|
Name |
Accession |
Description |
Interval |
E-value |
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
26-489 |
0e+00 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 657.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 26 TYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFCTLP 102
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQgirSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 103 LELRGFQIVSLDDIEFAGTditmndlmdntldiqYDTLnetvvpkdspsniLNTSFNIDDIASIMFTSGTTGPQKAVPQT 182
Cdd:TIGR01923 81 LEEKDFQADSLDRIEAAGR---------------YETS-------------LSASFNMDQIATLMFTSGTTGKPKAVPHT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 183 FRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNaeQILTMIKNERITHISLVPQTLNW 262
Cdd:TIGR01923 133 FRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVPTQLNR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 263 LMQQGLHePHDLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPQMLHERPDtVGMPSANVDVKVKNPN 342
Cdd:TIGR01923 211 LLDEGGH-NENLRKILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVTTATPEMLHARPD-VGRPLAGREIKIKVDN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 343 KEGHGELMIKGANVMNGYLYPTDLTDTFE-NGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGI 421
Cdd:TIGR01923 289 KEGHGEIMVKGANLMKGYLYQGELTPAFEqQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGI 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1853634356 422 SDAVCIGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:TIGR01923 369 QEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
24-491 |
0e+00 |
|
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: 632.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 24 SYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLifct 100
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALgvrKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 101 lplelrgfqivslddiefagtditmndlmdntldiqydtlnetvvpkdspsnilntsfniDDIASIMFTSGTTGPQKAVP 180
Cdd:cd05912 77 ------------------------------------------------------------DDIATIMYTSGTTGKPKGVQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 181 QTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTL 260
Cdd:cd05912 97 QTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTML 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 261 NWLMQQGLH-EPHDLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPQMLHERPDTVGMPSANVDVKVK 339
Cdd:cd05912 177 QRLLEILGEgYPNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIE 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 340 NPN--KEGHGELMIKGANVMNGYLYPTDLT-DTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAK 416
Cdd:cd05912 257 DDGqpPYEVGEILLKGPNVTKGYLNRPDATeESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLL 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 417 QFPGISDAVCIGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd05912 337 SHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1-489 |
7.05e-150 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 436.70 E-value: 7.05e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 1 MDFWLYKQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMIN 77
Cdd:PRK03640 4 MPNWLKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALgvkKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 78 TRLTPNEMKNQMRSIDVQLIFCTLPLElrgfqivsldDIEFAGTDITMNDLMDNTLDIQydtlnetvvpkdspsnILNTS 157
Cdd:PRK03640 84 TRLSREELLWQLDDAEVKCLITDDDFE----------AKLIPGISVKFAELMNGPKEEA----------------EIQEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 158 FNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFN 237
Cdd:PRK03640 138 FDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLVPQTLNWLMQQgLHE---PHDLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLT 314
Cdd:PRK03640 218 AEKINKLLQTGGVTIISVVSTMLQRLLER-LGEgtyPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASQIVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 315 ATPQMLHERPDTVGMPSANVDVKVKNPNKEG----HGELMIKGANVMNGYLY-PTDLTDTFENGYFNTGDIAEIDHEGYV 389
Cdd:PRK03640 297 LSPEDALTKLGSAGKPLFPCELKIEKDGVVVppfeEGEIVVKGPNVTKGYLNrEDATRETFQDGWFKTGDIGYLDEEGFL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 390 MIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKH 469
Cdd:PRK03640 377 YVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKR 456
|
490 500
....*....|....*....|
gi 1853634356 470 FEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHEL 476
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-489 |
1.15e-130 |
|
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: 386.47 E-value: 1.15e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 4 WLYKQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRL 80
Cdd:COG0318 4 LLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALgvgPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 81 TPNEMKNQMRSIDVQLIFCtlplelrgfqivslddiefagtditmndlmdntldiqydtlnetvvpkdspsnilntsfni 160
Cdd:COG0318 84 TAEELAYILEDSGARALVT------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 ddiASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDKFNAE 239
Cdd:COG0318 103 ---ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLLPRFDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMIKNERITHISLVPQTLNWLMQQGLHEPHD---LQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTA 315
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARLLRHPEFARYDlssLRLVVSGGAPLPPELLERFEErFGVRIVEGYGLTETSPVVTVN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 316 TPQMLHERPDTVGMPSANVDVKVKNPN----KEGH-GELMIKGANVMNGYLYPTDLT-DTFENGYFNTGDIAEIDHEGYV 389
Cdd:COG0318 260 PEDPGERRPGSVGRPLPGVEVRIVDEDgrelPPGEvGEIVVRGPNVMKGYWNDPEATaEAFRDGWLRTGDLGRLDEDGYL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 390 MIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVP 467
Cdd:COG0318 340 YIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrPGAELDAEELRAFLRERLARYKVP 419
|
490 500
....*....|....*....|..
gi 1853634356 468 KHFEKVDTLPYTSTGKLQRNKL 489
Cdd:COG0318 420 RRVEFVDELPRTASGKIDRRAL 441
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
162-485 |
1.61e-121 |
|
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: 358.91 E-value: 1.61e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQI 241
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 242 LTMIKNERITHISLVPQTLNWLMQQGLHEPHD---LQKILLGGAKLSATMIETALQY-NLPIYNSFGMTETCSQFLTATP 317
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDlssLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 318 QMLHERPDTVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYLYPTDLTD-TFENGYFNTGDIAEIDHEGYVMI 391
Cdd:cd04433 161 DDDARKPGSVGRPVPGVEVRIVDPDGGelppgEIGELVVRGPSVMKGYWNNPEATAaVDEDGWYRTGDLGRLDEDGYLYI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 392 YDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKH 469
Cdd:cd04433 241 VGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVlrPGADLDAEELRAHVRERLAPYKVPRR 320
|
330
....*....|....*.
gi 1853634356 470 FEKVDTLPYTSTGKLQ 485
Cdd:cd04433 321 VVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
5-486 |
4.57e-96 |
|
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: 297.21 E-value: 4.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 5 LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLT 81
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALgvaKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 82 PNEMKnqmrsidvqlifctlplelrgFQIvslddiefagtditmndlmdntldiqydtlnetvvpKDSPSNILntsfnID 161
Cdd:cd17631 81 PPEVA---------------------YIL------------------------------------ADSGAKVL-----FD 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVI-EGFTVRIVDKFNAEQ 240
Cdd:cd17631 99 DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLlRGGTVVILRKFDPET 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 241 ILTMIKNERITHISLVPQTLNWLMQQGLHEPHD---LQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATP 317
Cdd:cd17631 179 VLDLIERHRVTSFFLVPTMIQALLQHPRFATTDlssLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 318 QMLHERPDTVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYL-YPTDLTDTFENGYFNTGDIAEIDHEGYVMI 391
Cdd:cd17631 259 EDHRRKLGSAGRPVFFVEVRIVDPDGRevppgEVGEIVVRGPHVMAGYWnRPEATAAAFRDGWFHTGDLGRLDEDGYLYI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 392 YDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKH 469
Cdd:cd17631 339 VDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVprPGAELDEDELIAHCRERLARYKIPKS 418
|
490
....*....|....*..
gi 1853634356 470 FEKVDTLPYTSTGKLQR 486
Cdd:cd17631 419 VEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
5-402 |
1.75e-91 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 284.59 E-value: 1.75e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 5 LYKQAQQNGHHIAI-TDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRL 80
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALgvgKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 81 TPNEMKNQMRSIDVQLIFCTlplelRGFQIVSLDDIEFAGTDITMNDLMDNTLDIQYDTLNETVVPKDSPsNILNTSFNI 160
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITD-----DALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVP-PPPPPPPDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCK----ESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDK 235
Cdd:pfam00501 155 DDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 236 FNA---EQILTMIKNERITHISLVPQTLNWLMQQGLHEPHD---LQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTET 308
Cdd:pfam00501 235 FPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALlssLRLVLSGGAPLPPELARRFRElFGGALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 CSQFLTATPQMLH-ERPDTVGMPSANVDVKVKNPNKEG------HGELMIKGANVMNGYLYPTDLT-DTF-ENGYFNTGD 379
Cdd:pfam00501 315 TGVVTTPLPLDEDlRSLGSVGRPLPGTEVKIVDDETGEpvppgePGELCVRGPGVMKGYLNDPELTaEAFdEDGWYRTGD 394
|
410 420
....*....|....*....|...
gi 1853634356 380 IAEIDHEGYVMIYDRRKDLIISG 402
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
5-489 |
7.16e-90 |
|
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: 282.14 E-value: 7.16e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 5 LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKA--YQQS-RVGLYIDNSIQSIILIHACWLANIEIAMINTRLT 81
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNlgVQPGdRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 82 PNEMKNQMRSIDVQLIFCTLPLElrgfqivslddiefagtditmnDLMDntldiQYDTLNETVVPKDspsnilntsfniD 161
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFT----------------------DLLA-----AGAPLGERVALTP------------E 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDH--DTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDKFNA 238
Cdd:cd05936 126 DVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLegDDVVLAALPLFHVFGLTVaLLLPLALGATIVLIPRFRP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 EQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILL---GGAKLSATMIETALQ-YNLPIYNSFGMTEtCSQFLT 314
Cdd:cd05936 206 IGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLcisGGAPLPVEVAERFEElTGVPIVEGYGLTE-TSPVVA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 315 ATPQMLHERPDTVGMPSANVDVKVKNPNKE----G-HGELMIKGANVMNGYLYPTDLTD-TFENGYFNTGDIAEIDHEGY 388
Cdd:cd05936 285 VNPLDGPRKPGSIGIPLPGTEVKIVDDDGEelppGeVGELWVRGPQVMKGYWNRPEETAeAFVDGWLRTGDIGYMDEDGY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 389 VMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKV 466
Cdd:cd05936 365 FFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVlkEGASLTEEEIIAFCREQLAGYKV 444
|
490 500
....*....|....*....|...
gi 1853634356 467 PKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05936 445 PRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
5-489 |
1.60e-87 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 277.84 E-value: 1.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 5 LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIIlihaCWLAnieIAMI----- 76
Cdd:PRK06187 12 LRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALgvkKGDRVAVFDWNSHEYLE----AYFA---VPKIgavlh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 77 --NTRLTPNEMKNQMRSIDVQLIFC---TLPLeLRGFqivsLDDIEFAGTDITMNDLMDNTLDIQYDTLNETVvpKDSPS 151
Cdd:PRK06187 85 piNIRLKPEEIAYILNDAEDRVVLVdseFVPL-LAAI----LPQLPTVRTVIVEGDGPAAPLAPEVGEYEELL--AAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 152 NILNTSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVR 231
Cdd:PRK06187 158 TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 232 IVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKI---LLGGAKLSATMIETALQ-YNLPIYNSFGMTE 307
Cdd:PRK06187 238 IPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLrlvIYGGAALPPALLREFKEkFGIDLVQGYGMTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 308 TCS--QFLTATPQMLH--ERPDTVGMPSANVDVKVKN------PNKEGH-GELMIKGANVMNGYL-YPTDLTDTFENGYF 375
Cdd:PRK06187 318 TSPvvSVLPPEDQLPGqwTKRRSAGRPLPGVEARIVDddgdelPPDGGEvGEIIVRGPWLMQGYWnRPEATAETIDGGWL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 376 NTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSE--SDISKAQL 453
Cdd:PRK06187 398 HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKpgATLDAKEL 477
|
490 500 510
....*....|....*....|....*....|....*.
gi 1853634356 454 IAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06187 478 RAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
162-486 |
1.32e-80 |
|
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: 253.41 E-value: 1.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQI 241
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 242 ltMIKNERITHISLVPQTLNWLMQ--QGLHEPHDLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQfLTATPQM 319
Cdd:cd17630 81 --DLAPPGVTHVSLVPTQLQRLLDsgQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQ-VATKRPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 320 LHERPDtVGMPSANVDVKVKNPnkeghGELMIKGANVMNGYLYPTDLTDTFENGYFNTGDIAEIDHEGYVMIYDRRKDLI 399
Cdd:cd17630 158 GFGRGG-VGVLLPGRELRIVED-----GEIWVGGASLAMGYLRGQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 400 ISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYT 479
Cdd:cd17630 232 ISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRT 311
|
....*..
gi 1853634356 480 STGKLQR 486
Cdd:cd17630 312 GGGKVDR 318
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
5-489 |
3.44e-79 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 255.98 E-value: 3.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 5 LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLT 81
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALgigKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 82 PNEMKNQMRSIDVQLIFCtlplelrgfqivsLDDieFAGTDITMndlMDNTLDIQYDTLNETvvPKDSPSNILNTSF--- 158
Cdd:PRK07656 91 ADEAAYILARGDAKALFV-------------LGL--FLGVDYSA---TTRLPALEHVVICET--EEDDPHTEKMKTFtdf 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 159 -------------NIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAV 224
Cdd:PRK07656 151 laagdpaerapevDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAgVNAPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 225 IEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILL---GGAKLSATMIEtALQYNLPIY- 300
Cdd:PRK07656 231 MRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLavtGAASMPVALLE-RFESELGVDi 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 301 --NSFGMTEtCSQFLTATPqmLHERPDTV----GMPSANVDVKVKNPNKEGH-----GELMIKGANVMNGYLypTDLTDT 369
Cdd:PRK07656 310 vlTGYGLSE-ASGVTTFNR--LDDDRKTVagtiGTAIAGVENKIVNELGEEVpvgevGELLVRGPNVMKGYY--DDPEAT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 370 FE----NGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-- 443
Cdd:PRK07656 385 AAaidaDGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVlk 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1853634356 444 SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07656 465 PGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
17-485 |
3.15e-77 |
|
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: 249.82 E-value: 3.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 17 AITDGQE--SYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRS 91
Cdd:cd05911 1 AQIDADTgkELTYAQLRTLSRRLAAGLRKLglkKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 92 IDVQLIFCTLPL----------ELRGFQIVSLDDIEFAGTDITmnDLMDNTLDIQYDtlNETVVPKDSPsnilntsfniD 161
Cdd:cd05911 81 SKPKVIFTDPDGlekvkeaakeLGPKDKIIVLDDKPDGVLSIE--DLLSPTLGEEDE--DLPPPLKDGK----------D 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTN--WLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAE 239
Cdd:cd05911 147 DTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNdvILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMIKNERITHISLVPQTLNWLMQQGLHEPHDL---QKILLGGAKLSATMIET--ALQYNLPIYNSFGMTETCSQFLT 314
Cdd:cd05911 227 LFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLsslRVILSGGAPLSKELQELlaKRFPNATIKQGYGMTETGGILTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 315 ATPqmLHERPDTVGMPSANVDVKVKNPNKEGH------GELMIKGANVMNGYLY-PTDLTDTF-ENGYFNTGDIAEIDHE 386
Cdd:cd05911 307 NPD--GDDKPGSVGRLLPNVEAKIVDDDGKDSlgpnepGEICVRGPQVMKGYYNnPEATKETFdEDGWLHTGDIGYFDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 387 GYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSE--SDISKAQLIAYLSQHLAKY 464
Cdd:cd05911 385 GYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKpgEKLTEKEVKDYVAKKVASY 464
|
490 500
....*....|....*....|....*
gi 1853634356 465 kvpKHFEK----VDTLPYTSTGKLQ 485
Cdd:cd05911 465 ---KQLRGgvvfVDEIPKSASGKIL 486
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
3-491 |
2.13e-75 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 245.54 E-value: 2.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 3 FWLYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAR----RLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINT 78
Cdd:PRK06839 6 YWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAyliyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 79 RLTPNEMKNQMRSIDVQLIFCtlplelrgfqivsldDIEFAGTditmndlmdnTLDIQYDTLNETVVPKDSPSNILNTSF 158
Cdd:PRK06839 86 RLTENELIFQLKDSGTTVLFV---------------EKTFQNM----------ALSMQKVSYVQRVISITSLKEIEDRKI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 159 ------NIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVL-LRAVIEGFTVR 231
Cdd:PRK06839 141 dnfvekNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 232 IVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILL---GGAKLSATMIETALQYNLPIYNSFGMTET 308
Cdd:PRK06839 221 VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWfynGGAPCPEELMREFIDRGFLFGQGFGMTET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 CSQFLTATPQMLHERPDTVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYLYPTDLT-DTFENGYFNTGDIAE 382
Cdd:PRK06839 301 SPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNkvevgEVGELLIRGPNVMKEYWNRPDATeETIQDGWLCTGDLAR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 383 IDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQH 460
Cdd:PRK06839 381 VDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSsvLIEKDVIEHCRLF 460
|
490 500 510
....*....|....*....|....*....|.
gi 1853634356 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK06839 461 LAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
16-489 |
2.34e-74 |
|
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: 242.60 E-value: 2.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 16 IAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSII-LIHACWLANIeIAMINTRLTPNEMKNQMRS 91
Cdd:cd05926 6 LVVPGSTPALTYADLAELVDDLARQLAALgikKGDRVAIALPNGLEFVVaFLAAARAGAV-VAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 92 IDVQLIF---CTLPLELRGFQIVSLDDIEFAgtditmNDLMDNTLDIQYDTLNetVVPKDSPSNILNTSFNIDDIASIMF 168
Cdd:cd05926 85 LGSKLVLtpkGELGPASRAASKLGLAILELA------LDVGVLIRAPSAESLS--NLLADKKNAKSEGVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 169 TSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDKFNAEQILTMIKN 247
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLvASLLSTLAAGGSVVLPPRFSASTFWPDVRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 248 ERITHISLVPQTLNWLMQ----QGLHEPHDLQKILLGGAKLSATmIETALQ--YNLPIYNSFGMTETCSQfLTATP-QML 320
Cdd:cd05926 237 YNATWYTAVPTIHQILLNrpepNPESPPPKLRFIRSCSASLPPA-VLEALEatFGAPVLEAYGMTEAAHQ-MTSNPlPPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 321 HERPDTVGMPSaNVDVKVKNPNKE-----GHGELMIKGANVMNGYLYPTDLT--DTFENGYFNTGDIAEIDHEGYVMIYD 393
Cdd:cd05926 315 PRKPGSVGKPV-GVEVRILDEDGEilppgVVGEICLRGPNVTRGYLNNPEANaeAAFKDGWFRTGDLGYLDADGYLFLTG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 394 RRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQHLAKYKVPKHFE 471
Cdd:cd05926 394 RIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGasVTEEELRAFCRKHLAAFKVPKKVY 473
|
490
....*....|....*...
gi 1853634356 472 KVDTLPYTSTGKLQRNKL 489
Cdd:cd05926 474 FVDELPKTATGKIQRRKV 491
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
21-489 |
1.88e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 213.90 E-value: 1.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 21 GQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLI 97
Cdd:PRK09088 19 LGRRWTYAELDALVGRLAAVLRRRgcvDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 98 fctlplelrgfqivsLDDIEFAGTDITMNDLMDNTLDIQYDTLNET-VVPKDSPSNILntsfniddiasimFTSGTTGPQ 176
Cdd:PRK09088 99 ---------------LGDDAVAAGRTDVEDLAAFIASADALEPADTpSIPPERVSLIL-------------FTSGTSGQP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 177 KAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVI-EGFTVRIVDKFNAEQILTMIKNER--ITHI 253
Cdd:PRK09088 151 KGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLaVGGSILVSNGFEPKRTLGRLGDPAlgITHY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 254 SLVPQTLNWLMQQGLHEPHDLQK---ILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQF-LTATPQMLHERPDTVGM 329
Cdd:PRK09088 231 FCVPQMAQAFRAQPGFDAAALRHltaLFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGTVFgMSVDCDVIRAKAGAAGI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 330 PSANVDVKVKNPNKEG-----HGELMIKGANVMNGYLY-PTDLTDTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISG 402
Cdd:PRK09088 311 PTPTVQTRVVDDQGNDcpagvPGELLLRGPNLSPGYWRrPQATARAFtGDGWFRTGDIARRDADGFFWVVDRKKDMFISG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 403 GENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTS 480
Cdd:PRK09088 391 GENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVpaDGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTA 470
|
....*....
gi 1853634356 481 TGKLQRNKL 489
Cdd:PRK09088 471 SGKLQKARL 479
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
9-489 |
5.93e-61 |
|
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: 207.86 E-value: 5.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 9 AQQNGHHIAITDGQ--ESYTYQNLYceasLLARRLKAYQQSRVGLYID-------NSIQSIILIHACWLANIEIAMINTR 79
Cdd:cd05904 15 ASAHPSRPALIDAAtgRALTYAELE----RRVRRLAAGLAKRGGRKGDvvlllspNSIEFPVAFLAVLSLGAVVTTANPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 80 LTPNEMKNQMRSIDVQLIFCTLPL--ELRGF--QIVSLDDIEFagtditmnDLMDNTLDIQYDTLNETVVPKDSPsniln 155
Cdd:cd05904 91 STPAEIAKQVKDSGAKLAFTTAELaeKLASLalPVVLLDSAEF--------DSLSFSDLLFEADEAEPPVVVIKQ----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 156 tsfniDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCK--ESLGFDHDTNWLSVLPIYHISGLSVLLRAVIE-GFTVRI 232
Cdd:cd05904 158 -----DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVagEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRlGATVVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 233 VDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQK---ILLGGAKLSATMIETALQyNLP---IYNSFGMT 306
Cdd:cd05904 233 MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSlrqIMSGAAPLGKELIEAFRA-KFPnvdLGQGYGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 307 E-TCSQFLTATPQMLHERPDTVGMPSANVDVKVKNPNKEGH------GELMIKGANVMNGYL---YPTDLTDTFEnGYFN 376
Cdd:cd05904 312 EsTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESlppnqtGELWIRGPSIMKGYLnnpEATAATIDKE-GWLH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 377 TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLI 454
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVrkPGSSLTEDEIM 470
|
490 500 510
....*....|....*....|....*....|....*
gi 1853634356 455 AYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05904 471 DFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
9-489 |
4.34e-59 |
|
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: 202.14 E-value: 4.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 9 AQQNGHHIAITDGQESYT----YQNLYCEASLLARRLKaYQQSRVGLYIDNsiqsiilIHACWLANIEIAM-------IN 77
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTwrqtYDRCRRLASALAALGI-SRGDTVAVLAPN-------TPAMYELHFGVPMagavlnaLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 78 TRLTPNEMKNQMRSIDVQLIFCtlplelrgfqivsldDIEFAGTDitmndlmdntLDIQYDTLNETVVPKDSpsnilnts 157
Cdd:cd12118 86 TRLDAEEIAFILRHSEAKVLFV---------------DREFEYED----------LLAEGDPDFEWIPPADE-------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 158 fniDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFN 237
Cdd:cd12118 133 ---WDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRKVD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLVPQTLNWLM----QQGLHEPHDLQkILLGGAKLSATMIETALQYNLPIYNSFGMTET----- 308
Cdd:cd12118 210 AKAIYDLIEKHKVTHFCGAPTVLNMLAnappSDARPLPHRVH-VMTAGAPPPAAVLAKMEELGFDVTHVYGLTETygpat 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 -C-----SQFLTATPQMLHERPDTVGMPSANvDVKVKNPNK--------EGHGELMIKGANVMNGYLYPTDLTD-TFENG 373
Cdd:cd12118 289 vCawkpeWDELPTEERARLKARQGVRYVGLE-EVDVLDPETmkpvprdgKTIGEIVFRGNIVMKGYLKNPEATAeAFRGG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLyFVSESDISKA-- 451
Cdd:cd12118 368 WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA-FVELKEGAKVte 446
|
490 500 510
....*....|....*....|....*....|....*....
gi 1853634356 452 -QLIAYLSQHLAKYKVPKHFEKVDtLPYTSTGKLQRNKL 489
Cdd:cd12118 447 eEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
18-489 |
2.92e-57 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 198.24 E-value: 2.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 18 ITDGQESYTYQNLYCEASLLA---RRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDV 94
Cdd:cd12119 19 HEGEVHRYTYAEVAERARRLAnalRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 95 QLIFCTLPLELRGFQIV-SLDDIE--FAGTDITMNDLMDNTLDIQYDTLNEtvvpkDSPSNILNTSFNIDDIASIMFTSG 171
Cdd:cd12119 99 RVVFVDRDFLPLLEAIApRLPTVEhvVVMTDDAAMPEPAGVGVLAYEELLA-----AESPEYDWPDFDENTAAAICYTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 172 TTGPQKAVPQTFRN--HYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGftVRIV---DKFNAEQILTMIK 246
Cdd:cd12119 174 TTGNPKGVVYSHRSlvLHAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAAMVG--AKLVlpgPYLDPASLAELIE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 247 NERITHISLVPQTLNWLMQQGLHEPHDLQ---KILLGGAKLSATMIETALQYNLPIYNSFGMTETC---------SQFLT 314
Cdd:cd12119 252 REGVTFAAGVPTVWQGLLDHLEANGRDLSslrRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSplgtvarppSEHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 315 ATPQMLHERPDTVGMPSANVDVKVKNPNK-------EGHGELMIKGANVMNGYLYPTDLTD-TFENGYFNTGDIAEIDHE 386
Cdd:cd12119 332 LSEDEQLALRAKQGRPVPGVELRIVDDDGrelpwdgKAVGELQVRGPWVTKSYYKNDEESEaLTEDGWLRTGDVATIDED 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 387 GYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKY 464
Cdd:cd12119 412 GYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVlkEGATVTAEELLEFLADKVAKW 491
|
490 500
....*....|....*....|....*
gi 1853634356 465 KVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd12119 492 WLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
161-489 |
8.12e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 194.43 E-value: 8.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLlRAVIEGFTVRIVDKFNAEQ 240
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFL-PTLLRGGTVIVLAKFDPAE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 241 ILTMIKNERITHISLVPQTLNWLMQQGLHEPHD---LQKILLGGAKLSATMIETALQYNLPIY-NSFGMTEtCSQFLTAT 316
Cdd:PRK06188 247 VLRAIEEQRITATFLVPTMIYALLDHPDLRTRDlssLETVYYGASPMSPVRLAEAIERFGPIFaQYYGQTE-APMVITYL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 317 PQMLHERPD-----TVGMPSANVDVKVKNPN----KEGH-GELMIKGANVMNGYLYPTDLT-DTFENGYFNTGDIAEIDH 385
Cdd:PRK06188 326 RKRDHDPDDpkrltSCGRPTPGLRVALLDEDgrevAQGEvGEICVRGPLVMDGYWNRPEETaEAFRDGWLHTGDVAREDE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 386 EGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAK 463
Cdd:PRK06188 406 DGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVlrPGAAVDAAELQAHVKERKGS 485
|
330 340
....*....|....*....|....*.
gi 1853634356 464 YKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06188 486 VHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
14-489 |
7.76e-54 |
|
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: 187.11 E-value: 7.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 14 HHIAITDGQESYTYQNLYCEASLLARRL----KAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKnqm 89
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLlalgKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 90 rsidvqlifctlplelrgfqivslddiefagtditmndlmdntldiqydtlnetVVPKDS-PSNILntsfnidDIASIMF 168
Cdd:cd05941 78 ------------------------------------------------------YVITDSePSLVL-------DPALILY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 169 TSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDKFNAEQILTMIKN 247
Cdd:cd05941 97 TSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLvNALLCPLFAGASVEFLPKFDPKEVAISRLM 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 248 ERITHISLVPQTLNWLMQQGLHEPHDLQKILLGGAKLSATMIETALQYNLPIYNSF------------GMTETcsqfLTA 315
Cdd:cd05941 177 PSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWeaitghtlleryGMTEI----GMA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 316 TPQMLHE--RPDTVGMPSANVDVKVKNPN------KEGHGELMIKGANVMNGYL-YPTDLTDTF-ENGYFNTGDIAEIDH 385
Cdd:cd05941 253 LSNPLDGerRPGTVGMPLPGVQARIVDEEtgeplpRGEVGEIQVRGPSVFKEYWnKPEATKEEFtDDGWFKTGDLGVVDE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 386 EGYVMIYDRRKDLII-SGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESD---ISKAQLIAYLSQHL 461
Cdd:cd05941 333 DGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaaaLSLEELKEWAKQRL 412
|
490 500
....*....|....*....|....*...
