136
Cdd:PRK04813 15 QPDFpayDYLGekLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVkAGHAYI-PVDVSSPAERIEM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 137 LINRSGANTIFysrSQEDKLLGIAD----NIKQVKNLVSYDLPTENSSKLAGEDkdlfflwdlintgnsirangnTQYdn 212
Cdd:PRK04813 94 IIEVAKPSLII---ATEELPLEILGipviTLDELKDIFATGNPYDFDHAVKGDD---------------------NYY-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 213 lpidpralavLLFTSGTTAKSKAVMLCHDNLC------VNIYDV-----CLT---VEFDkndtlLSVLPLHHTFeATAGF 278
Cdd:PRK04813 148 ----------IIFTSGTTGKPKGVQISHDNLVsftnwmLEDFALpegpqFLNqapYSFD-----LSVMDLYPTL-ASGGT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 279 LLPLSRggkiAMNDGLRHIAKNLQQSKTSILIAVP------LLLETLHKTILRKAT-----GDAkvakkykLGLSLAKAL 347
Cdd:PRK04813 212 LVALPK----DMTANFKQLFETLPQLPINVWVSTPsfadmcLLDPSFNEEHLPNLThflfcGEE-------LPHKTAKKL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 348 nkiKLNFNDkifAEIhkglgghlrllvcggaaiepqiladFNDWG-------ITAIQgygVTEcsPIISNNRPkykehAS 420
Cdd:PRK04813 281 ---LERFPS---ATI-------------------------YNTYGpteatvaVTSIE---ITD--EMLDQYKR-----LP 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 421 AGLPTPHVEVKIINEDEN-----GIGEIIARGPNVMLGYYEDPEKTAEA---IDSEGFYHTGDYGYIDDrGFIYITGRka 492
Cdd:PRK04813 320 IGYAKPDSPLLIIDEEGTklpdgEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGYLED-GLLFYQGR-- 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1360655949 493 niI---VTKNGKNIFPEEIEFVLLKENIIEE-VVVYGERDEYGEQIItAEVFP 541
Cdd:PRK04813 397 --IdfqIKLNGYRIELEEIEQNLRQSSYVESaVVVPYNKDHKVQYLI-AYVVP 446
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
43-608 |
2.33e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 85.45 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 43 DPVALRELDPRSEaainfrinpdneyrgITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLAtvCG-LAI 121
Cdd:PRK05857 29 EAIALRRCDGTSA---------------LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLA--CAkLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 122 IAPM-DKELPANEVENLINRSGANTIFYSRSqedkllGIADNIKQVKNLVSYDLPTENSSKLAGEdkdlfflwdliNTGN 200
Cdd:PRK05857 92 IAVMaDGNLPIAAIERFCQITDPAAALVAPG------SKMASSAVPEALHSIPVIAVDIAAVTRE-----------SEHS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 201 SIRANGNTQYDNLPIDPRALavlLFTSGTTAKSKAVMLCHDNLcVNIYDVCLT-----VEFDKNDTLLSVLPLHHTfeat 275
Cdd:PRK05857 155 LDAASLAGNADQGSEDPLAM---IFTSGTTGEPKAVLLANRTF-FAVPDILQKeglnwVTWVVGETTYSPLPATHI---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 276 agfllplsrGGKIAMNDGLRHIAKNLQQSKtsiliavpllletlHKTILRKATGDAKVAKKYKLGLSLAKALNKIKLNFN 355
Cdd:PRK05857 227 ---------GGLWWILTCLMHGGLCVTGGE--------------NTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 356 DKifaeihkglgGHLRLLVCGGAAIepqILAD---FNDWGITAIQGYGVTE------CSPIISNNRPKYkEHASAGLPTP 426
Cdd:PRK05857 284 TV----------PSLRLVGYGGSRA---IAADvrfIEATGVRTAQVYGLSEtgctalCLPTDDGSIVKI-EAGAVGRPYP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 427 HVEVKIINEDENG-----------IGEIIARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANII 495
Cdd:PRK05857 350 GVDVYLAATDGIGptapgagpsasFGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 496 VTkNGKNIFPEEIefvllkENIIEEVVVYGERDEYGeqiITAEVFPSVEELAKVLETNakdidtsvLTGSVAEGLVKDAI 575
Cdd:PRK05857 429 IC-GGVNIAPDEV------DRIAEGVSGVREAACYE---IPDEEFGALVGLAVVASAE--------LDESAARALKHTIA 490
|
570 580 590
....*....|....*....|....*....|...
gi 1360655949 576 SKANKELQNFKKVKDIVLRAEpFPRNTSKKILR 608
Cdd:PRK05857 491 ARFRRESEPMARPSTIVIVTD-IPRTQSGKVMR 522
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
405-609 |
1.05e-16 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 83.52 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 405 SPIISNNR---PKYKEHASAGLPTPHVEVKIINED-----ENGIGEIIARGP---NVMLGYYEDPE--KTAEAIDSEGFY 471
Cdd:cd05967 394 WPITANPVglePLPIKAGSPGKPVPGYQVQVLDEDgepvgPNELGNIVIKLPlppGCLLTLWKNDErfKKLYLSKFPGYY 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 472 HTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAEVfpsveelakVLE 551
Cdd:cd05967 474 DTGDAGYKDEDGYLFIMGRTDDVINVA-GHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLV---------VLK 543
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1360655949 552 TNAKDIDTSVLTGSVAegLVKDAISKankeLQNFKKVkdIVLRAepFPRNTSKKILRN 609
Cdd:cd05967 544 EGVKITAEELEKELVA--LVREQIGP----VAAFRLV--IFVKR--LPKTRSGKILRR 591
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
216-610 |
1.11e-16 |
|
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: 82.98 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 216 DPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLL---SvlplhHTFEAT-AGFLLPLSRGGKIA-- 289
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqfaS-----YTFDVSiLEIFTTLAAGGCLCip 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 290 -----MNDglrhIAKNLQQSKTSILIAVPllletlhktilrkatgdakvakkyklglSLAKALNKIKLNfndkifaeihk 364
Cdd:cd05918 179 seedrLND----LAGFINRLRVTWAFLTP----------------------------SVARLLDPEDVP----------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 365 glggHLRLLVCGGAAIEPqilADFNDW--GITAIQGYGVTECSPIISNNRPKYKEHASA-GLPTP---HVeVKIINEDE- 437
Cdd:cd05918 216 ----SLRTLVLGGEALTQ---SDVDTWadRVRLINAYGPAECTIAATVSPVVPSTDPRNiGRPLGatcWV-VDPDNHDRl 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 438 ---NGIGEIIARGPNVMLGYYEDPEKTAEA-IDSEG------------FYHTGDYGYIDDRGFIYITGRKANIIvtK-NG 500
Cdd:cd05918 288 vpiGAVGELLIEGPILARGYLNDPEKTAAAfIEDPAwlkqegsgrgrrLYRTGDLVRYNPDGSLEYVGRKDTQV--KiRG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 501 KNIFPEEIEFVLLK---ENIIEEVVVYGERDEYGEQIITAEVFPSVEELakvleTNAKDIDTSVLTGSVAEGLVKDAISK 577
Cdd:cd05918 366 QRVELGEIEHHLRQslpGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSS-----GSGDGDSLFLEPSDEFRALVAELRSK 440
|
410 420 430
....*....|....*....|....*....|...
gi 1360655949 578 ANKELQNFkKVKDIVLRAEPFPRNTSKKILRNK 610
Cdd:cd05918 441 LRQRLPSY-MVPSVFLPLSHLPLTASGKIDRRA 472
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
213-551 |
1.91e-16 |
|
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: 83.37 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 213 LPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLhhTFEATAG-FLLPLSRGGKIAM- 290
Cdd:COG1020 612 VPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASL--SFDASVWeIFGALLSGATLVLa 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 291 -NDGLR---HIAKNLQQSKTSILIAVPLLLETLhktilrkatgdakvakkyklglslakalnkiklnfndkifAEIHKGL 366
Cdd:COG1020 690 pPEARRdpaALAELLARHRVTVLNLTPSLLRAL----------------------------------------LDAAPEA 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 367 GGHLRLLVCGGAAIEPQILADFND--WGITAIQGYGVTECSpIISNNRPKYKEHASA-----GLPTPHVEVKIIneDENG 439
Cdd:COG1020 730 LPSLRLVLVGGEALPPELVRRWRArlPGARLVNLYGPTETT-VDSTYYEVTPPDADGgsvpiGRPIANTRVYVL--DAHL 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 -------IGEIIARGPNVMLGYYEDPEKTAEA--IDSEGF-----YHTGDYGY------------IDD----RGFiyitg 489
Cdd:COG1020 807 qpvpvgvPGELYIGGAGLARGYLNRPELTAERfvADPFGFpgarlYRTGDLARwlpdgnleflgrADDqvkiRGF----- 881
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1360655949 490 RkaniivtkngknIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAEVFPSVEELAKVLE 551
Cdd:COG1020 882 R------------IELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAAL 931
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
67-488 |
2.06e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 82.48 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 67 EYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTI 146
Cdd:PRK06164 32 EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 147 FYsrsqEDKLLGIadNIKQVKNLVSYD-LPTENSSKLAGEDKD-----LFFLWDLINTGNSIRANGNTQYDnlPIDPRAL 220
Cdd:PRK06164 112 VV----WPGFKGI--DFAAILAAVPPDaLPPLRAIAVVDDAADatpapAPGARVQLFALPDPAPPAAAGER--AADPDAG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 221 AVLLFTSGTTAKSKAVM------LCHDNLCVNIYDVcltvefDKNDTLLSVLPLHHTFeATAGFLLPLSRGGkiamndgl 294
Cdd:PRK06164 184 ALLFTTSGTTSGPKLVLhrqatlLRHARAIARAYGY------DPGAVLLAALPFCGVF-GFSTLLGALAGGA-------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 295 rhiaknlqqsktsiliavPLLLEtlhktilrkATGDAKVAkkyklglslAKAL--NKIKLNF-NDKIFAEIHKGLGG--- 368
Cdd:PRK06164 249 ------------------PLVCE---------PVFDAART---------ARALrrHRVTHTFgNDEMLRRILDTAGErad 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 369 --HLRLlvCGGAAIEP---QILADFNDWGITAIQGYGVTECSPIISNNR---PKYKEHASAGLP-TPHVEVKIINEDENG 439
Cdd:PRK06164 293 fpSARL--FGFASFAPalgELAALARARGVPLTGLYGSSEVQALVALQPatdPVSVRIEGGGRPaSPEARVRARDPQDGA 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1360655949 440 I------GEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYI-DDRGFIYIT 488
Cdd:PRK06164 371 LlpdgesGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTrGDGQFVYQT 426
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
216-598 |
2.55e-16 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 82.50 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 216 DPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDT-LLSVLPLHHTfeATAGFLL-PLSRGGK---IAM 290
Cdd:cd17632 221 DDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASiTLNFMPMSHI--AGRISLYgTLARGGTayfAAA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 291 NDgLRHIAKNLQQSKTSILIAVPLLLETLHKTILrkatgdAKVAKKYKLGLSLAKALNKIKLNFNDKIfaeihkgLGGHL 370
Cdd:cd17632 299 SD-MSTLFDDLALVRPTELFLVPRVCDMLFQRYQ------AELDRRSVAGADAETLAERVKAELRERV-------LGGRL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 371 RLLVCGGAAIEPQILAdFNDW--GITAIQGYGVTECSPIISNN---RPKYKEHASAGLP--------TPHVEvkiinede 437
Cdd:cd17632 365 LAAVCGSAPLSAEMKA-FMESllDLDLHDGYGSTEAGAVILDGvivRPPVLDYKLVDVPelgyfrtdRPHPR-------- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 438 ngiGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGD---------YGYIDdrgfiyitgRKANIIVTKNGKNIFPEEI 508
Cdd:cd17632 436 ---GELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDvmaelgpdrLVYVD---------RRNNVLKLSQGEFVTVARL 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 509 EFVLLKENIIEEVVVYG--ERdEYgeqiITAEVFPSVEELAkvletnakDIDTSVLTGSVAEGLvkDAISKANkELQNFK 586
Cdd:cd17632 504 EAVFAASPLVRQIFVYGnsER-AY----LLAVVVPTQDALA--------GEDTARLRAALAESL--QRIAREA-GLQSYE 567
|
410
....*....|..