gi 1853634356 462 AKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05941 413 APYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
161-489 |
1.03e-53 |
|
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: 186.82 E-value: 1.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFD-HDTNWLSVlPIYHISG-LSVLLRAVIEGFTVRIVDKFNA 238
Cdd:cd05903 93 DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGpGDVFLVAS-PMAHQTGfVYGFTLPLLLGAPVVLQDIWDP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 EQILTMIKNERITHI----SLVPQTLNWLMQQGLHEPHdLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFL 313
Cdd:cd05903 172 DKALALMREHGVTFMmgatPFLTDLLNAVEEAGEPLSR-LRTFVCGGATVPRSLARRAAElLGAKVCSAYGSTECPGAVT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 314 TATPQMLHERPDTVGMPSANVDVKV-----KNPNKEGHGELMIKGANVMNGYLYPTDLT-DTFENGYFNTGDIAEIDHEG 387
Cdd:cd05903 251 SITPAPEDRRLYTDGRPLPGVEIKVvddtgATLAPGVEGELLSRGPSVFLGYLDRPDLTaDAAPEGWFRTGDLARLDEDG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 388 YVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSES--DISKAQLIAYLSQH-LAKY 464
Cdd:cd05903 331 YLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSgaLLTFDELVAYLDRQgVAKQ 410
|
330 340
....*....|....*....|....*
gi 1853634356 465 KVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05903 411 YWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
9-484 |
6.56e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 186.68 E-value: 6.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 9 AQQNGHHIAITDGQESYTYQNL--YCE---ASLLARRLKAYQqsRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPN 83
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELdaAVNrvaAALLDLGLKKGD--RVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 84 EMKNQMRSIDVQLIFC------TLPLELRGFQIVSLDDIEFAGTDitmnDLMDNTLDIQYDTLNETVVPkdsPSNILNts 157
Cdd:PRK08316 99 ELAYILDHSGARAFLVdpalapTAEAALALLPVDTLILSLVLGGR----EAPGGWLDFADWAEAGSVAE---PDVELA-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 158 fnIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDKF 236
Cdd:PRK08316 170 --DDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVfLGPYLYVGATNVILDAP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 237 NAEQILTMIKNERIThiSL-VPQTLnW--LMQQGLHEPHD---LQKILLGGAKLSATMIETaLQYNLP---IYNSFGMTE 307
Cdd:PRK08316 248 DPELILRTIEAERIT--SFfAPPTV-WisLLRHPDFDTRDlssLRKGYYGASIMPVEVLKE-LRERLPglrFYNCYGQTE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 308 TCSqflTAT---PQMLHERPDTVGMPSANVDVKV----KNPNKEGH-GELMIKGANVMNGYLYPTDLT-DTFENGYFNTG 378
Cdd:PRK08316 324 IAP---LATvlgPEEHLRRPGSAGRPVLNVETRVvdddGNDVAPGEvGEIVHRSPQLMLGYWDDPEKTaEAFRGGWFHSG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 379 DIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQ------VPKlyfvSESDISKAQ 452
Cdd:PRK08316 401 DLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEavtavvVPK----AGATVTEDE 476
|
490 500 510
....*....|....*....|....*....|..
gi 1853634356 453 LIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKL 484
Cdd:PRK08316 477 LIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
166-486 |
8.21e-53 |
|
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: 181.06 E-value: 8.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 166 IMFTSGTTGPQKAVpqtFRNH--YASAIGCKESLGFDHDTNWLSVL-PIYHISGLSVLLRAVIEGFTVRIVDKFNAEQIL 242
Cdd:cd17633 5 IGFTSGTTGLPKAY---YRSErsWIESFVCNEDLFNISGEDAILAPgPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 243 TMIKNERITHISLVPQTLNWLMQQGLHEpHDLQKILLGGAKLSATMIETALQY--NLPIYNSFGMTETcsQFLTATPQML 320
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALARTLEPE-SKIKSIFSSGQKLFESTKKKLKNIfpKANLIEFYGTSEL--SFITYNFNQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 321 HERPDTVGMPSANVDVKVKNPNKEGHGELMIKGANVMNGYLYPTDLTdtfENGYFNTGDIAEIDHEGYVMIYDRRKDLII 400
Cdd:cd17633 159 SRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGGFSN---PDGWMSVGDIGYVDEEGYLYLVGRESDMII 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 401 SGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESdISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTS 480
Cdd:cd17633 236 IGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDK-LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTS 314
|
....*.
gi 1853634356 481 TGKLQR 486
Cdd:cd17633 315 SGKIAR 320
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
48-489 |
2.96e-52 |
|
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: 182.68 E-value: 2.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 48 RVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMknqmrsidvqlifctlplelrgfqivslddiEFagtditmnd 127
Cdd:cd05935 28 RVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKEREL-------------------------------EY--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 128 lmdntldiqydtlnetvVPKDSPSNILNTSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLS 207
Cdd:cd05935 68 -----------------ILNDSGAKVAVVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 208 VLPIYHISGL-SVLLRAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILL---GGAK 283
Cdd:cd05935 131 CLPLFHVTGFvGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVltgGGAP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 284 LSATMIE-----TALQYNlpiyNSFGMTETCSQflTATPQMLHERPDTVGMPSANVDVKVKN--------PNKEGhgELM 350
Cdd:cd05935 211 MPPAVAEkllklTGLRFV----EGYGLTETMSQ--THTNPPLRPKLQCLGIP*FGVDARVIDietgrelpPNEVG--EIV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 351 IKGANVMNGYL-YPTDLTDTF--ENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAV 425
Cdd:cd05935 283 VRGPQIFKGYWnRPEETEESFieIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVC 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1853634356 426 CIGHPDDTWGQVPKLYFV----SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05935 363 VISVPDERVGEEVKAFIVlrpeYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
76-489 |
5.01e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 184.60 E-value: 5.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 76 INTRLTPNEMKNQMRSIDVQLIFCTLPLElrGFQIVSLDDIEFAGTDITMNDLMDNTLdIQYDTLNETVVPKDSPSNILN 155
Cdd:PRK07786 97 VNFRLTPPEIAFLVSDCGAHVVVTEAALA--PVATAVRDIVPLLSTVVVAGGSSDDSV-LGYEDLLAEAGPAHAPVDIPN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 156 tsfniDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFD--HDTNWLSVlPIYHISGLSVLLRAVIEGFTVRI- 232
Cdd:PRK07786 174 -----DSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADinSDVGFVGV-PLFHIAGIGSMLPGLLLGAPTVIy 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 233 -VDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQ-KILLGGAKLSATMIETALQYNLP---IYNSFGMTE 307
Cdd:PRK07786 248 pLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLAlRVLSWGAAPASDTLLRQMAATFPeaqILAAFGQTE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 308 ----TCsqfltatpqMLH-----ERPDTVGMPSANVDVKVKNPNKE----GH-GELMIKGANVMNGYLY-PTDLTDTFEN 372
Cdd:PRK07786 328 mspvTC---------MLLgedaiRKLGSVGKVIPTVAARVVDENMNdvpvGEvGEIVYRAPTLMSGYWNnPEATAEAFAG 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 373 GYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV---SESDIS 449
Cdd:PRK07786 399 GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAvrnDDAALT 478
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1853634356 450 KAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07786 479 LEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
141-489 |
1.04e-50 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 179.03 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 141 NETVVPKDSPSNILNTSFNIDDIASIMF-TSGTTGPQKAVPQTFRNHYASAIGCKESlgFDHDT-NWLSVLPIYHISGLS 218
Cdd:PRK07445 99 LDQLKLSHPPPLPSQGILPNLETGWIMIpTGGSSGQIRFAIHTWETLTASVQGFQRY--FQLQQvNSFCVLPLYHVSGLM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 219 VLLRAVIEGFTVRIVDkfnaeqiLTMIKNERITH-------ISLVPQTLNWLMQQGLHEPHDLQKILLGGAKLSATMIET 291
Cdd:PRK07445 177 QFMRSFLTGGKLVILP-------YKRLKSGQELPpnpsdffLSLVPTQLQRLLQLRPQWLAQFRTILLGGAPAWPSLLEQ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 292 ALQYNLPIYNSFGMTETCSQFLTATPQMLHERPDTVG--MPSANVDVKvknPNKEGHgeLMIKGANVMNGYlYPtDLTDT 369
Cdd:PRK07445 250 ARQLQLRLAPTYGMTETASQIATLKPDDFLAGNNSSGqvLPHAQITIP---ANQTGN--ITIQAQSLALGY-YP-QILDS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 370 feNGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQ-VPKLYFVSESDI 448
Cdd:PRK07445 323 --QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEvVTAIYVPKDPSI 400
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1853634356 449 SKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07445 401 SLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
162-486 |
2.85e-50 |
|
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: 174.61 E-value: 2.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDKFNAEQ 240
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAgIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 241 ILTMIKNERITHISLVPQtlnwLMQQGLHEPH----DLQKI---LLGGAKLSATMIETaLQYNLPIYN---SFGMTETCS 310
Cdd:cd17638 81 ILEAIERERITVLPGPPT----LFQSLLDHPGrkkfDLSSLraaVTGAATVPVELVRR-MRSELGFETvltAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 311 QFLTATPQMLHERPDTVGMPSANVDVKVKNPnkeghGELMIKGANVMNGYLYPTDLTDTF--ENGYFNTGDIAEIDHEGY 388
Cdd:cd17638 156 ATMCRPGDDAETVATTCGRACPGFEVRIADD-----GEVLVRGYNVMQGYLDDPEATAEAidADGWLHTGDVGELDERGY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 389 VMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDISKAQ--LIAYLSQHLAKYKV 466
Cdd:cd17638 231 LRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEedVIAWCRERLANYKV 310
|
330 340
....*....|....*....|
gi 1853634356 467 PKHFEKVDTLPYTSTGKLQR 486
Cdd:cd17638 311 PRFVRFLDELPRNASGKVMK 330
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
2-489 |
6.16e-50 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 179.17 E-value: 6.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 2 DFWlYKQAQQNGHHIAITDGQ-ESYTYQNLYCEASLLARRLK----------AYQQS-------------RVG------- 50
Cdd:PRK06087 27 DYW-QQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLakgiepgdrvAFQLPgwceftiiylaclKVGavsvpll 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 51 --------LYIDNSIQSIILIHACWLANIeiamiNTRLTPNEMKNQMRSIDvqlifctlplelrgfQIVSLDDIEFAGTD 122
Cdd:PRK06087 106 pswreaelVWVLNKCQAKMFFAPTLFKQT-----RPVDLILPLQNQLPQLQ---------------QIVGVDKLAPATSS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 123 ITMNDLMDNtldiqYDTLNETVvpkdspsnilntSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHD 202
Cdd:PRK06087 166 LSLSQIIAD-----YEPLTTAI------------TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 203 TNWLSVLPIYHISG-LSVLLRAVIEGFTVRIVDKFNAEQILTMIKNERITHIS----LVPQTLNWLMQQGLHEPhDLQKI 277
Cdd:PRK06087 229 DVFMMPAPLGHATGfLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLgatpFIYDLLNLLEKQPADLS-ALRFF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 278 LLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPQMLHERPDTVGMPSANVDVKVKNPNKE----GH-GELMIK 352
Cdd:PRK06087 308 LCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKtlppGCeGEEASR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 353 GANVMNGYLYPTDLTDTF--ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHP 430
Cdd:PRK06087 388 GPNVFMGYLDEPELTARAldEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMP 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1853634356 431 DDTWGQVPKLYFV---SESDISKAQLIAYLS-QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06087 468 DERLGERSCAYVVlkaPHHSLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
161-489 |
1.47e-49 |
|
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: 173.23 E-value: 1.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDK-FNA 238
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLgVLACLTHGATMVFPSPsFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 EQILTMIKNERITHISLVP----QTLNwLMQQGLHEPHDLQKILLGGAKLSATMIETALQ-YNLP-IYNSFGMTET---C 309
Cdd:cd05917 82 LAVLEAIEKEKCTALHGVPtmfiAELE-HPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEvMNMKdVTIAYGMTETspvS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 310 SQFLTATPQmlHERPDTVGMPSANVDVKVKNPnkEG--------HGELMIKGANVMNGYLYPTDLTDTFEN--GYFNTGD 379
Cdd:cd05917 161 TQTRTDDSI--EKRVNTVGRIMPHTEAKIVDP--EGgivppvgvPGELCIRGYSVMKGYWNDPEKTAEAIDgdGWLHTGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 380 IAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYL 457
Cdd:cd05917 237 LAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRlkEGAELTEEDIKAYC 316
|
330 340 350
....*....|....*....|....*....|..
gi 1853634356 458 SQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05917 317 KGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
20-428 |
1.43e-48 |
|
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: 173.17 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 20 DGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIeiamintrltpnemknqmrsIDVQl 96
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALgvePGDRVAILSRNRPEWTIADLAILAIGA--------------------VPVP- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 97 IFCTLPLElrgfqivslddiefagtditmndlmdntlDIQYdTLNetvvpkDSPSNILNTSfNIDDIASIMFTSGTTGPQ 176
Cdd:cd05907 60 IYPTSSAE-----------------------------QIAY-ILN------DSEAKALFVE-DPDDLATIIYTSGTTGRP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 177 KAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHI----SGLSVLLRAvieGFTVRIVdkFNAEQILTMIKNERITH 252
Cdd:cd05907 103 KGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVferrAGLYVPLLA---GARIYFA--SSAETLLDDLSEVRPTV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 253 ISLVPQTL----NWLMQQGLHEphdLQKILL-------------GGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTA 315
Cdd:cd05907 178 FLAVPRVWekvyAAIKVKAVPG---LKRKLFdlavggrlrfaasGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLN 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 316 TPQMLheRPDTVGMPSANVDVKVKNpnkegHGELMIKGANVMNGYLYPTDLT--DTFENGYFNTGDIAEIDHEGYVMIYD 393
Cdd:cd05907 255 PPGDN--RIGTVGKPLPGVEVRIAD-----DGEILVRGPNVMLGYYKNPEATaeALDADGWLHTGDLGEIDEDGFLHITG 327
|
410 420 430
....*....|....*....|....*....|....*.
gi 1853634356 394 RRKDLII-SGGENIYPYQIETVAKQFPGISDAVCIG 428
Cdd:cd05907 328 RKKDLIItSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
161-486 |
2.23e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 175.19 E-value: 2.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCK---ESLGfDHDTNWLSVLPIYHISGLS-VLLRAVIEGFTVRIVDKF 236
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKawvPGLG-DGPERVLAALPMFHAYGLTlCLTLAVSIGGELVLLPAP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 237 NAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKI---LLGGAKLSATMIET--ALQYNLpIYNSFGMTETcSQ 311
Cdd:PRK05605 298 DIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVrnaFSGAMALPVSTVELweKLTGGL-LVEGYGLTET-SP 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 312 FLTATPQMLHERPDTVGMPSANVDVKVKNPNKEGH-------GELMIKGANVMNGYLYPTDLT-DTFENGYFNTGDIAEI 383
Cdd:PRK05605 376 IIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDPDEtmpdgeeGELLVRGPQVFKGYWNRPEETaKSFLDGWFRTGDVVVM 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 384 DHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQ--VPKLYFVSESDISKAQLIAYLSQHL 461
Cdd:PRK05605 456 EEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEevVAAVVLEPGAALDPEGLRAYCREHL 535
|
330 340
....*....|....*....|....*
gi 1853634356 462 AKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK05605 536 TRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
154-492 |
2.79e-48 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 174.99 E-value: 2.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 154 LNTSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIV 233
Cdd:PLN02860 165 LDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 234 DKFNAEQILTMIKNERITHISLVPQTLNWL-----MQQGLHEPHDLQKILLGGAKLSATMIETALQY--NLPIYNSFGMT 306
Cdd:PLN02860 245 PKFDAKAALQAIKQHNVTSMITVPAMMADLisltrKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLfpNAKLFSAYGMT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 307 ETCSQ--FLT----------ATPQMLHERPDT---------VGMPSANVDVKVKNPNKEGHGELMIKGANVMNGY--LYP 363
Cdd:PLN02860 325 EACSSltFMTlhdptlespkQTLQTVNQTKSSsvhqpqgvcVGKPAPHVELKIGLDESSRVGRILTRGPHVMLGYwgQNS 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 364 TDLTDTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDD----------- 432
Cdd:PLN02860 405 ETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSrltemvvacvr 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1853634356 433 -----TWGQVPKLYFVSESDISKAQLIAYLS-QHLAKYKVPKHF-EKVDTLPYTSTGKLQRNKLYRG 492
Cdd:PLN02860 485 lrdgwIWSDNEKENAKKNLTLSSETLRHHCReKNLSRFKIPKLFvQWRKPFPLTTTGKIRRDEVRRE 551
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
7-489 |
9.02e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 171.89 E-value: 9.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 7 KQAQQNGHHIAITDGQESYTYQNLYCEASLLARRL--KAYQQSRVGLYIDNSIQSIILI----HACWLAnieiAMINTRL 80
Cdd:PRK07638 9 KHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLneKESKNKTIAILLENRIEFLQLFagaaMAGWTC----VPLDIKW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 81 TPNEMKNQMRSIDVQLIFCTlplelrGFQIVSLDDIEFAGTDItmndlmdntldiqyDTLNETVvpkdspSNILNTSFNI 160
Cdd:PRK07638 85 KQDELKERLAISNADMIVTE------RYKLNDLPDEEGRVIEI--------------DEWKRMI------EKYLPTYAPI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIAS----IMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHisglSVLLRAVIE----GFTVRI 232
Cdd:PRK07638 139 ENVQNapfyMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVH----SLFLYGAIStlyvGQTVHL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 233 VDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLqKILLGGAKLSATMIEtALQYNLP---IYNSFGMTETc 309
Cdd:PRK07638 215 MRKFIPNQVLDKLETENISVMYTVPTMLESLYKENRVIENKM-KIISSGAKWEAEAKE-KIKNIFPyakLYEFYGASEL- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 310 sQFLTA-TPQMLHERPDTVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYLYPTDLTDTF-ENGYFNTGDIAE 382
Cdd:PRK07638 292 -SFVTAlVDEESERRPNSVGRPFHNVQVRICNEAGEevqkgEIGTVYVKSPQFFMGYIIGGVLARELnADGWMTVRDVGY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 383 IDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDisKAQLIAYLSQHLA 462
Cdd:PRK07638 371 EDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSAT--KQQLKSFCLQRLS 448
|
490 500
....*....|....*....|....*..
gi 1853634356 463 KYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07638 449 SFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
4-489 |
1.01e-47 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 173.37 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 4 WLYKQAQQNGHHIAI-----TDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAM 75
Cdd:COG0365 14 CLDRHAEGRGDKVALiwegeDGEERTLTYAELRREVNRFANALRALgvkKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 76 INTRLTPNEMKNQMRSIDVQLIFCTLPLELRGFQIVSLDDIEFA----------------GTDITMNDlmdntlDIQYDT 139
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEAleelpslehvivvgrtGADVPMEG------DLDWDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 140 L----NETVVPKDSPSnilntsfniDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKEsLGFDH----------DTNW 205
Cdd:COG0365 168 LlaaaSAEFEPEPTDA---------DDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAK-YVLDLkpgdvfwctaDIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 206 lsvlpIYHIS---------GLSVLLravIEGftvrIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEP--HD- 273
Cdd:COG0365 238 -----ATGHSyivygpllnGATVVL---YEG----RPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLkkYDl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 274 --LQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTATPqMLHERPDTVGMPSANVDVKVKNPnkEGH---- 346
Cdd:COG0365 306 ssLRLLGSAGEPLNPEVWEWWYEaVGVPIVDGWGQTETGGIFISNLP-GLPVKPGSMGKPVPGYDVAVVDE--DGNpvpp 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 347 ---GELMIKGAN--VMNGYLYPTDLT-----DTFEnGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAK 416
Cdd:COG0365 383 geeGELVIKGPWpgMFRGYWNDPERYretyfGRFP-GWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALV 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1853634356 417 QFPGISDAVCIGHPDDTWGQVPKLYFV-----SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:COG0365 462 SHPAVAEAAVVGVPDEIRGQVVKAFVVlkpgvEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-489 |
2.26e-47 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 169.39 E-value: 2.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 48 RVGLYIDNSIQSIilihACWLANIEIAM----INTRLTPNEMKNQMRSIDVQLIFCtlplelrgfqivslddiefagtdi 123
Cdd:cd05934 30 RVALMLDNCPEFL----FAWFALAKLGAvlvpINTALRGDELAYIIDHSGAQLVVV------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 124 tmndlmdntldiqydtlnetvvpkdspsnilntsfnidDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDT 203
Cdd:cd05934 82 --------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 204 NWLSVLPIYHISGLSV-LLRAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQglhEPHDLQK-----I 277
Cdd:cd05934 124 VYLTVLPLFHINAQAVsVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQ---PPSPDDRahrlrA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 278 LLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPQmlHERPDTVGMPSANVDVKVKNPNkeGH-------GELM 350
Cdd:cd05934 201 AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDE--PRRPGSIGRPAPGYEVRIVDDD--GQelpagepGELV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 351 IKGAN---VMNGYLY-PTDLTDTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVC 426
Cdd:cd05934 277 IRGLRgwgFFKGYYNmPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAV 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 427 IGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05934 357 VAVPDEVGEDEVKAVVVLRPGetLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
4-467 |
1.82e-46 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 167.74 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 4 WLYKQ-AQQNGHHIAITDGQESYTYQNLYCEASLLARRLKA---YQQSRVGLYIDNSIQSIIlihaCWLANIE----IAM 75
Cdd:PRK09029 7 WPWRHwAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQqgvVEGSGVALRGKNSPETLL----AYLALLQcgarVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 76 INTRLTPNEMKNQMRSIDVQLIFCtlplelrgfqivsLDDiefagtditmndlmdntlDIQYDTLneTVVPKDSPSNILN 155
Cdd:PRK09029 83 LNPQLPQPLLEELLPSLTLDFALV-------------LEG------------------ENTFSAL--TSLHLQLVEGAHA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 156 TSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDK 235
Cdd:PRK09029 130 VAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQGIVWRWLYAGATLVVRDK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 236 FNAEQILTMiknerITHISLVPQTLNWLMQQgLHEPHDLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSqflTA 315
Cdd:PRK09029 210 QPLEQALAG-----CTHASLVPTQLWRLLDN-RSEPLSLKAVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMAS---TV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 316 TPQMLHERPDtVGMPSANVDVKVKNpnkeghGELMIKGANVMNGYLY---PTDLTDtfENGYFNTGDIAEIDhEGYVMIY 392
Cdd:PRK09029 281 CAKRADGLAG-VGSPLPGREVKLVD------GEIWLRGASLALGYWRqgqLVPLVN--DEGWFATRDRGEWQ-NGELTIL 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 393 DRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVP 467
Cdd:PRK09029 351 GRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVNLAEWLQDKLARFQQP 425
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
14-489 |
6.65e-46 |
|
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: 166.92 E-value: 6.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 14 HHIAITD--GQESYTYQNLYCE-----ASLLARRLKayQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEM- 85
Cdd:cd05923 16 DACAIADpaRGLRLTYSELRARieavaARLHARGLR--PGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 86 ----KNQMRSIDVQLIfcTLPLE---LRGFQIVSLDDIEFAGTDITMNDLmdntldiqydtlnetvvPKDSPSNILNTSF 158
Cdd:cd05923 94 elieRGEMTAAVIAVD--AQVMDaifQSGVRVLALSDLVGLGEPESAGPL-----------------IEDPPREPEQPAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 159 niddiasIMFTSGTTGPQKA--VPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDK 235
Cdd:cd05923 155 -------VFYTSGTTGLPKGavIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFfAVLVAALALDGTYVVVEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 236 FNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDL---QKILLGGAKLSATMIETaLQYNLP--IYNSFGMTETCS 310
Cdd:cd05923 228 FDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLsslRHVTFAGATMPDAVLER-VNQHLPgeKVNIYGTTEAMN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 311 QFLTATPqmlheRPDTVGMPSANVDVKVKN---------PNKEgHGELMIK--GANVMNGYLYPTDLTDT-FENGYFNTG 378
Cdd:cd05923 307 SLYMRDA-----RTGTEMRPGFFSEVRIVRiggspdealANGE-EGELIVAaaADAAFTGYLNQPEATAKkLQDGWYRTG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 379 DIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQ-VPKLYFVSESDISKAQLIAY- 456
Cdd:cd05923 381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQsVTACVVPREGTLSADELDQFc 460
|
490 500 510
....*....|....*....|....*....|...
gi 1853634356 457 LSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05923 461 RASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
16-489 |
6.71e-46 |
|
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: 167.70 E-value: 6.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 16 IAITDG--QESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMR 90
Cdd:cd17642 34 IAFTDAhtGVNYSYAEYLEMSVRLAEALKKYglkQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 91 SIDVQLIFCTLplelRGFQ--------------IVSLDDIEFAGTDITMNDLMDNTLDIQYDTlnetvvpkdspSNILNT 156
Cdd:cd17642 114 ISKPTIVFCSK----KGLQkvlnvqkklkiiktIIILDSKEDYKGYQCLYTFITQNLPPGFNE-----------YDFKPP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 157 SFNID-DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDH---DTNWLSVLPIYHISGLSVLLRAVIEGFTVRI 232
Cdd:cd17642 179 SFDRDeQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQiipDTAILTVIPFHHGFGMFTTLGYLICGFRVVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 233 VDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHD---LQKILLGGAKLSATMIE-TALQYNLP-IYNSFGMTE 307
Cdd:cd17642 259 MYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDlsnLHEIASGGAPLSKEVGEaVAKRFKLPgIRQGYGLTE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 308 TCSQFLTaTPQMlHERPDTVGMPSANVDVKVKNPNK------EGHGELMIKGANVMNGYLYPTDLTDTF--ENGYFNTGD 379
Cdd:cd17642 339 TTSAILI-TPEG-DDKPGAVGKVVPFFYAKVVDLDTgktlgpNERGELCVKGPMIMKGYVNNPEATKALidKDGWLHSGD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 380 IAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESD--ISKAQLIAYL 457
Cdd:cd17642 417 IAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGktMTEKEVMDYV 496
|
490 500 510
....*....|....*....|....*....|...
gi 1853634356 458 SQHLAKYKVPKHFEK-VDTLPYTSTGKLQRNKL 489
Cdd:cd17642 497 ASQVSTAKRLRGGVKfVDEVPKGLTGKIDRRKI 529
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
156-491 |
7.77e-46 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 168.98 E-value: 7.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 156 TSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIEGFTV---- 230
Cdd:PRK07529 208 RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVtGLAPLARGAHVvlat 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 231 --------------RIVDKFnaeqiltmikneRITHISLVPQTLNWLMQQ--GLHEPHDLQKILLGGAKLSATMIETALQ 294
Cdd:PRK07529 288 pqgyrgpgvianfwKIVERY------------RINFLSGVPTVYAALLQVpvDGHDISSLRYALCGAAPLPVEVFRRFEA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 295 YN-LPIYNSFGMTE-TCSQflTATPQMLHERPDTVGMPSANVDVKVKNPNKEGH----------GELMIKGANVMNGYLY 362
Cdd:PRK07529 356 ATgVRIVEGYGLTEaTCVS--SVNPPDGERRIGSVGLRLPYQRVRVVILDDAGRylrdcavdevGVLCIAGPNVFSGYLE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 363 PTDLTDTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLY 441
Cdd:PRK07529 434 AAHNKGLWlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAY 513
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1853634356 442 --FVSESDISKAQLIAYLSQHLA-KYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK07529 514 vqLKPGASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
166-486 |
1.22e-45 |
|
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: 162.44 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 166 IMFTSGTTG-PQKAVpQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQILTM 244
Cdd:cd17637 5 IIHTAAVAGrPRGAV-LSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 245 IKNERITHISLVPQTLNWLMQQGLHEPHDLQKI-LLGGAKLSATMIETALQYNLPIYNSFGMTETcSQFLTATPqmLHER 323
Cdd:cd17637 84 IEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLrHVLGLDAPETIQRFEETTGATFWSLYGQTET-SGLVTLSP--YRER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 324 PDTVGMPSANVDVKV----KNPNKEGH-GELMIKGANVMNGYLYPTDLTD-TFENGYFNTGDIAEIDHEGYvMIYDRR-- 395
Cdd:cd17637 161 PGSAGRPGPLVRVRIvddnDRPVPAGEtGEIVVRGPLVFQGYWNLPELTAyTFRNGWHHTGDLGRFDEDGY-LWYAGRkp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 396 -KDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKHFEK 472
Cdd:cd17637 240 eKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVlkPGATLTADELIEFVGSRIARYKKPRYVVF 319
|
330
....*....|....