gi 1360655949 587 KVKDIVLRAEPF 598
Cdd:cd17632 568 IPRDFLIETEPF 579
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
220-608 |
5.98e-16 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 80.60 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 220 LAVLLFTSGTTAKSKAVMLCH-------DNLCVNIydvcltVEFDKNDTLLSVLPLHHTFeATAGFLL-PLSRGGKIAMN 291
Cdd:cd05958 99 ICILAFTSGTTGAPKATMHFHrdplasaDRYAVNV------LRLREDDRFVGSPPLAFTF-GLGGVLLfPFGVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 292 DGL--RHIAKNLQQSKTSILIAVPllletlhkTILRKATGDAKVAKKyklglslakalnkiklnfndkifaeihkgLGGH 369
Cdd:cd05958 172 EEAtpDLLLSAIARYKPTVLFTAP--------TAYRAMLAHPDAAGP-----------------------------DLSS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDEN-----GIGEI 443
Cdd:cd05958 215 LRKCVSAGEALPAALHRAWKEaTGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNpvpdgTIGRL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 444 IARGPNvmlGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVV 523
Cdd:cd05958 295 AVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVEDVLLQHPAVAECAV 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 524 YGERDEYGEQIITAEVFPSVEELAkvletnakdidtsvltgsvAEGLVKDAISKANKELQNFKKVKDIVLRAEpFPRNTS 603
Cdd:cd05958 371 VGHPDESRGVVVKAFVVLRPGVIP-------------------GPVLARELQDHAKAHIAPYKYPRAIEFVTE-LPRTAT 430
|
....*
gi 1360655949 604 KKILR 608
Cdd:cd05958 431 GKLQR 435
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
71-534 |
6.72e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 80.89 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATV-CGLAIIaPMDKELPANEVENLINRSGANTIFYS 149
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAErSGLYYT-CVNSHLTPAEAAYIVDDSGARALITS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 150 RSQEDKLLGIADNIKQVKNLVSYDLPTEnsskLAGEDKdlfflwdlintgnsiRANGNTQYDNLPIDPRALAV-LLFTSG 228
Cdd:PRK13391 104 AAKLDVARALLKQCPGVRHRLVLDGDGE----LEGFVG---------------YAEAVAGLPATPIADESLGTdMLYSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 229 TTAKSKAVM--LCHDNLC--VNIYDVCLT-VEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMN--DGLRHIAKnL 301
Cdd:PRK13391 165 TTGRPKGIKrpLPEQPPDtpLPLTAFLQRlWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEhfDAEQYLAL-I 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 302 QQSKTSILIAVPllleTLHKTILRKAtgdAKVAKKYKLGlSLAKAlnkiklnfndkifaeIHkglgghlrllvcGGAAIE 381
Cdd:PRK13391 244 EEYGVTHTQLVP----TMFSRMLKLP---EEVRDKYDLS-SLEVA---------------IH------------AAAPCP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 382 PQILADFNDW-GITAIQGYGVTECSPIISNNRPKYKEH-ASAGLP---TPHVEvkiineDENG-------IGEIIARGpN 449
Cdd:PRK13391 289 PQVKEQMIDWwGPIIHEYYAATEGLGFTACDSEEWLAHpGTVGRAmfgDLHIL------DDDGaelppgePGTIWFEG-G 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 450 VMLGYYEDPEKTAEAIDSEGFYHT-GDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYG-ER 527
Cdd:PRK13391 362 RPFEYLNDPAKTAEARHPDGTWSTvGDIGYVDEDGYLYLTDRAAFMIIS-GGVNIYPQEAENLLITHPKVADAAVFGvPN 440
|
....*..
gi 1360655949 528 DEYGEQI 534
Cdd:PRK13391 441 EDLGEEV 447
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
369-557 |
7.61e-16 |
|
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: 80.59 E-value: 7.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 369 HLRLLVCGGAAIEPQILADF-NDWGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIIneDENGI------- 440
Cdd:cd05928 292 SLQHCVTGGEPLNPEVLEKWkAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQII--DDNGNvlppgte 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 441 GEIIAR-GPN----VMLGYYEDPEKTAEAIDSEgFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKE 515
Cdd:cd05928 370 GDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGD-FYLTGDRGIMDEDGYFWFMGRADDVINS-SGYRIGPFEVESALIEH 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1360655949 516 NIIEEVVVYGERDEYGEQIITAEV-----FPS--VEELAKVLETNAKDI 557
Cdd:cd05928 448 PAVVESAVVSSPDPIRGEVVKAFVvlapqFLShdPEQLTKELQQHVKSV 496
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
69-557 |
7.83e-16 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 80.70 E-value: 7.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTI-- 146
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLit 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 147 ---FYSRSQEDKLLGIAD-----NIKQVKNLVSYDLPTENSSKLAGEDkdlfFLWDlintgnSIRANGNTQYDNLPIDPR 218
Cdd:cd17634 163 adgGVRAGRSVPLKKNVDdalnpNVTSVEHVIVLKRTGSDIDWQEGRD----LWWR------DLIAKASPEHQPEAMNAE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 219 ALAVLLFTSGTTAKSKAVMlcHDNlcvNIYDVCLTVEFdkndtllsvlplHHTFEATAG----------------FLL-- 280
Cdd:cd17634 233 DPLFILYTSGTTGKPKGVL--HTT---GGYLVYAATTM------------KYVFDYGPGdiywctadvgwvtghsYLLyg 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 281 PLSRGGKIAMNDGL------RHIAKNLQQSKTSILIAVPLLLETLhktilrKATGDAKVAKKyklGLSLAKALNKIKLNF 354
Cdd:cd17634 296 PLACGATTLLYEGVpnwptpARMWQVVDKHGVNILYTAPTAIRAL------MAAGDDAIEGT---DRSSLRILGSVGEPI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 355 NDKIFAEIHKGLGGHLRLLVcggaaiepqiladfNDWGITAIQGYgvtecspIISNNRPKYKEHA-SAGLPTPHVEVKII 433
Cdd:cd17634 367 NPEAYEWYWKKIGKEKCPVV--------------DTWWQTETGGF-------MITPLPGAIELKAgSATRPVFGVQPAVV 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 434 NEDEN-----GIGEII--ARGPNVMLGYYEDPEKTAEAIDS--EGFYHTGDYGYIDDRGFIYITGRKANIIvTKNGKNIF 504
Cdd:cd17634 426 DNEGHpqpggTEGNLVitDPWPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVI-NVAGHRLG 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1360655949 505 PEEIEFVLLKENIIEEVVVYGERDE------YGEQIITAEVFPSVEELAKVLETNAKDI 557
Cdd:cd17634 505 TAEIESVLVAHPKVAEAAVVGIPHAikgqapYAYVVLNHGVEPSPELYAELRNWVRKEI 563
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
69-539 |
8.14e-16 |
|
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: 80.32 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATV-CGlAIIAPMDKELPANEVENLINRSGANTIF 147
Cdd:cd12117 21 RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLkAG-AAYVPLDPELPAERLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 148 YSRSQEDKLLGIADNIKQVKNLVSYDLPTENSsklagedkdlfflwdlintgnsirangntqydnlPIDPRALAVLLFTS 227
Cdd:cd12117 100 TDRSLAGRAGGLEVAVVIDEALDAGPAGNPAV----------------------------------PVSPDDLAYVMYTS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 228 GTTAKSKAVMLCHDNLCVNIYDVCLtVEFDKNDTLLSVLPLhhTFEAtAGFLL--PLSRGGKIAMNDGlrhiaknlqqsk 305
Cdd:cd12117 146 GSTGRPKGVAVTHRGVVRLVKNTNY-VTLGPDDRVLQTSPL--AFDA-STFEIwgALLNGARLVLAPK------------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 306 tsiliAVPLLLETLHKTIlrkATGDAKVakkyklgLSLAKALnkiklnFNdkIFAEIHKGLGGHLRLLVCGGAAIEP--- 382
Cdd:cd12117 210 -----GTLLDPDALGALI---AEEGVTV-------LWLTAAL------FN--QLADEDPECFAGLRELLTGGEVVSPphv 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 383 -QILADFNdwGITAIQGYGVTE------CSPIisnnrPKYKEHASA---GLPTPHVEVKIINED----ENGI-GEIIARG 447
Cdd:cd12117 267 rRVLAACP--GLRLVNGYGPTEnttfttSHVV-----TELDEVAGSipiGRPIANTRVYVLDEDgrpvPPGVpGELYVGG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 448 PNVMLGYYEDPEKTAE------AIDSEGFYHTGDY-GYIDDRGFIYItGRkANIIVTKNGKNIFPEEIEFVLLKENIIEE 520
Cdd:cd12117 340 DGLALGYLNRPALTAErfvadpFGPGERLYRTGDLaRWLPDGRLEFL-GR-IDDQVKIRGFRIELGEIEAALRAHPGVRE 417
|
490
....*....|....*....
gi 1360655949 521 VVVYGERDEYGEQIITAEV 539
Cdd:cd12117 418 AVVVVREDAGGDKRLVAYV 436
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
398-539 |
1.27e-15 |
|
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: 78.50 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 398 GYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDENGI-----GEIIARGPNVMLGYYEDPEKTAEAIDSeGFYH 472
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVpdgevGEIVARGPTVMAGYWNRPEVNARRTRG-GWHH 220
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1360655949 473 TGDYGYIDDRGFIYITGRKANIIvtKNGK-NIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAEV 539
Cdd:cd17636 221 TNDLGRREPDGSLSFVGPKTRMI--KSGAeNIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIV 286
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
214-539 |
5.50e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 77.80 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 214 PIDPRA--LAVLLFTSGTTAKSKAVMLCHDNLCVNiyDVCLTVEFD--KNDTLLSVLPLHHTFEATAGFLLPLSRGGKIA 289
Cdd:PRK07867 146 FRVADPddLFMLIFTSGTSGDPKAVRCTHRKVASA--GVMLAQRFGlgPDDVCYVSMPLFHSNAVMAGWAVALAAGASIA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 290 MndglrhiaknlqQSKTSiliaVPLLLETLHKTilrKATGDAKVAKKykLGLSLA------KALNKIKLNFNDKifaeih 363
Cdd:PRK07867 224 L------------RRKFS----ASGFLPDVRRY---GATYANYVGKP--LSYVLAtperpdDADNPLRIVYGNE------ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 364 kglgghlrllvcgGAAIEpqiLADFND-WGITAIQGYGVTECSPIISnnRPKYKEHASAGLPTPHVEV------------ 430
Cdd:PRK07867 277 -------------GAPGD---IARFARrFGCVVVDGFGSTEGGVAIT--RTPDTPPGALGPLPPGVAIvdpdtgtecppa 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 431 -----KIINEDEnGIGEII-ARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIF 504
Cdd:PRK07867 339 edadgRLLNADE-AIGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLG 415
|
330 340 350
....*....|....*....|....*....|....*.
gi 1360655949 505 PEEIEFVLLKENIIEEVVVYGERD-EYGEQIITAEV 539
Cdd:PRK07867 416 TAPIERILLRYPDATEVAVYAVPDpVVGDQVMAALV 451
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
71-531 |
6.37e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 77.22 E-value: 6.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATV-CGlAIIAPMDKELPANEVENLINRSGANTIFYS 149
Cdd:PRK09029 29 LTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLqCG-ARVLPLNPQLPQPLLEELLPSLTLDFALVL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 150 rsqedkllgiadnikqvknlvsydlptenssklagEDKDLFFLWDLINTGNSIRANgntqydNLPIDPRALAVLLFTSGT 229
Cdd:PRK09029 108 -----------------------------------EGENTFSALTSLHLQLVEGAH------AVAWQPQRLATMTLTSGS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 230 TAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDT-LLSvLPLHHTfeATAGFLLP-LSRGGKIAMNDGLrHIAKNLQQSKTS 307
Cdd:PRK09029 147 TGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSwLLS-LPLFHV--SGQGIVWRwLYAGATLVVRDKQ-PLEQALAGCTHA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 308 ILIAVPL--LLETLHKTILRKATgdakvakkyklglslakalnkiklnfndkifaeihkglgghlrLLvcGGAAIEPQIL 385
Cdd:PRK09029 223 SLVPTQLwrLLDNRSEPLSLKAV-------------------------------------------LL--GGAAIPVELT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 386 ADFNDWGITAIQGYGVTECSPIISNNRpkYKEHASAGLPTPHVEVKIINedengiGEIIARGPNVMLGYYEDPEKTAeAI 465
Cdd:PRK09029 258 EQAEQQGIRCWCGYGLTEMASTVCAKR--ADGLAGVGSPLPGREVKLVD------GEIWLRGASLALGYWRQGQLVP-LV 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1360655949 466 DSEGFYHTGDYGYIDDrGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEV-VVYGERDEYG 531
Cdd:PRK09029 329 NDEGWFATRDRGEWQN-GELTILGRLDNLFFS-GGEGIQPEEIERVINQHPLVQQVfVVPVADAEFG 393
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
69-541 |
7.33e-15 |
|
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: 77.33 E-value: 7.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFY 148
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 149 SRSQEDKLLGIADNIkqvknlvsydlptenssklagedkdLFFLWDLINTGNSIRAngntqydnlPIDPRALAVLLFTSG 228
Cdd:cd12116 91 DDALPDRLPAGLPVL-------------------------LLALAAAAAAPAAPRT---------PVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 229 TTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVlplhhtfeATAGF-------LLPLSRGGKIAM------NDGLR 295
Cdd:cd12116 137 STGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAV--------TTYAFdisllelLLPLLAGARVVIapretqRDPEA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 296 hIAKNLQQSKTSILIAVPLLLETLHKTILRKATGdakvakkyklglslakalnkiklnfndkifaeihkglgghLRLLvC 375
Cdd:cd12116 209 -LARLIEAHSITVMQATPATWRMLLDAGWQGRAG----------------------------------------LTAL-C 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 376 GGAAIEPQILADFNDWGITAIQGYGVTE------CSPIisnnRPKyKEHASAGLPTPHVEVKIIneDENG-------IGE 442
Cdd:cd12116 247 GGEALPPDLAARLLSRVGSLWNLYGPTEttiwstAARV----TAA-AGPIPIGRPLANTQVYVL--DAALrpvppgvPGE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 443 IIARGPNVMLGYYEDPEKTAEAIDSEGF-------YHTGDYGYIDDRGFIYITGRKANIIvtK-NGKNIFPEEIEFVLLK 514
Cdd:cd12116 320 LYIGGDGVAQGYLGRPALTAERFVPDPFagpgsrlYRTGDLVRRRADGRLEYLGRADGQV--KiRGHRIELGEIEAALAA 397
|
490 500
....*....|....*....|....*..
gi 1360655949 515 ENIIEEVVVYGeRDEYGEQIITAEVFP 541
Cdd:cd12116 398 HPGVAQAAVVV-REDGGDRRLVAYVVL 423
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
217-511 |
9.12e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 77.12 E-value: 9.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 217 PRAL--AVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGF--LLPLSRGGKIAMND 292
Cdd:cd05910 82 PKADepAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLtsVIPDMDPTRPARAD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 293 GlRHIAKNLQQSKTSILIAVPLLLETLhktilrkatgdakvakkyklglSLAKALNKIKLNfndkifaeihkglggHLRL 372
Cdd:cd05910 162 P-QKLVGAIRQYGVSIVFGSPALLERV----------------------ARYCAQHGITLP---------------SLRR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 373 LVCGGAAIEPQILADFNDW---GITAIQGYGVTECSPIIS-NNRPKYKEHASA---------GLPTPHVEVKIINEDEN- 438
Cdd:cd05910 204 VLSAGAPVPIALAARLRKMlsdEAEILTPYGATEALPVSSiGSRELLATTTAAtsggagtcvGRPIPGVRVRIIEIDDEp 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 439 -------------GIGEIIARGPNVMLGYYEDPEKTAEA-ID--SEGFYH-TGDYGYIDDRGFIYITGRKANIIVTkNGK 501
Cdd:cd05910 284 iaewddtlelprgEIGEITVTGPTVTPTYVNRPVATALAkIDdnSEGFWHrMGDLGYLDDEGRLWFCGRKAHRVIT-TGG 362
|
330
....*....|
gi 1360655949 502 NIFPEEIEFV 511
Cdd:cd05910 363 TLYTEPVERV 372
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
223-552 |
1.01e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 75.88 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 223 LLFTSGTTAKSKAVMLCHDNlcvnIYDVCL------TVEFDKND------------TLLSVLPLHHTFEATAGFLLPLSr 284
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQED----IFRMLMggadfgTGEFTPSEdahkaaaaaagtVMFPAPPLMHGTGSWTAFGGLLG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 285 GGKIAMNDgLRHIAKNLqqsktsiliavpllLETL--HKTILRKATGDAkVAKkyklglSLAKALnkiklnfndkifaei 362
Cdd:cd05924 83 GQTVVLPD-DRFDPEEV--------------WRTIekHKVTSMTIVGDA-MAR------PLIDAL--------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 363 hKGLGGH----LRLLVCGGAAIEPQILADFNDW--GITAIQGYGVTECSPI-ISNNRPKYKEHASAGLPTPHVEV----- 430
Cdd:cd05924 126 -RDAGPYdlssLFAISSGGALLSPEVKQGLLELvpNITLVDAFGSSETGFTgSGHSAGSGPETGPFTRANPDTVVldddg 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 431 KIINEDENGIGEIIARGpNVMLGYYEDPEKTAEA---IDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEE 507
Cdd:cd05924 205 RVVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINT-GGEKVFPEE 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1360655949 508 IEFVLLKENIIEEVVVYGERDE-YGEQIIT----AEVF-PSVEELAKVLET 552
Cdd:cd05924 283 VEEALKSHPAVYDVLVVGRPDErWGQEVVAvvqlREGAgVDLEELREHCRT 333
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
68-544 |
1.02e-14 |
|
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: 76.82 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 68 YRG--ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANT 145
Cdd:cd17645 19 DRGqsLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 146 IFYsrsqedkllgiadnikqvknlvsydlptenssklagedkdlfflwdlintgnsirangntqydnlpiDPRALAVLLF 225
Cdd:cd17645 99 LLT-------------------------------------------------------------------NPDDLAYVIY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 226 TSGTTAKSKAVMLCHDNLcVNI---YDVCLTVEFDKNDTLLSVLplhhTFEATAGFLLP-LSRGGKIamndglrHIaknL 301
Cdd:cd17645 112 TSGSTGLPKGVMIEHHNL-VNLcewHRPYFGVTPADKSLVYASF----SFDASAWEIFPhLTAGAAL-------HV---V 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 302 QQSKTSILIAVPLLLETLHKTILRKATGdakvakkyklglslakalnkiklnfndkiFAEIHKGLGGH-LRLLVCGGaai 380
Cdd:cd17645 177 PSERRLDLDALNDYFNQEGITISFLPTG-----------------------------AAEQFMQLDNQsLRVLLTGG--- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 381 epQILADFNDWGITAIQGYGVTECSpIISNNRPKYKEHAS--AGLPTPHVEVKIINED-----ENGIGEIIARGPNVMLG 453
Cdd:cd17645 225 --DKLKKIERKGYKLVNNYGPTENT-VVATSFEIDKPYANipIGKPIDNTRVYILDEAlqlqpIGVAGELCIAGEGLARG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 454 YYEDPEKTAEA------IDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFPEEIEFVLLKENIIEEVVVYGER 527
Cdd:cd17645 302 YLNRPELTAEKfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIR-GYRIEPGEIEPFLMNHPLIELAAVLAKE 380
|
490
....*....|....*..
gi 1360655949 528 DEYGEQIITAEVFPSVE 544
Cdd:cd17645 381 DADGRKYLVAYVTAPEE 397
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
64-537 |
1.19e-14 |
|
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: 76.60 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 64 PDN-----EYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLI 138
Cdd:cd17655 11 PDHtavvfEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 139 NRSGANTIFysrSQEDKLLGIAdNIKQVKNLVSYDLPTENSSKLAgedkdlfflwdlintgnsirangntqydnLPIDPR 218
Cdd:cd17655 91 EDSGADILL---TQSHLQPPIA-FIGLIDLLDEDTIYHEESENLE-----------------------------PVSKSD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 219 ALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHhtFEATAGFLLPlsrggkiamndglrhia 298
Cdd:cd17655 138 DLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASIS--FDASVTEIFA----------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 299 knlqqsktsiliavPLLL-ETLHktILRKATGDAkvakkyklGLSLAKALNKIKLNFND------KIFAEIHKGLGGHLR 371
Cdd:cd17655 199 --------------SLLSgNTLY--IVRKETVLD--------GQALTQYIRQNRITIIDltpahlKLLDAADDSEGLSLK 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 372 LLVCGGAAIEP----QILADFNDwGITAIQGYGVTECS------PIISNNRPKykEHASAGLPTPHVEVKIIneDENG-- 439
Cdd:cd17655 255 HLIVGGEALSTelakKIIELFGT-NPTITNAYGPTETTvdasiyQYEPETDQQ--VSVPIGKPLGNTRIYIL--DQYGrp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 -----IGEIIARGPNVMLGYYEDPEKTAEA------IDSEGFYHTGDYGYIDDRGFIYITGRKANiIVTKNGKNIFPEEI 508
Cdd:cd17655 330 qpvgvAGELYIGGEGVARGYLNRPELTAEKfvddpfVPGERMYRTGDLARWLPDGNIEFLGRIDH-QVKIRGYRIELGEI 408
|
490 500
....*....|....*....|....*....
gi 1360655949 509 EFVLLKENIIEEVVVYGERDEYGEQIITA 537
Cdd:cd17655 409 EARLLQHPDIKEAVVIARKDEQGQNYLCA 437
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
69-570 |
2.68e-14 |
|
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: 75.77 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFY 148
Cdd:cd17646 22 RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 149 SRSQEDKLLGIADnikqVKNLVSYDLPTENSSKLAgedkdlfflwdlintgnsirangntqydnLPIDPRALAVLLFTSG 228
Cdd:cd17646 102 TADLAARLPAGGD----VALLGDEALAAPPATPPL-----------------------------VPPRPDNLAYVIYTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 229 TTAKSKAVMLCHDNLcVNiYDVCLTVEF--DKNDTLLSVLPLhhTFE-ATAGFLLPLSRGGK--IAMNDGLR---HIAKN 300
Cdd:cd17646 149 STGRPKGVMVTHAGI-VN-RLLWMQDEYplGPGDRVLQKTPL--SFDvSVWELFWPLVAGARlvVARPGGHRdpaYLAAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 301 LQQSKTSILIAVPLLLETLhktilrkatgdakvakkyklgLSLAKAlnkiklnfndkifaeihkGLGGHLRLLVCGGAAI 380
Cdd:cd17646 225 IREHGVTTCHFVPSMLRVF---------------------LAEPAA------------------GSCASLRRVFCSGEAL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 381 EPQILADFND-WGITAIQGYGVTECSPIISNNR---PKYKEHASAGLPTPHVEVKIINEDEN----G-IGEIIARGPNVM 451
Cdd:cd17646 266 PPELAARFLAlPGAELHNLYGPTEAAIDVTHWPvrgPAETPSVPIGRPVPNTRLYVLDDALRpvpvGvPGELYLGGVQLA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 452 LGYYEDPEKTAEAIDSEGF------YHTGDYGYIDDRGFIYITGRkANIIVTKNGKNIFPEEIEFVLLKENIIEEVVVYG 525
Cdd:cd17646 346 RGYLGRPALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFLGR-SDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVA 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1360655949 526 ERDEYGEQIITAEVfpsveelakVLETNAKDIDTSVLTGSVAEGL 570
Cdd:cd17646 425 RAAPAGAARLVGYV---------VPAAGAAGPDTAALRAHLAERL 460
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
211-609 |
4.20e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 75.45 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 211 DNLPIDPRALAVLLFTSGTTAKSKAVMLCH-------DNLCvniydvCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLS 283
Cdd:PRK06060 138 GYEPMGGDALAYATYTSGTTGPPKAAIHRHadpltfvDAMC------RKALRLTPEDTGLCSARMYFAYGLGNSVWFPLA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 284 RGGKIAMND---GLRHIAKNLQQSKTSILIAVPllletlhktilrkatgdakvakkyklglslakalnkiklNFNDKIFA 360
Cdd:PRK06060 212 TGGSAVINSapvTPEAAAILSARFGPSVLYGVP---------------------------------------NFFARVID 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 361 EIHKGLGGHLRLLVCGGAAIEPQILADFNDW--GITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINED-- 436
Cdd:PRK06060 253 SCSPDSFRSLRCVVSAGEALELGLAERLMEFfgGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDgt 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 437 ---ENGIGEIIARGPNVMLGYYEDPEKTAEaidSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLL 513
Cdd:PRK06060 333 tagPGVEGDLWVRGPAIAKGYWNRPDSPVA---NEGWLDTRDRVCIDSDGWVTYRCRADDTEVI-GGVNVDPREVERLII 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 514 KENIIEEVVVYGERDEYGEQIITAEVFPSVEELakvletnakdIDTSVLtgsvaeglvKDAISKANKELQNFkKVKDIVL 593
Cdd:PRK06060 409 EDEAVAEAAVVAVRESTGASTLQAFLVATSGAT----------IDGSVM---------RDLHRGLLNRLSAF-KVPHRFA 468
|
410
....*....|....*.