gi 1853634356 473 VDTLPYTSTGKLQR 486
Cdd:cd17637 320 VEALPKTADGSIDR 333
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
9-489 |
2.07e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 166.64 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 9 AQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEM 85
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALgvrAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 86 KNQMRSIDVQLIF---------CTLPLELRGFQ--IVSLDDIEFAG-TDITMNDLMDNTldiqydtlNETVVPK-DSPSN 152
Cdd:PRK07788 139 AEVAAREGVKALVyddeftdllSALPPDLGRLRawGGNPDDDEPSGsTDETLDDLIAGS--------STAPLPKpPKPGG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 153 IlntsfniddiasIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRI 232
Cdd:PRK07788 211 I------------VILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 233 VDKFNAEQILTMIKNERITHISLVPQTLNWLMQqglHEPHDLQK--------ILLGGAKLSATMIETAL-QYNLPIYNSF 303
Cdd:PRK07788 279 RRRFDPEATLEDIAKHKATALVVVPVMLSRILD---LGPEVLAKydtsslkiIFVSGSALSPELATRALeAFGPVLYNLY 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 304 GMTEtCSQFLTATPQMLHERPDTVGMPSANVDVKV----KNPNKEGH-GELMIKGANVMNGYlyptdlTDT----FENGY 374
Cdd:PRK07788 356 GSTE-VAFATIATPEDLAEAPGTVGRPPKGVTVKIldenGNEVPRGVvGRIFVGNGFPFEGY------TDGrdkqIIDGL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 375 FNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSE--SDISKAQ 452
Cdd:PRK07788 429 LSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKApgAALDEDA 508
|
490 500 510
....*....|....*....|....*....|....*..
gi 1853634356 453 LIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07788 509 IKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
160-483 |
1.22e-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.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 160.34 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 160 IDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIV----- 233
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVtLLTPLASGAHVVLAgpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 234 -DKFNAEQILTMIKNERITHISLVPQTLNWLMQQglhePHD-----LQKILLGGAKLSATM---IETALqyNLPIYNSFG 304
Cdd:cd05944 81 rNPGLFDNFWKLVERYRITSLSTVPTVYAALLQV----PVNadissLRFAMSGAAPLPVELrarFEDAT--GLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 305 MTEtCSQFLTATPQMLHERPDTVGMPSANVDVKVKNPNKEGH----------GELMIKGANVMNGYLYPTDLTDTF-ENG 373
Cdd:cd05944 155 LTE-ATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRllrdcapdevGEICVAGPGVFGGYLYTEGNKNAFvADG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLY--FVSESDISKA 451
Cdd:cd05944 234 WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYvqLKPGAVVEEE 313
|
330 340 350
....*....|....*....|....*....|...
gi 1853634356 452 QLIAYLSQHLA-KYKVPKHFEKVDTLPYTSTGK 483
Cdd:cd05944 314 ELLAWARDHVPeRAAVPKHIEVLEELPVTAVGK 346
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
26-484 |
1.39e-44 |
|
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: 163.27 E-value: 1.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 26 TYQNLYCEASLLARRLKAY--QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFCT--- 100
Cdd:cd05909 9 TYRKLLTGAIALARKLAKMtkEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSkqf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 101 --------LPLELRGFQIVSLDDIE-----------FAGTDITMNDLMdntldiqydtLNETVVPKDSpsnilntsfniD 161
Cdd:cd05909 89 ieklklhhLFDVEYDARIVYLEDLRakiskadkckaFLAGKFPPKWLL----------RIFGVAPVQP-----------D 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIEGFTVRIV-DKFNAE 239
Cdd:cd05909 148 DPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGcLWLPLLSGIKVVFHpNPLDYK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMIKNERITHISLVPQTLNWLMQQGlhEPHD---LQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTA 315
Cdd:cd05909 228 KIPELIYDKKATILLGTPTFLRGYARAA--HPEDfssLRLVVAGAEKLKDTLRQEFQEkFGIRILEGYGTTECSPVISVN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 316 TPQMlHERPDTVGMPSANVDVKVKNPnkEGH--------GELMIKGANVMNGYLYPTDLTDT-FENGYFNTGDIAEIDHE 386
Cdd:cd05909 306 TPQS-PNKEGTVGRPLPGMEVKIVSV--ETHeevpigegGLLLVRGPNVMLGYLNEPELTSFaFGDGWYDTGDIGKIDGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 387 GYVMIYDRRKDLIISGGENIYPYQIETVA-KQFPGISDAVCIGHPDDTWGQVPKLyFVSESDISKAQLIAYLSQH-LAKY 464
Cdd:cd05909 383 GFLTITGRLSRFAKIAGEMVSLEAIEDILsEILPEDNEVAVVSVPDGRKGEKIVL-LTTTTDTDPSSLNDILKNAgISNL 461
|
490 500
....*....|....*....|
gi 1853634356 465 KVPKHFEKVDTLPYTSTGKL 484
Cdd:cd05909 462 AKPSYIHQVEEIPLLGTGKP 481
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
4-489 |
1.53e-44 |
|
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: 163.78 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 4 WLYKQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIeI---AMIN 77
Cdd:COG1021 30 LLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALglrPGDRVVVQLPNVAEFVIVFFALFRAGA-IpvfALPA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 78 TRLTpnEMKNQMRSID-VQLIFCTlplELRGFqivslDDIEFAGTDITMNDLMDNTL-------DIQYDTLNETVVPKDS 149
Cdd:COG1021 109 HRRA--EISHFAEQSEaVAYIIPD---RHRGF-----DYRALARELQAEVPSLRHVLvvgdageFTSLDALLAAPADLSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 150 PSNilntsfNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLS--VLLRAVIEG 227
Cdd:COG1021 179 PRP------DPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSspGVLGVLYAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 228 FTVRIVDKFNAEQILTMIKNERITHISLVP-QTLNWLmQQGLHEPHD---LQKILLGGAKLS---ATMIETA----LQyn 296
Cdd:COG1021 253 GTVVLAPDPSPDTAFPLIERERVTVTALVPpLALLWL-DAAERSRYDlssLRVLQVGGAKLSpelARRVRPAlgctLQ-- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 297 lpiyNSFGMTE-----TcsqfltatpqmlheRPD--------TVGMP-SANVDVKV----KNPNKEGH-GELMIKGANVM 357
Cdd:COG1021 330 ----QVFGMAEglvnyT--------------RLDdpeeviltTQGRPiSPDDEVRIvdedGNPVPPGEvGELLTRGPYTI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 358 NGYlY--PTDLTDTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTW 434
Cdd:COG1021 392 RGY-YraPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYL 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1853634356 435 GQVPKLYFV-SESDISKAQLIAYL-SQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:COG1021 471 GERSCAFVVpRGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
161-489 |
1.75e-44 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 163.12 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLR-AVIEGFTVRIVDKFNAE 239
Cdd:PRK07514 156 DDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNvALLAGASMIFLPKFDPD 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMIKneRITHISLVPQTLNWLMQQGLHEPHDLQKILL---GGAKLSA-TMIETALQYNLPIYNSFGMTETCsqFLTA 315
Cdd:PRK07514 236 AVLALMP--RATVMMGVPTFYTRLLQEPRLTREAAAHMRLfisGSAPLLAeTHREFQERTGHAILERYGMTETN--MNTS 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 316 TPQMLHERPDTVGMPSANVDVKVKNPnKEGH-------GELMIKGANVMNGYLYPTDLTDT-F-ENGYFNTGDIAEIDHE 386
Cdd:PRK07514 312 NPYDGERRAGTVGFPLPGVSLRVTDP-ETGAelppgeiGMIEVKGPNVFKGYWRMPEKTAEeFrADGFFITGDLGKIDER 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 387 GYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIG--HPDdtWGQ------VPKlyfvSESDISKAQLIAYLS 458
Cdd:PRK07514 391 GYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGvpHPD--FGEgvtavvVPK----PGAALDEAAILAALK 464
|
330 340 350
....*....|....*....|....*....|.
gi 1853634356 459 QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07514 465 GRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
162-489 |
3.77e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 163.19 E-value: 3.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYH------------ISGLSVLLRaviegft 229
Cdd:PRK08162 183 DAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHcngwcfpwtvaaRAGTNVCLR------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 230 vrivdKFNAEQILTMIKNERITHISLVPQTLNWLmqqgLHEPHDLQ-------KILLGGAKLSATMIETALQYNLPIYNS 302
Cdd:PRK08162 256 -----KVDPKLIFDLIREHGVTHYCGAPIVLSAL----INAPAEWRagidhpvHAMVAGAAPPAAVIAKMEEIGFDLTHV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 303 FGMTET------CSQF-----LTATPQMLHERPDTVGMPSANvDVKVKNPNK--------EGHGELMIKGANVMNGYLYP 363
Cdd:PRK08162 327 YGLTETygpatvCAWQpewdaLPLDERAQLKARQGVRYPLQE-GVTVLDPDTmqpvpadgETIGEIMFRGNIVMKGYLKN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 364 TDLTD-TFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLyF 442
Cdd:PRK08162 406 PKATEeAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCA-F 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1853634356 443 VSESD---ISKAQLIAYLSQHLAKYKVPKHFEkVDTLPYTSTGKLQRNKL 489
Cdd:PRK08162 485 VELKDgasATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVL 533
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
5-429 |
1.11e-43 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 162.58 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 5 LYKQAQQNGHHIAI---TDGQ-ESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANieiAM-- 75
Cdd:COG1022 17 LRRRAARFPDRVALrekEDGIwQSLTWAEFAERVRALAAGLLALgvkPGDRVAILSDNRPEWVIADLAILAAG---AVtv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 76 -INTRLTPNEMKNQMRSIDVQLIFC--------------TLPlELRgfQIVSLDDIEFAGTD--ITMNDLMDNTLDIQYD 138
Cdd:COG1022 94 pIYPTSSAEEVAYILNDSGAKVLFVedqeqldkllevrdELP-SLR--HIVVLDPRGLRDDPrlLSLDELLALGREVADP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 139 TLNETVVPKDSPsnilntsfniDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLS 218
Cdd:COG1022 171 AELEARRAAVKP----------DDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 219 VLLRAVIEGFTVRIVDkfNAEQILTMIKNERITHISLVP---------------------QTL-NWLMQQGL-HEPHDLQ 275
Cdd:COG1022 241 VSYYALAAGATVAFAE--SPDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkRKLfRWALAVGRrYARARLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 276 ----------------KILL----------------GGAKLSATMIE--TALqyNLPIYNSFGMTETCSqflTATPQMLH 321
Cdd:COG1022 319 gkspslllrlkhaladKLVFsklrealggrlrfavsGGAALGPELARffRAL--GIPVLEGYGLTETSP---VITVNRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 322 E-RPDTVGMPSANVDVKVknpnkEGHGELMIKGANVMNGYLYPTDLT-DTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDL 398
Cdd:COG1022 394 DnRIGTVGPPLPGVEVKI-----AEDGEILVRGPNVMKGYYKNPEATaEAFdADGWLHTGDIGELDEDGFLRITGRKKDL 468
|
490 500 510
....*....|....*....|....*....|..
gi 1853634356 399 II-SGGENIYPYQIETVAKQFPGISDAVCIGH 429
Cdd:COG1022 469 IVtSGGKNVAPQPIENALKASPLIEQAVVVGD 500
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
161-489 |
1.15e-43 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 161.76 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLR-AVIEGFTVRIVDKFNAE 239
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMmPVMLGATAVLQDIWDPA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMIKNERITHISLVPQTLNWLMQQGLHEPHD---LQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTa 315
Cdd:PRK13295 277 RAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPvssLRTFLCAGAPIPGALVERARAaLGAKIVSAWGMTENGAVTLT- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 316 TPQMLHERPDTV-GMPSANVDVKVKNPNKEG-----HGELMIKGANVMNGYLYPTDLTDTFENGYFNTGDIAEIDHEGYV 389
Cdd:PRK13295 356 KLDDPDERASTTdGCPLPGVEVRVVDADGAPlpagqIGRLQVRGCSNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYI 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 390 MIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQ------VPKlyfvSESDISKAQLIAYL-SQHLA 462
Cdd:PRK13295 436 RISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGEracafvVPR----PGQSLDFEEMVEFLkAQKVA 511
|
330 340
....*....|....*....|....*..
gi 1853634356 463 KYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK13295 512 KQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
161-489 |
1.89e-43 |
|
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: 158.65 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGF-DHDTNWLSVLP--IYHI--SGLSVLL----RAVIEGftvr 231
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLrPDDIHWNIADPgwAKGAwsSFFGPWLlgatVFVYEG---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 232 ivDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHE--PHDLQKILLGGAKLSATMIETAL-QYNLPIYNSFGMTET 308
Cdd:cd05972 157 --PRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSykFSHLRLVVSAGEPLNPEVIEWWRaATGLPIRDGYGQTET 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 ---CSQFLTATPqmlheRPDTVGMPSANVDVKVKN-------PNKEGHGELMIKGANVMNGYL-YPTDLTDTFENGYFNT 377
Cdd:cd05972 235 gltVGNFPDMPV-----KPGSMGRPTPGYDVAIIDddgrelpPGEEGDIAIKLPPPGLFLGYVgDPEKTEASIRGDYYLT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 378 GDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-----SESDISKAQ 452
Cdd:cd05972 310 GDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVltsgyEPSEELAEE 389
|
330 340 350
....*....|....*....|....*....|....*..
gi 1853634356 453 LIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05972 390 LQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
161-489 |
1.02e-42 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 159.45 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLG-FDHDTNWLSV--LPIYHISGLSV--LLRAVIEGFTVRIVDK 235
Cdd:PRK08974 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGpLLHPGKELVVtaLPLYHIFALTVncLLFIELGGQNLLITNP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 236 FNAEQILTMIKNERITHISLVPQTLN-WLMQQGLHEPhDLQKILL---GGA---KLSATMIETALQYNLpiYNSFGMTEt 308
Cdd:PRK08974 286 RDIPGFVKELKKYPFTAITGVNTLFNaLLNNEEFQEL-DFSSLKLsvgGGMavqQAVAERWVKLTGQYL--LEGYGLTE- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 CSQFLTATPQMLHERPDTVGMPSANVDVKVKN------PNKEGhGELMIKGANVMNGYLY-PTDLTDTFENGYFNTGDIA 381
Cdd:PRK08974 362 CSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDddgnevPPGEP-GELWVKGPQVMLGYWQrPEATDEVIKDGWLATGDIA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 382 EIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-SESDISKAQLIAYLSQH 460
Cdd:PRK08974 441 VMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVkKDPSLTEEELITHCRRH 520
|
330 340
....*....|....*....|....*....
gi 1853634356 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK08974 521 LTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-489 |
1.06e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 157.60 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 48 RVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSI----DVQLIFCTLPL--ELRGFQIVSLDDIEFAGT 121
Cdd:cd05922 20 RVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLvadaGGRIVLADAGAadRLRDALPASPDPGTVLDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 122 DitmndlmdntlDIQYDTLNETVVPKDSPsnilntsfnidDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDH 201
Cdd:cd05922 100 D-----------GIRAARASAPAHEVSHE-----------DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 202 DTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQ-ILTMIKNERITHISLVPQTLNWLMQQGLHE---PHdLQKI 277
Cdd:cd05922 158 DDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDaFWEDLREHGATGLAGVPSTYAMLTRLGFDPaklPS-LRYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 278 LLGGAKLSATMIEtALQYNLP---IYNSFGMTETCSQFLTATPQMLHERPDTVGMPSANVDVKVKN------PNKEgHGE 348
Cdd:cd05922 237 TQAGGRLPQETIA-RLRELLPgaqVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDddgtptPPGE-PGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 349 LMIKGANVMNGYL----YPTDLTDTfeNGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDA 424
Cdd:cd05922 315 IVHRGPNVMKGYWndppYRRKEGRG--GGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 425 VCIGHPDDTWGQVpKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05922 393 AAVGLPDPLGEKL-ALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
14-489 |
1.09e-42 |
|
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: 156.92 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 14 HHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLAN-----IEIAmintrlTPNEM 85
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERgvgPGDLVAVLLERSLEMVVAILAVLKAGaayvpLDPS------YPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 86 KNQMrsidvqlifctlplelrgfqivsLDDiefAGTDItmndlmdntldiqydtlnetvvpkdspsnILNTSfniDDIAS 165
Cdd:cd05930 76 LAYI-----------------------LED---SGAKL-----------------------------VLTDP---DDLAY 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 166 IMFTSGTTGPQKAVP---QTFRNHYASAigcKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDK---FNAE 239
Cdd:cd05930 98 VIYTSGSTGKPKGVMvehRGLVNLLLWM---QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEevrKDPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMIKNERITHISLVPQTLNWLMQQGLHE-PHDLQKILLGGAKLSATMIETALQYNLP--IYNSFGMTET--CSQFLT 314
Cdd:cd05930 175 ALADLLAEEGITVLHLTPSLLRLLLQELELAaLPSLRLVLVGGEALPPDLVRRWRELLPGarLVNLYGPTEAtvDATYYR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 315 ATPQMLHERPDTVGMPSANVDVKVKNPN----KEGH-GELMIKGANVMNGYLYPTDLT------DTFENG--YFNTGDIA 381
Cdd:cd05930 255 VPPDDEEDGRVPIGRPIPNTRVYVLDENlrpvPPGVpGELYIGGAGLARGYLNRPELTaerfvpNPFGPGerMYRTGDLV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 382 EIDHEGyVMIYDRRKDLIIS-GGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSES--DISKAQLIAYLS 458
Cdd:cd05930 335 RWLPDG-NLEFLGRIDDQVKiRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLA 413
|
490 500 510
....*....|....*....|....*....|.
gi 1853634356 459 QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05930 414 ERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
17-489 |
1.12e-42 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 159.80 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 17 AITDGQESYTYQNLYCEASLLARRLKAYQQSRvglyidNSIQSIIL--IHACWLANIEIAM-------INTRLTPNEMKN 87
Cdd:PLN03102 32 SIIYGKTRFTWPQTYDRCCRLAASLISLNITK------NDVVSVLApnTPAMYEMHFAVPMagavlnpINTRLDATSIAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 88 QMRSIDVQLIFCTL---PLELRGFQIVSLDDIEFAGTDITMNDLmDNTLDIQYDTLN-ETVVPKDSPSNILNTSF----N 159
Cdd:PLN03102 106 ILRHAKPKILFVDRsfePLAREVLHLLSSEDSNLNLPVIFIHEI-DFPKRPSSEELDyECLIQRGEPTPSLVARMfriqD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 160 IDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCkeSLGFDHDTN--WLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFN 237
Cdd:PLN03102 185 EHDPISLNYTSGTTADPKGVVISHRGAYLSTLSA--IIGWEMGTCpvYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLVPQTLNWLMQ-QGLHEPHDLQ--KILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFL- 313
Cdd:PLN03102 263 APEIYKNIEMHNVTHMCCVPTVFNILLKgNSLDLSPRSGpvHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLf 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 314 ----------TATPQM-LHERPDTVGMPSANVDVKVKNPNK------EGHGELMIKGANVMNGYLY-PTDLTDTFENGYF 375
Cdd:PLN03102 343 cewqdewnrlPENQQMeLKARQGVSILGLADVDVKNKETQEsvprdgKTMGEIVIKGSSIMKGYLKnPKATSEAFKHGWL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 376 NTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV---SESDI---- 448
Cdd:PLN03102 423 NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVlekGETTKedrv 502
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1853634356 449 -----SKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PLN03102 503 dklvtRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
161-489 |
1.12e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 159.16 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTN---WLSVLPIYHISGLSV--LLRAVIEGFTVRIVdk 235
Cdd:PRK05677 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGceiLIAPLPLYHIYAFTFhcMAMMLIGNHNILIS-- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 236 fNAEQILTMIKNERITHIS-LVpqTLNWLMQqGLHEPHDLQKILLGGAKLSAT--MietALQY----------NLPIYNS 302
Cdd:PRK05677 285 -NPRDLPAMVKELGKWKFSgFV--GLNTLFV-ALCNNEAFRKLDFSALKLTLSggM---ALQLataerwkevtGCAICEG 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 303 FGMTETcSQFLTATPqMLHERPDTVGMPSANVDVKVKNPNKE----GH-GELMIKGANVMNGYLYPTDLTDTF--ENGYF 375
Cdd:PRK05677 358 YGMTET-SPVVSVNP-SQAIQVGTIGIPVPSTLCKVIDDDGNelplGEvGELCVKGPQVMKGYWQRPEATDEIldSDGWL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 376 NTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESD--ISKAQL 453
Cdd:PRK05677 436 KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGetLTKEQV 515
|
330 340 350
....*....|....*....|....*....|....*.
gi 1853634356 454 IAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK05677 516 MEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
34-491 |
1.37e-42 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 159.24 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 34 ASLLARRLKAYQQSRVGLYIDNSIQ-SIILIHACWLANIEIAMiNTRLTPNEMKNQMRSIDVQLIFCTL----PLELRGF 108
Cdd:PLN02574 80 AAGLYHVMGVRQGDVVLLLLPNSVYfPVIFLAVLSLGGIVTTM-NPSSSLGEIKKRVVDCSVGLAFTSPenveKLSPLGV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 109 QIVSL-DDIEFagtditmndlmdNTLDIQYDTLNETVvpKDSPSNILNTSFNIDDIASIMFTSGTTGPQKAVPQTFRNHY 187
Cdd:PLN02574 159 PVIGVpENYDF------------DSKRIEFPKFYELI--KEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 188 AS-------------AIGCkeslgfdhDTNWLSVLPIYHISGLSVLLRAVIE-GFTVRIVDKFNAEQILTMIKNERITHI 253
Cdd:PLN02574 225 AMvelfvrfeasqyeYPGS--------DNVYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRFDASDMVKVIDRFKVTHF 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 254 SLVPQTLNWLMQQ----GLHEPHDLQKILLGGAKLSATMIETALQyNLP---IYNSFGMTETCSQFLTATPQMLHERPDT 326
Cdd:PLN02574 297 PVVPPILMALTKKakgvCGEVLKSLKQVSCGAAPLSGKFIQDFVQ-TLPhvdFIQGYGMTESTAVGTRGFNTEKLSKYSS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 327 VGMPSANVDVKVKN--------PNkeGHGELMIKGANVMNGYLYPTDLTDT--FENGYFNTGDIAEIDHEGYVMIYDRRK 396
Cdd:PLN02574 376 VGLLAPNMQAKVVDwstgcllpPG--NCGELWIQGPGVMKGYLNNPKATQStiDKDGWLRTGDIAYFDEDGYLYIVDRLK 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 397 DLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKHFEKVD 474
Cdd:PLN02574 454 EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVrrQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQ 533
|
490
....*....|....*..
gi 1853634356 475 TLPYTSTGKLQRNKLYR 491
Cdd:PLN02574 534 SIPKSPAGKILRRELKR 550
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
24-485 |
5.50e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 157.04 E-value: 5.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 24 SYTYQNLYCEAsllaRRLKAYQQS--------RVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQ 95
Cdd:PRK08314 35 AISYRELLEEA----ERLAGYLQQecgvrkgdRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 96 LIFCTLPLELRGFQIVSLDDIE------FAGT-----DITMNDLMDNTLDIQ----------YDTLNETVVPKdsPSNIl 154
Cdd:PRK08314 111 VAIVGSELAPKVAPAVGNLRLRhvivaqYSDYlpaepEIAVPAWLRAEPPLQalapggvvawKEALAAGLAPP--PHTA- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 155 ntsfNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIV 233
Cdd:PRK08314 188 ----GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMvHSMNAPIYAGATVVLM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 234 DKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILL---GGAKLSATMIETAL-QYNLPIYNSFGMTETC 309
Cdd:PRK08314 264 PRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYiggGGAAMPEAVAERLKeLTGLDYVEGYGLTETM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 310 SQFLTATPQmlHERPDTVGMPSANVDVKVKNP--------NKEGhgELMIKGANVMNGYLYPTDLT-DTF-E-NG--YFN 376
Cdd:PRK08314 344 AQTHSNPPD--RPKLQCLGIPTFGVDARVIDPetleelppGEVG--EIVVHGPQVFKGYWNRPEATaEAFiEiDGkrFFR 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 377 TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV----SESDISKAQ 452
Cdd:PRK08314 420 TGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVlrpeARGKTTEEE 499
|
490 500 510
....*....|....*....|....*....|...
gi 1853634356 453 LIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQ 485
Cdd:PRK08314 500 IIAWAREHMAAYKYPRIVEFVDSLPKSGSGKIL 532
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
161-489 |
3.30e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 154.27 E-value: 3.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVI-EGFTVRIVDKFNAE 239
Cdd:PRK06145 149 TDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLwVGGTLRIHREFDPE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKI---LLGGAKLSATMIE--TALQYNLPIYNSFGMTETCS--QF 312
Cdd:PRK06145 229 AVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLawcIGGGEKTPESRIRdfTRVFTRARYIDAYGLTETCSgdTL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 313 LTATPQMlhERPDTVGMPSANVDVKVKN-------PNKEGhgELMIKGANVMNGYLY-PTDLTDTFENGYFNTGDIAEID 384
Cdd:PRK06145 309 MEAGREI--EKIGSTGRALAHVEIRIADgagrwlpPNMKG--EICMRGPKVTKGYWKdPEKTAEAFYGDWFRSGDVGYLD 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 385 HEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLA 462
Cdd:PRK06145 385 EEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVlnPGATLTLEALDRHCRQRLA 464
|
330 340
....*....|....*....|....*..
gi 1853634356 463 KYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06145 465 SFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
25-486 |
3.35e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 155.32 E-value: 3.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 25 YTYQNLYCEASLLARRLKA--YQQ-SRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFCT- 100
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLAlgVQPgDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 101 ------------------------------LPlELRGfqIVSLDDIEFAGtditmndlMDNTLDIQydTLNETVVPKDSp 150
Cdd:PRK12583 126 afktsdyhamlqellpglaegqpgalacerLP-ELRG--VVSLAPAPPPG--------FLAWHELQ--ARGETVSREAL- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 151 sNILNTSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGF-DHDTNWLSVlPIYHISG--LSVLLRAVIEG 227
Cdd:PRK12583 192 -AERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLtEHDRLCVPV-PLYHCFGmvLANLGCMTVGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 228 FTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQK----ILLGGAKLSATMIETALQYNLP-IYNS 302
Cdd:PRK12583 270 CLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSlrtgIMAGAPCPIEVMRRVMDEMHMAeVQIA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 303 FGMTETCS-QFLTATPQMLHERPDTVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYLYPTDLT--DTFENGY 374
Cdd:PRK12583 350 YGMTETSPvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGAtvprgEIGELCTRGYSVMKGYWNNPEATaeSIDEDGW 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 375 FNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESD--ISKAQ 452
Cdd:PRK12583 430 MHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGhaASEEE 509
|
490 500 510
....*....|....*....|....*....|....
gi 1853634356 453 LIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK12583 510 LREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
31-489 |
1.32e-40 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 153.64 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 31 YCEASLLARRLKAYQQS-------RVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFCtlpl 103
Cdd:PRK07059 51 YGELDELSRALAAWLQSrglakgaRVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVV---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 104 eLRGF-----QIVslddiefAGTDI------TMNDLmdntLDIQYDTLNETV--VPKDSPSNIL--NTSFNI-------- 160
Cdd:PRK07059 127 -LENFattvqQVL-------AKTAVkhvvvaSMGDL----LGFKGHIVNFVVrrVKKMVPAWSLpgHVRFNDalaegarq 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 ---------DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDT-------NWLSVLPIYHISGLSV--LLR 222
Cdd:PRK07059 195 tfkpvklgpDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKkprpdqlNFVCALPLYHIFALTVcgLLG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 223 AVIEGFTVRIVdkfNAEQILTMIKNERITHISLVPqTLNWLMQQGLHEPH----DLQKILL---GGAKLSATMIETALQY 295
Cdd:PRK07059 275 MRTGGRNILIP---NPRDIPGFIKELKKYQVHIFP-AVNTLYNALLNNPDfdklDFSKLIVangGGMAVQRPVAERWLEM 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 296 N-LPIYNSFGMTETcSQFLTATPQMLHERPDTVGMPSANVDVKVKN------PNKEGhGELMIKGANVMNGYLYPTDLTD 368
Cdd:PRK07059 351 TgCPITEGYGLSET-SPVATCNPVDATEFSGTIGLPLPSTEVSIRDddgndlPLGEP-GEICIRGPQVMAGYWNRPDETA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 369 --TFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-SE 445
Cdd:PRK07059 429 kvMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVkKD 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1853634356 446 SDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07059 509 PALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
156-489 |
2.39e-40 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 152.67 E-value: 2.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 156 TSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYAS---AIGCKESLGFDHDTNW-------LSVLPIYHISGLSV--LLRA 223
Cdd:PRK12492 202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqVRACLSQLGPDGQPLMkegqevmIAPLPLYHIYAFTAncMCMM 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 224 VIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILL----GGAKLSATMIETALQYNLPI 299
Cdd:PRK12492 282 VSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLtnsgGTALVKATAERWEQLTGCTI 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 300 YNSFGMTETcSQFLTATPQMLHERPDTVGMPSANVDVKVKN------PNKEgHGELMIKGANVMNGYLYPTDLTDTF--E 371
Cdd:PRK12492 362 VEGYGLTET-SPVASTNPYGELARLGTVGIPVPGTALKVIDddgnelPLGE-RGELCIKGPQVMKGYWQQPEATAEAldA 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 372 NGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-SESDISK 450
Cdd:PRK12492 440 EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVaRDPGLSV 519
|
330 340 350
....*....|....*....|....*....|....*....