gi 1360655949 594 RAEPFPRNTSKKILRN 609
Cdd:PRK06060 469 VVDRLPRTPNGKLVRG 484
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-544 |
4.32e-14 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 75.03 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 429 EVKIINEDEN-----GIGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIvTKNGKNI 503
Cdd:PRK10946 364 EVWVADADGNplpqgEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQI-NRGGEKI 442
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1360655949 504 FPEEIEFVLLK-ENIIEEVVVYGERDEYGEQ----IITAEVFPSVE 544
Cdd:PRK10946 443 AAEEIENLLLRhPAVIHAALVSMEDELMGEKscafLVVKEPLKAVQ 488
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
71-544 |
8.19e-14 |
|
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: 74.05 E-value: 8.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSR 150
Cdd:cd17656 14 LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 SQEDKLlgiADNIKQVknlvsydlptenssklagedkdlFFLWDLIntgnsirANGNTQYDNLPIDPRALAVLLFTSGTT 230
Cdd:cd17656 94 HLKSKL---SFNKSTI-----------------------LLEDPSI-------SQEDTSNIDYINNSDDLLYIIYTSGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 231 AKSKAVMLCHDNLcVNIydvcltvefdkndtllsvlpLHHTFEATAgfllpLSRGGKIamndgLRHIAKNLQQSKTSILI 310
Cdd:cd17656 141 GKPKGVQLEHKNM-VNL--------------------LHFEREKTN-----INFSDKV-----LQFATCSFDVCYQEIFS 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 311 AVpLLLETLHktILRKATG------DAKVAKKYKLGLSLAKALnkIKLNFNDKIFAE-IHKGLGghlRLLVCGGAAIEPQ 383
Cdd:cd17656 190 TL-LSGGTLY--IIREETKrdveqlFDLVKRHNIEVVFLPVAF--LKFIFSEREFINrFPTCVK---HIITAGEQLVITN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 384 ILAD-FNDWGITAIQGYGVTECSPIIS---NNRPKYKEHASAGLPTPHVEVKIINEDEN-----GIGEIIARGPNVMLGY 454
Cdd:cd17656 262 EFKEmLHEHNVHLHNHYGPSETHVVTTytiNPEAEIPELPPIGKPISNTWIYILDQEQQlqpqgIVGELYISGASVARGY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 455 YEDPEKTAEAIDSEGF------YHTGDYG-YIDDrGFIYITGRkANIIVTKNGKNIFPEEIEFVLLKENIIEEVVVYGER 527
Cdd:cd17656 342 LNRQELTAEKFFPDPFdpnermYRTGDLArYLPD-GNIEFLGR-ADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKA 419
|
490
....*....|....*..
gi 1360655949 528 DEYGEQIITAEVFPSVE 544
Cdd:cd17656 420 DDKGEKYLCAYFVMEQE 436
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
370-523 |
8.41e-14 |
|
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: 73.76 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQILADFND-WGITAIQGYGVTECSPIISNNRPKYKEHASAGLPTPHVEVKIINEDENGI--GEII-- 444
Cdd:cd05974 202 LREVVGAGEPLNPEVIEQVRRaWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPAteGEVAld 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 445 ---ARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKNGKnIFPEEIEFVLLKENIIEEV 521
Cdd:cd05974 282 lgdTRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR-ISPFELESVLIEHPAVAEA 359
|
..
gi 1360655949 522 VV 523
Cdd:cd05974 360 AV 361
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
71-550 |
2.83e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.45 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTifysr 150
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQL----- 3157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 sqedkllgiadnikqvknlvsydLPTENSSKLAGEDKDLFFLWDlintgnsiRANGNTQYDNLPI--DPRALAVLLFTSG 228
Cdd:PRK12316 3158 -----------------------LLSQSHLRLPLAQGVQVLDLD--------RGDENYAEANPAIrtMPENLAYVIYTSG 3206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 229 TTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLhhTFEATA-GFLLPLSRGGKIAMNDglrhiaknlqqskTS 307
Cdd:PRK12316 3207 STGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF--SFDVFVeELFWPLMSGARVVLAG-------------PE 3271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 308 ILIAVPLLLETLHKTILrkatgdaKVAKKYKLGLSlakalnkiklnfndKIFAEIHKGLGGHLRLLVCGGAAIEPQILAD 387
Cdd:PRK12316 3272 DWRDPALLVELINSEGV-------DVLHAYPSMLQ--------------AFLEEEDAHRCTSLKRIVCGGEALPADLQQQ 3330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 388 FNDwGITAIQGYGVTECS--PIISNNRPKYKEHASAGLPTPHVEVKIINEDEN-----GIGEIIARGPNVMLGYYEDPEK 460
Cdd:PRK12316 3331 VFA-GLPLYNLYGPTEATitVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEpvpvgALGELYLGGEGLARGYHNRPGL 3409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 461 TAEAIDSEGF------YHTGDYGYIDDRGFIYITGRkANIIVTKNGKNIFPEEIEFVLLKENIIEEVVVYgerDEYGEQI 534
Cdd:PRK12316 3410 TAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGR-VDHQVKIRGFRIELGEIEARLLEHPWVREAVVL---AVDGRQL 3485
|
490 500
....*....|....*....|.
gi 1360655949 535 ITAEVFPSV-----EELAKVL 550
Cdd:PRK12316 3486 VAYVVPEDEagdlrEALKAHL 3506
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
41-539 |
3.16e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 72.62 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 41 LKDPVALRELDPRSEaainfrinpdneyRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLA 120
Cdd:PRK04319 57 RKDKVALRYLDASRK-------------EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 121 IIAPMDKELPANEVENLINRSGANTIFYSRSQEDKLlgIADNIKQVKNLVSYDLPTENSSKLagedkdlfflWDLintgN 200
Cdd:PRK04319 124 IVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEEGPGT----------LDF----N 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 201 SIRANGNTQYDNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYdvcltvefdkndTLLSVLPLHHT--FEATA-- 276
Cdd:PRK04319 188 ALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQ------------TGKYVLDLHEDdvYWCTAdp 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 277 --------GFLLPLSRGgkiAMN--DGLRHIAKN----LQQSKTSILIAVPllletlhkTILR---KATGDakVAKKYKL 339
Cdd:PRK04319 256 gwvtgtsyGIFAPWLNG---ATNviDGGRFSPERwyriLEDYKVTVWYTAP--------TAIRmlmGAGDD--LVKKYDL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 340 GlslakalnkiklnfndkifaeihkglggHLRLLVCGGAAIEPQILAdfndWGITAiqgYGV--------TECSPI-ISN 410
Cdd:PRK04319 323 S----------------------------SLRHILSVGEPLNPEVVR----WGMKV---FGLpihdnwwmTETGGImIAN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 411 N-----RPkykehASAGLPTPHVEVKIINEDENG-----IGEI-IARG-PNVMLGYYEDPEKTAEAIdSEGFYHTGDYGY 478
Cdd:PRK04319 368 YpamdiKP-----GSMGKPLPGIEAAIVDDQGNElppnrMGNLaIKKGwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAY 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1360655949 479 IDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDE-YGEqIITAEV 539
Cdd:PRK04319 442 MDEDGYFWFQGRVDDVIKT-SGERVGPFEVESKLMEHPAVAEAGVIGKPDPvRGE-IIKAFV 501
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
194-511 |
3.19e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 72.49 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 194 DLINTGNSIRANGNTqydnlPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFD-KNDTLLSVLPLHHTF 272
Cdd:PRK05851 133 DLATAAHTNRSASLT-----PPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDaATDVGCSWLPLYHDM 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 273 EATagFLLPLSRGGKiamndglrhiakNLQQSKTSILIAVPL-LLETLHKTilrKATGDAKVAKKYKLGLSLAKALNKIK 351
Cdd:PRK05851 208 GLA--FLLTAALAGA------------PLWLAPTTAFSASPFrWLSWLSDS---RATLTAAPNFAYNLIGKYARRVSDVD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 352 LnfndkifaeihkglgGHLRLLVCGGAAIEPQILADFND----WGI---TAIQGYGVTECSPIISNNRP----------- 413
Cdd:PRK05851 271 L---------------GALRVALNGGEPVDCDGFERFATamapFGFdagAAAPSYGLAESTCAVTVPVPgiglrvdevtt 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 414 ----KYKEHASAGLPTPHVEVKIINEDE------NGIGEIIARGPNVMLGYY-EDPektaeaIDSEGFYHTGDYGYIDDR 482
Cdd:PRK05851 336 ddgsGARRHAVLGNPIPGMEVRISPGDGaagvagREIGEIEIRGASMMSGYLgQAP------IDPDDWFPTGDLGYLVDG 409
|
330 340
....*....|....*....|....*....
gi 1360655949 483 GFIyITGRKANIIvTKNGKNIFPEEIEFV 511
Cdd:PRK05851 410 GLV-VCGRAKELI-TVAGRNIFPTEIERV 436
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
61-554 |
6.22e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 72.30 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 61 RINPDN-----EYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVE 135
Cdd:PRK12316 4562 RMTPDAvavvfDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLA 4641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 136 NLINRSGANTIFySRSQEDKLLGIADNIKqvknlvSYDL-PTENssklagedkdlfflWDlintgnsiranGNTQYD-NL 213
Cdd:PRK12316 4642 YMMEDSGAALLL-TQSHLLQRLPIPDGLA------SLALdRDED--------------WE-----------GFPAHDpAV 4689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 214 PIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLhhTFEATA-GFLLPLSRGGKIAMND 292
Cdd:PRK12316 4690 RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF--SFDGSHeGLYHPLINGASVVIRD 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 293 GLRHIAKNLQQ----SKTSILIAVPLLLETLhktiLRKATGDAKVAKkyklglslakalnkiklnfndkifaeihkglgg 368
Cdd:PRK12316 4768 DSLWDPERLYAeiheHRVTVLVFPPVYLQQL----AEHAERDGEPPS--------------------------------- 4810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 369 hLRLLVCGGAAIEPQILADFndWGITA----IQGYGVTECS--PIISNNRPKYKEHASA---GLPTPHVEVKIINEDEN- 438
Cdd:PRK12316 4811 -LRVYCFGGEAVAQASYDLA--WRALKpvylFNGYGPTETTvtVLLWKARDGDACGAAYmpiGTPLGNRSGYVLDGQLNp 4887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 439 ----GIGEIIARGPNVMLGYYEDPEKTAE-----AIDSEG--FYHTGDYGYIDDRGFIYITGRkANIIVTKNGKNIFPEE 507
Cdd:PRK12316 4888 lpvgVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGR-VDHQVKIRGFRIELGE 4966
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1360655949 508 IEFVLLKENIIEEVVVYGERDEYGEQIItAEVFPSVEELAKVLETNA 554
Cdd:PRK12316 4967 IEARLREHPAVREAVVIAQEGAVGKQLV-GYVVPQDPALADADEAQA 5012
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
207-552 |
1.18e-12 |
|
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: 70.16 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 207 NTQYDNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLcVNiYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLP-LSRG 285
Cdd:cd17644 95 DAQISVLLTQPENLAYVIYTSGSTGKPKGVMIEHQSL-VN-LSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVtLLSG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 286 GKIAMNDG-----LRHIAKNLQQSKTSILIAVPLLLetlHKTILrkatgdakvakkyKLGLSLAKALNkiklnfndkifa 360
Cdd:cd17644 173 ATLVLRPEemrssLEDFVQYIQQWQLTVLSLPPAYW---HLLVL-------------ELLLSTIDLPS------------ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 361 eihkglggHLRLLVCGGAAIEP---QILADFNDWGITAIQGYGVTECSPIISNNRPKYKEHASA-----GLPTPHVEVKI 432
Cdd:cd17644 225 --------SLRLVIVGGEAVQPelvRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNItsvpiGRPIANTQVYI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 433 IneDEN------GI-GEIIARGPNVMLGYYEDPEKTAEAI--------DSEGFYHTGDYG-YIDDrGFIYITGRKANiIV 496
Cdd:cd17644 297 L--DENlqpvpvGVpGELHIGGVGLARGYLNRPELTAEKFishpfnssESERLYKTGDLArYLPD-GNIEYLGRIDN-QV 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1360655949 497 TKNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITA------EVFPSVEELAKVLET 552
Cdd:cd17644 373 KIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAyivphyEESPSTVELRQFLKA 434
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
360-555 |
1.22e-12 |
|
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: 70.24 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 360 AEIHKGLGGHLRLLVCGGAAIEPQIladfNDW-----GITAIQGYGVTECSPIISNNR-PKYKEHA-SAGLPTPHVEVKI 432
Cdd:cd05973 197 AEVPARPKGRLRRVSSAGEPLTPEV----IRWfdaalGVPIHDHYGQTELGMVLANHHaLEHPVHAgSAGRAMPGWRVAV 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 433 INEDENGIGE--------IIARGPNVML-GYYEDPEKTAEAidseGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNI 503
Cdd:cd05973 273 LDDDGDELGPgepgrlaiDIANSPLMWFrGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITM-SGYRI 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1360655949 504 FPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAEV-----FPSVEELAKVLETNAK 555
Cdd:cd05973 348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVvlrggHEGTPALADELQLHVK 404
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
223-532 |
2.74e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 69.49 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 223 LLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTfeatAGFLLPLSRGGKIAMNDGLRHI-AKNL 301
Cdd:PLN02479 200 LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHC----NGWCFTWTLAALCGTNICLRQVtAKAI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 302 QQS----KTSILIAVPLLLETLHKtilrkatgdakvAKKYKLGLSLAKALNkiklnfndkifaeihkglgghlrlLVCGG 377
Cdd:PLN02479 276 YSAianyGVTHFCAAPVVLNTIVN------------APKSETILPLPRVVH------------------------VMTAG 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 378 AAIEPQILADFNDWGITAIQGYGVTEC--SPIISNNRPKYKE---------HASAGLPTPHVE---------VKIINEDE 437
Cdd:PLN02479 320 AAPPPSVLFAMSEKGFRVTHTYGLSETygPSTVCAWKPEWDSlppeeqarlNARQGVRYIGLEgldvvdtktMKPVPADG 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 438 NGIGEIIARGPNVMLGYYEDPEKTAEAIdSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENI 517
Cdd:PLN02479 400 KTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIIS-GGENISSLEVENVVYTHPA 477
|
330
....*....|....*.