gi 1853634356 451 AQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK12492 520 EELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
39-489 |
2.47e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 152.88 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 39 RRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFCTLPLELRGFQIVSLDDIEF 118
Cdd:PRK06710 67 QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 119 AGTdITMNDLMDNTLDIQYDTLNE---TVVPKDSPSNIL----------NTSFNI-----DDIASIMFTSGTTGPQKAVP 180
Cdd:PRK06710 147 VIV-TRIADFLPFPKNLLYPFVQKkqsNLVVKVSESETIhlwnsvekevNTGVEVpcdpeNDLALLQYTGGTTGFPKGVM 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 181 QTFRNHYASAI-------GCKESlgfdhDTNWLSVLPIYHISGLSVLLR-AVIEGFTVRIVDKFNAEQILTMIKNERITH 252
Cdd:PRK06710 226 LTHKNLVSNTLmgvqwlyNCKEG-----EEVVLGVLPFFHVYGMTAVMNlSIMQGYKMVLIPKFDMKMVFEAIKKHKVTL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 253 ISLVPQTLNWLMQQGLHEPHDLQKI---LLGGAKLSATMIETALQYNL-PIYNSFGMTEtcSQFLTATPQMLHER-PDTV 327
Cdd:PRK06710 301 FPGAPTIYIALLNSPLLKEYDISSIracISGSAPLPVEVQEKFETVTGgKLVEGYGLTE--SSPVTHSNFLWEKRvPGSI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 328 GMPSANVDVKVKNPN-----KEGH-GELMIKGANVMNGYL-YPTDLTDTFENGYFNTGDIAEIDHEGYVMIYDRRKDLII 400
Cdd:PRK06710 379 GVPWPDTEAMIMSLEtgealPPGEiGEIVVKGPQIMKGYWnKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIV 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 401 SGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPY 478
Cdd:PRK06710 459 ASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGteCSEEELNQFARKYLAAYKVPKVYEFRDELPK 538
|
490
....*....|.
gi 1853634356 479 TSTGKLQRNKL 489
Cdd:PRK06710 539 TTVGKILRRVL 549
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
7-489 |
3.67e-40 |
|
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: 150.94 E-value: 3.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 7 KQAQQNGHHIAITDGQESYTYQNLYCEASLLAR--RLKAYQQSR-VGLYIDNSIQSIILIHACWLAN-----IEIAMINT 78
Cdd:cd17655 5 EQAEKTPDHTAVVFEDQTLTYRELNERANQLARtlREKGVGPDTiVGIMAERSLEMIVGILGILKAGgaylpIDPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 79 RltpnemknqmrsidVQLIfctlplelrgfqivsLDDiefAGTDI--TMNDLMDNTLDIQY-DTLNETVVPKDSPSNILN 155
Cdd:cd17655 85 R--------------IQYI---------------LED---SGADIllTQSHLQPPIAFIGLiDLLDEDTIYHEESENLEP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 156 TSfNIDDIASIMFTSGTTGPQKAVPQTFRN--HYASA------------IGCKESLGFDhdtnwLSVLPIYHisglSVLL 221
Cdd:cd17655 133 VS-KSDDLAYVIYTSGSTGKPKGVMIEHRGvvNLVEWankviyqgehlrVALFASISFD-----ASVTEIFA----SLLS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 222 RAVIegFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILLGGAKLSATMIET---ALQYNLP 298
Cdd:cd17655 203 GNTL--YIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKiieLFGTNPT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 299 IYNSFGMTETCsqfLTATPQMLHERPDT-----VGMPSANVDVKV----KNPNKEG-HGELMIKGANVMNGYLYPTDLT- 367
Cdd:cd17655 281 ITNAYGPTETT---VDASIYQYEPETDQqvsvpIGKPLGNTRIYIldqyGRPQPVGvAGELYIGGEGVARGYLNRPELTa 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 -----DTFENG--YFNTGDIAE------------IDHEgyVMIYDRRKDLiisgGEniypyqIETVAKQFPGISDAVCIG 428
Cdd:cd17655 358 ekfvdDPFVPGerMYRTGDLARwlpdgnieflgrIDHQ--VKIRGYRIEL----GE------IEARLLQHPDIKEAVVIA 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1853634356 429 HPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17655 426 RKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
24-489 |
4.45e-39 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 148.68 E-value: 4.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 24 SYTYQNLYCE---ASLLARRLKAYQQSRVGLYIDNSIQSIIlihaCW--LANIEIAM--INTRLTPNEMKNQMRSIDVQL 96
Cdd:PRK08008 37 RYSYLELNEEinrTANLFYSLGIRKGDKVALHLDNCPEFIF----CWfgLAKIGAIMvpINARLLREESAWILQNSQASL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 97 IFCT---LPL--ELRGFQIVSLDDIEFAGT-----DITMNdlMDNTLDIQYDTLNETVVpkdspsniLNTsfniDDIASI 166
Cdd:PRK08008 113 LVTSaqfYPMyrQIQQEDATPLRHICLTRValpadDGVSS--FTQLKAQQPATLCYAPP--------LST----DDTAEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 167 MFTSGTTGPQKAVPQT-----FRNHYASAIGCkeslgFDHDTNWLSVLPIYHIS-GLSVLLRAVIEGFTVRIVDKFNAEQ 240
Cdd:PRK08008 179 LFTSGTTSRPKGVVIThynlrFAGYYSAWQCA-----LRDDDVYLTVMPAFHIDcQCTAAMAAFSAGATFVLLEKYSARA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 241 ILTMIKNERITHISLVPQTLNWLMQQGLHE---PHDLQKILLGgAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTAT 316
Cdd:PRK08008 254 FWGQVCKYRATITECIPMMIRTLMVQPPSAndrQHCLREVMFY-LNLSDQEKDAFEErFGVRLLTSYGMTETIVGIIGDR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 317 PQMLHERPdTVGMPSANVDVKVKNpnKEGH-------GELMIKGA---NVMNGYLYPTDLT-DTFE-NGYFNTGDIAEID 384
Cdd:PRK08008 333 PGDKRRWP-SIGRPGFCYEAEIRD--DHNRplpageiGEICIKGVpgkTIFKEYYLDPKATaKVLEaDGWLHTGDTGYVD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 385 HEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLY--FVSESDISKAQLIAYLSQHLA 462
Cdd:PRK08008 410 EEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFvvLNEGETLSEEEFFAFCEQNMA 489
|
490 500
....*....|....*....|....*..
gi 1853634356 463 KYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK08008 490 KFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
166-489 |
6.94e-39 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 148.37 E-value: 6.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 166 IMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQILTMI 245
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVTRRRFDPEATLDLI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 246 KNERITHISLVPQTLNWLMQQglhEPHDLQKILLGGAKLSAT---------MIETALQYNLPIYNSFGMTETcSQFLTAT 316
Cdd:PRK13382 281 DRHRATGLAVVPVMFDRIMDL---PAEVRNRYSGRSLRFAAAsgsrmrpdvVIAFMDQFGDVIYNNYNATEA-GMIATAT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 317 PQMLHERPDTVGMPSANVDVKVKNPN----KEGH-GELMIKGANVMNGYLYPTdlTDTFENGYFNTGDIAEIDHEGYVMI 391
Cdd:PRK13382 357 PADLRAAPDTAGRPAEGTEIRILDQDfrevPTGEvGTIFVRNDTQFDGYTSGS--TKDFHDGFMASGDVGYLDENGRLFV 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 392 YDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDISKAQ--LIAYLSQHLAKYKVPKH 469
Cdd:PRK13382 435 VGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPetLKQHVRDNLANYKVPRD 514
|
330 340
....*....|....*....|
gi 1853634356 470 FEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK13382 515 IVVLDELPRGATGKILRREL 534
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
73-489 |
7.90e-39 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 148.42 E-value: 7.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 73 IAMINTrLTPnEMKNQMRSidvQLIFCTLPlELRgfQIVSLDDIEFAGTdITMNDLMDNTLDIQYDTLNEtvvpkdspsn 152
Cdd:PRK08315 131 VAMLYE-LAP-ELATCEPG---QLQSARLP-ELR--RVIFLGDEKHPGM-LNFDELLALGRAVDDAELAA---------- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 153 iLNTSFNIDDIASIMFTSGTTGPQKAVPQTFRN--HYASAIGckESLGF-DHDTNWLSVlPIYHISGLsVL--LRAVIEG 227
Cdd:PRK08315 192 -RQATLDPDDPINIQYTSGTTGFPKGATLTHRNilNNGYFIG--EAMKLtEEDRLCIPV-PLYHCFGM-VLgnLACVTHG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 228 FT-VRIVDKFNAEQILTMIKNERITHISLVPqTLNWLMqqgLHEP----HDLQK----ILLGGAKLSATMIETALQYNLP 298
Cdd:PRK08315 267 ATmVYPGEGFDPLATLAAVEEERCTALYGVP-TMFIAE---LDHPdfarFDLSSlrtgIMAGSPCPIEVMKRVIDKMHMS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 299 -IYNSFGMTETcS----QFLTATPqmLHERPDTVGMPSANVDVKVKNPNKeGH-------GELMIKGANVMNGYlY--PT 364
Cdd:PRK08315 343 eVTIAYGMTET-SpvstQTRTDDP--LEKRVTTVGRALPHLEVKIVDPET-GEtvprgeqGELCTRGYSVMKGY-WndPE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 365 DLTDTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQ------V 437
Cdd:PRK08315 418 KTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEevcawiI 497
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1853634356 438 PKlyfvSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK08315 498 LR----PGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKM 545
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
164-489 |
1.07e-38 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 147.54 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 164 ASIMFTSGTTGPQKAV---PQTfRNHYASAIGCKESL-GFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAE 239
Cdd:PRK12406 155 QSMIYTSGTTGHPKGVrraAPT-PEQAAAAEQMRALIyGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDPE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMIKNERITHISLVPQTLNWLMQ--QGLHEPHD---LQKILLGGAKLSA----TMIEtalQYNLPIYNSFGMTETcS 310
Cdd:PRK12406 234 ELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDvssLRHVIHAAAPCPAdvkrAMIE---WWGPVIYEYYGSTES-G 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 311 QFLTATPQMLHERPDTVGMPSANVDVKV----KNPNKEGH-GELMIKGAnVMNGYLY---PTDLTDTFENGYFNTGDIAE 382
Cdd:PRK12406 310 AVTFATSEDALSHPGTVGKAAPGAELRFvdedGRPLPQGEiGEIYSRIA-GNPDFTYhnkPEKRAEIDRGGFITSGDVGY 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 383 IDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVpkLYFVSESD----ISKAQLIAYLS 458
Cdd:PRK12406 389 LDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEA--LMAVVEPQpgatLDEADIRAQLK 466
|
330 340 350
....*....|....*....|....*....|.
gi 1853634356 459 QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK12406 467 ARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
4-489 |
1.24e-38 |
|
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: 146.70 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 4 WLYKQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIE--IAMINT 78
Cdd:cd05920 20 LLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLgirPGDRVVVQLPNVAEFVVLFFALLRLGAVpvLALPSH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 79 RLtpnemknqmrsidvqlifctlpLELRGFqivslddIEFAGTDITMNDlmDNTLDIQYDTLNETVVPKdspsnilntsf 158
Cdd:cd05920 100 RR----------------------SELSAF-------CAHAEAVAYIVP--DRHAGFDHRALARELAES----------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 159 nIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV--LLRAVIEGFTVRIVDKF 236
Cdd:cd05920 138 -IPEVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPDP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 237 NAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILL---GGAKLSATM---IETALqyNLPIYNSFGMTETcs 310
Cdd:cd05920 217 SPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLlqvGGARLSPALarrVPPVL--GCTLQQVFGMAEG-- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 311 qFLTATpqmlheRPD--------TVGMP-SANVDVKV----KNPNKEGH-GELMIKGANVMNGYlY--PTDLTDTF-ENG 373
Cdd:cd05920 293 -LLNYT------RLDdpdeviihTQGRPmSPDDEIRVvdeeGNPVPPGEeGELLTRGPYTIRGY-YraPEHNARAFtPDG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-SESDISKAQ 452
Cdd:cd05920 365 FYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVlRDPPPSAAQ 444
|
490 500 510
....*....|....*....|....*....|....*...
gi 1853634356 453 LIAYLSQH-LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05920 445 LRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
157-489 |
1.91e-38 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 147.21 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 157 SFNIDDIASIMFTSGTTGPQKAVPQTFRNH--YASAIGCKESLGFDHDTNWLSVLPIYH-------ISGLSVLLRAVIEG 227
Cdd:PRK06018 173 TFDENTAAGMCYTSGTTGDPKGVLYSHRSNvlHALMANNGDALGTSAADTMLPVVPLFHanswgiaFSAPSMGTKLVMPG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 228 ftvrivDKFNAEQILTMIKNERITHISLVPQTlnWLM------QQGLHEPHdLQKILLGGAKLSATMIETALQYNLPIYN 301
Cdd:PRK06018 253 ------AKLDGASVYELLDTEKVTFTAGVPTV--WLMllqymeKEGLKLPH-LKMVVCGGSAMPRSMIKAFEDMGVEVRH 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 302 SFGMTETC--SQFLTATPQMLHERPD-------TVGMPSANVDVKVKNP-NKE------GHGELMIKGANVMNGYlYPTD 365
Cdd:PRK06018 324 AWGMTEMSplGTLAALKPPFSKLPGDarldvlqKQGYPPFGVEMKITDDaGKElpwdgkTFGRLKVRGPAVAAAY-YRVD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 366 LTDTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSE 445
Cdd:PRK06018 403 GEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLK 482
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1853634356 446 SD--ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06018 483 PGetATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
148-486 |
4.95e-38 |
|
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: 144.89 E-value: 4.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 148 DSPSNILNTSFNiDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIE 226
Cdd:cd05914 77 HSEAKAIFVSDE-DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFtLLLPLLN 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 227 GFTVRIVDKFNAEQILTMIKNErITHISLVPQ----------------TLNWLMQQGLHEPHDLQK-------------- 276
Cdd:cd05914 156 GAHVVFLDKIPSAKIIALAFAQ-VTPTLGVPVplviekifkmdiipklTLKKFKFKLAKKINNRKIrklafkkvheafgg 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 277 ----ILLGGAKLSATMIETALQYNLPIYNSFGMTEtCSQFLTATPQMlHERPDTVGMPSANVDVKVKNPNKEGH-GELMI 351
Cdd:cd05914 235 nikeFVIGGAKINPDVEEFLRTIGFPYTIGYGMTE-TAPIISYSPPN-RIRLGSAGKVIDGVEVRIDSPDPATGeGEIIV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 352 KGANVMNGYlY--PTDLTDTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISG-GENIYPYQIET--VAKQFPGIS--- 422
Cdd:cd05914 313 RGPNVMKGY-YknPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAkiNNMPFVLESlvv 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1853634356 423 ----DAVCIGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKY----KVPKHFEKvdtLPYTSTGKLQR 486
Cdd:cd05914 392 vqekKLVALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYkkisKVKIVKEE---FEKTPKGKIKR 460
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
160-489 |
6.95e-38 |
|
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: 143.80 E-value: 6.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 160 IDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGF-DHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVD-KFN 237
Cdd:cd05969 88 PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLhPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLVPQTLNWLMQQG--LHEPHDLQK---ILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQ 311
Cdd:cd05969 168 AESWYGIIERVKVTVWYTAPTAIRMLMKEGdeLARKYDLSSlrfIHSVGEPLNPEAIRWGMEvFGVPIHDTWWQTETGSI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 312 FLTATPQMlHERPDTVGMPSANVDVKVKNPNKEG-----HGELMIKGA--NVMNGYLY-PTDLTDTFENGYFNTGDIAEI 383
Cdd:cd05969 248 MIANYPCM-PIKPGSMGKPLPGVKAAVVDENGNElppgtKGILALKPGwpSMFRGIWNdEERYKNSFIDGWYLTGDLAYR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 384 DHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-----SESDISKAQLIAYLS 458
Cdd:cd05969 327 DEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlkegfEPSDELKEEIINFVR 406
|
330 340 350
....*....|....*....|....*....|.
gi 1853634356 459 QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05969 407 QKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
31-489 |
1.13e-37 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 145.40 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 31 YCEASLLARRLKAY--------QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLI----- 97
Cdd:PRK08751 53 YREADQLVEQFAAYllgelqlkKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLvvidn 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 98 FCTlplelrgfqivSLDDIeFAGTDIT------MNDLMDNTldiQYDTLNETV--VPKDSPSNILNTSFNI--------- 160
Cdd:PRK08751 133 FGT-----------TVQQV-IADTPVKqvittgLGDMLGFP---KAALVNFVVkyVKKLVPEYRINGAIRFrealalgrk 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 ----------DDIASIMFTSGTTGPQKAVPQTFRNHYASA------IGCKESLGFDHDTnWLSVLPIYHISGLSV--LLR 222
Cdd:PRK08751 198 hsmptlqiepDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqahqwLAGTGKLEEGCEV-VITALPLYHIFALTAngLVF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 223 AVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQ--KILLGGAKlsATMIETALQYN---- 296
Cdd:PRK08751 277 MKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSslKMTLGGGM--AVQRSVAERWKqvtg 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 297 LPIYNSFGMTETcSQFLTATPQMLHERPDTVGMPSANVDVKVKNPNKEGH-----GELMIKGANVMNGYLYPTDLTDTF- 370
Cdd:PRK08751 355 LTLVEAYGLTET-SPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLaigeiGELCIKGPQVMKGYWKRPEETAKVm 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 371 -ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDIS 449
Cdd:PRK08751 434 dADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPAL 513
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1853634356 450 KAQLI-AYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK08751 514 TAEDVkAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
162-486 |
1.81e-37 |
|
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: 140.47 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGC-KESLGFDHDTNWLSVLPIYHISGLSVLLRAVIE-GFTVRIVDKFNAE 239
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHgGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMIKNERITHISLVPQTLNWL---MQQGLHEPHDLQKILLGGAKLSATMIETALQY-NLPIYNSFGMTETCSQFLTA 315
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLvseLKSANATVPSLRLIGYGGSRAIAADVRFIEATgLTNTAQVYGLSETGTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 316 TPQMLHErPDTVGMPSANVDVKVKNPN-----KEGHGELMIKGANVMNGYLYPTDLT-DTFENGYFNTGDIAEIDHEGYV 389
Cdd:cd17635 162 TDDDSIE-INAVGRPYPGVDVYLAATDgiagpSASFGTIWIKSPANMLGYWNNPERTaEVLIDGWVNTGDLGERREDGFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 390 MIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQ-LIAYLSQHLAKYKV 466
Cdd:cd17635 241 FITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVasAELDENAIRaLKHTIRRELEPYAR 320
|
330 340
....*....|....*....|
gi 1853634356 467 PKHFEKVDTLPYTSTGKLQR 486
Cdd:cd17635 321 PSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
161-491 |
5.38e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 139.41 E-value: 5.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGfdHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVD---KFN 237
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG--GPGQWLLALPAHHIAGLQVLVRSVIAGSEPVELDvsaGFD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMI---KNERiTHISLVPQTLNWLMQ--QGLHEPHDLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSqf 312
Cdd:PRK07824 113 PTALPRAVaelGGGR-RYTSLVPMQLAKALDdpAATAALAELDAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSG-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 313 ltatpqmlherpDTV--GMPSANVDVKVKNpnkeghGELMIKGANVMNGYLYPTDLTDTFENGYFNTGDIAEIDhEGYVM 390
Cdd:PRK07824 190 ------------GCVydGVPLDGVRVRVED------GRIALGGPTLAKGYRNPVDPDPFAEPGWFRTDDLGALD-DGVLT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 391 IYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQvpKLYFVSESDISKAQLIAYLSQH----LAKYKV 466
Cdd:PRK07824 251 VLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQ--RVVAAVVGDGGPAPTLEALRAHvartLDRTAA 328
|
330 340
....*....|....*....|....*
gi 1853634356 467 PKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK07824 329 PRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
164-489 |
8.73e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 142.54 E-value: 8.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 164 ASIMFTSGTTGPQKAVPQTFRN---H-YASAIgcKESLGFDHDTNWLSVLPIYHIS--GL--SVLL---RAVIEGftvri 232
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRStvlHaYGAAL--PDAMGLSARDAVLPVVPMFHVNawGLpySAPLtgaKLVLPG----- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 233 vDKFNAEQILTMIKNERITHISLVP----QTLNWLMQQGLhEPHDLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTE 307
Cdd:PRK07008 252 -PDLDGKSLYELIEAERVTFSAGVPtvwlGLLNHMREAGL-RFSTLRRTVIGGSACPPAMIRTFEDeYGVEVIHAWGMTE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 308 TCSQFLTATPQMLH-ERPDTV--------GMPSANVDVKVKNPN-KE------GHGELMIKGANVMNGYlYPTDlTDTFE 371
Cdd:PRK07008 330 MSPLGTLCKLKWKHsQLPLDEqrkllekqGRVIYGVDMKIVGDDgRElpwdgkAFGDLQVRGPWVIDRY-FRGD-ASPLV 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 372 NGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSE--SDIS 449
Cdd:PRK07008 408 DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRpgAEVT 487
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1853634356 450 KAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK07008 488 REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
146-489 |
1.06e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 142.49 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 146 PKDSPSNILNTSFNIDDIASIMFTSGTTGPQKAVPQTFRNH-YASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRA 223
Cdd:PRK06178 194 LRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMvYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFgLLFP 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 224 VIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQ-GLHEpHDLQKILLGGA-----KLS------------ 285
Cdd:PRK06178 274 LFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHpRFAE-YDLSSLRQVRVvsfvkKLNpdyrqrwraltg 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 286 ATMIETAlqynlpiynsFGMTET--CSQFlTATPQM----LHERPDTVGMPSANVDVKVKN-------PNKEgHGELMIK 352
Cdd:PRK06178 353 SVLAEAA----------WGMTEThtCDTF-TAGFQDddfdLLSQPVFVGLPVPGTEFKICDfetgellPLGA-EGEIVVR 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 353 GANVMNGYLYPTDLT-DTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPD 431
Cdd:PRK06178 421 TPSLLKGYWNKPEATaEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPD 500
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1853634356 432 DTWGQVPkLYFVS---ESDISKAQLIAYLSQHLAKYKVPKhFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06178 501 PDKGQVP-VAFVQlkpGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
161-489 |
4.15e-36 |
|
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: 138.75 E-value: 4.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASA-IGCKESLGFDHDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDKF-N 237
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdAMAREALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWpT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILL---GGAKLSATMIETALQYNL-PIYNSFGMTETCSQFL 313
Cdd:cd05919 171 AERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLcvsAGEALPRGLGERWMEHFGgPILDGIGATEVGHIFL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 314 TATPQMLheRPDTVGMPSANVDVKVKNPnkEGH-------GELMIKGANVMNGYLYPTDLTD-TFENGYFNTGDIAEIDH 385
Cdd:cd05919 251 SNRPGAW--RLGSTGRPVPGYEIRLVDE--EGHtippgeeGDLLVRGPSAAVGYWNNPEKSRaTFNGGWYRTGDKFCRDA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 386 EGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKA---QLIAYLSQH 460
Cdd:cd05919 327 DGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVlkSPAAPQESlarDIHRHLLER 406
|
330 340
....*....|....*....|....*....
gi 1853634356 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05919 407 LSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
5-484 |
6.65e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 139.79 E-value: 6.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 5 LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLT 81
Cdd:PRK07470 13 LRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARgvrKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 82 PNEMKNQMRSIDVQLIFC--TLPLELRGFQIVSLDD---IEFAGTDITmndlmdntLDIqydtlnETVVPKDSPSNILNT 156
Cdd:PRK07470 93 PDEVAYLAEASGARAMIChaDFPEHAAAVRAASPDLthvVAIGGARAG--------LDY------EALVARHLGARVANA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 157 SFNIDDIASIMFTSGTTGPQKAVPQT-------FRNHYASAIGckeslGFDHDTNWLSVLPIYHISGLSVLLRaVIEGFT 229
Cdd:PRK07470 159 AVDHDDPCWFFFTSGTTGRPKAAVLThgqmafvITNHLADLMP-----GTTEQDASLVVAPLSHGAGIHQLCQ-VARGAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 230 VRIV--DKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHD---LQKILLGGAKLSATMIETAL--------QYn 296
Cdd:PRK07470 233 TVLLpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDhssLRYVIYAGAPMYRADQKRALaklgkvlvQY- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 297 lpiynsFGMTEtCSQFLTATPQMLHERPD-------TVGMPSANVDVKVK----NPNKEGH-GELMIKGANVMNGYL-YP 363
Cdd:PRK07470 312 ------FGLGE-VTGNITVLPPALHDAEDgpdarigTCGFERTGMEVQIQddegRELPPGEtGEICVIGPAVFAGYYnNP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 364 TDLTDTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV 443
Cdd:PRK07470 385 EANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCV 464
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1853634356 444 SE--SDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKL 484
Cdd:PRK07470 465 ARdgAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
161-489 |
7.99e-36 |
|
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: 137.95 E-value: 7.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFR---NHYASAIGCKESLGFDHDTNWLSVLPIYhISGL-SVLLRAVIEGFTV--RIVD 234
Cdd:cd05971 88 DDPALIIYTSGTTGPPKGALHAHRvllGHLPGVQFPFNLFPRDGDLYWTPADWAW-IGGLlDVLLPSLYFGVPVlaHRMT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 235 KFNAEQILTMIKNERITHISLVPQTLNWLMQQG---LHEPHDLQKILLGGAKLSATMIETAL-QYNLPIYNSFGMTEtCS 310
Cdd:cd05971 167 KFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGeqlKHAQVKLRAIATGGESLGEELLGWAReQFGVEVNEFYGQTE-CN 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 311 QFLTATPQMLHERPDTVGMPSANVDVKVKN-------PNKEGHGELMIKGANVMNGYLY-PTDLTDTFENGYFNTGDIAE 382
Cdd:cd05971 246 LVIGNCSALFPIKPGSMGKPIPGHRVAIVDdngtplpPGEVGEIAVELPDPVAFLGYWNnPSATEKKMAGDWLLTGDLGR 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 383 IDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-----SESDISKAQLIAYL 457
Cdd:cd05971 326 KDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpgeTPSDALAREIQELV 405
|
330 340 350
....*....|....*....|....*....|..
gi 1853634356 458 SQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05971 406 KTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
166-489 |
3.37e-35 |
|
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: 137.12 E-value: 3.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 166 IMFTSGTTGPQKAVPQTF---RNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQIL 242
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLpggPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 243 TMIKNERITHISLVPQTLNWLMQQGLHEPH-----DLQKILLGGAKLSATMIETALQYNLP-IYNSFGMTEtCSQFLTAT 316
Cdd:cd05929 210 RLIERYRVTFAQFVPTMFVRLLKLPEAVRNaydlsSLKRVIHAAAPCPPWVKEQWIDWGGPiIWEYYGGTE-GQGLTIIN 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 317 PQMLHERPDTVGMPSANvDVKVKN-------PNKEGhgELMIKGANvmnGYLYPTDLTDT----FENGYFNTGDIAEIDH 385
Cdd:cd05929 289 GEEWLTHPGSVGRAVLG-KVHILDedgnevpPGEIG--EVYFANGP---GFEYTNDPEKTaaarNEGGWSTLGDVGYLDE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 386 EGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYF-----VSESDISKAQLIAYLSQH 460
Cdd:cd05929 363 DGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapgADAGTALAEELIAFLRDR 442
|
330 340
....*....|....*....|....*....