gi 1360655949 518 IEEVVVYGERDE-YGE 532
Cdd:PLN02479 478 VLEASVVARPDErWGE 493
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
215-608 |
3.18e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.20 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 215 IDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKN--DTLLSVLPLHHTFEATAGFLLPLSRGGK-IAMN 291
Cdd:PRK05691 163 LQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLIGGLLQPIFSGVPcVLMS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 292 DGLrhiaknlqqsktsiLIAVPL-LLETLHK---TIlrkaTGDAKVAkkYKLGLSLAK--ALNKIKLNfndkifaeihkg 365
Cdd:PRK05691 243 PAY--------------FLERPLrWLEAISEyggTI----SGGPDFA--YRLCSERVSesALERLDLS------------ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 366 lggHLRLLVCGGAAIEPQILADFND----WGITA---IQGYGVTECSPIISNNRPKY-------------KEHA------ 419
Cdd:PRK05691 291 ---RWRVAYSGSEPIRQDSLERFAEkfaaCGFDPdsfFASYGLAEATLFVSGGRRGQgipaleldaealaRNRAepgtgs 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 420 ---SAGLPTPHVEVKIINE------DENGIGEIIARGPNVMLGYYEDPEKTAEAI---DSEGFYHTGDYGYIDDrGFIYI 487
Cdd:PRK05691 368 vlmSCGRSQPGHAVLIVDPqslevlGDNRVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDLGFLRD-GELFV 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 488 TGRKANIIVTKnGKNIFPEEIEFVLlkENIIEE-----VVVYGERDEYGEQI-ITAEVFPSVEELAKvletnakdidtsv 561
Cdd:PRK05691 447 TGRLKDMLIVR-GHNLYPQDIEKTV--EREVEVvrkgrVAAFAVNHQGEEGIgIAAEISRSVQKILP------------- 510
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1360655949 562 ltgsvAEGLVKdAISKANKELqnFKKVKDIVLRAEP--FPRNTSKKILR 608
Cdd:PRK05691 511 -----PQALIK-SIRQAVAEA--CQEAPSVVLLLNPgaLPKTSSGKLQR 551
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
71-556 |
4.97e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 68.66 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLD-LGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYS 149
Cdd:PRK05620 39 TTFAAIGARAAALAHALHDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 150 RSQEDKLLGIADNIKQVKNLVSydLPTENSSKLAGEDKDLFFLWDLintgNSIRANGNTQYDNLPIDPRALAVLLFTSGT 229
Cdd:PRK05620 119 PRLAEQLGEILKECPCVRAVVF--IGPSDADSAAAHMPEGIKVYSY----EALLDGRSTVYDWPELDETTAAAICYSTGT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 230 TAKSKAVMLCHDNL---CVNIYDV-CLTVEFDKndTLLSVLPLHHTfeatagfllpLSRGGKIAmndglrhiaknlqqsk 305
Cdd:PRK05620 193 TGAPKGVVYSHRSLylqSLSLRTTdSLAVTHGE--SFLCCVPIYHV----------LSWGVPLA---------------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 306 tSILIAVPLLL-------ETLHKTIlrkATGDAKVAKKY-KLGLSLAKALNKiklNFNDKIfaeihkglggHLRLLVCGG 377
Cdd:PRK05620 245 -AFMSGTPLVFpgpdlsaPTLAKII---ATAMPRVAHGVpTLWIQLMVHYLK---NPPERM----------SLQEIYVGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 378 AAIEPQILADFND-WGITAIQGYGVTECSPIISNNRP----------KYKEhaSAGLPTPHVEVKIINEDE------NGI 440
Cdd:PRK05620 308 SAVPPILIKAWEErYGVDVVHVWGMTETSPVGTVARPpsgvsgearwAYRV--SQGRFPASLEYRIVNDGQvmestdRNE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 441 GEIIARGPNVMLGYYEDP----------------EKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIF 504
Cdd:PRK05620 386 GEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRS-GGEWIY 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1360655949 505 PEEIEFVLLKENIIEEVVVYGERDE-YGEQ----IITAEVFPSVEELAKVLETNAKD 556
Cdd:PRK05620 465 SAQLENYIMAAPEVVECAVIGYPDDkWGERplavTVLAPGIEPTRETAERLRDQLRD 521
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
216-542 |
6.17e-12 |
|
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: 68.11 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 216 DPRALAVLLFTSGTTAKSKAVMLCHDNLcVNIYDVCLTvEFDKnDTLLSVLPLHHT------FEatagFLLPLSRGGKIA 289
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNA-AAFLQWAAA-AFSA-EELAGVLASTSIcfdlsvFE----LFGPLATGGKVV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 290 MNDGLRHIAKNLQQSKTSILIAVPllletlhktilrkatgdakvakkyklglSLAKALNKiklnfndkifaeiHKGLGGH 369
Cdd:cd12115 176 LADNVLALPDLPAAAEVTLINTVP----------------------------SAAAELLR-------------HDALPAS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQILADF--NDWGITAIQGYGVTE------CSPIisnnRPKYKEHASAGLPTPHVEVKIIneDENG-- 439
Cdd:cd12115 215 VRVVNLAGEPLPRDLVQRLyaRLQVERVVNLYGPSEdttystVAPV----PPGASGEVSIGRPLANTQAYVL--DRALqp 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 -----IGEIIARGPNVMLGYYEDPEKTAEAIDSEGF------YHTGDYGYIDDRGFIYITGRKANiIVTKNGKNIFPEEI 508
Cdd:cd12115 289 vplgvPGELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRPDGLLEFLGRADN-QVKVRGFRIELGEI 367
|
330 340 350
....*....|....*....|....*....|....
gi 1360655949 509 EFVLLKENIIEEVVVYGERDEYGEQIITAEVFPS 542
Cdd:cd12115 368 EAALRSIPGVREAVVVAIGDAAGERRLVAYIVAE 401
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
69-532 |
7.86e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 68.05 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKV-IILAET--RYEwyitylatvCGLAIiaPMdkelpANEVENLIN-RSGAN 144
Cdd:PRK08162 42 RRRTWAETYARCRRLASALARRGIGRGDTVaVLLPNIpaMVE---------AHFGV--PM-----AGAVLNTLNtRLDAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 145 TI-FYSRSQEDKLLgIADN---------IKQVKNL----VSYDLPTENSSKLAGEDKDLFFLwdlintgnsirANGNTQY 210
Cdd:PRK08162 106 SIaFMLRHGEAKVL-IVDTefaevareaLALLPGPkplvIDVDDPEYPGGRFIGALDYEAFL-----------ASGDPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 211 D-NLPIDP-RALAvLLFTSGTTAKSKAVMLCHD----NLCVNIydvcLTVEFDKNDTLLSVLPLHHTfeatAGFLLPLSr 284
Cdd:PRK08162 174 AwTLPADEwDAIA-LNYTSGTTGNPKGVVYHHRgaylNALSNI----LAWGMPKHPVYLWTLPMFHC----NGWCFPWT- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 285 ggkIAMNDG----LRH-----IAKNLQQSKTSILIAVPLLLETLhktilrkatGDAKVAKKyklglslakalnkiklnfn 355
Cdd:PRK08162 244 ---VAARAGtnvcLRKvdpklIFDLIREHGVTHYCGAPIVLSAL---------INAPAEWR------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 356 dkifaeihKGLGGHLRLLVcGGAAIEPQILADFNDWGITAIQGYGVTE-------CS--------PIISNNRPKYKE--- 417
Cdd:PRK08162 293 --------AGIDHPVHAMV-AGAAPPAAVIAKMEEIGFDLTHVYGLTEtygpatvCAwqpewdalPLDERAQLKARQgvr 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 418 -HASAGL---------PTPHvevkiineDENGIGEIIARGPNVMLGYYEDPEKTAEAIDSeGFYHTGDYGYIDDRGFIYI 487
Cdd:PRK08162 364 yPLQEGVtvldpdtmqPVPA--------DGETIGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKI 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1360655949 488 TGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVVYGERDE-YGE 532
Cdd:PRK08162 435 KDRSKDIIIS-GGENISSIEVEDVLYRHPAVLVAAVVAKPDPkWGE 479
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
370-610 |
1.01e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 67.71 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQILADFND-WGITAIQGYGVTE------CSPIISNNRPKYKEHASAGLPtphveVKIIneDENG--- 439
Cdd:PRK13383 294 LRVVMSSGDRLDPTLGQRFMDtYGDILYNGYGSTEvgigalATPADLRDAPETVGKPVAGCP-----VRIL--DRNNrpv 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 ----IGEIIARGPNVMLGYYEDPEKTAeaIDseGFYHTGDYGYIDDRGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKE 515
Cdd:PRK13383 367 gprvTGRIFVGGELAGTRYTDGGGKAV--VD--GMTSTGDMGYLDNAGRLFIVGREDDMIIS-GGENVYPRAVENALAAH 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 516 NIIEEVVVYGERDE-YGEQIItaevfpsveelAKVLETNAKDIDTSVLtgsvaEGLVKDAISKankelqnFKKVKDIVLR 594
Cdd:PRK13383 442 PAVADNAVIGVPDErFGHRLA-----------AFVVLHPGSGVDAAQL-----RDYLKDRVSR-------FEQPRDINIV 498
|
250
....*....|....*.
gi 1360655949 595 AEpFPRNTSKKILRNK 610
Cdd:PRK13383 499 SS-IPRNPTGKVLRKE 513
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
67-552 |
2.56e-11 |
|
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: 66.21 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 67 EYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATV-CGLAIIaPMDKELPANEVENLINRSGANT 145
Cdd:cd17651 17 EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILkAGAAYV-PLDPAYPAERLAFMLADAGPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 146 IFysrSQEDkllgiadnikqvknlVSYDLPTEnssklagEDKDLFFLWDLINTGNSIRANgntqydnLPIDPRALAVLLF 225
Cdd:cd17651 96 VL---THPA---------------LAGELAVE-------LVAVTLLDQPGAAAGADAEPD-------PALDADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 226 TSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLhhTFEATAGFLLP-LSRGGKIAM-NDGLRH----IAK 299
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGL--GFDVSVQEIFStLCAGATLVLpPEEVRTdppaLAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 300 NLQQSKTSILIAVPLLLEtlhktilrkatgdakvakkyklglSLAKALNKiklnfndkifaeiHKGLGGHLRLLVCGG-A 378
Cdd:cd17651 222 WLDEQRISRVFLPTVALR------------------------ALAEHGRP-------------LGVRLAALRYLLTGGeQ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 379 AIEPQILADFNDW--GITAIQGYGVTE----CSPIISNNRPKYKEHASAGLPTPHVEVKIIneDENG-------IGEIIA 445
Cdd:cd17651 265 LVLTEDLREFCAGlpGLRLHNHYGPTEthvvTALSLPGDPAAWPAPPPIGRPIDNTRVYVL--DAALrpvppgvPGELYI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 446 RGPNVMLGYYEDPEKTAEAIDSEGF------YHTGDYGYIDDRGFIYITGRkANIIVTKNGKNIFPEEIEFVLLKENIIE 519
Cdd:cd17651 343 GGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGR-ADDQVKIRGFRIELGEIEAALARHPGVR 421
|
490 500 510
....*....|....*....|....*....|....*....