gi 1853634356 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05929 443 LSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
14-489 |
3.42e-35 |
|
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: 137.80 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 14 HHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMIN---TRLTPNEMKN 87
Cdd:cd05906 29 TYIDADGSEEFQSYQDLLEDARRLAAGLRQLglrPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvppTYDEPNARLR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 88 QMRSIDVQLifcTLPLELRGFQIVSldDIEFAGTDITMNDLMDNTLDIQYDTLNETVVPKDSPsnilntsfniDDIASIM 167
Cdd:cd05906 109 KLRHIWQLL---GSPVVLTDAELVA--EFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRP----------DDLALLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 168 FTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVL-LRAVIEGftvrivdkfnAEQI----- 241
Cdd:cd05906 174 LTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLG----------CQQVhvpte 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 242 ---------LTMIKNERIThISLVPQTLNWLMQQGLHEPHD-------LQKILLGGAKLSATMIETALQ----YNLP--- 298
Cdd:cd05906 244 eiladplrwLDLIDRYRVT-ITWAPNFAFALLNDLLEEIEDgtwdlssLRYLVNAGEAVVAKTIRRLLRllepYGLPpda 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 299 IYNSFGMTETCS------QFLTATPQMLHERPDtVGMPSANVDVKVKNPNKEGH-----GELMIKGANVMNGYLYPTDLT 367
Cdd:cd05906 323 IRPAFGMTETCSgviysrSFPTYDHSQALEFVS-LGRPIPGVSMRIVDDEGQLLpegevGRLQVRGPVVTKGYYNNPEAN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 -DTF-ENGYFNTGDIAEIDHeGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGI---SDAVCIGHPDDTWGQVPKLYF 442
Cdd:cd05906 402 aEAFtEDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsFTAAFAVRDPGAETEELAIFF 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1853634356 443 VSESDISKA--QLIAYLSQHLAK-------YKVPkhFEKvDTLPYTSTGKLQRNKL 489
Cdd:cd05906 481 VPEYDLQDAlsETLRAIRSVVSRevgvspaYLIP--LPK-EEIPKTSLGKIQRSKL 533
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
17-489 |
1.92e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 135.51 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 17 AITDGQESYTYQNLYCEASLLARRLK----AYQQSrVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSI 92
Cdd:PRK13383 53 AIIDDDGALSYRELQRATESLARRLTrdgvAPGRA-VGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 93 DVQLIFCtlplelrgfqivsldDIEF----AGTDitmndlmDNTLDIQYDTL---NETVVPKDSPSNILntsfniddias 165
Cdd:PRK13383 132 HISTVVA---------------DNEFaeriAGAD-------DAVAVIDPATAgaeESGGRPAVAAPGRI----------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 166 IMFTSGTTGPQKAVPQtfRNHYASAIGCKESLgfdHDTNWLSV-------LPIYHISGLSVLLRAVIEGFTVRIVDKFNA 238
Cdd:PRK13383 179 VLLTSGTTGKPKGVPR--APQLRSAVGVWVTI---LDRTRLRTgsrisvaMPMFHGLGLGMLMLTIALGGTVLTHRHFDA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 EQILTMIKNERITHISLVPQTLNWLMQ-----QGLHEPHDLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQF 312
Cdd:PRK13383 254 EAALAQASLHRADAFTAVPVVLARILElpprvRARNPLPQLRVVMSSGDRLDPTLGQRFMDtYGDILYNGYGSTEVGIGA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 313 LtATPQMLHERPDTVGMPSANVDVKVKNPNKEGHGElMIKGANVMNGYLYPTDLTD----TFENGYFNTGDIAEIDHEGY 388
Cdd:PRK13383 334 L-ATPADLRDAPETVGKPVAGCPVRILDRNNRPVGP-RVTGRIFVGGELAGTRYTDgggkAVVDGMTSTGDMGYLDNAGR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 389 VMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSE--SDISKAQLIAYLSQHLAKYKV 466
Cdd:PRK13383 412 LFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHpgSGVDAAQLRDYLKDRVSRFEQ 491
|
490 500
....*....|....*....|...
gi 1853634356 467 PKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK13383 492 PRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
161-486 |
2.26e-34 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 135.40 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYAS--AIGCKESLGfDHDTNwLSVLPIYHISGL-SVLLRAVIEGFTVRIV--DK 235
Cdd:PRK05852 176 PDDAMIMFTGGTTGLPKMVPWTHANIASSvrAIITGYRLS-PRDAT-VAVMPLYHGHGLiAALLATLASGGAVLLParGR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 236 FNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEP-----HDLQKILLGGAKLSAtmiETAL----QYNLPIYNSFGMT 306
Cdd:PRK05852 254 FSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPsgrkpAALRFIRSCSAPLTA---ETAQalqtEFAAPVVCAFGMT 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 307 ETCSQFLTATPQMLHERPD---TVGM--PSANVDVKVKNPnkEGH-------GELMIKGANVMNGYLY-PTDLTDTFENG 373
Cdd:PRK05852 331 EATHQVTTTQIEGIGQTENpvvSTGLvgRSTGAQIRIVGS--DGLplpagavGEVWLRGTTVVRGYLGdPTITAANFTDG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDI--SKA 451
Cdd:PRK05852 409 WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAppTAE 488
|
330 340 350
....*....|....*....|....*....|....*
gi 1853634356 452 QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK05852 489 ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
161-489 |
2.82e-34 |
|
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: 133.76 E-value: 2.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIG-CKESLGFDHDTNWLSVLPIYHISGLS-VLLRAVIEGFTVRIVDKFNA 238
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRyAVNVLRLREDDRFVGSPPLAFTFGLGgVLLFPFGVGASGVLLEEATP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 EQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILLGGAKLSATMIETALQYN----LPIYNSFGMTETCSQFLT 314
Cdd:cd05958 177 DLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKeatgIPIIDGIGSTEMFHIFIS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 315 ATPQmlHERPDTVGMPSANVDVKV----KNPNKEGH-GELMIKGANvmnGYLYPTDLT--DTFENGYFNTGDIAEIDHEG 387
Cdd:cd05958 257 ARPG--DARPGATGKPVPGYEAKVvddeGNPVPDGTiGRLAVRGPT---GCRYLADKRqrTYVQGGWNITGDTYSRDPDG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 388 YVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESD-ISKAQLIAYLSQH----LA 462
Cdd:cd05958 332 YFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGvIPGPVLARELQDHakahIA 411
|
330 340
....*....|....*....|....*..
gi 1853634356 463 KYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05958 412 PYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
161-489 |
2.00e-33 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 133.05 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIM--FTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYH------------ISGLSVLLRAVie 226
Cdd:PLN02479 193 DEWQSIAlgYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHcngwcftwtlaaLCGTNICLRQV-- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 227 gftvrivdkfNAEQILTMIKNERITHISLVPQTLNWLMQQGLHE-----PHDLQkILLGGAKLSATMIETALQYNLPIYN 301
Cdd:PLN02479 271 ----------TAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSEtilplPRVVH-VMTAGAAPPPSVLFAMSEKGFRVTH 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 302 SFGMTET------CS------QFLTATPQMLHERPDT--VGMPSANV-DVKVKNP---NKEGHGELMIKGANVMNGYLY- 362
Cdd:PLN02479 340 TYGLSETygpstvCAwkpewdSLPPEEQARLNARQGVryIGLEGLDVvDTKTMKPvpaDGKTMGEIVMRGNMVMKGYLKn 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 363 PTDLTDTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYF 442
Cdd:PLN02479 420 PKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFV 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1853634356 443 VSESDISK-------AQLIAYLSQHLAKYKVPKHFeKVDTLPYTSTGKLQRNKL 489
Cdd:PLN02479 500 TLKPGVDKsdeaalaEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVL 552
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
15-489 |
1.33e-32 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 129.72 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 15 HIAITDGQESYTYQNLyCEASL-LARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMR 90
Cdd:cd12116 3 ATAVRDDDRSLSYAEL-DERANrLAARLRARgvgPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 91 SIDVQLIFCTLPLELRGFQI--VSLDDIEFAGtditmndlmdntldIQYDTLNETVVPkdspsnilntsfniDDIASIMF 168
Cdd:cd12116 82 DAEPALVLTDDALPDRLPAGlpVLLLALAAAA--------------AAPAAPRTPVSP--------------DDLAYVIY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 169 TSGTTGPQKAVPQTFRN--HYASAIGckESLGFDHDTNWLSVLPI-YHISGLSVLLrAVIEGFTVRIVDK---FNAEQIL 242
Cdd:cd12116 134 TSGSTGRPKGVVVSHRNlvNFLHSMR--ERLGLGPGDRLLAVTTYaFDISLLELLL-PLLAGARVVIAPRetqRDPEALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 243 TMIKNERITHISLVPQTLNWLMQQGLHEPHDLqKILLGGAKLSATMIETALQYNLPIYNSFGMTET----CSQFLTATpq 318
Cdd:cd12116 211 RLIEAHSITVMQATPATWRMLLDAGWQGRAGL-TALCGGEALPPDLAARLLSRVGSLWNLYGPTETtiwsTAARVTAA-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 319 mlhERPDTVGMPSANVDVKV----KNPNKEGH-GELMIKGANVMNGYLYPTDLTDT-------FENG--YFNTGDIAEID 384
Cdd:cd12116 288 ---AGPIPIGRPLANTQVYVldaaLRPVPPGVpGELYIGGDGVAQGYLGRPALTAErfvpdpfAGPGsrLYRTGDLVRRR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 385 HEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDdtwGQVPKL--YFVSESD--ISKAQLIAYLSQH 460
Cdd:cd12116 365 ADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED---GGDRRLvaYVVLKAGaaPDAAALRAHLRAT 441
|
490 500
....*....|....*....|....*....
gi 1853634356 461 LAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd12116 442 LPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
162-489 |
1.45e-32 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 130.48 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDH--DTNWLSVLPIYHISGLSVLLRAVIEGF-TVRIVDKFNA 238
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMigQVVTLGLIPFFHIYGITGICCATLRNKgKVVVMSRFEL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 EQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQK-----ILLGGAKLSATMIeTALQYNLP---IYNSFGMTE-TC 309
Cdd:PLN02330 265 RTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKlklqaIMTAAAPLAPELL-TAFEAKFPgvqVQEAYGLTEhSC 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 310 SQFLTATPQMLH--ERPDTVGMPSANVDVKVKNPN------KEGHGELMIKGANVMNGYLYPTDLTDTF--ENGYFNTGD 379
Cdd:PLN02330 344 ITLTHGDPEKGHgiAKKNSVGFILPNLEVKFIDPDtgrslpKNTPGELCVRSQCVMQGYYNNKEETDRTidEDGWLHTGD 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 380 IAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYL 457
Cdd:PLN02330 424 IGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVinPKAKESEEDILNFV 503
|
330 340 350
....*....|....*....|....*....|..
gi 1853634356 458 SQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PLN02330 504 AANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
13-489 |
5.17e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 128.27 E-value: 5.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 13 GHHIAITDGQ---------ESYTYQNLYCEASLLA---RRLKAYQQSRVGLYIDNSIQsiiLIHACWLA---NIEIAMIN 77
Cdd:PRK13391 4 GIHAQTTPDKpavimastgEVVTYRELDERSNRLAhlfRSLGLKRGDHVAIFMENNLR---YLEVCWAAersGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 78 TRLTPNEMKNQMRSIDVQLIFCTLplelRGFQIVSLDDIEFAGTDITMNDLMDNTLDiQYDTLNETVvpKDSPSNIlnts 157
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSA----AKLDVARALLKQCPGVRHRLVLDGDGELE-GFVGYAEAV--AGLPATP---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 158 fnIDDI---ASIMFTSGTTGPQKAV--------PQTFRNHYASaigCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIE 226
Cdd:PRK13391 150 --IADEslgTDMLYSSGTTGRPKGIkrplpeqpPDTPLPLTAF---LQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 227 GFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLM-----QQGLHEPHDLQKILLGGAKLSATMIETALQYNLP-IY 300
Cdd:PRK13391 225 GGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLklpeeVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPiIH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 301 NSFGMTETCSQFLTATPQMLhERPDTVGMPSAnvdvkvknpnkeghGELMIKGANvmnGYLYPTDLTDT--FENG----Y 374
Cdd:PRK13391 305 EYYAATEGLGFTACDSEEWL-AHPGTVGRAMF--------------GDLHILDDD---GAELPPGEPGTiwFEGGrpfeY 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 375 FN-----------------TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQV 437
Cdd:PRK13391 367 LNdpaktaearhpdgtwstVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEE 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1853634356 438 PKLYF-----VSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK13391 447 VKAVVqpvdgVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
168-489 |
5.79e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 128.10 E-value: 5.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 168 FTSGTTGPQKAV--PQTFRNHYASAIGCKESLGFDH----DTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQI 241
Cdd:PRK08276 147 YSSGTTGRPKGIkrPLPGLDPDEAPGMMLALLGFGMyggpDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEEA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 242 LTMIKNERITHISLVPQTLNWLMQ--QGLHEPHD---LQKILLGGA----KLSATMIEtalqYNLPI-YNSFGMTETCSq 311
Cdd:PRK08276 227 LALIERYRVTHSQLVPTMFVRMLKlpEEVRARYDvssLRVAIHAAApcpvEVKRAMID----WWGPIiHEYYASSEGGG- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 312 FLTATPQMLHERPDTVGMPSANVdVKVKNPNKE-----GHGELMIKganvMNGYL--YPTDLTDTFEN----GYFNTGDI 380
Cdd:PRK08276 302 VTVITSEDWLAHPGSVGKAVLGE-VRILDEDGNelppgEIGTVYFE----MDGYPfeYHNDPEKTAAArnphGWVTVGDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 381 AEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQ-----VPKLYFVSESDISKAQLIA 455
Cdd:PRK08276 377 GYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGErvkavVQPADGADAGDALAAELIA 456
|
330 340 350
....*....|....*....|....*....|....
gi 1853634356 456 YLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK08276 457 WLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
17-492 |
5.30e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 125.10 E-value: 5.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 17 AITDGQESYTYQNLYCEASLLARRLKayQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQL 96
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVAERVA--GARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 97 IFCTLPLELRGFQIVslddiefagtditmndlmdntlDIQYDTLNETVVPKDSPsnilntsfniDDIASIMFTSGTTGPQ 176
Cdd:PRK07787 96 WLGPAPDDPAGLPHV----------------------PVRLHARSWHRYPEPDP----------DAPALIVYTSGTTGPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 177 KAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLsVL-----LRAvieGFTVRIVDKFNAEQIltmiKNERIT 251
Cdd:PRK07787 144 KGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGL-VLgvlgpLRI---GNRFVHTGRPTPEAY----AQALSE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 252 HISL---VPQtlnwlMQQGLHEPHDLQKILL-------GGAKLSATMIE--TALQYNLPIyNSFGMTET---CSQFLTAT 316
Cdd:PRK07787 216 GGTLyfgVPT-----VWSRIAADPEAARALRgarllvsGSAALPVPVFDrlAALTGHRPV-ERYGMTETlitLSTRADGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 317 PqmlheRPDTVGMPSANVDVKVKNPNK-------EGHGELMIKGANVMNGYLYPTDLT-DTF-ENGYFNTGDIAEIDHEG 387
Cdd:PRK07787 290 R-----RPGWVGLPLAGVETRLVDEDGgpvphdgETVGELQVRGPTLFDGYLNRPDATaAAFtADGWFRTGDVAVVDPDG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 388 YVMIYDRRK-DLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKV 466
Cdd:PRK07787 365 MHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHKR 444
|
490 500
....*....|....*....|....*.
gi 1853634356 467 PKHFEKVDTLPYTSTGKLQRNKLYRG 492
Cdd:PRK07787 445 PREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
200-482 |
8.16e-31 |
|
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: 121.64 E-value: 8.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 200 DHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILL 279
Cdd:cd17636 39 DEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 280 G-GAKLSATMI---ETALQYNLPIYnsfGMTETCSqfLTATPQMLHERPDTVGMPSANVDVKVKNPnkEGH-------GE 348
Cdd:cd17636 119 SpAAPEWNDMAtvdTSPWGRKPGGY---GQTEVMG--LATFAALGGGAIGGAGRPSPLVQVRILDE--DGRevpdgevGE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 349 LMIKGANVMNGYLYPTDLT-DTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCI 427
Cdd:cd17636 192 IVARGPTVMAGYWNRPEVNaRRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1853634356 428 GHPDDTWGQVPKLYFVSESD--ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTG 482
Cdd:cd17636 272 GVPDPRWAQSVKAIVVLKPGasVTEAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
8-489 |
2.62e-30 |
|
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: 123.08 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLtPNE 84
Cdd:cd12117 6 QAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAgvgPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL-PAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 85 MKNQMrsidvqlifctlpLELRGFQIVsLDDIEFAGTDitmNDLMDNTLDIQydtlnetvVPKDSPSNILNTSFNIDDIA 164
Cdd:cd12117 85 RLAFM-------------LADAGAKVL-LTDRSLAGRA---GGLEVAVVIDE--------ALDAGPAGNPAVPVSPDDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 165 SIMFTSGTTGPQKAVPQTFRNhyasaigckeSLGFDHDTNWLSVLP---IYHISGLSV------LLRAVIEGFTVRIVDK 235
Cdd:cd12117 140 YVMYTSGSTGRPKGVAVTHRG----------VVRLVKNTNYVTLGPddrVLQTSPLAFdastfeIWGALLNGARLVLAPK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 236 ---FNAEQILTMIKNERITHISLVPQTLNWLMQQ------GLHEphdlqkILLGGAKLSATMIETALQYN--LPIYNSFG 304
Cdd:cd12117 210 gtlLDPDALGALIAEEGVTVLWLTAALFNQLADEdpecfaGLRE------LLTGGEVVSPPHVRRVLAACpgLRLVNGYG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 305 MTE--TCSQFLTATPQMLHERPDTVGMPSANVDVKVKNPNkeGH-------GELMIKGANVMNGYLYPTDLT------DT 369
Cdd:cd12117 284 PTEntTFTTSHVVTELDEVAGSIPIGRPIANTRVYVLDED--GRpvppgvpGELYVGGDGLALGYLNRPALTaerfvaDP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 370 FENG---YFnTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSES 446
Cdd:cd12117 362 FGPGerlYR-TGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG 440
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1853634356 447 DISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd12117 441 ALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
7-489 |
4.30e-30 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 123.19 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 7 KQAQQNGHHIAI--TDGQESYTYQNLYCEASLLARRLKA---YQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLT 81
Cdd:PRK05857 22 EQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAqsvSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 82 PNEMKNQMRSIDVQLIfctLPLELRGFQIVSLDDIEFAGTDITMNdlmdNTLDIQYDTLN-ETVVPKDSPSnilntsFNI 160
Cdd:PRK05857 102 IAAIERFCQITDPAAA---LVAPGSKMASSAVPEALHSIPVIAVD----IAAVTRESEHSlDAASLAGNAD------QGS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYA-SAIGCKESLGF----DHDTNWlSVLPIYHISGLSVLLRAVIEGFTVrIVDK 235
Cdd:PRK05857 169 EDPLAMIFTSGTTGEPKAVLLANRTFFAvPDILQKEGLNWvtwvVGETTY-SPLPATHIGGLWWILTCLMHGGLC-VTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 236 FNAEQILTMIKNERITHISLVPQTLNWLMQQ----GLHEPhDLQKILLGGAKLSAT---MIETALQYNLPIYnsfGMTET 308
Cdd:PRK05857 247 ENTTSLLEILTTNAVATTCLVPTLLSKLVSElksaNATVP-SLRLVGYGGSRAIAAdvrFIEATGVRTAQVY---GLSET 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 -CSQFLTATPQMLHERPD--TVGMPSANVDVKVKNPNKEG-----------HGELMIKGANVMNGYL-YPTDLTDTFENG 373
Cdd:PRK05857 323 gCTALCLPTDDGSIVKIEagAVGRPYPGVDVYLAATDGIGptapgagpsasFGTLWIKSPANMLGYWnNPERTAEVLIDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDISKAQL 453
Cdd:PRK05857 403 WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAA 482
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1853634356 454 IAYLSQHLAKYK-------VPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK05857 483 RALKHTIAARFRresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
162-489 |
4.73e-30 |
|
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: 122.96 E-value: 4.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTfrnHYASAIGCKESLGFdhdtnWLSVLP---IYHIS-------GLSVLLRAVIEGFTVR 231
Cdd:cd05928 175 EPMAIYFTSGTTGSPKMAEHS---HSSLGLGLKVNGRY-----WLDLTAsdiMWNTSdtgwiksAWSSLFEPWIQGACVF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 232 I--VDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGL--HEPHDLQKILLGGAKLSATMIET-ALQYNLPIYNSFGMT 306
Cdd:cd05928 247 VhhLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLssYKFPSLQHCVTGGEPLNPEVLEKwKAQTGLDIYEGYGQT 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 307 ETCsqFLTATPQMLHERPDTVGMPSANVDVKVKN-------PNKEGHGELMIKGAN---VMNGYLYPTDLTDTFENG-YF 375
Cdd:cd05928 327 ETG--LICANFKGMKIKPGSMGKASPPYDVQIIDdngnvlpPGTEGDIGIRVKPIRpfgLFSGYVDNPEKTAATIRGdFY 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 376 NTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDIS---KAQ 452
Cdd:cd05928 405 LTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLshdPEQ 484
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1853634356 453 LIAYLSQHL----AKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05928 485 LTKELQQHVksvtAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
16-489 |
1.01e-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: 121.71 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 16 IAITDGQESYTYQNLYCEASLLA---RRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMK-----N 87
Cdd:cd05959 21 TAFIDDAGSLTYAELEAEARRVAgalRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAyyledS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 88 QMRSIDVQLIFCTLplelrgFQIVSLDDIEFAGTDITMNDLMDNTLDIQYdtlnETVVPKDSPS-NILNTSfnIDDIASI 166
Cdd:cd05959 101 RARVVVVSGELAPV------LAAALTKSEHTLVVLIVSGGAGPEAGALLL----AELVAAEAEQlKPAATH--ADDPAFW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 167 MFTSGTTGPQKAVPQTFRNHYASA-IGCKESLGFDHDTNWLSVLPIYHISGL--SVLLRAVIEGFTVRIVDKFNAEQILT 243
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLFFAYGLgnSLTFPLSVGATTVLMPERPTPAAVFK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 244 MIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILL---GGAKLSATMIE--TALqYNLPIYNSFGMTETCSQFLTATPQ 318
Cdd:cd05959 249 RIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLcvsAGEALPAEVGErwKAR-FGLDILDGIGSTEMLHIFLSNRPG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 319 MLheRPDTVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYLYPTDLT-DTFENGYFNTGDIAEIDHEGYVMIY 392
Cdd:cd05959 328 RV--RYGTTGKPVPGYEVELRDEDGGdvadgEPGELYVRGPSSATMYWNNRDKTrDTFQGEWTRTGDKYVRDDDGFYTYA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 393 DRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-----SESDISKAQLIAYLSQHLAKYKVP 467
Cdd:cd05959 406 GRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpgyEDSEALEEELKEFVKDRLAPYKYP 485
|
490 500
....*....|....*....|..
gi 1853634356 468 KHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05959 486 RWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
161-489 |
1.47e-29 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 121.81 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCK--ESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEG----FTVRIVD 234
Cdd:PRK05620 181 TTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRttDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGtplvFPGPDLS 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 235 kfnAEQILTMIKNE--RITHisLVPQTLNWLMQQGLHEPHD---LQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTET 308
Cdd:PRK05620 261 ---APTLAKIIATAmpRVAH--GVPTLWIQLMVHYLKNPPErmsLQEIYVGGSAVPPILIKAWEErYGVDVVHVWGMTET 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 CSQfltatpqmlherpDTVGMPSANV-------------------------DVKVKNPNKEGHGELMIKGANVMNGYLYP 363
Cdd:PRK05620 336 SPV-------------GTVARPPSGVsgearwayrvsqgrfpasleyrivnDGQVMESTDRNEGEIQVRGNWVTASYYHS 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 364 -----------------TDLTDTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAV 425
Cdd:PRK05620 403 pteegggaastfrgedvEDANDRFtADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECA 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1853634356 426 CIGHPDDTWGQVPKLYFVSESDISKA-----QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK05620 483 VIGYPDDKWGERPLAVTVLAPGIEPTretaeRLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
17-483 |
1.99e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 121.15 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 17 AITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSID 93
Cdd:PRK07798 21 ALVCGDRRLTYAELEERANRLAHYLIAQglgPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 94 VQ-LIF--------CTLPLELRGFQ-IVSLDDiefaGTDitmNDLMDNTLDiqYDTL-----NETVVPKDSPsnilntsf 158
Cdd:PRK07798 101 AVaLVYerefaprvAEVLPRLPKLRtLVVVED----GSG---NDLLPGAVD--YEDAlaagsPERDFGERSP-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 159 niDDIAsIMFTSGTTGPQKAV----PQTFR------NHYAS---------AIGCKESLGfdhdTNWLSVLPIYHISGLSV 219
Cdd:PRK07798 164 --DDLY-LLYTGGTTGMPKGVmwrqEDIFRvllggrDFATGepiedeeelAKRAAAGPG----MRRFPAPPLMHGAGQWA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 220 LLRAVIEGFTVRI--VDKFNAEQILTMIKNERITHISLV------PqtlnwlMQQGLHEPHD-----LQKILLGGAKLSA 286
Cdd:PRK07798 237 AFAALFSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVgdamarP------LLDALEARGPydlssLFAIASGGALFSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 287 TmIETALQYNLP---IYNSFGMTETCSQ-FLTATPQMLHERPDTVGMpsaNVDVKV----KNPNKEGHGEL-MI-KGANV 356
Cdd:PRK07798 311 S-VKEALLELLPnvvLTDSIGSSETGFGgSGTVAKGAVHTGGPRFTI---GPRTVVldedGNPVEPGSGEIgWIaRRGHI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 357 MNGYlY--PTDLTDTFE--NG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHP 430
Cdd:PRK07798 387 PLGY-YkdPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVP 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 431 DDTWGQ-VPKLYFVSE-SDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGK 483
Cdd:PRK07798 466 DERWGQeVVAVVQLREgARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
8-489 |
3.11e-29 |
|
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: 122.27 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLAN-----IEIAMintr 79
Cdd:COG1020 485 QAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALgvgPGDLVGVCLERSLEMVVALLAVLKAGaayvpLDPAY---- 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 80 ltPNEMKNQM-RSIDVQLIFCTLPLELR----GFQIVSLDDIEFAGTditmndlmdntldiqydtlnetvvPKDSPSNIL 154
Cdd:COG1020 561 --PAERLAYMlEDAGARLVLTQSALAARlpelGVPVLALDALALAAE------------------------PATNPPVPV 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 155 NTsfniDDIASIMFTSGTTGPQKAVPQTFRN--HYASAIGckESLGFDHDTNWLSVLPIyhiS-GLSV--LLRAVIEGFT 229
Cdd:COG1020 615 TP----DDLAYVIYTSGSTGRPKGVMVEHRAlvNLLAWMQ--RRYGLGPGDRVLQFASL---SfDASVweIFGALLSGAT 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 230 VRIVDK---FNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILLGGAKLSATMIETALQY--NLPIYNSFG 304
Cdd:COG1020 686 LVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARlpGARLVNLYG 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 305 MTET--CSQFLTATPQMLHERPDTVGMPSANVDVKVKNPNKE----G-HGELMIKGANVMNGYLYPTDLT------DTFE 371
Cdd:COG1020 766 PTETtvDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQpvpvGvPGELYIGGAGLARGYLNRPELTaerfvaDPFG 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 372 NG---YFNTGDIA------EIDHEGyvmiydrRKD--LIISG-----GEniypyqIETVAKQFPGISDAVCIGHPDdtwG 435
Cdd:COG1020 846 FPgarLYRTGDLArwlpdgNLEFLG-------RADdqVKIRGfrielGE------IEAALLQHPGVREAVVVARED---A 909
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1853634356 436 QVPKL---YFVSE--SDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:COG1020 910 PGDKRlvaYVVPEagAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1-484 |
9.65e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 120.80 E-value: 9.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 1 MDFWLYKQAQQNGHHIAITD-GQESYTYQNLYCEASLLARRLKAY--QQSRVGLYIDNSIQSIILIHACWLANIEIAMIN 77
Cdd:PRK08633 617 LAEAWIDTAKRNWSRLAVADsTGGELSYGKALTGALALARLLKRElkDEENVGILLPPSVAGALANLALLLAGKVPVNLN 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 78 TRLTPNEMKNQMRSIDVQLI-----FCTlPLELRGFQIVSLDDIEFagtdITMNDLMDN--TLDIQYDTLNETVVPKDSP 150
Cdd:PRK08633 697 YTASEAALKSAIEQAQIKTVitsrkFLE-KLKNKGFDLELPENVKV----IYLEDLKAKisKVDKLTALLAARLLPARLL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 151 SNILNTSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIEGF- 228
Cdd:PRK08633 772 KRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVtLWLPLLEGIk 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 229 TVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILL---GGAKL-SATMIETALQYNLPIYNSFG 304
Cdd:PRK08633 852 VVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLvvaGAEKLkPEVADAFEEKFGIRILEGYG 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 305 MTET------------CSQFLTATPQmlheRPDTVGMPSANVDVKVKNPN-----KEGH-GELMIKGANVMNGYLYPTDL 366
Cdd:PRK08633 932 ATETspvasvnlpdvlAADFKRQTGS----KEGSVGMPLPGVAVRIVDPEtfeelPPGEdGLILIGGPQVMKGYLGDPEK 1007
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 367 T-----DTFENGYFNTGDIAEIDHEGYVMIYDR--RKDLIisGGENIYPYQIETVAKQFPGISDAVCI--GHPDDTWG-Q 436
Cdd:PRK08633 1008 TaevikDIDGIGWYVTGDKGHLDEDGFLTITDRysRFAKI--GGEMVPLGAVEEELAKALGGEEVVFAvtAVPDEKKGeK 1085
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1853634356 437 VPKLYFVSESDISKAQLIAyLSQHLAKYKVPKHFEKVDTLPYTSTGKL 484
Cdd:PRK08633 1086 LVVLHTCGAEDVEELKRAI-KESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
155-486 |
2.37e-28 |
|
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: 117.98 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 155 NTSFNIDDIASIMFTSGTTGPQKAVPQTFR---NHYASAI---GCKEslGFDH----DTNWLSVL--PIYH--ISGLSVL 220
Cdd:cd05970 179 NSYPCGEDILLVYFSSGTTGMPKMVEHDFTyplGHIVTAKywqNVRE--GGLHltvaDTGWGKAVwgKIYGqwIAGAAVF 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 221 lraviegftVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLhEPHDLQKI---LLGGAKLSATMIETALQYN- 296
Cdd:cd05970 257 ---------VYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDL-SRYDLSSLrycTTAGEALNPEVFNTFKEKTg 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 297 LPIYNSFGMTETCSQflTATPQMLHERPDTVGMPSANVDVKVKNPN----KEGH-GELMIKGAN-----VMNGYLYPTDL 366
Cdd:cd05970 327 IKLMEGFGQTETTLT--IATFPWMEPKPGSMGKPAPGYEIDLIDREgrscEAGEeGEIVIRTSKgkpvgLFGGYYKDAEK 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 367 T-DTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSE 445
Cdd:cd05970 405 TaEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLA 484
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1853634356 446 SDISKAQ-LIAYLSQHLAK----YKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:cd05970 485 KGYEPSEeLKKELQDHVKKvtapYKYPRIVEFVDELPKTISGKIRR 530
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
161-489 |
2.51e-28 |
|
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: 116.80 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDT-NWLSVLPIYHISGLSVLLRAVIEGFTVRIVD---KF 236
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPdevKL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 237 NAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQ--KILLGG-----AKLSATMIETALQyNLPIYNSFGMTETC 309
Cdd:cd17650 173 DPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSamRLLIVGsdgckAQDFKTLAARFGQ-GMRIINSYGVTEAT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 310 ---SQFLTATPQMLHERPDTVGMPSANVDVKV----KNPNKEG-HGELMIKGANVMNGYLYPTDLT------DTFENG-- 373
Cdd:cd17650 252 idsTYYEEGRDPLGDSANVPIGRPLPNTAMYVlderLQPQPVGvAGELYIGGAGVARGYLNRPELTaerfveNPFAPGer 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDtwGQVPKL--YFVSESDISKA 451
Cdd:cd17650 332 MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK--GGEARLcaYVVAAATLNTA 409
|
330 340 350
....*....|....*....|....*....|....*...