gi 1360655949 520 EVVVYGERDEYGEQIITA------EVFPSVEELAKVLET 552
Cdd:cd17651 422 EAVVLAREDRPGEKRLVAyvvgdpEAPVDAAELRAALAT 460
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
71-548 |
2.82e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.11 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSR 150
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 151 SQEDKLlgiadnikqvknlvsyDLPTENSSKLAGEDKDLFflwdlintgnSIRANGNTQydnLPIDPRALAVLLFTSGTT 230
Cdd:PRK12467 618 HLLAQL----------------PVPAGLRSLCLDEPADLL----------CGYSGHNPE---VALDPDNLAYVIYTSGST 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 231 AKSKAVMLCHDNLcVNIydVCLTVE---FDKNDTLLSVlplhHTFEATAG---FLLPLSRGGK--IAMNDGLRHIAKNLQ 302
Cdd:PRK12467 669 GQPKGVAISHGAL-ANY--VCVIAErlqLAADDSMLMV----STFAFDLGvteLFGALASGATlhLLPPDCARDAEAFAA 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 303 QSKT---SILIAVPLLLETLHKtilrkatgDAKVAkkyklglslakalnkiklnfndkifaeihkgLGGHLRLLVCGGAA 379
Cdd:PRK12467 742 LMADqgvTVLKIVPSHLQALLQ--------ASRVA-------------------------------LPRPQRALVCGGEA 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 380 IEPQILADFNDWGITA--IQGYGVTECSpIISNNRPKYKEHASA-----GLPTPHVEVKIINEDEN-----GIGEIIARG 447
Cdd:PRK12467 783 LQVDLLARVRALGPGArlINHYGPTETT-VGVSTYELSDEERDFgnvpiGQPLANLGLYILDHYLNpvpvgVVGELYIGG 861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 448 PNVMLGYYEDPEKTAE-------AIDSEGFYHTGDYGYIDDRGFIYITGRkANIIVTKNGKNIFPEEIEFVLLKENIIEE 520
Cdd:PRK12467 862 AGLARGYHRRPALTAErfvpdpfGADGGRLYRTGDLARYRADGVIEYLGR-MDHQVKIRGFRIELGEIEARLLAQPGVRE 940
|
490 500
....*....|....*....|....*...
gi 1360655949 521 VVVYGERDEYGEQIITAEVFPSVEELAK 548
Cdd:PRK12467 941 AVVLAQPGDAGLQLVAYLVPAAVADGAE 968
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
69-546 |
3.87e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 66.72 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 69 RGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFY 148
Cdd:PRK12467 1598 QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 149 SRSQEDKLlgiadnikqvknlvsydlPtenssklAGEDKDLFFLwDLINTGNSIRANGNTQydnLPIDPRALAVLLFTSG 228
Cdd:PRK12467 1678 QSHLQARL------------------P-------LPDGLRSLVL-DQEDDWLEGYSDSNPA---VNLAPQNLAYVIYTSG 1728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 229 TTAKSKAVMLCHDNLcVNIYdvCLTVE---FDKNDTLLSVLPLHHTFeATAGFLLPLSRGGKIAMNDGLRH-----IAKN 300
Cdd:PRK12467 1729 STGRPKGAGNRHGAL-VNRL--CATQEayqLSAADVVLQFTSFAFDV-SVWELFWPLINGARLVIAPPGAHrdpeqLIQL 1804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 301 LQQSKTSILIAVPLLLETLhktilrkatgdAKVAKKYKLGLSLakalnkiklnfndkifaeihkglgghlRLLVCGGAAI 380
Cdd:PRK12467 1805 IERQQVTTLHFVPSMLQQL-----------LQMDEQVEHPLSL---------------------------RRVVCGGEAL 1846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 381 EP----QILADFNDWGItaIQGYGVTECSP-----IISNNRPKYKEHASAGLPTPHVEVKIINEDENG-----IGEIIAR 446
Cdd:PRK12467 1847 EVealrPWLERLPDTGL--FNLYGPTETAVdvthwTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPvpigvAGELYLG 1924
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 447 GPNVMLGYYEDPEKTAEAIDSEGF-------YHTGDYGYIDDRGFIYITGRkANIIVTKNGKNIFPEEIEFVLLKENIIE 519
Cdd:PRK12467 1925 GVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRADGVIEYLGR-IDHQVKIRGFRIELGEIEARLREQGGVR 2003
|
490 500
....*....|....*....|....*..
gi 1360655949 520 EVVVYGERDEYGEQIItAEVFPSVEEL 546
Cdd:PRK12467 2004 EAVVIAQDGANGKQLV-AYVVPTDPGL 2029
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
223-539 |
3.95e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 65.44 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 223 LLFTSGTTAKSKAVMLCHDNLCVNI--YDVCLTVEFDknDTLLSVLPLHHTFEATAGFLLPLSRGGK--IAMNDGLRHIA 298
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIDREIeaYNEALNCEQD--ETPIVACPVTHSYGLICGVLAALTRGSKpvIITNKNPKFAL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 299 KNLQQSKTSILIAVPLLLETLHktilRKATGDAKVAKKYKLGLSLAKALnkiklnfndkiFAEIhKGLGGHLrllvcgga 378
Cdd:PRK08308 184 NILRNTPQHILYAVPLMLHILG----RLLPGTFQFHAVMTSGTPLPEAW-----------FYKL-RERTTYM-------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 379 aiepqiladfndwgitaIQGYGVTE--CspiISNNrPKYKEHASAGLPTPHVEVKIiNEDENGIGEIIARgpnvmlgyye 456
Cdd:PRK08308 240 -----------------MQQYGCSEagC---VSIC-PDMKSHLDLGNPLPHVSVSA-GSDENAPEEIVVK---------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 457 dpektaeAIDSEgfYHTGDYGYIDDRGFIYITGRKANIIvTKNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIIT 536
Cdd:PRK08308 288 -------MGDKE--IFTKDLGYKSERGTLHFMGRMDDVI-NVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVK 357
|
...
gi 1360655949 537 AEV 539
Cdd:PRK08308 358 AKV 360
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
216-535 |
6.47e-11 |
|
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: 64.70 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 216 DPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLhhTFEATA-GFLLPLSRGGKIAMND-- 292
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASF--NFDGAHeQLLPPLICGACVVLRPde 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 293 ---GLRHIAKNLQQSKTSILIAVPLLLETLHKTILRKATGDAkvakkyklglslakalnkiklnfndkifaeihkglgGH 369
Cdd:cd17649 170 lwaSADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRP------------------------------------PS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQILADFNDWGITAIQGYGVTEC--SPIISNNRPKYKEHASA---GLPTPHVEVKIINEDEN-----G 439
Cdd:cd17649 214 LRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEAtvTPLVWKCEAGAARAGASmpiGRPLGGRSAYILDADLNpvpvgV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 440 IGEIIARGPNVMLGYYEDPEKTAEAIDSEGF-------YHTGDYGYIDDRGFIYITGRkANIIVTKNGKNIFPEEIEFVL 512
Cdd:cd17649 294 TGELYIGGEGLARGYLGRPELTAERFVPDPFgapgsrlYRTGDLARWRDDGVIEYLGR-VDHQVKIRGFRIELGEIEAAL 372
|
330 340
....*....|....*....|...
gi 1360655949 513 LKENIIEEVVVYGERDEYGEQII 535
Cdd:cd17649 373 LEHPGVREAAVVALDGAGGKQLV 395
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
214-542 |
6.87e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 64.30 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 214 PIDPrALAVLLFTSGTTAKSKAVMLCHDNLcvniydvcltvefdkndtLLSVLPLHHTFEATAGFLLPLSRggkiamndg 293
Cdd:PRK07824 32 PIDD-DVALVVATSGTTGTPKGAMLTAAAL------------------TASADATHDRLGGPGQWLLALPA--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 294 lRHIAkNLQQSKTSILIAV-PLLL---ETLHKTILRKATGDAKVAKKYK--LGLSLAKALNkiklnfndkifaeiHKGLG 367
Cdd:PRK07824 84 -HHIA-GLQVLVRSVIAGSePVELdvsAGFDPTALPRAVAELGGGRRYTslVPMQLAKALD--------------DPAAT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 368 GHLRLL---VCGGAAIEPQILADFNDWGITAIQGYGVTE-CSPIISNnrpkykehasaGLPTPHVEVKIINedengiGEI 443
Cdd:PRK07824 148 AALAELdavLVGGGPAPAPVLDAAAAAGINVVRTYGMSEtSGGCVYD-----------GVPLDGVRVRVED------GRI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 444 IARGPNVMLGYYEDPEKTAEAidSEGFYHTGDYGYIDDrGFIYITGRKANIIVTkNGKNIFPEEIEFVLLKENIIEEVVV 523
Cdd:PRK07824 211 ALGGPTLAKGYRNPVDPDPFA--EPGWFRTDDLGALDD-GVLTVLGRADDAIST-GGLTVLPQVVEAALATHPAVADCAV 286
|
330
....*....|....*....
gi 1360655949 524 YGERDEYGEQIITAEVFPS 542
Cdd:PRK07824 287 FGLPDDRLGQRVVAAVVGD 305
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
72-500 |
8.71e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 64.73 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSRS 151
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 152 QEDKLLGIADNIKQVKNLVSY----DLPTENSSKLAGEDkdlfflwdLIntgnsirANGNTQYDNLPIDPRALAVLLFTS 227
Cdd:PRK07008 121 FLPLVDALAPQCPNVKGWVAMtdaaHLPAGSTPLLCYET--------LV-------GAQDGDYDWPRFDENQASSLCYTS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 228 GTTAKSKAVMLCHDNLCVNIYDVCL--TVEFDKNDTLLSVLPLHHTFEATAGFLLPLSrGGKIAMN----DGlrhiaKNL 301
Cdd:PRK07008 186 GTTGNPKGALYSHRSTVLHAYGAALpdAMGLSARDAVLPVVPMFHVNAWGLPYSAPLT-GAKLVLPgpdlDG-----KSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 302 QQsktsiliavplLLETlhktilRKATGDAKVAKKYkLGLslakaLNKIKLNfndkifaeihkGLG-GHLRLLVCGGAAI 380
Cdd:PRK07008 260 YE-----------LIEA------ERVTFSAGVPTVW-LGL-----LNHMREA-----------GLRfSTLRRTVIGGSAC 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 381 EPQILADF-NDWGITAIQGYGVTECSPIISNNRPKYKEHASA-----------GLPTPHVEVKIINE-------DENGIG 441
Cdd:PRK07008 306 PPAMIRTFeDEYGVEVIHAWGMTEMSPLGTLCKLKWKHSQLPldeqrkllekqGRVIYGVDMKIVGDdgrelpwDGKAFG 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1360655949 442 EIIARGPNVMLGYYedpeKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKANIIvtKNG 500
Cdd:PRK07008 386 DLQVRGPWVIDRYF----RGDASPLVDGWFPTGDVATIDADGFMQITDRSKDVI--KSG 438
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
211-542 |
1.96e-10 |
|
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: 63.26 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 211 DNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFD-KNDTLLSVLPLhhTFEATAG-FLLPLSRGGK- 287
Cdd:cd17650 86 KLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDsFPVRLLQMASF--SFDVFAGdFARSLLNGGTl 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 288 IAMNDGLR----HIAKNLQQSKTSILIAVPLLLETLHKTILRkatgdakvakkyklglslakalNKIKLNFndkifaeih 363
Cdd:cd17650 164 VICPDEVKldpaALYDLILKSRITLMESTPALIRPVMAYVYR----------------------NGLDLSA--------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 364 kglgghLRLLVCGG---AAIEPQILADFNDWGITAIQGYGVTECSpIISNnrpkYKEHASAGL----------PTPHVEV 430
Cdd:cd17650 213 ------MRLLIVGSdgcKAQDFKTLAARFGQGMRIINSYGVTEAT-IDST----YYEEGRDPLgdsanvpigrPLPNTAM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 431 KIINEDEN----GI-GEIIARGPNVMLGYYEDPEKTAEAIDSEGF------YHTGDYGYIDDRGFIYITGRkANIIVTKN 499
Cdd:cd17650 282 YVLDERLQpqpvGVaGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGR-VDHQVKIR 360
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1360655949 500 GKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAEVFPS 542
Cdd:cd17650 361 GFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAA 403
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
44-609 |
5.51e-10 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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: 62.06 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 44 PVALREldpRSEAAINFRINPDNEYrgiTYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIA 123
Cdd:cd05915 4 AAALFG---RKEVVSRLHTGEVHRT---TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 124 PMDKELPANEVENLINRSGANTIFYsrsqEDKLLGIAD-NIKQVKNLVsyDLPTENSSKLAGEDkdlfFLwdlintgnsi 202
Cdd:cd05915 78 TANPRLSPKEIAYILNHAEDKVLLF----DPNLLPLVEaIRGELKTVQ--HFVVMDEKAPEGYL----AY---------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 203 rANGNTQYDNL-PIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKND--TLLSVLPLHH--------T 271
Cdd:cd05915 138 -EEALGEEADPvRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEkdVVLPVVPMFHvnawclpyA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 272 FEATAGFLLPLSRggkiAMNDGLrhIAKNLQQSKTSILIAVPLLLETLhktilrkatgdakvakkyklglslAKALNKIK 351
Cdd:cd05915 217 ATLVGAKQVLPGP----RLDPAS--LVELFDGEGVTFTAGVPTVWLAL------------------------ADYLESTG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 352 LNFNdkifaeihkglgghLRLLVCGGAAIEPQILADFND---------WGITAIQGYGVT-------ECSPIISNNRPKY 415
Cdd:cd05915 267 HRLK--------------TLRRLVVGGSAAPRSLIARFErmgvevrqgYGLTETSPVVVQnfvkshlESLSEEEKLTLKA 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 416 KE---HASAGLPTPHVEVKIINEDENGIGEIIARGPNVMLGYYEDPEKTAEAIDSEGFYHTGDYGYIDDRGFIYITGRKA 492
Cdd:cd05915 333 KTglpIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLK 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 493 NIIvTKNGKNIFPEEIEFVLLKENIIEEVVVYGERDE-YGEqiitaevfpSVEELAKVLETNAKDidtsvltgsvaeglv 571
Cdd:cd05915 413 DLI-KSGGEWISSVDLENALMGHPKVKEAAVVAIPHPkWQE---------RPLAVVVPRGEKPTP--------------- 467
|
570 580 590
....*....|....*....|....*....|....*...
gi 1360655949 572 KDAISKANKELQNFKKVKDIVLRAEPFPRNTSKKILRN 609
Cdd:cd05915 468 EELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKR 505
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
33-510 |
2.44e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 60.13 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 33 YAEENAFLLKDPVALRELDprseaainFRINPDNEYRGITYRQVNEDRKALGsAMLDLGISKDDKVIILAETRYEWYITY 112
Cdd:PRK07769 26 HVERWAKVRGDKLAYRFLD--------FSTERDGVARDLTWSQFGARNRAVG-ARLQQVTKPGDRVAILAPQNLDYLIAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 113 LATVCGLAIIAPM-DKELPANeVENLinrsganTIFYSRSQEDKLLGIADNIKQVKNLVSyDLPTENSSKLAGEDkdlff 191
Cdd:PRK07769 97 FGALYAGRIAVPLfDPAEPGH-VGRL-------HAVLDDCTPSAILTTTDSAEGVRKFFR-ARPAKERPRVIAVD----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 192 lwdlintgnSIRANGNTQYDNLPIDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHT 271
Cdd:PRK07769 163 ---------AVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 272 FeataGF---LLPLSRGGKIAMNDGLRHIAKNLQQSKTsiLIAVPllletlhktilRKATGDAKVAKKYKLGLSLAKALN 348
Cdd:PRK07769 234 M----GLitvLLPALLGHYITFMSPAAFVRRPGRWIRE--LARKP-----------GGTGGTFSAAPNFAFEHAAARGLP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 349 KiklnfNDKIFAEIHKGLGghlrlLVCGGAAIEPQILADFND----WGI--TAIQ-GYGVTEC----SPIISNNRPK--- 414
Cdd:PRK07769 297 K-----DGEPPLDLSNVKG-----LLNGSEPVSPASMRKFNEafapYGLppTAIKpSYGMAEAtlfvSTTPMDEEPTviy 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 415 ----------------YKEHASAGLPTPHVEVK----IINED------ENGIGEIIARGPNVMLGYYEDPEKTAEAID-- 466
Cdd:PRK07769 367 vdrdelnagrfvevpaDAPNAVAQVSAGKVGVSewavIVDPEtaselpDGQIGEIWLHGNNIGTGYWGKPEETAATFQni 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1360655949 467 ---------SEG------FYHTGDYG-YIDdrGFIYITGR-KANIIVtkNGKNIFPEEIEF 510
Cdd:PRK07769 447 lksrlseshAEGapddalWVRTGDYGvYFD--GELYITGRvKDLVII--DGRNHYPQDLEY 503
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
71-519 |
2.57e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 60.14 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 71 ITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYL------ATVCGLaiiapmdkeLPANEVENLINR---- 140
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLscarigATHCVL---------FDGYSVKSLIDRieti 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 141 ------SGANTIFysrsqEDKLLGIADNIKQVKNLVSY-----------DLPTENSSKLAGEDKDLFFLWDLINTGNSIR 203
Cdd:PTZ00237 164 tpkliiTTNYGIL-----NDEIITFTPNLKEAIELSTFkpsnvitlfrnDITSESDLKKIETIPTIPNTLSWYDEIKKIK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 204 ANGNTQ-YDNLPIDPRALAVLLFTSGTTAKSKAVMLCHDN--LCVNIYDVCLtVEFDKNDTLLSvlplHH-----TFEAt 275
Cdd:PTZ00237 239 ENNQSPfYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPhlVGLKYYWRSI-IEKDIPTVVFS----HSsigwvSFHG- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 276 aGFLLPLSRGGKIAMNDG----LRHIAKNL----QQSKTSILIAVPllletlhKTI--LRKATGDAKVAK-KYKLGlsla 344
Cdd:PTZ00237 313 -FLYGSLSLGNTFVMFEGgiikNKHIEDDLwntiEKHKVTHTLTLP-------KTIryLIKTDPEATIIRsKYDLS---- 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 345 kalnkiklnfndkifaeihkglggHLRLLVCGGAAIEPQIlADF--NDWGITAIQGYGVTE--CSPIISNNRPKyKEHAS 420
Cdd:PTZ00237 381 ------------------------NLKEIWCGGEVIEESI-PEYieNKLKIKSSRGYGQTEigITYLYCYGHIN-IPYNA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 421 AGLPTPHVEVKIINED-----ENGIGEIIAR---GPNVMLGYYEDPEKTAEAIDS-EGFYHTGDYGYIDDRGFIYITGRK 491
Cdd:PTZ00237 435 TGVPSIFIKPSILSEDgkelnVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRS 514
|
490 500
....*....|....*....|....*....
gi 1360655949 492 ANIIvTKNGKNIFPEEIEFVLLKE-NIIE 519
Cdd:PTZ00237 515 DDQI-KISGNKVQLNTIETSILKHpLVLE 542
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
370-542 |
1.32e-08 |
|
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: 57.32 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 370 LRLLVCGGAAIEPQILAD----FNDWGITAIQGYGVTECS-----PIISNNRPKYKEHASAGLPTPHVEVKIINEDEN-- 438
Cdd:cd17643 212 LRYVIFGGEALEAAMLRPwagrFGLDRPQLVNMYGITETTvhvtfRPLDAADLPAAAASPIGRPLPGLRVYVLDADGRpv 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 439 ---GIGEIIARGPNVMLGYYEDPEKTAEAIDSEGF-------YHTGDYG-YIDDRGFIYItGRkANIIVTKNGKNIFPEE 507
Cdd:cd17643 292 ppgVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLArRLPDGELEYL-GR-ADEQVKIRGFRIELGE 369
|
170 180 190
....*....|....*....|....*....|....*
gi 1360655949 508 IEFVLLKENIIEEVVVYGERDEYGEQIITAEVFPS 542
Cdd:cd17643 370 IEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAD 404
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
63-608 |
1.64e-08 |
|
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: 57.50 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 63 NPDNEYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSG 142
Cdd:cd05968 84 GEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 143 ANTI-----FYSRSQEDKLLGIADNIK----QVKNLV-----SYDLPTENSsklagedKDLFflWDLINTGNSIRANGNT 208
Cdd:cd05968 164 AKALitadgFTRRGREVNLKEEADKACaqcpTVEKVVvvrhlGNDFTPAKG-------RDLS--YDEEKETAGDGAERTE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 209 qydnlPIDPralAVLLFTSGTTAKSKAVMLCHDNLCVN-IYDVCLTVEFDKNDTLLSVLPLhhtfeataGFLL-P----- 281
Cdd:cd05968 235 -----SEDP---LMIIYTSGTTGKPKGTVHVHAGFPLKaAQDMYFQFDLKPGDLLTWFTDL--------GWMMgPwlifg 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 282 -LSRGGKIAMNDGL------RHIAKNLQQSKTSILIAVPLLLETLhktilrKATGDAKVAKKYKLGLSLAKALNK-IKLN 353
Cdd:cd05968 299 gLILGATMVLYDGApdhpkaDRLWRMVEDHEITHLGLSPTLIRAL------KPRGDAPVNAHDLSSLRVLGSTGEpWNPE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 354 FNDKIFAEIhkgLGGHLRLLvcggaaiepqiladfNDWGITAIQGyGVTECSPIisnnRPkYKEHASAGlPTPHVEVKII 433
Cdd:cd05968 373 PWNWLFETV---GKGRNPII---------------NYSGGTEISG-GILGNVLI----KP-IKPSSFNG-PVPGMKADVL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 434 NEDENGI----GEIIARGPNVML--GYYEDPEKTAEAIDS--EGFYHTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFP 505
Cdd:cd05968 428 DESGKPArpevGELVLLAPWPGMtrGFWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFYILGRSDDTINVA-GKRVGP 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 506 EEIEFVLLKENIIEEVVVYGERDEY-GEQIItaevfpsveeLAKVLETNAkdidtsvltgSVAEGLVKDAISKANKELQN 584
Cdd:cd05968 507 AEIESVLNAHPAVLESAAIGVPHPVkGEAIV----------CFVVLKPGV----------TPTEALAEELMERVADELGK 566
|
570 580
....*....|....*....|....