gi 1853634356 452 QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17650 410 ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
26-425 |
3.32e-28 |
|
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: 115.83 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 26 TYQNLYCEASLLARRLKAY----QQSRVGLYIDNSIQSIILIHACWLAN-----IEIAMintrltPNEMKNQM-RSIDVQ 95
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAggvgPGDRVAVLLERSAELVVAILAVLKAGaayvpLDPAY------PAERLAFIlEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 96 LIFCTLPLELRgfqivslddieFAGTDITMNDLMDNTLDIQYDTLNETVVPKDSPSnilntsfniDDIASIMFTSGTTGP 175
Cdd:TIGR01733 75 LLLTDSALASR-----------LAGLVLPVILLDPLELAALDDAPAPPPPDAPSGP---------DDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 176 QKAVPQTFR---NHYASAIGCKE-----------SLGFDhdtnwLSVLPIY--HISGLSVLLRaviegftVRIVDKFNAE 239
Cdd:TIGR01733 135 PKGVVVTHRslvNLLAWLARRYGldpddrvlqfaSLSFD-----ASVEEIFgaLLAGATLVVP-------PEDEERDDAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILLGGAKLSATMIETALQ--YNLPIYNSFGMTET---CSQFLT 314
Cdd:TIGR01733 203 LLAALIAEHPVTVLNLTPSLLALLAAALPPALASLRLVILGGEALTPALVDRWRArgPGARLINLYGPTETtvwSTATLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 315 ATPQMLHERPDTVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYLYPTDLT-DTF-ENGY--------FNTGD 379
Cdd:TIGR01733 283 DPDDAPRESPVPIGRPLANTRLYVLDDDLRpvpvgVVGELYIGGPGVARGYLNRPELTaERFvPDPFaggdgarlYRTGD 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1853634356 380 IAEIDHEGYVMIYDRRKDLI-ISG-----GEniypyqIETVAKQFPGISDAV 425
Cdd:TIGR01733 363 LVRYLPDGNLEFLGRIDDQVkIRGyrielGE------IEAALLRHPGVREAV 408
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
6-491 |
3.53e-28 |
|
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: 116.25 E-value: 3.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 6 YKQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAYQQ---SRVGLYIDNS------IQSIILIHACWLAnieiamI 76
Cdd:cd17653 4 ERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVvpgDVVPLLSDRSlemlvaILAILKAGAAYVP------L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 77 NTRLTPNEMKNQMRSIDVQLIFCTlplelrgfqivslddiefagtditmndlmdntldiqydtlnetvvpkDSPsnilnt 156
Cdd:cd17653 78 DAKLPSARIQAILRTSGATLLLTT-----------------------------------------------DSP------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 157 sfniDDIASIMFTSGTTGPQKAVPQTFRN--HYASAIGckESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVD 234
Cdd:cd17653 105 ----DDLAYIIFTSGSTGIPKGVMVPHRGvlNYVSQPP--ARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 235 kfNAEQILTMIKNERITHISlvPQTLNWLMQQGLhePHdLQKILLGGAKLSATMIETALQyNLPIYNSFGMTE-TCSqfl 313
Cdd:cd17653 179 --PSDPFAHVARTVDALMST--PSILSTLSPQDF--PN-LKTIFLGGEAVPPSLLDRWSP-GRRLYNAYGPTEcTIS--- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 314 TATPQMLHERPDTVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYLYPTDLT------DTFENG--YFNTGDI 380
Cdd:cd17653 248 STMTELLPGQPVTIGKPIPNSTCYILDADLQpvpegVVGEICISGVQVARGYLGNPALTaskfvpDPFWPGsrMYRTGDY 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 381 AEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQF-PGISDAVCIGHPDdtwgqvpKLY-FVSESDISKAQLIAYLS 458
Cdd:cd17653 328 GRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSqPEVTQAAAIVVNG-------RLVaFVTPETVDVDGLRSELA 400
|
490 500 510
....*....|....*....|....*....|...
gi 1853634356 459 QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd17653 401 KHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
20-489 |
9.07e-28 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 116.23 E-value: 9.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 20 DGQESYTYQnlYCEASLLARRLKA-------YQQSRVGLYIDNSIQSIilihacwLANIEIAMI-------NTRLTPNEM 85
Cdd:PLN02246 44 DGATGRVYT--YADVELLSRRVAAglhklgiRQGDVVMLLLPNCPEFV-------LAFLGASRRgavtttaNPFYTPAEI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 86 KNQMRSIDVQLIFcTLPL---ELRGFQIVslDDIefagTDITMNDLMDNTLDIQYDTL-NETVVPKdspsnilnTSFNID 161
Cdd:PLN02246 115 AKQAKASGAKLII-TQSCyvdKLKGLAED--DGV----TVVTIDDPPEGCLHFSELTQaDENELPE--------VEISPD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAI----GCKESLGFDHDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDKF 236
Cdd:PLN02246 180 DVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFHSDDVILCVLPMFHIYSLnSVLLCGLRVGAAILIMPKF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 237 NAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKI--LLGGAklsATM---IETALQYNLP---IYNSFGMTET 308
Cdd:PLN02246 260 EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIrmVLSGA---APLgkeLEDAFRAKLPnavLGQGYGMTEA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 ------CSQFlTATPqmLHERPDTVGMPSANVDVKVKNP--------NKEGhgELMIKGANVMNGYLYPTDLT----Dtf 370
Cdd:PLN02246 337 gpvlamCLAF-AKEP--FPVKSGSCGTVVRNAELKIVDPetgaslprNQPG--EICIRGPQIMKGYLNDPEATantiD-- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 371 ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDI 448
Cdd:PLN02246 410 KDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVrsNGSEI 489
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1853634356 449 SKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PLN02246 490 TEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
161-483 |
1.83e-27 |
|
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: 113.25 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIAsIMFTSGTTGPQKAVpqTFRNH--YASAIGckeslGFDHDT-------------------NWLSVLPIYHISGLSV 219
Cdd:cd05924 4 DDLY-ILYTGGTTGMPKGV--MWRQEdiFRMLMG-----GADFGTgeftpsedahkaaaaaagtVMFPAPPLMHGTGSWT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 220 LLRAVIEGFTVRIVD-KFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHD-----LQKILLGGAKLSATMIE--T 291
Cdd:cd05924 76 AFGGLLGGQTVVLPDdRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPydlssLFAISSGGALLSPEVKQglL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 292 ALQYNLPIYNSFGMTETCSQFLTATPQMLHER-------PDTVgmpSANVDVKVKNPNKEGHGELMIKGaNVMNGYLY-P 363
Cdd:cd05924 156 ELVPNITLVDAFGSSETGFTGSGHSAGSGPETgpftranPDTV---VLDDDGRVVPPGSGGVGWIARRG-HIPLGYYGdE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 364 TDLTDTFE--NG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQ--V 437
Cdd:cd05924 232 AKTAETFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQevV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1853634356 438 PKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGK 483
Cdd:cd05924 312 AVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
36-431 |
2.78e-27 |
|
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: 115.01 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 36 LLARRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFCTlplelRGFQIVSLDD 115
Cdd:cd05927 22 LRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD-----AGVKVYSLEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 116 IEFAGTDItmndlmdntldiqydtlNETVVPKDSpsnilntsfniDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKE 195
Cdd:cd05927 97 FEKLGKKN-----------------KVPPPPPKP-----------EDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 196 SLG----FDHDTNWLSVLPIYHIsglsvLLRAVIE-----GFTVRIVDKfNAEQILTMIKNERITHISLVPQTLN----- 261
Cdd:cd05927 149 ILEilnkINPTDVYISYLPLAHI-----FERVVEAlflyhGAKIGFYSG-DIRLLLDDIKALKPTVFPGVPRVLNriydk 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 262 -------------WL-----------MQQGLHEPH-----------------DLQKILLGGAKLSATmIETALQYNL--P 298
Cdd:cd05927 223 ifnkvqakgplkrKLfnfalnyklaeLRSGVVRASpfwdklvfnkikqalggNVRLMLTGSAPLSPE-VLEFLRVALgcP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 299 IYNSFGMTETCSqflTATPQMLHER-PDTVGMPSANVDVKVKN-PNKE-------GHGELMIKGANVMNGYLYPTDLTD- 368
Cdd:cd05927 302 VLEGYGQTECTA---GATLTLPGDTsVGHVGGPLPCAEVKLVDvPEMNydakdpnPRGEVCIRGPNVFSGYYKDPEKTAe 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1853634356 369 TF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETVAKQFPGISDA-----------VCIGHPD 431
Cdd:cd05927 379 ALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIfvygdslksflVAIVVPD 454
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
15-489 |
3.01e-27 |
|
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: 114.11 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 15 HIAITDGQESYTYQNLYCEASLLARRLK---AYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRS 91
Cdd:cd17656 4 AVAVVFENQKLTYRELNERSNQLARFLRekgVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 92 IDVQLIF----CTLPLELRGFQIVSLDDIEFAGTDitmndlmdntldiqydtlnetvvpkdspSNIlNTSFNIDDIASIM 167
Cdd:cd17656 84 SGVRVVLtqrhLKSKLSFNKSTILLEDPSISQEDT----------------------------SNI-DYINNSDDLLYII 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 168 FTSGTTGPQKAVPQTFRNhyasaigCKESLGFDHD-TNWLSVLPIYHISGLSV------LLRAVIEGFTVRIVD---KFN 237
Cdd:cd17656 135 YTSGTTGKPKGVQLEHKN-------MVNLLHFEREkTNINFSDKVLQFATCSFdvcyqeIFSTLLSGGTLYIIReetKRD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLvPQTLnWLMQQGLHE-----PHDLQKILLGGAKL--SATMIETALQYNLPIYNSFGMTET-C 309
Cdd:cd17656 208 VEQLFDLVKRHNIEVVFL-PVAF-LKFIFSEREfinrfPTCVKHIITAGEQLviTNEFKEMLHEHNVHLHNHYGPSEThV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 310 SQFLTATPQMLHERPDTVGMPSANVDVKVKNPNKEGH-----GELMIKGANVMNGYLYPTDLT------DTFENG--YFN 376
Cdd:cd17656 286 VTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQpqgivGELYISGASVARGYLNRQELTaekffpDPFDPNerMYR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 377 TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDISKAQLIAY 456
Cdd:cd17656 366 TGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREY 445
|
490 500 510
....*....|....*....|....*....|...
gi 1853634356 457 LSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17656 446 LAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
5-489 |
1.84e-26 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 112.39 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 5 LYKQAQqnGHHIAITDGQESYTYQNLYCEASLLARRL-----KAYQQSRVGLyiDNSIQSIILIHAcwLANIEIAMINTR 79
Cdd:PRK10946 31 LTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLrrqgiKPGDTALVQL--GNVAEFYITFFA--LLKLGVAPVNAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 80 LTPN--EMKNQMRSIDVQLIfctlplelrgfqIVSLDDIEFAgtditmNDLMDNTLDIQYDTLNETVVPKDSPSNILN-- 155
Cdd:PRK10946 105 FSHQrsELNAYASQIEPALL------------IADRQHALFS------DDDFLNTLVAEHSSLRVVLLLNDDGEHSLDda 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 156 ----------TSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV--LLRA 223
Cdd:PRK10946 167 inhpaedftaTPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYPMSSpgALGV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 224 VIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLN-WLMQ----QGLHEPHDLQKILLGGAKLSATM-------IET 291
Cdd:PRK10946 247 FLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSlWLQAiaegGSRAQLASLKLLQVGGARLSETLarripaeLGC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 292 ALQynlpiyNSFGMTETCSQF--LTATPQMLHerpDTVGMP-SANVDVKVK----NPNKEGH-GELMIKGANVMNGYlY- 362
Cdd:PRK10946 327 QLQ------QVFGMAEGLVNYtrLDDSDERIF---TTQGRPmSPDDEVWVAdadgNPLPQGEvGRLMTRGPYTFRGY-Yk 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 363 -PTDLTDTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKL 440
Cdd:PRK10946 397 sPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1853634356 441 YFVSESDISKAQLIAYL-SQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK10946 477 FLVVKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1-489 |
1.86e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 112.53 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 1 MDFW--LYKQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAM 75
Cdd:PRK06164 10 DTLAslLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQgvrRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 76 INTRLTPNEM-----KNQMRSIDVQLIFCTLPLE--LRGFQIVSLDDIE-FAGTDITMNDLMDNTLdiqYDTLNETVVPK 147
Cdd:PRK06164 90 VNTRYRSHEVahilgRGRARWLVVWPGFKGIDFAaiLAAVPPDALPPLRaIAVVDDAADATPAPAP---GARVQLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 148 DSPSNILNTSFNIDDIASIMFT-SGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIE 226
Cdd:PRK06164 167 PAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 227 GFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGlHEPHDLQKI-LLGGAKLSATMIE---TALQYNLPIYNS 302
Cdd:PRK06164 247 GAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTA-GERADFPSArLFGFASFAPALGElaaLARARGVPLTGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 303 FGMTETCSQFL--TATPQMLHeRPDTVGMP-SANVDVKVKNPNKEG------HGELMIKGANVMNGYLYPTDLT-DTF-E 371
Cdd:PRK06164 326 YGSSEVQALVAlqPATDPVSV-RIEGGGRPaSPEARVRARDPQDGAllpdgeSGEIEIRAPSLMRGYLDNPDATaRALtD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 372 NGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDtwGQVPKLYFVSESDISKA 451
Cdd:PRK06164 405 DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKTVPVAFVIPTDGASP 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1853634356 452 Q---LIAYLSQHLAKYKVPKHFEKVDTLPYTSTG---KLQRNKL 489
Cdd:PRK06164 483 DeagLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
7-489 |
2.29e-26 |
|
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: 111.67 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 7 KQAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKA---YQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRlTPN 83
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRArgvGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA-YPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 84 EMKNQMRSiDVQlifctlplelrGFQIVSLDDIEFAGTDitmnDLMDNTLDIQYDTLNETVVPKDSPSNIlntsfniDDI 163
Cdd:cd17651 82 ERLAFMLA-DAG-----------PVLVLTHPALAGELAV----ELVAVTLLDQPGAAAGADAEPDPALDA-------DDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 164 ASIMFTSGTTGPQKAVPQTFRN-------HYASAIGCKE-------SLGFDhdtnwLSVLPIyhisgLSVLLRA---VIE 226
Cdd:cd17651 139 AYVIYTSGSTGRPKGVVMPHRSlanlvawQARASSLGPGartlqfaGLGFD-----VSVQEI-----FSTLCAGatlVLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 227 GFTVRivdkFNAEQILTMIKNERITHISLVPQTLNWLMQQGLH---EPHDLQKILLGGAKLSATMIETALQYNLP---IY 300
Cdd:cd17651 209 PEEVR----TDPPALAAWLDEQRISRVFLPTVALRALAEHGRPlgvRLAALRYLLTGGEQLVLTEDLREFCAGLPglrLH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 301 NSFGMTETcsQFLTA--TPQMLHERPDT--VGMPSANVDVKVKNPNKE----GH-GELMIKGANVMNGYLYPTDLT---- 367
Cdd:cd17651 285 NHYGPTET--HVVTAlsLPGDPAAWPAPppIGRPIDNTRVYVLDAALRpvppGVpGELYIGGAGLARGYLNRPELTaerf 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 --DTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV 443
Cdd:cd17651 363 vpDPFVPGarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1853634356 444 S--ESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17651 443 GdpEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
137-489 |
2.55e-26 |
|
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: 111.92 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 137 YDTLNETVVP---KDSPSNILNTSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLG-FDHDTNW-LSVLPI 211
Cdd:cd17639 61 YATLGEDALIhslNETECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPeLLGPDDRyLAYLPL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 212 YHISGLSV----LLRAVIEGF-TVR-IVDKFNAE-----------------QILTMIK---NERITHISLVPQTLNWLMQ 265
Cdd:cd17639 141 AHIFELAAenvcLYRGGTIGYgSPRtLTDKSKRGckgdltefkptlmvgvpAIWDTIRkgvLAKLNPMGGLKRTLFWTAY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 266 Q----GLHEPHD-------------------LQKILLGGAKLSAtmiETALQYNL---PIYNSFGMTETCSqflTATPQM 319
Cdd:cd17639 221 QsklkALKEGPGtplldelvfkkvraalggrLRYMLSGGAPLSA---DTQEFLNIvlcPVIQGYGLTETCA---GGTVQD 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 320 LHE-RPDTVGMPSANVDVKVKNPNKEGH--------GELMIKGANVMNGYLYPTDLT--DTFENGYFNTGDIAEIDHEGY 388
Cdd:cd17639 295 PGDlETGRVGPPLPCCEIKLVDWEEGGYstdkppprGEILIRGPNVFKGYYKNPEKTkeAFDGDGWFHTGDIGEFHPDGT 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 389 VMIYDRRKDLI-ISGGENIYPYQIETVAKQFPgISDAVCI-GHPDDTW---------GQVPKL---YFVSESD----ISK 450
Cdd:cd17639 375 LKIIDRKKDLVkLQNGEYIALEKLESIYRSNP-LVNNICVyADPDKSYpvaivvpneKHLTKLaekHGVINSEweelCED 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1853634356 451 AQLIAYLSQHLAKYKVPKHFEKVDTLPY---------------TSTGKLQRNKL 489
Cdd:cd17639 454 KKLQKAVLKSLAETARAAGLEKFEIPQGvvlldeewtpenglvTAAQKLKRKEI 507
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
147-489 |
9.34e-26 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 109.32 E-value: 9.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 147 KDS-PSNILNTSfniDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLsvlpIYHISG--LSV--LL 221
Cdd:cd17643 81 ADSgPSLLLTDP---DDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdFSVweIW 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 222 RAVIEGFTVRIVDKFNA---EQILTMIKNERITHISLVPQTLNWLMQ---QGLHEPHDLQKILLGGAKLSATMIET-ALQ 294
Cdd:cd17643 154 GALLHGGRLVVVPYEVArspEDFARLLRDEGVTVLNQTPSAFYQLVEaadRDGRDPLALRYVIFGGEALEAAMLRPwAGR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 295 YNLP---IYNSFGMTETC--SQFLTATPQMLHERPDTV---GMPSANVDVKVKNPNKE---GHGELMIKGANVMNGYLYP 363
Cdd:cd17643 234 FGLDrpqLVNMYGITETTvhVTFRPLDAADLPAAAASPigrPLPGLRVYVLDADGRPVppgVVGELYVSGAGVARGYLGR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 364 TDLT------DTFENG---YFNTGDIA------EIDHEGyvmiydRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIG 428
Cdd:cd17643 314 PELTaerfvaNPFGGPgsrMYRTGDLArrlpdgELEYLG------RADEQVKIRGFRIELGEIEAALATHPSVRDAAVIV 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1853634356 429 HPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17643 388 REDEPGDTRLVAYVVadDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
148-488 |
6.14e-25 |
|
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: 107.44 E-value: 6.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 148 DSPSNIL---NTSfniDDIASIMFTSGTTGPQKAVPQTFRN--HYASAIGCKESLgfDHDTNWLSVLPIYHISGLS---- 218
Cdd:cd17640 75 HSESVALvveNDS---DDLATIIYTSGTTGNPKGVMLTHANllHQIRSLSDIVPP--QPGDRFLSILPIWHSYERSaeyf 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 219 VLLRAVIEGFTvrivdkfnaeQILTM---IKNERITHISLVP---QTLNWLMQQGLHEPHDLQKILLGGAkLSATMIETA 292
Cdd:cd17640 150 IFACGCSQAYT----------SIRTLkddLKRVKPHYIVSVPrlwESLYSGIQKQVSKSSPIKQFLFLFF-LSGGIFKFG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 293 L-------QY--------NLPIYNSFGMTETcSQFLTATpqmLHERP--DTVGMPSANVDVKVKNPN------KEGHGEL 349
Cdd:cd17640 219 IsgggalpPHvdtffeaiGIEVLNGYGLTET-SPVVSAR---RLKCNvrGSVGRPLPGTEIKIVDPEgnvvlpPGEKGIV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 350 MIKGANVMNGYLYPTDLTDTF--ENGYFNTGDIAEIDHEGYVMIYDRRKDLII-SGGENIYPYQIETVAKQFPGISDAVC 426
Cdd:cd17640 295 WVRGPQVMKGYYKNPEATSKVldSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMV 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 427 IGH----------PD----DTWGQVPKLYFVSE--SDISKAQLIAYLSQHLAKY----KVPKHFEKVDTL-----PY--- 478
Cdd:cd17640 375 VGQdqkrlgalivPNfeelEKWAKESGVKLANDrsQLLASKKVLKLYKNEIKDEisnrPGFKSFEQIAPFalleePFien 454
|
410
....*....|...
gi 1853634356 479 ---TSTGKLQRNK 488
Cdd:cd17640 455 gemTQTMKIKRNV 467
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
164-489 |
8.33e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 107.40 E-value: 8.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 164 ASIMFTSGTTGPQKAVPQTFRNHYASAIG------CKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFN 237
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQPDLPGRDVDAPGdpivaiARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLVPQTLNWLMQ-----QGLHEPHDLQKILLGGAKLSATMIETALQYNLPI-YNSFGMTETCSQ 311
Cdd:PRK13390 231 AQATLGHVERYRITVTQMVPTMFVRLLKldadvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIvYEYYSSTEAHGM 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 312 FLTATPQMLhERPDTVGMpSANVDVKVknPNKEGH-------GELMIKGANVMNGYLYPTDLTDTFENG----YFNTGDI 380
Cdd:PRK13390 311 TFIDSPDWL-AHPGSVGR-SVLGDLHI--CDDDGNelpagriGTVYFERDRLPFRYLNDPEKTAAAQHPahpfWTTVGDL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 381 AEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWG-QVPKLYFVSE----SDISKAQLIA 455
Cdd:PRK13390 387 GSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGeQVKAVIQLVEgirgSDELARELID 466
|
330 340 350
....*....|....*....|....*....|....
gi 1853634356 456 YLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK13390 467 YTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
9-489 |
2.85e-24 |
|
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: 105.02 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 9 AQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRlTPNEm 85
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLgldAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS-SPAE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 86 knQMRSIdvqlifctlplelrgfqivslddIEFAGTDITMNDlmdntldiqydtlnetvvpkdspsnilntsfnIDDIAS 165
Cdd:cd05945 79 --RIREI-----------------------LDAAKPALLIAD--------------------------------GDDNAY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 166 IMFTSGTTGPQKAVPQTFRN--HYASAIgCKESLGFDHDtNWLSVLPiYHISgLSV--LLRAVIEGFTVRIVDK---FNA 238
Cdd:cd05945 102 IIFTSGSTGRPKGVQISHDNlvSFTNWM-LSDFPLGPGD-VFLNQAP-FSFD-LSVmdLYPALASGATLVPVPRdatADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 EQILTMIKNERITHISLVPQTLNWLMQQGLHEPH---DLQKILLGGAKLSATMIEtALQYNLP---IYNSFGMTET---C 309
Cdd:cd05945 178 KQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPEslpSLRHFLFCGEVLPHKTAR-ALQQRFPdarIYNTYGPTEAtvaV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 310 SQF-LTATPQMLHER-PdtVGMPSANVDVKVKN----PNKEGH-GELMIKGANVMNGYLYPTDLTDTF---ENGY--FNT 377
Cdd:cd05945 257 TYIeVTPEVLDGYDRlP--IGYAKPGAKLVILDedgrPVPPGEkGELVISGPSVSKGYLNNPEKTAAAffpDEGQraYRT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 378 GDIAEIDHEGYVmIYDRRKDLIIS-GGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSE--SDISKAQLI 454
Cdd:cd05945 335 GDLVRLEADGLL-FYRGRLDFQVKlNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKpgAEAGLTKAI 413
|
490 500 510
....*....|....*....|....*....|....*.
gi 1853634356 455 -AYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05945 414 kAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
275-428 |
3.25e-24 |
|
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: 105.90 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 275 QKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPQMLheRPDTVGMPSANVDVKVKNPNKEGHGELMIKGA 354
Cdd:cd05933 323 QKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAY--RLLSCGKALPGCKTKIHNPDADGIGEICFWGR 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1853634356 355 NVMNGYLYPTDLTDTF--ENGYFNTGDIAEIDHEGYVMIYDRRKDLII-SGGENIYPYQIE-TVAKQFPGISDAVCIG 428
Cdd:cd05933 401 HVFMGYLNMEDKTEEAidEDGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENVPPVPIEdAVKKELPIISNAMLIG 478
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
161-491 |
3.55e-24 |
|
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: 104.52 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGF-DHDTNWLSVLP------IYHISG------LSVLLRAvieG 227
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLrPEDSFWNAADPgwayglYYAITGplalghPTILLEG---G 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 228 FTVrivdkfnaEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHD----LQKILLGGAKLSATMIE-TALQYNLPIYNS 302
Cdd:cd05973 165 FSV--------ESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARpkgrLRRVSSAGEPLTPEVIRwFDAALGVPIHDH 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 303 FGMTE----TCSQFLTATPqmLHERPDTVGMPSANVDVKVKNPNKEGHGELMIKGANVMNGYL-----YPTDLTDTFENG 373
Cdd:cd05973 237 YGQTElgmvLANHHALEHP--VHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLmwfrgYQLPDTPAIDGG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-----SESDI 448
Cdd:cd05973 315 YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrgghEGTPA 394
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1853634356 449 SKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd05973 395 LADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
15-489 |
4.32e-24 |
|
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: 104.79 E-value: 4.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 15 HIAITDGQESYTYQNLYCEASLLARRLKA----YQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLtPNEMknqmr 90
Cdd:cd17648 3 RVAVVYGDKRLTYRELNERANRLAHYLLSvaeiRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSY-PDER----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 91 sidVQLIfctlpLELRGFQIVslddiefagtdITmndlmdntldiqydtlnetvvpkdspsnilntsfNIDDIASIMFTS 170
Cdd:cd17648 77 ---IQFI-----LEDTGARVV-----------IT----------------------------------NSTDLAYAIYTS 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 171 GTTGPQKAVPQTFRnhyaSAIGCKESL-----GFDHDTNWLSVLPIYhISGLSV--LLRAVIEGFTVRIVD---KFNAEQ 240
Cdd:cd17648 104 GTTGKPKGVLVEHG----SVVNLRTSLseryfGRDNGDEAVLFFSNY-VFDFFVeqMTLALLNGQKLVVPPdemRFDPDR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 241 ILTMIKNERITHISLVPQTLNwlmQQGLHEPHDLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETcSQFLTATPQM 319
Cdd:cd17648 179 FYAYINREKVTYLSGTPSVLQ---QYDLARLPHLKRVDAAGEEFTAPVFEKLRSrFAGLIINAYGPTET-TVTNHKRFFP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 320 LHERPD-TVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYLYPTDLT-DTF-ENGY--------------FNT 377
Cdd:cd17648 255 GDQRFDkSLGRPVRNTKCYVLNDAMKrvpvgAVGELYLGGDGVARGYLNRPELTaERFlPNPFqteqerargrnarlYKT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 378 GDIAEIDHEGYVMiYDRRKDLIIS-GGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKL-----YFVSESD-ISK 450
Cdd:cd17648 335 GDLVRWLPSGELE-YLGRNDFQVKiRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQkylvgYYLPEPGhVPE 413
|
490 500 510
....*....|....*....|....*....|....*....
gi 1853634356 451 AQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17648 414 SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
26-483 |
3.64e-23 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 103.51 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 26 TYQNLYCEASLLARRLKAY--QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFCTlpl 103
Cdd:PRK06814 660 TYRKLLTGAFVLGRKLKKNtpPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTS--- 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 104 elRGFqivslddIEFAGTDiTMNDLMDNTLDIQY-DTLNETVVPKDSPSNILNTSF--------NIDDIASIMFTSGTTG 174
Cdd:PRK06814 737 --RAF-------IEKARLG-PLIEALEFGIRIIYlEDVRAQIGLADKIKGLLAGRFplvyfcnrDPDDPAVILFTSGSEG 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 175 PQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIEGFTV---------RIVDKF----NAeQ 240
Cdd:PRK06814 807 TPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGgLVLPLLSGVKVflypsplhyRIIPELiydtNA-T 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 241 IL----TMIKN-ERITHislvpqtlnwlmqqglhePHD---LQKILLGGAKLSATMIET-ALQYNLPIYNSFGMTETCSQ 311
Cdd:PRK06814 886 ILfgtdTFLNGyARYAH------------------PYDfrsLRYVFAGAEKVKEETRQTwMEKFGIRILEGYGVTETAPV 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 312 FLTATPqmLHERPDTVGMPSANVDVKV-KNPNKEGHGELMIKGANVMNGYLYPTD--LTDTFENGYFNTGDIAEIDHEGY 388
Cdd:PRK06814 948 IALNTP--MHNKAGTVGRLLPGIEYRLePVPGIDEGGRLFVRGPNVMLGYLRAENpgVLEPPADGWYDTGDIVTIDEEGF 1025
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 389 VMIYDRRKDLIISGGENIYPYQIETVAKQF-PGISDAVcIGHPDDTWGQVPKLyFVSESDISKAQLIAYLSQH-LAKYKV 466
Cdd:PRK06814 1026 ITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHAA-VSIPDARKGERIIL-LTTASDATRAAFLAHAKAAgASELMV 1103
|
490
....*....|....*..
gi 1853634356 467 PKHFEKVDTLPYTSTGK 483
Cdd:PRK06814 1104 PAEIITIDEIPLLGTGK 1120
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
162-489 |
7.03e-23 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 101.76 E-value: 7.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQI 241
Cdd:PRK06155 181 DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGF 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 242 LTMIKNERITHISLVPQTLNWLMQQ--GLHEPHDLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPQm 319
Cdd:PRK06155 261 WPAVRRHGATVTYLLGAMVSILLSQpaRESDRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGS- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 320 lhERPDTVGMPSANVDVKVKNPNKEG-----HGELMIKGAN---VMNGYL-YPTDLTDTFENGYFNTGDIAEIDHEGYVM 390
Cdd:PRK06155 340 --QRPGSMGRLAPGFEARVVDEHDQElpdgePGELLLRADEpfaFATGYFgMPEKTVEAWRNLWFHTGDRVVRDADGWFR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 391 IYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSE--SDISKAQLIAYLSQHLAKYKVPK 468
Cdd:PRK06155 418 FVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRdgTALEPVALVRHCEPRLAYFAVPR 497
|
330 340
....*....|....*....|.
gi 1853634356 469 HFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06155 498 YVEFVAALPKTENGKVQKFVL 518
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
161-489 |
3.86e-22 |
|
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: 99.08 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISG-LSVLLRAVIEGFTVrivdkFNAE 239
Cdd:cd05932 137 EQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTErVFVEGGSLYGGVLV-----AFAE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMI---KNERITHISLVPQTlnW-LMQQGLHEPHDLQK--ILL---------------------------GGAKLSA 286
Cdd:cd05932 212 SLDTFVedvQRARPTLFFSVPRL--WtKFQQGVQDKIPQQKlnLLLkipvvnslvkrkvlkglgldqcrlagcGSAPVPP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 287 TMIETALQYNLPIYNSFGMTETCSQFLTATPqmLHERPDTVGMPSANVDVKVKNpnkegHGELMIKGANVMNG-YLYPTD 365
Cdd:cd05932 290 ALLEWYRSLGLNILEAYGMTENFAYSHLNYP--GRDKIGTVGNAGPGVEVRISE-----DGEILVRSPALMMGyYKDPEA 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 366 LTDTF-ENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETVAKQFPGIsDAVCI---GHPDDTWGQVPKL 440
Cdd:cd05932 363 TAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRV-EMVCVigsGLPAPLALVVLSE 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 441 YFVSESDIS-KAQLIAYLSQHLAkyKVPKHFEK---------------VDTLPYTSTGKLQRNKL 489
Cdd:cd05932 442 EARLRADAFaRAELEASLRAHLA--RVNSTLDSheqlagivvvkdpwsIDNGILTPTLKIKRNVL 504
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-489 |
4.86e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 100.62 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIhacwLANIEIAMINTRLTPNE 84
Cdd:PRK12467 521 QARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAgvgPDVLVGIAVERSIEMVVGL----LAVLKAGGAYVPLDPEY 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 85 mknqmrsidvqlifctlPLELRGFQivsLDD--IEFAGTDITMNDLMDNTLDIQYDTLNETVVPKDSPSNiLNTSFNID- 161
Cdd:PRK12467 597 -----------------PQDRLAYM---LDDsgVRLLLTQSHLLAQLPVPAGLRSLCLDEPADLLCGYSG-HNPEVALDp 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 -DIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDK---FN 237
Cdd:PRK12467 656 dNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRD 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLVPQTLNWLMQQGLHE-PHDLQKILLGGAKLSATMIET--ALQYNLPIYNSFGMTETC--SQF 312
Cdd:PRK12467 736 AEAFAALMADQGVTVLKIVPSHLQALLQASRVAlPRPQRALVCGGEALQVDLLARvrALGPGARLINHYGPTETTvgVST 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 313 LTATPQMLHERPDTVGMPSANVDVKV----KNPNKEG-HGELMIKGANVMNGYLYPTDLT------DTF-ENG--YFNTG 378
Cdd:PRK12467 816 YELSDEERDFGNVPIGQPLANLGLYIldhyLNPVPVGvVGELYIGGAGLARGYHRRPALTaerfvpDPFgADGgrLYRTG 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 379 DIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQ-----VPKLYFVS-ESDISKAQ 452
Cdd:PRK12467 896 DLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQlvaylVPAAVADGaEHQATRDE 975
|
490 500 510
....*....|....*....|....*....|....*..
gi 1853634356 453 LIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK12467 976 LKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
162-491 |
5.47e-22 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 98.66 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 162 DIASIMFTSGTTGPQKAVPQTFRNHY--ASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAV-IEGFTVRIVDKFNA 238
Cdd:cd05915 154 AACGMAYTTGTTGLPKGVVYSHRALVlhSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATlVGAKQVLPGPRLDP 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 EQILTMIKNERITHISLVPQTLNWLM--QQGLHE--PHDLQkILLGGAKLSATMIETALQYNLPIYNSFGMTET------ 308
Cdd:cd05915 234 ASLVELFDGEGVTFTAGVPTVWLALAdyLESTGHrlKTLRR-LVVGGSAAPRSLIARFERMGVEVRQGYGLTETspvvvq 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 C-------------SQFLTATPQMLH-------ERPDTVGMPSANVDVKVknpnkeghgeLMIKGANVMNGYLYPTDLTD 368
Cdd:cd05915 313 NfvkshleslseeeKLTLKAKTGLPIplvrlrvADEEGRPVPKDGKALGE----------VQLKGPWITGGYYGNEEATR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 369 T--FENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYF-VSE 445
Cdd:cd05915 383 SalTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVvPRG 462
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1853634356 446 SDISKAQLIAYLSQHLAKYK-VPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd05915 463 EKPTPEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
161-489 |
1.45e-21 |
|
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: 97.05 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQtfrNHYASAIGCKESLGFDHDTNWLSVLPIYHIS---GLSVLLRAVIEGFTVRIVDK-- 235
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAV---SHGPLAAHCQATAERYGLTPGDRELQFASFNfdgAHEQLLPPLICGACVVLRPDel 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 236 -FNAEQILTMIKNERITHISLVP----QTLNWLMQQGLHEPHDLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETcs 310
Cdd:cd17649 171 wASADELAEMVRELGVTVLDLPPaylqQLAEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEA-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 311 qflTATPQMLHERPDT----VGMP--------SANVDVKVKNPNKEGH-GELMIKGANVMNGYLYPTDLT-DTF-ENGYF 375
Cdd:cd17649 249 ---TVTPLVWKCEAGAaragASMPigrplggrSAYILDADLNPVPVGVtGELYIGGEGLARGYLGRPELTaERFvPDPFG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 376 N-------TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKlYFVSESDI 448
Cdd:cd17649 326 ApgsrlyrTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVA-YVVLRAAA 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1853634356 449 SKAQLIAYLSQHLAK----YKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17649 405 AQPELRAQLRTALRAslpdYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
8-489 |
2.14e-21 |
|
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: 96.74 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANieiamintrltpne 84
Cdd:cd17644 9 QVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLgvkSESLVGICVERSLEMIIGLLAILKAG-------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 85 mknqmrsidvqlifctlplelrGFQIVslddiefagtditmndlmdntLDIQYDTLNETVVPKDSPSNILNTsfNIDDIA 164
Cdd:cd17644 75 ----------------------GAYVP---------------------LDPNYPQERLTYILEDAQISVLLT--QPENLA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 165 SIMFTSGTTGPQKAV---PQTFRNHYASAI-----------GCKESLGFDhdtnwLSVLPIYH--ISGLSVLLRAViegf 228
Cdd:cd17644 110 YVIYTSGSTGKPKGVmieHQSLVNLSHGLIkeygitssdrvLQFASIAFD-----VAAEEIYVtlLSGATLVLRPE---- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 229 TVRivdkFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHE----PHDLQKILLGGAKLSATMIET---ALQYNLPIYN 301
Cdd:cd17644 181 EMR----SSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLStidlPSSLRLVIVGGEAVQPELVRQwqkNVGNFIQLIN 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 302 SFGMTE-----TCSQFLTATPQMLHERPdtVGMPSANVDVKVKNPNK-----EGHGELMIKGANVMNGYLYPTDLT---- 367
Cdd:cd17644 257 VYGPTEatiaaTVCRLTQLTERNITSVP--IGRPIANTQVYILDENLqpvpvGVPGELHIGGVGLARGYLNRPELTaekf 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 --DTFENGYFN----TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLY 441
Cdd:cd17644 335 isHPFNSSESErlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAY 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1853634356 442 FV--SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17644 415 IVphYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
161-489 |
5.07e-21 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 95.40 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNA-- 238
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELlp 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 -EQILTMIKNERITHISLVPQTLNWLMQQGLhePhDLQKILLGGAKLSATMIETALQYNLpIYNSFGMTET--CSqflTA 315
Cdd:cd17652 173 gEPLADLLREHRITHVTLPPAALAALPPDDL--P-DLRTLVVAGEACPAELVDRWAPGRR-MINAYGPTETtvCA---TM 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 316 TPQMLHERPDTVGMPSANVDVKVKNPNKE----G-HGELMIKGANVMNGYLYPTDLT------DTF----ENGYfNTGDI 380
Cdd:cd17652 246 AGPLPGGGVPPIGRPVPGTRVYVLDARLRpvppGvPGELYIAGAGLARGYLNRPGLTaerfvaDPFgapgSRMY-RTGDL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 381 AEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESD--ISKAQLIAYLS 458
Cdd:cd17652 325 ARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLA 404
|
330 340 350
....*....|....*....|....*....|.
gi 1853634356 459 QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17652 405 ERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
161-491 |
7.55e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 94.56 E-value: 7.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDH-DTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVD--KFN 237
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPgDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNyaRFD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLVPQTLNWLMQQGLHEPH-DLQKILLGGAKLSATMIETALQ-YNLPIYNSFGMTETCSQFLTA 315
Cdd:cd05974 165 AKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDvKLREVVGAGEPLNPEVIEQVRRaWGLTIRDGYGQTETTALVGNS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 316 TPQMLheRPDTVGMPSANVDVKV----KNPNKEGHGELMI---KGANVMNGYLY-PTDLTDTFENGYFNTGDIAEIDHEG 387
Cdd:cd05974 245 PGQPV--KAGSMGRPLPGYRVALldpdGAPATEGEVALDLgdtRPVGLMKGYAGdPDKTAHAMRGGYYRTGDIAMRDEDG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 388 YVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-----SESDISKAQLIAYLSQHLA 462
Cdd:cd05974 323 YLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyEPSPETALEIFRFSRERLA 402
|
330 340
....*....|....*....|....*....
gi 1853634356 463 KYKVPKHFEKVDtLPYTSTGKLQRNKLYR 491
Cdd:cd05974 403 PYKRIRRLEFAE-LPKTISGKIRRVELRR 430
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-491 |
1.13e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.18 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNE 84
Cdd:PRK12316 3066 QVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERgvgPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEER 3145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 85 MKNQMRSIDVQLIFCTLPLELRGFQIVSLDDIEFAGTDITMNDLMDNTLDiqydtlnetvvpkdspsnilntsfniDDIA 164
Cdd:PRK12316 3146 LAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMP--------------------------ENLA 3199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 165 SIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNA---EQI 241
Cdd:PRK12316 3200 YVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWrdpALL 3279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 242 LTMIKNERITHISLVPQTLNWLMQQ-GLHEPHDLQKILLGGAKLSATMIETALQyNLPIYNSFGMTETCSQFLTATPQML 320
Cdd:PRK12316 3280 VELINSEGVDVLHAYPSMLQAFLEEeDAHRCTSLKRIVCGGEALPADLQQQVFA-GLPLYNLYGPTEATITVTHWQCVEE 3358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 321 HERPDTVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYLYPTDLT------DTFENG--YFNTGDIAEIDHEG 387
Cdd:PRK12316 3359 GKDAVPIGRPIANRACYILDGSLEpvpvgALGELYLGGEGLARGYHNRPGLTaerfvpDPFVPGerLYRTGDLARYRADG 3438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 388 YVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIghpdDTWGQVPKLYFVSESDISKAQ--LIAYLSQHLAKYK 465
Cdd:PRK12316 3439 VIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGDLReaLKAHLKASLPEYM 3514
|
490 500
....*....|....*....|....*.
gi 1853634356 466 VPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK12316 3515 VPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-489 |
1.70e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.79 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLtPNE 84
Cdd:PRK12316 520 QVERTPEAPALAFGEETLDYAELNRRANRLAHALIERgvgPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY-PAE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 85 MKNQM-RSIDVQLIFC------TLPLElRGFQIVSLDDI--EFAGtditmndlmdntldiqydtlnetvvpkdSPSNILN 155
Cdd:PRK12316 599 RLAYMlEDSGVQLLLSqshlgrKLPLA-AGVQVLDLDRPaaWLEG----------------------------YSEENPG 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 156 TSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIV-- 233
Cdd:PRK12316 650 TELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAap 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 234 -DKFNAEQILTMIKNERITHISLVPQTLNWLMQ-QGLHEPHDLQKILLGGAKLSATMIETALQyNLP---IYNSFGMTEt 308
Cdd:PRK12316 730 gDHRDPAKLVELINREGVDTLHFVPSMLQAFLQdEDVASCTSLRRIVCSGEALPADAQEQVFA-KLPqagLYNLYGPTE- 807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 csqfltATPQMLH-----ERPDTV--GMPSANVDVKV----KNPNKEG-HGELMIKGANVMNGYLYPTDLT------DTF 370
Cdd:PRK12316 808 ------AAIDVTHwtcveEGGDSVpiGRPIANLACYIldanLEPVPVGvLGELYLAGRGLARGYHGRPGLTaerfvpSPF 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 371 ENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPddtwGQVPKLYFVSESD- 447
Cdd:PRK12316 882 VAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEg 957
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1853634356 448 -ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK12316 958 gDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
161-489 |
3.96e-20 |
|
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: 92.77 E-value: 3.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHdtnWLSVLPIYHIS-GLSV--LLRAVIEGFTVRIVDkfN 237
Cdd:cd12115 105 DDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEE---LAGVLASTSICfDLSVfeLFGPLATGGKVVLAD--N 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLVPQTLNWLMQQGLHePHDLQKILLGGAKLSATMIETaLQYNLP---IYNSFGMTE--TCSQF 312
Cdd:cd12115 180 VLALPDLPAAAEVTLINTVPSAAAELLRHDAL-PASVRVVNLAGEPLPRDLVQR-LYARLQverVVNLYGPSEdtTYSTV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 313 LTATPQmlHERPDTVGMPSANVDVKV----KNPNKEG-HGELMIKGANVMNGYLYPTDLT------DTFENG--YFNTGD 379
Cdd:cd12115 258 APVPPG--ASGEVSIGRPLANTQAYVldraLQPVPLGvPGELYIGGAGVARGYLGRPGLTaerflpDPFGPGarLYRTGD 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 380 IAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSE--SDISKAQLIAYL 457
Cdd:cd12115 336 LVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEpgAAGLVEDLRRHL 415
|
330 340 350
....*....|....*....|....*....|..
gi 1853634356 458 SQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd12115 416 GTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
161-486 |
6.68e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 92.65 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTG-P------QKAVPQtfrnHYASAigcKESLGF-DHDTNWLSVLPIYhISGLSV-----LLRAVieg 227
Cdd:PRK04319 205 EDGAILHYTSGSTGkPkgvlhvHNAMLQ----HYQTG---KYVLDLhEDDVYWCTADPGW-VTGTSYgifapWLNGA--- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 228 ftVRIVD--KFNAEQILTMIKNERITHISLVPQTLNWLMQQG--LHEPHD---LQKILLGGAKLSATMIETALQ-YNLPI 299
Cdd:PRK04319 274 --TNVIDggRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddLVKKYDlssLRHILSVGEPLNPEVVRWGMKvFGLPI 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 300 YNSFGMTETCSQFLTATPQMlHERPDTVGMPSANVDVK-VKN------PNKEGhgELMIKGA--NVMNGYLY-PTDLTDT 369
Cdd:PRK04319 352 HDNWWMTETGGIMIANYPAM-DIKPGSMGKPLPGIEAAiVDDqgnelpPNRMG--NLAIKKGwpSMMRGIWNnPEKYESY 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 370 FENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLyFVS----- 444
Cdd:PRK04319 429 FAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKA-FVAlrpgy 507
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1853634356 445 -ESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK04319 508 ePSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMR 550
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-491 |
6.77e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 93.69 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 8 QAQQNGHHIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNE 84
Cdd:PRK12467 1583 QAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALgvgPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRER 1662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 85 MKNQMRSIDVQLIFCTLPLELR-----GFQIVSLDDIefagtditmNDLMDNtldiqydtlnetvvpkDSPSN-ILNTSf 158
Cdd:PRK12467 1663 LAYMIEDSGIELLLTQSHLQARlplpdGLRSLVLDQE---------DDWLEG----------------YSDSNpAVNLA- 1716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 159 nIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWL---------SVLPIYH--ISGLSVLLRAVIEg 227
Cdd:PRK12467 1717 -PQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLqftsfafdvSVWELFWplINGARLVIAPPGA- 1794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 228 ftvrivdKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLH--EPHDLQKILLGGAKLSATMIETALQyNLP---IYNS 302
Cdd:PRK12467 1795 -------HRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQveHPLSLRRVVCGGEALEVEALRPWLE-RLPdtgLFNL 1866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 303 FGMTETCSQFL--TATPQMLHERPDT-VGMPSANVDVKVK----NPNKEG-HGELMIKGANVMNGYLYPTDLT------D 368
Cdd:PRK12467 1867 YGPTETAVDVThwTCRRKDLEGRDSVpIGQPIANLSTYILdaslNPVPIGvAGELYLGGVGLARGYLNRPALTaerfvaD 1946
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 369 TFENG---YFNTGDIAE------------IDHEgyVMIYDRRKDLiisgGEniypyqIETVAKQFPGISDAVCIGHpDDT 433
Cdd:PRK12467 1947 PFGTVgsrLYRTGDLARyradgvieylgrIDHQ--VKIRGFRIEL----GE------IEARLREQGGVREAVVIAQ-DGA 2013
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1853634356 434 WGQ------VPKLYFVSESDI----SKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK12467 2014 NGKqlvayvVPTDPGLVDDDEaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
7-489 |
4.89e-19 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 89.93 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 7 KQAQQNGHHIAITDGQESYTYQnlycEASLLARRLKAYQQSR-------VGLYIDNSIQSIilihACWLANIEI----AM 75
Cdd:PRK08279 45 EAAARHPDRPALLFEDQSISYA----ELNARANRYAHWAAARgvgkgdvVALLMENRPEYL----AAWLGLAKLgavvAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 76 INTRLTPNEMKNQMRSIDVQLI---------FCTLPLELRGFQIVSLDDIEFAGTDITMNDLMDntLDIQYDTLNetvvp 146
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLivgeelveaFEEARADLARPPRLWVAGGDTLDDPEGYEDLAA--AAAGAPTTN----- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 147 KDSPSNILntsfnIDDIASIMFTSGTTGPQKAVPQTfrnHY---ASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRA 223
Cdd:PRK08279 190 PASRSGVT-----AKDTAFYIYTSGTTGLPKAAVMS---HMrwlKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 224 VI-EGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHE---PHDLQKILlgGAKLSATMIETALQY---- 295
Cdd:PRK08279 262 VLaAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPtdrDHRLRLMI--GNGLRPDIWDEFQQRfgip 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 296 -----------NLPIYNSFGMTETC--SQFLTATPQMLHE-RPDTvGMPSANVD---VKVKnpnKEGHGEL--MIKGANV 356
Cdd:PRK08279 340 rilefyaasegNVGFINVFNFDGTVgrVPLWLAHPYAIVKyDVDT-GEPVRDADgrcIKVK---PGEVGLLigRITDRGP 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 357 MNGYlypTD--------LTDTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVc 426
Cdd:PRK08279 416 FDGY---TDpeasekkiLRDVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAV- 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 427 ighpddTWG-QVP-----------KLYFVSESDIskAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK08279 492 ------VYGvEVPgtdgragmaaiVLADGAEFDL--AALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDL 558
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
152-491 |
7.44e-19 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 88.95 E-value: 7.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 152 NILNTSFNIDDIASIMFTSGTTG-PQKAVPQTFRNHYASAIGCKESLGFDHDTNWlSVLPIYHISGLSVLLRAVI-EGFT 229
Cdd:cd05940 72 NVSSAKHLVVDAALYIYTSGTTGlPKAAIISHRRAWRGGAFFAGSGGALPSDVLY-TCLPLYHSTALIVGWSACLaSGAT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 230 VRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHE---PHDLQKILlgGAKLSATMIETAL-QYNLP-IYNSFG 304
Cdd:cd05940 151 LVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPterKHKVRMIF--GNGLRPDIWEEFKeRFGVPrIAEFYA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 305 MTETCSQFLTatpqmLHERPDTVG---------MPSANV--DVKVKNP--NKEGH---------GELM--IKGANVMNGY 360
Cdd:cd05940 229 ATEGNSGFIN-----FFGKPGAIGrnpsllrkvAPLALVkyDLESGEPirDAEGRcikvprgepGLLIsrINPLEPFDGY 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 361 LYPTD-----LTDTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHP-DD 432
Cdd:cd05940 304 TDPAAtekkiLRDVFKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPG 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1853634356 433 TWGQ--VPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd05940 384 TDGRagMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
166-486 |
1.00e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 88.17 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 166 IMFTSGTTGPQKAVPQTFRN------HYASAIGCKEslgfdhDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIVDKFNA 238
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEidreieAYNEALNCEQ------DETPIVACPVTHSYGLiCGVLAALTRGSKPVIITNKNP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 EQILTMIKNERiTHISLVPQTLNWLMQQGLHEPHDLQKILLGGAKLSATMIETALQYNLPIYNSFGMTET-CsqfLTATP 317
Cdd:PRK08308 180 KFALNILRNTP-QHILYAVPLMLHILGRLLPGTFQFHAVMTSGTPLPEAWFYKLRERTTYMMQQYGCSEAgC---VSICP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 318 QMlhERPDTVGMPSANVDVKVkNPNKEGHGELMIKganvmngylyptdlTDTFEngyFNTGDIAEIDHEGYVMIYDRRKD 397
Cdd:PRK08308 256 DM--KSHLDLGNPLPHVSVSA-GSDENAPEEIVVK--------------MGDKE---IFTKDLGYKSERGTLHFMGRMDD 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 398 LIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLP 477
Cdd:PRK08308 316 VINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIP 395
|
....*....
gi 1853634356 478 YTSTGKLQR 486
Cdd:PRK08308 396 KNANGKVSR 404
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
5-484 |
1.06e-18 |
|
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: 89.17 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 5 LYKQAQQNGHHIA-ITDGQE-----SYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHACWLANIEIAM 75
Cdd:cd17634 59 LDRHLRENGDRTAiIYEGDDtsqsrTISYRELHREVCRFAGTLLDLgvkKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 76 INTRLTPNEMKNQMRSIDVQLIFcTLPLELRGFQIVSL-----DDIEFAGTDITMNDLMDNT---------LDIQYDTLN 141
Cdd:cd17634 139 IFGGFAPEAVAGRIIDSSSRLLI-TADGGVRAGRSVPLkknvdDALNPNVTSVEHVIVLKRTgsdidwqegRDLWWRDLI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 142 ETVVPKDSPSNIlntsfNIDDIASIMFTSGTTGPQKAV-----------PQTFRNHYASAIG----CKESLGFDHDTNWL 206
Cdd:cd17634 218 AKASPEHQPEAM-----NAEDPLFILYTSGTTGKPKGVlhttggylvyaATTMKYVFDYGPGdiywCTADVGWVTGHSYL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 207 SVLPIyhISGLSVLLravIEGftvrIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLH--EPHDLQKI-LLGGA- 282
Cdd:cd17634 293 LYGPL--ACGATTLL---YEG----VPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDaiEGTDRSSLrILGSVg 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 283 -----KLSATMIETALQYNLPIYNSFGMTETCSQFLTATPQMLHERPDT-----VGMPSANVDVKvKNPNKEGH-GELMI 351
Cdd:cd17634 364 epinpEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSatrpvFGVQPAVVDNE-GHPQPGGTeGNLVI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 352 kGANVMNGYL--------YPTDLTDTFENGYFnTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISD 423
Cdd:cd17634 443 -TDPWPGQTRtlfgdherFEQTYFSTFKGMYF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE 520
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1853634356 424 AVCIGHPDDTWGQVPKLYFV-----SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKL 484
Cdd:cd17634 521 AAVVGIPHAIKGQAPYAYVVlnhgvEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
144-486 |
2.62e-18 |
|
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: 87.68 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 144 VVPKDSPSNILNTSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGL-SVLLR 222
Cdd:cd05931 132 LLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLiGGLLT 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 223 AVIEGFT---------VRivdkfNAEQILTMIKNERITHiSLVP-----QTLNWLMQQGLhEPHDLQ--KILLGGAK--L 284
Cdd:cd05931 212 PLYSGGPsvlmspaafLR-----RPLRWLRLISRYRATI-SAAPnfaydLCVRRVRDEDL-EGLDLSswRVALNGAEpvR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 285 SATM---IETALQYNLP---IYNSFGMTETC----SQFLTATPQMLHERPD--------------------TVGMPSANV 334
Cdd:cd05931 285 PATLrrfAEAFAPFGFRpeaFRPSYGLAEATlfvsGGPPGTGPVVLRVDRDalagravavaaddpaarelvSCGRPLPDQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 335 DVKVKNPN-----KEGH-GELMIKGANVMNGYLYPTDLTD-TF-------ENGYFNTGDIAEIdHEGYVMIYDRRKDLII 400
Cdd:cd05931 365 EVRIVDPEtgrelPDGEvGEIWVRGPSVASGYWGRPEATAeTFgalaatdEGGWLRTGDLGFL-HDGELYITGRLKDLII 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 401 SGGENIYPYQIETVAKQFPG---ISDAVCIGHPDDtwgQVPKLYFVSESDISK-----AQLIAYLSQHLAK-YKVPKH-- 469
Cdd:cd05931 444 VRGRNHYPQDIEATAEEAHPalrPGCVAAFSVPDD---GEERLVVVAEVERGAdpadlAAIAAAIRAAVAReHGVAPAdv 520
|
410
....*....|....*...