gi 1360655949 585 FKKVKDIVLrAEPFPRNTSKKILR 608
Cdd:cd05968 567 PLSPERILF-VKDLPKTRNAKVMR 589
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
30-535 |
4.58e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 56.71 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 30 ASLYAEENAFLLKDPVAlRELDPRSEAAINFRI------NPDN-----EYRGITYRQVNEDRKALGSAMLDLGISKDDKV 98
Cdd:PRK12467 3070 PTLAAHERRQVLHAWNA-TAAAYPSERLVHQLIeaqvarTPEApalvfGDQQLSYAELNRRANRLAHRLIAIGVGPDVLV 3148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 99 IILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSRSQEDKLlgiadniKQVKNLVSYDLpten 178
Cdd:PRK12467 3149 GVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQL-------PAPAGDTALTL---- 3217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 179 ssklagedkDLFFLWDLINTGNSIRangntqydnlpIDPRALAVLLFTSGTTAKSKAVMLCHD---NLCVNIYDVCltvE 255
Cdd:PRK12467 3218 ---------DRLDLNGYSENNPSTR-----------VMGENLAYVIYTSGSTGKPKGVGVRHGalaNHLCWIAEAY---E 3274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 256 FDKNDTLLSVLPLhhTFEATA-GFLLPLSRGGKIAMNDG-LRHIAKNLQQ---SKTSILIAVPLLLETlhktilrkatgd 330
Cdd:PRK12467 3275 LDANDRVLLFMSF--SFDGAQeRFLWTLICGGCLVVRDNdLWDPEELWQAihaHRISIACFPPAYLQQ------------ 3340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 331 akvakkyklglslakalnkiklnfndkiFAEIHKGLGGH-LRLLVCGGAAIEP----QILADFNDWGITaiQGYGVTEC- 404
Cdd:PRK12467 3341 ----------------------------FAEDAGGADCAsLDIYVFGGEAVPPaafeQVKRKLKPRGLT--NGYGPTEAv 3390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 405 -SPII----SNNRPKyKEHASAGLPTPHVEVKIIneDENG-------IGEIIARGPNVMLGYYEDPEKTAEAIDSEGF-- 470
Cdd:PRK12467 3391 vTVTLwkcgGDAVCE-APYAPIGRPVAGRSIYVL--DGQLnpvpvgvAGELYIGGVGLARGYHQRPSLTAERFVADPFsg 3467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 471 -----YHTGDYGYIDDRGFIYITGRkANIIVTKNGKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQII 535
Cdd:PRK12467 3468 sggrlYRTGDLARYRADGVIEYLGR-IDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLV 3536
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-523 |
5.62e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.33 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 72 TYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEWYITYLATVCGLAIIAPMDKELPANEVENLINRSGANTIFYSRS 151
Cdd:PRK05691 3747 SYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAA 3826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 152 QEDKLLGIADnikqvknlvsydlptenssKLAGEDKDLFFLWDLINTGNSIRANGNTqYDNlpidPRALAVLLFTSGTTA 231
Cdd:PRK05691 3827 CREQARALLD-------------------ELGCANRPRLLVWEEVQAGEVASHNPGI-YSG----PDNLAYVIYTSGSTG 3882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 232 KSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPlhHTFEATA-GFLLPLSRGGKIAM--NDGLRH---IAKNLQQSK 305
Cdd:PRK05691 3883 LPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTAS--QSFDISVwQFLAAPLFGARVEIvpNAIAHDpqgLLAHVQAQG 3960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 306 TSILIAVPLLLETLhktilrkatgdakvakkyklglslakalnkiklnfndkiFAEIHKGLGGhLRLLVCGGAAIEPQIL 385
Cdd:PRK05691 3961 ITVLESVPSLIQGM---------------------------------------LAEDRQALDG-LRWMLPTGEAMPPELA 4000
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 386 AdfnDW-----GITAIQGYGVTECSPIISNNRPKYKEHASA----GLPTPHVEVKIINEDEN-----GIGEIIARGPNVM 451
Cdd:PRK05691 4001 R---QWlqrypQIGLVNAYGPAECSDDVAFFRVDLASTRGSylpiGSPTDNNRLYLLDEALElvplgAVGELCVAGTGVG 4077
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1360655949 452 LGYYEDPEKTAEAI-------DSEGFYHTGDYGYIDDRGFIYITGRkANIIVTKNGKNIFPEEIEFVLLKENIIEEVVV 523
Cdd:PRK05691 4078 RGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGR-IDHQVKIRGYRIELGEIEARLHEQAEVREAAV 4155
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
420-608 |
1.10e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 54.95 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 420 SAGLPTPHVeVKIINED---EN---GIGEIIARGPNVMLGYYEDPEKT-----AEAID-SEG-----FYHTGDYGYIDDr 482
Cdd:PRK05850 372 SYGSPRSPT-VRIVDPDtciECpagTVGEIWVHGDNVAAGYWQKPEETertfgATLVDpSPGtpegpWLRTGDLGFISE- 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 483 GFIYITGR-KANIIVtkNGKNIFPEEIefvllkENIIEEVVvyGER-------DEYGEQIITaevfpsVEELAKVLETna 554
Cdd:PRK05850 450 GELFIVGRiKDLLIV--DGRNHYPDDI------EATIQEIT--GGRvaaisvpDDGTEKLVA------IIELKKRGDS-- 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1360655949 555 kDIDTSVLTGSVaEGLVKDAISKANKelqnfKKVKDIVLRAeP--FPRNTSKKILR 608
Cdd:PRK05850 512 -DEEAMDRLRTV-KREVTSAISKSHG-----LSVADLVLVA-PgsIPITTSGKIRR 559
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
418-608 |
3.53e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 53.21 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 418 HASAGLPTPHVEVKIINED------ENGIGEIIARGPNVMLGYYEDPEKT------------------AEAIDSEGFYHT 473
Cdd:PRK12476 401 HVSCGQVARSQWAVIVDPDtgaelpDGEVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlaegshaDGAADDGTWLRT 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 474 GDYG-YIDdrGFIYITGRKANIIVTkNGKNIFPEEIEFV------LLKENIIEEVVVYGERDEygEQIITAEVFPSveel 546
Cdd:PRK12476 481 GDLGvYLD--GELYITGRIADLIVI-DGRNHYPQDIEATvaeaspMVRRGYVTAFTVPAEDNE--RLVIVAERAAG---- 551
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1360655949 547 akvletnakdidtsvlTGSVAEGLVKDAISKANKElQNFKKVKDI-VLRAEPFPRNTSKKILR 608
Cdd:PRK12476 552 ----------------TSRADPAPAIDAIRAAVSR-RHGLAVADVrLVPAGAIPRTTSGKLAR 597
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
216-527 |
3.18e-06 |
|
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: 50.09 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 216 DPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDT----LLSVLPLHHTFEATagfLLPLSRGGKIAMN 291
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDeavlFFSNYVFDFFVEQM---TLALLNGQKLVVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 292 DGlrhiaknlqqsktSILIAVPLLLETLHKTILRKATGDAKVAKKYKLG-LSLAKALNKIKLNFNDKIFAEIHKGLGGHL 370
Cdd:cd17648 169 PD-------------EMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLArLPHLKRVDAAGEEFTAPVFEKLRSRFAGLI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 371 rllvcggaaiepqiladfndwgitaIQGYGVTECSpIISNNRPKYKEHA---SAGLPTPHVEVKIINEDE-----NGIGE 442
Cdd:cd17648 236 -------------------------INAYGPTETT-VTNHKRFFPGDQRfdkSLGRPVRNTKCYVLNDAMkrvpvGAVGE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 443 IIARGPNVMLGYYEDPEKTAEAIDSEGF--------------YHTGDYGYIDDRGFIYITGRkANIIVTKNGKNIFPEEI 508
Cdd:cd17648 290 LYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLGR-NDFQVKIRGQRIEPGEV 368
|
330 340
....*....|....*....|
gi 1360655949 509 EFVLLK-ENIIEEVVVYGER 527
Cdd:cd17648 369 EAALASyPGVRECAVVAKED 388
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
215-525 |
1.27e-05 |
|
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: 48.20 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 215 IDPRALAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMND-- 292
Cdd:cd05937 84 VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRkf 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 293 GLRHIAKNLQQSKTSILIAVPLLLETLHKTILRKATGDAKVAKKYKLGLSlAKALNKIKLNFNDKIFAEIHKGLGGHLRL 372
Cdd:cd05937 164 SASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLR-PDIWERFRERFNVPEIGEFYAATEGVFAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 373 LVCGGaaiepqiladfNDWGITAIQGYGV----------------TECSPIISNNRPKYKEHASAGLPtphvevkiined 436
Cdd:cd05937 243 TNHNV-----------GDFGAGAIGHHGLirrwkfenqvvlvkmdPETDDPIRDPKTGFCVRAPVGEP------------ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 437 engiGEIIARGPNVML----GYYEDPEKTAEAI------DSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFPE 506
Cdd:cd05937 300 ----GEMLGRVPFKNReafqGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWK-SENVSTT 374
|
330
....*....|....*....
gi 1360655949 507 EIEFVLLKENIIEEVVVYG 525
Cdd:cd05937 375 EVADVLGAHPDIAEANVYG 393
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
63-525 |
2.48e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 47.18 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 63 NPDN-----EYRGITYRQVNEDRKALGSAMLDLGISKDDKVIILAETRYEwyitYLATVCGL----AIIApmdkelpane 133
Cdd:PRK08279 50 HPDRpallfEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPE----YLAAWLGLaklgAVVA---------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 134 venLINRSgantifysrsQEDKLLGIADNIKQVKNL-VSYDL--PTENSSKLAGEDKDLFFLWDLINTGNSIRANGNTQY 210
Cdd:PRK08279 116 ---LLNTQ----------QRGAVLAHSLNLVDAKHLiVGEELveAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 211 DNLPIDPRAL---------AVLLFTSGTTAKSKAVMLCHdNLCVNIYDV-CLTVEFDKNDTLLSVLPLHHtfeATAGFLL 280
Cdd:PRK08279 183 AGAPTTNPASrsgvtakdtAFYIYTSGTTGLPKAAVMSH-MRWLKAMGGfGGLLRLTPDDVLYCCLPLYH---NTGGTVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 281 P---LSRGGKIAMND--GLRHIAKNLQQSKTSILIAVPLLLETLhktilrkatgdakvakkyklglslakalnkikLNfn 355
Cdd:PRK08279 259 WssvLAAGATLALRRkfSASRFWDDVRRYRATAFQYIGELCRYL--------------------------------LN-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 356 dkifAEIHKGLGGHlRLLVCGGAAIEPQILADFND-WGITAI-QGYGVTECSPIISN--NRPKykehaSAG-----LPTP 426
Cdd:PRK08279 305 ----QPPKPTDRDH-RLRLMIGNGLRPDIWDEFQQrFGIPRIlEFYAASEGNVGFINvfNFDG-----TVGrvplwLAHP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 427 HVEVKIINE------DENG-------------IGEIIARGPnvmLGYYEDPEKTAEAIDSEGF------YHTGDYGYIDD 481
Cdd:PRK08279 375 YAIVKYDVDtgepvrDADGrcikvkpgevgllIGRITDRGP---FDGYTDPEASEKKILRDVFkkgdawFNTGDLMRDDG 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1360655949 482 RGFIYITGR-------KaniivtknGKNIFPEEIEFVLLKENIIEEVVVYG 525
Cdd:PRK08279 452 FGHAQFVDRlgdtfrwK--------GENVATTEVENALSGFPGVEEAVVYG 494
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
419-608 |
4.02e-05 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 46.79 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 419 ASAGLPTPHVEVKIINEDENGI-----GEIIARG--PNVMLGYYEDPEKTAEAIDSE--GFYHTGDYGYIDDRGFIYITG 489
Cdd:cd05966 410 GSATRPFFGIEPAILDEEGNEVegeveGYLVIKRpwPGMARTIYGDHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITG 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 490 RKANIIvtkN--GKNIFPEEIEFVLLKENIIEEVVVYGERDEYGEQIITAEVfpsveelakVLETNAKDidtsvltgsvA 567
Cdd:cd05966 490 RVDDVI---NvsGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFV---------TLKDGEEP----------S 547
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1360655949 568 EGLVKDAISKANKELQNFKKVKDIVLrAEPFPRNTSKKILR 608
Cdd:cd05966 548 DELRKELRKHVRKEIGPIATPDKIQF-VPGLPKTRSGKIMR 587
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
214-280 |
1.04e-03 |
|
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: 41.89 E-value: 1.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 214 PIDPRALAVLLFTSGTTAKSKAVMLCHDNL--CVNIYDVC-LTVEfdknDTLLSVLPLHHtfeaTAGFLL 280
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVlqCSGFLSLCgVTAD----DVIYITLPLYH----SSGFLL 201
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
420-490 |
1.19e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 42.05 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 420 SAGLPTPHVEVKIINEDENGIGE------IIARG-PNVMLGYYEDPEKTAEAIDSE--GFYHTGDYGYIDDRGFIYITGR 490
Cdd:PRK00174 425 SATRPLPGIQPAVVDEEGNPLEGgeggnlVIKDPwPGMMRTIYGDHERFVKTYFSTfkGMYFTGDGARRDEDGYYWITGR 504
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
220-525 |
1.26e-03 |
|
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: 41.57 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 220 LAVLLFTSGTTAKSKAVMLCHDNLCVNIYDVCLTVEFDKNDTLLSVLPLHHTFEATAGFLLPLSRGGKIAMNDGL--RHI 297
Cdd:cd05940 83 AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFsaSNF 162
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 298 AKNLQQSKTSILIAVPLLLETLhktilrkatgdakvakkyklglslakalnkikLNFNDKIFAEIHKglgghLRLlVCGG 377
Cdd:cd05940 163 WDDIRKYQATIFQYIGELCRYL--------------------------------LNQPPKPTERKHK-----VRM-IFGN 204
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 378 AaIEPQILADFND-WGITAI-QGYGVTECSPIISN--NRP-------------------KYKEHASAGLPTPHVEVKIIN 434
Cdd:cd05940 205 G-LRPDIWEEFKErFGVPRIaEFYAATEGNSGFINffGKPgaigrnpsllrkvaplalvKYDLESGEPIRDAEGRCIKVP 283
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360655949 435 EDENG--IGEIIARGPnvMLGYYeDPEKTAEAI------DSEGFYHTGDYGYIDDRGFIYITGRKANIIVTKnGKNIFPE 506
Cdd:cd05940 284 RGEPGllISRINPLEP--FDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWK-GENVSTT 359
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330
....*....|....*....
gi 1360655949 507 EIEFVLLKENIIEEVVVYG 525
Cdd:cd05940 360 EVAAVLGAFPGVEEANVYG 378
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