gi 1853634356 470 -FEKVDTLPYTSTGKLQR 486
Cdd:cd05931 521 vLVRPGSIPRTSSGKIQR 538
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
161-489 |
2.69e-18 |
|
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: 87.33 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQK--AVPQT--------FRNHY----ASAIGCKESLGFDhdtnwLSV----LPIyhISGLSVLLr 222
Cdd:cd17646 138 DNLAYVIYTSGSTGRPKgvMVTHAgivnrllwMQDEYplgpGDRVLQKTPLSFD-----VSVwelfWPL--VAGARLVV- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 223 AVIEGFTvrivdkfNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHD-LQKILLGGAKLSATMIETALQ-YNLPIY 300
Cdd:cd17646 210 ARPGGHR-------DPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSCAsLRRVFCSGEALPPELAARFLAlPGAELH 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 301 NSFGMTEtcsqfltATPQMLHE--RPDT------VGMPSANVDVKVKNPnkEGH-------GELMIKGANVMNGYLYPTD 365
Cdd:cd17646 283 NLYGPTE-------AAIDVTHWpvRGPAetpsvpIGRPVPNTRLYVLDD--ALRpvpvgvpGELYLGGVQLARGYLGRPA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 366 LT------DTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQV 437
Cdd:cd17646 354 LTaerfvpDPFGPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAAR 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 438 PKLYFVSESD---ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17646 434 LVGYVVPAAGaagPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
4-489 |
3.25e-18 |
|
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: 87.21 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 4 WLYKQAQQNGHHIAI--TDGqeSYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQSIILIHA------CWLAnIE 72
Cdd:cd05918 4 LIEERARSQPDAPAVcaWDG--SLTYAELDRLSSRLAHHLRSLgvgPGVFVPLCFEKSKWAVVAMLAvlkaggAFVP-LD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 73 IAMINTRLtpnemKNQMRSIDVQLIFCTLPlelrgfqivslddiefagtditmndlmdntldiqydtlnetvvpkdspsn 152
Cdd:cd05918 81 PSHPLQRL-----QEILQDTGAKVVLTSSP-------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 153 ilntsfniDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWL---------SVLPIyhisgLSVLLRa 223
Cdd:cd05918 106 --------SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqfasytfdvSILEI-----FTTLAA- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 224 vieGFTVRI---VDKFN--AEQILTMikneRITHISLVPQTLNWLmqqglhEPHD---LQKILLGGAKLSATMIET-ALQ 294
Cdd:cd05918 172 ---GGCLCIpseEDRLNdlAGFINRL----RVTWAFLTPSVARLL------DPEDvpsLRTLVLGGEALTQSDVDTwADR 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 295 YNLpiYNSFGMTEtCSQFLTATPQMLHERPDTVGMPSANVD--VKVKNPNKEGH----GELMIKGANVMNGYL------- 361
Cdd:cd05918 239 VRL--INAYGPAE-CTIAATVSPVVPSTDPRNIGRPLGATCwvVDPDNHDRLVPigavGELLIEGPILARGYLndpekta 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 362 --YPTDLTDTFENGY------FNTGDIAEIDHEGyVMIYDRRKD--LIISG-----GEniypyqIE-TVAKQFPGISD-- 423
Cdd:cd05918 316 aaFIEDPAWLKQEGSgrgrrlYRTGDLVRYNPDG-SLEYVGRKDtqVKIRGqrvelGE------IEhHLRQSLPGAKEvv 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 424 ----------------AVCIGHPDDTWGQVPKLYFVSESD---ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKL 484
Cdd:cd05918 389 vevvkpkdgssspqlvAFVVLDGSSSGSGDGDSLFLEPSDefrALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKI 468
|
....*
gi 1853634356 485 QRNKL 489
Cdd:cd05918 469 DRRAL 473
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
35-429 |
4.14e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 87.41 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 35 SLLARRLKAyqQSRVGLYIDNSIQSIILIHACWLANIEIAMIntrlTPN---------EMKNQMRSIDVQLIFC-TLPLE 104
Cdd:PRK12582 96 ALLDLGLDP--GRPVMILSGNSIEHALMTLAAMQAGVPAAPV----SPAyslmshdhaKLKHLFDLVKPRVVFAqSGAPF 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 105 LRGFQIVSLDDIEFagtdITMNDLMDNTLDIQYDTLNETVVPKDSPSNIlnTSFNIDDIASIMFTSGTTGPQKAVPQTFR 184
Cdd:PRK12582 170 ARALAALDLLDVTV----VHVTGPGEGIASIAFADLAATPPTAAVAAAI--AAITPDTVAKYLFTSGSTGMPKAVINTQR 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 185 NHYASAIGCKESLGFDHDT------NWlsvLPIYHISGLSVLLRAV-IEGFTVRIVD-KFNAEQILTMIKNER---ITHI 253
Cdd:PRK12582 244 MMCANIAMQEQLRPREPDPpppvslDW---MPWNHTMGGNANFNGLlWGGGTLYIDDgKPLPGMFEETIRNLReisPTVY 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 254 SLVPQTLNWL---MQQ--GLHEP--HDLQKILLGGAKLS----ATMIETALQ---YNLPIYNSFGMTETcsqflTATPQM 319
Cdd:PRK12582 321 GNVPAGYAMLaeaMEKddALRRSffKNLRLMAYGGATLSddlyERMQALAVRttgHRIPFYTGYGATET-----APTTTG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 320 LH---ERPDTVGMPSANVDVKVKnPNKEGHgELMIKGANVMNGYLYPTDLT-DTF-ENGYFNTGDIAE-IDHEGYV--MI 391
Cdd:PRK12582 396 THwdtERVGLIGLPLPGVELKLA-PVGDKY-EVRVKGPNVTPGYHKDPELTaAAFdEEGFYRLGDAARfVDPDDPEkgLI 473
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1853634356 392 YDRR--KDLIISGGE--NIYPYQIETVAKQFPGISDAVCIGH 429
Cdd:PRK12582 474 FDGRvaEDFKLSTGTwvSVGTLRPDAVAACSPVIHDAVVAGQ 515
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
15-486 |
5.75e-18 |
|
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: 86.17 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 15 HIAITDGQESYTYQNLYCEASLLARRLKAY---QQSRVGLYIDNSIQ------SIILIHACWLanieiamintrltpnem 85
Cdd:cd12114 3 ATAVICGDGTLTYGELAERARRVAGALKAAgvrPGDLVAVTLPKGPEqvvavlGILAAGAAYV----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 86 knqmrSIDVQLifctlPLElRGFQIVSLDDIEFAGTDitmnDLMDNTLDIQYDTLNETVVPKDSPSNILNTSFNIDDIAS 165
Cdd:cd12114 66 -----PVDIDQ-----PAA-RREAILADAGARLVLTD----GPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 166 IMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSV------LPIYHISGLsvlLRAvieGFTVRIVD---KF 236
Cdd:cd12114 131 VIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALsslsfdLSVYDIFGA---LSA---GATLVLPDearRR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 237 NAEQILTMIKNERITHISLVPQ----TLNWLMQQGLHePHDLQKILLGG----AKLSATMieTALQYNLPIYNSFGMTET 308
Cdd:cd12114 205 DPAHWAELIERHGVTLWNSVPAllemLLDVLEAAQAL-LPSLRLVLLSGdwipLDLPARL--RALAPDARLISLGGATEA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 C--SQFLTATPQMLHERPDTVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYLYPTDLTDT-FEN-----GYF 375
Cdd:cd12114 282 SiwSIYHPIDEVPPDWRSIPYGRPLANQRYRVLDPRGRdcpdwVPGELWIGGRGVALGYLGDPELTAArFVThpdgeRLY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 376 NTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTwgqVPKL--YFVSESD---ISK 450
Cdd:cd12114 362 RTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG---GKRLaaFVVPDNDgtpIAP 438
|
490 500 510
....*....|....*....|....*....|....*.
gi 1853634356 451 AQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:cd12114 439 DALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
161-421 |
1.76e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 85.05 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTN-WLSVLPIYH----ISGLSVLLRAVIEGFTVRIVDk 235
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDvMVSWLPLFHdmgmVGFLTVPMYFGAELVKVTPMD- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 236 FNAEQIL--TMIKNERIThISLVPqtlNW--------LMQQGLHEPHDLQ--KILLGGAKL--SATM---IETALQYNLP 298
Cdd:PRK07768 231 FLRDPLLwaELISKYRGT-MTAAP---NFayallarrLRRQAKPGAFDLSslRFALNGAEPidPADVedlLDAGARFGLR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 299 ---IYNSFGMTET------------------CSQFLTATPQML-----HERP-DTVGMPSANVDVKV-----KNPNKEGH 346
Cdd:PRK07768 307 peaILPAYGMAEAtlavsfspcgaglvvdevDADLLAALRRAVpatkgNTRRlATLGPPLPGLEVRVvdedgQVLPPRGV 386
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1853634356 347 GELMIKGANVMNGYLY---PTDLTDtfENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGI 421
Cdd:PRK07768 387 GVIELRGESVTPGYLTmdgFIPAQD--ADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGV 462
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
131-433 |
2.42e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 85.16 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 131 NTLDIQYDTLNETVVPKDSPSNILNTSFNI-----DDIASIMFTSGTTGPQKAVPQTFRNHYASAIG-CKES--LGFDHD 202
Cdd:PTZ00342 269 KDLKEKAKKLGISIILFDDMTKNKTTNYKIqnedpDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPlCKHSifKKYNPK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 203 TNwLSVLPIYHISGLSVLLRAVIEGFTVRIVDK-------------------------------------------FNAE 239
Cdd:PTZ00342 349 TH-LSYLPISHIYERVIAYLSFMLGGTINIWSKdinyfskdiynskgnilagvpkvfnriytnimteinnlpplkrFLVK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 240 QILTMIKN----------ERITHISL-VPQTLNwlmqqglhePhDLQKILLGGAKLSATMI-ETALQYNLPIYNSFGMTE 307
Cdd:PTZ00342 428 KILSLRKSnnnggfskflEGITHISSkIKDKVN---------P-NLEVILNGGGKLSPKIAeELSVLLNVNYYQGYGLTE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 308 TCSQFLTAtpQMLHERPDTVGMP-SANVDVKVK---------NPNKeghGELMIKGANVMNGYLYPTDLTD-TF-ENGYF 375
Cdd:PTZ00342 498 TTGPIFVQ--HADDNNTESIGGPiSPNTKYKVRtwetykatdTLPK---GELLIKSDSIFSGYFLEKEQTKnAFtEDGYF 572
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1853634356 376 NTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETVAKQFPGISDavCIGHPDDT 433
Cdd:PTZ00342 573 KTGDIVQINKNGSLTFLDRSKGLVkLSQGEYIETDMLNNLYSQISFINF--CVVYGDDS 629
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
24-486 |
4.42e-17 |
|
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: 84.08 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 24 SYTYQNLYCEASLLA---RRLKAYQQSRVGLYIDnSIQSIILIhacWLANIEIAMI-------------NTRLTPNEMKn 87
Cdd:cd05968 91 TLTYGELLYEVKRLAnglRALGVGKGDRVGIYLP-MIPEIVPA---FLAVARIGGIvvpifsgfgkeaaATRLQDAEAK- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 88 qmrsidvqLIFCTLPLELRGFQIVSLDDIEFA-----GTD-------ITMNDLMDNTLDIQYDTLNETVVPKDSPSNIln 155
Cdd:cd05968 166 --------ALITADGFTRRGREVNLKEEADKAcaqcpTVEkvvvvrhLGNDFTPAKGRDLSYDEEKETAGDGAERTES-- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 156 tsfniDDIASIMFTSGTTGPQKAvpqTFRNHYASAIGCKESLGFDHDTN------WLSVLPiyHISGLSVLLRAVIEGFT 229
Cdd:cd05968 236 -----EDPLMIIYTSGTTGKPKG---TVHVHAGFPLKAAQDMYFQFDLKpgdlltWFTDLG--WMMGPWLIFGGLILGAT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 230 VRIVDKF----NAEQILTMIKNERITHISLVPQTLNWLMQQGLH--EPHDLQKILLGGAKLSAT-------MIETALQYN 296
Cdd:cd05968 306 MVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKPRGDApvNAHDLSSLRVLGSTGEPWnpepwnwLFETVGKGR 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 297 LPIYNSFGMTETC--------------SQFLTATPqmlherpdtvGMPSANVDVKvKNPNKEGHGEL--------MIKG- 353
Cdd:cd05968 386 NPIINYSGGTEISggilgnvlikpikpSSFNGPVP----------GMKADVLDES-GKPARPEVGELvllapwpgMTRGf 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 354 ----ANVMNGYLyptdltDTFENGYFNtGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGH 429
Cdd:cd05968 455 wrdeDRYLETYW------SRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGV 527
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1853634356 430 PDDTWGQVPKLYFV-----SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:cd05968 528 PHPVKGEAIVCFVVlkpgvTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
161-489 |
5.56e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.62 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVP---QTFRNH---YASAIGC--------KESLGFDhdtnwLSVLPIYH--ISGLSVLLRAV 224
Cdd:PRK12316 4694 DNLAYVIYTSGSTGRPKGVAvshGSLVNHlhaTGERYELtpddrvlqFMSFSFD-----GSHEGLYHplINGASVVIRDD 4768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 225 iegftvrivDKFNAEQILTMIKNERITHISLVPQTLNWLMQ--QGLHEPHDLQKILLGGAKLSATMIETALQ--YNLPIY 300
Cdd:PRK12316 4769 ---------SLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEhaERDGEPPSLRVYCFGGEAVAQASYDLAWRalKPVYLF 4839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 301 NSFGMTETcsqflTATPQMLHERPDT--------VGMPSANVDVKV----KNPNKEGH-GELMIKGANVMNGYLYPTDLT 367
Cdd:PRK12316 4840 NGYGPTET-----TVTVLLWKARDGDacgaaympIGTPLGNRSGYVldgqLNPLPVGVaGELYLGGEGVARGYLERPALT 4914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 ------DTF-ENG--YFNTGDIAEIDHEGyVMIYDRRKD-------LIISGGEniypyqIETVAKQFPGISDAVCIGHPD 431
Cdd:PRK12316 4915 aerfvpDPFgAPGgrLYRTGDLARYRADG-VIDYLGRVDhqvkirgFRIELGE------IEARLREHPAVREAVVIAQEG 4987
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1853634356 432 DTWGQ-----VPKLYFVSESDISKA----QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK12316 4988 AVGKQlvgyvVPQDPALADADEAQAelrdELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
148-489 |
1.13e-16 |
|
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: 82.22 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 148 DSPSNILNTsfNIDDIASIMFTSGTTGPQKAVPQTFRN------HYASAIGCKES------LGFDHDTNWLSVLPIYHIs 215
Cdd:cd17645 93 DSSAKILLT--NPDDLAYVIYTSGSTGLPKGVMIEHHNlvnlceWHRPYFGVTPAdkslvyASFSFDASAWEIFPHLTA- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 216 glsvllravieGFTVRIVD---KFNAEQILTMIKNERIThISLVP-QTLNWLMQQglhEPHDLQKILLGGAKLsatmiET 291
Cdd:cd17645 170 -----------GAALHVVPserRLDLDALNDYFNQEGIT-ISFLPtGAAEQFMQL---DNQSLRVLLTGGDKL-----KK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 292 ALQYNLPIYNSFGMTEtCSQFLTATPQMLHERPDTVGMPSANVDVKVKNPN----KEG-HGELMIKGANVMNGYLYPTDL 366
Cdd:cd17645 230 IERKGYKLVNNYGPTE-NTVVATSFEIDKPYANIPIGKPIDNTRVYILDEAlqlqPIGvAGELCIAGEGLARGYLNRPEL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 367 T------DTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVP 438
Cdd:cd17645 309 TaekfivHPFVPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYL 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1853634356 439 KLYFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17645 389 VAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
26-489 |
6.23e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 80.63 E-value: 6.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 26 TYQNLYCEASLLARRLKAYQQ---SRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIF---- 98
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAepgSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFvqdk 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 99 ---------CTLPLELRGfqIVSLddiefagTDITmNDLMDNTLDIQ---YDTLNETVVPKDSPSNILNTSFNidDIASI 166
Cdd:PLN02430 158 kikellepdCKSAKRLKA--IVSF-------TSVT-EEESDKASQIGvktYSWIDFLHMGKENPSETNPPKPL--DICTI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 167 MFTSGTTGPQKAVPQTFRNHYASAIG---CKESlgFD----HDTNWLSVLPIYHI-----------SGLSV--------- 219
Cdd:PLN02430 226 MYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQ--FEdkmtHDDVYLSFLPLAHIldrmieeyffrKGASVgyyhgdlna 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 220 -----------LLRAVIEGFTvRIVDKF-NAEQILTMIKneRITHISLVPQTLNWlMQQGLHEPH--------------- 272
Cdd:PLN02430 304 lrddlmelkptLLAGVPRVFE-RIHEGIqKALQELNPRR--RLIFNALYKYKLAW-MNRGYSHKKaspmadflafrkvka 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 273 ----DLQKILLGGAKLSaTMIETALQYNLPIY--NSFGMTETCSQFLTATPQ---MLherpDTVGMPSANVDVKVKNPNK 343
Cdd:PLN02430 380 klggRLRLLISGGAPLS-TEIEEFLRVTSCAFvvQGYGLTETLGPTTLGFPDemcML----GTVGAPAVYNELRLEEVPE 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 344 EGH--------GELMIKGANVMNGYLYPTDLT-DTFENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIET 413
Cdd:PLN02430 455 MGYdplgepprGEICVRGKCLFSGYYKNPELTeEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLEN 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 414 VAKQFPGISD-------------AVCIGHPDDT--W----GQVPKLYFVSESDISKAQLIAYLSQHLAKYKVpKHFEKV- 473
Cdd:PLN02430 535 VYGQNPIVEDiwvygdsfksmlvAVVVPNEENTnkWakdnGFTGSFEELCSLPELKEHILSELKSTAEKNKL-RGFEYIk 613
|
570 580
....*....|....*....|....*..
gi 1853634356 474 ----DTLPY-------TSTGKLQRNKL 489
Cdd:PLN02430 614 gvilETKPFdverdlvTATLKKRRNNL 640
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
26-406 |
1.69e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 79.09 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 26 TYQNLYCEASLLARRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFCTLPLEL 105
Cdd:PRK06334 47 SYNQVRKAVIALATKVSKYPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 106 RGFQIVSlDDIEFAGTDITMND------LMDNTLDIQYDTLnetvvpkdsPSNILNTSFNI-----DDIASIMFTSGTTG 174
Cdd:PRK06334 127 HLAQTHG-EDAEYPFSLIYMEEvrkelsFWEKCRIGIYMSI---------PFEWLMRWFGVsdkdpEDVAVILFTSGTEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 175 PQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGL-SVLLRAVIEGFTVRIV-DKFNAEQILTMIKNERITH 252
Cdd:PRK06334 197 LPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCTLFPLLSGVPVVFAyNPLYPKKIVEMIDEAKVTF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 253 ISLVPQTLNWLMQQGLHEPHDLQK---ILLGGAKLSATMIETALQY--NLPIYNSFGMTEtCSQFLTATPQMLHERPDTV 327
Cdd:PRK06334 277 LGSTPVFFDYILKTAKKQESCLPSlrfVVIGGDAFKDSLYQEALKTfpHIQLRQGYGTTE-CSPVITINTVNSPKHESCV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 328 GMPSANVDVKV-----KNPNKEGH-GELMIKGANVMNGYLyPTDLTDTF-----ENGYFnTGDIAEIDHEGYVMIYDRRK 396
Cdd:PRK06334 356 GMPIRGMDVLIvseetKVPVSSGEtGLVLTRGTSLFSGYL-GEDFGQGFvelggETWYV-TGDLGYVDRHGELFLKGRLS 433
|
410
....*....|
gi 1853634356 397 DLIISGGENI 406
Cdd:PRK06334 434 RFVKIGAEMV 443
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
335-488 |
3.45e-15 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 78.12 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 335 DVKVKNPNKEGHGELMI-----KGANVMNGYLYPTDLTDTFE-NGYFNTGDIAEIdHEGYVMIYDRRKDLIISGGENIYP 408
Cdd:PRK09192 395 EIEIRNEAGMPLPERVVghicvRGPSLMSGYFRDEESQDVLAaDGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWP 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 409 YQIETVAKQFPGI--SDAVCIGHPDDTWGQVPKLYFVSESDI-SKAQLIAYLSQHL-AKYKVPKHFEKV--DTLPYTSTG 482
Cdd:PRK09192 474 QDIEWIAEQEPELrsGDAAAFSIAQENGEKIVLLVQCRISDEeRRGQLIHALAALVrSEFGVEAAVELVppHSLPRTSSG 553
|
....*.
gi 1853634356 483 KLQRNK 488
Cdd:PRK09192 554 KLSRAK 559
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
161-429 |
3.80e-15 |
|
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: 77.86 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDT-----NWlsvLPIYHISGLSVLLRAVI-EGFTVRIVD 234
Cdd:cd05921 165 DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppvlvDW---LPWNHTFGGNHNFNLVLyNGGTLYIDD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 235 -KFNAEQILTMIKNER---ITHISLVPQTLNWLMQ-----QGLHEP--HDLQKILLGGAKLSATMIEtALQ--------Y 295
Cdd:cd05921 242 gKPMPGGFEETLRNLReisPTVYFNVPAGWEMLVAalekdEALRRRffKRLKLMFYAGAGLSQDVWD-RLQalavatvgE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 296 NLPIYNSFGMTETCSQFLTATpqMLHERPDTVGMPSANVDVKVKnPNkEGHGELMIKGANVMNGYLYPTDLT-DTF-ENG 373
Cdd:cd05921 321 RIPMMAGLGATETAPTATFTH--WPTERSGLIGLPAPGTELKLV-PS-GGKYEVRVKGPNVTPGYWRQPELTaQAFdEEG 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1853634356 374 YFNTGD---IAEIDHEGYVMIYDRR--KDLIISGGE--NIYPYQIETVAKQFPGISDAVCIGH 429
Cdd:cd05921 397 FYCLGDaakLADPDDPAKGLVFDGRvaEDFKLASGTwvSVGPLRARAVAACAPLVHDAVVAGE 459
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
161-489 |
5.86e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 78.29 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTfrnHYASAigckESLGFDHDTnwlsvlpiYHISGLSVLLRAVIEGFTVRIVDKF---- 236
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNT---HAALA----ERLQWMQAT--------YALDDSDVLMQKAPISFDVSVWECFwpli 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 237 --------------NAEQILTMIKNERITHISLVPQtlnwLMQQGLHEP-----HDLQKILLGGAKLSATMIETALQyNL 297
Cdd:PRK05691 1338 tgcrlvlagpgehrDPQRIAELVQQYGVTTLHFVPP----LLQLFIDEPlaaacTSLRRLFSGGEALPAELRNRVLQ-RL 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 298 P---IYNSFGMTETCSQFLTATPQMLHERPDTVGMPSANVDVKVK----NPNKEG-HGELMIKGANVMNGYLYPTDLT-- 367
Cdd:PRK05691 1413 PqvqLHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLdaelNLLPPGvAGELCIGGAGLARGYLGRPALTae 1492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 ----DTF-ENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHpDDTWGQVPKL 440
Cdd:PRK05691 1493 rfvpDPLgEDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVG 1571
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1853634356 441 YFVSE--SDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK05691 1572 YYTGEagQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
26-483 |
6.87e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 77.44 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 26 TYQNLYCEASLLARRLKAYQQ--SRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFCT--- 100
Cdd:PRK08043 233 SYRKLLKKTLFVGRILEKYSVegERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSrqf 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 101 --------LPLELRGFQIVSLDDIEfagTDITMNDlmdnTLDIQYDTL--NETVVPKDSpsnilntsfniDDIASIMFTS 170
Cdd:PRK08043 313 ldkgklwhLPEQLTQVRWVYLEDLK---DDVTTAD----KLWIFAHLLmpRLAQVKQQP-----------EDAALILFTS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 171 GTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSV-LLRAVIEGFTV---------RIVDKFNAEQ 240
Cdd:PRK08043 375 GSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVgLFTPLLTGAEVflypsplhyRIVPELVYDR 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 241 ILTMI--------KNERITHislvpqtlnwlmqqglhePHD---LQKILLGGAKLSATMIETAL-QYNLPIYNSFGMTEt 308
Cdd:PRK08043 455 NCTVLfgtstflgNYARFAN------------------PYDfarLRYVVAGAEKLQESTKQLWQdKFGLRILEGYGVTE- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 309 CSQFLTATPQMLhERPDTVGMPSANVDVK-VKNPNKEGHGELMIKGANVMNGYL---YPTDL-TDTFEN-------GYFN 376
Cdd:PRK08043 516 CAPVVSINVPMA-AKPGTVGRILPGMDARlLSVPGIEQGGRLQLKGPNIMNGYLrveKPGVLeVPTAENargemerGWYD 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 377 TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQF-PGISDAVCIgHPDDTWGQVPKLyFVSESDISKAQLIA 455
Cdd:PRK08043 595 TGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVsPDKQHATAI-KSDASKGEALVL-FTTDSELTREKLQQ 672
|
490 500
....*....|....*....|....*....
gi 1853634356 456 YLSQH-LAKYKVPKHFEKVDTLPYTSTGK 483
Cdd:PRK08043 673 YAREHgVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
164-489 |
1.05e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.52 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 164 ASIMFTSGTTGPQKAVpqtFRNHYASAIGCKE-----------------SLGFDHDTNWLSVlPIyhISGLSVLLRAviE 226
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGV---VVSHGEIAMHCQAvierfgmraddcelhfySINFDAASERLLV-PL--LCGARVVLRA--Q 2407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 227 GftvrivdKFNAEQILTMIKNERITHISLVP----QTLNWLMQQGLHEPhdLQKILLGGAKLSA---TMIETALQYNLpI 299
Cdd:PRK05691 2408 G-------QWGAEEICQLIREQQVSILGFTPsygsQLAQWLAGQGEQLP--VRMCITGGEALTGehlQRIRQAFAPQL-F 2477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 300 YNSFGMTETCSQFLTA-TPQMLHErpDTVGMPSANV---------DVKVKNPNKEGHGELMIKGANVMNGYLYPTDLT-- 367
Cdd:PRK05691 2478 FNAYGPTETVVMPLAClAPEQLEE--GAASVPIGRVvgarvayilDADLALVPQGATGELYVGGAGLAQGYHDRPGLTae 2555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 ----DTFE-NG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHpDDTWGQVPKL 440
Cdd:PRK05691 2556 rfvaDPFAaDGgrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAG 2634
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1853634356 441 YFVSE----SDISKAQL----IAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK05691 2635 YLVSAvagqDDEAQAALrealKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
161-429 |
2.41e-14 |
|
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: 75.54 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNhyasAIG-CKESLGFDH---DTNWLSVLPIYHI-SGLSVLLRAVIEGFTVRIVDK 235
Cdd:cd17641 158 EDVAVLCTTSGTTGKPKLAMLSHGN----FLGhCAAYLAADPlgpGDEYVSVLPLPWIgEQMYSVGQALVCGFIVNFPEE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 236 ----------------FNA----EQILTMIK---------------------------NERITHISLVPQTLNWLMQQGL 268
Cdd:cd17641 234 petmmedlreigptfvLLPprvwEGIAADVRarmmdatpfkrfmfelgmklglraldrGKRGRPVSLWLRLASWLADALL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 269 HEP-------HDLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETC-SQFLTATPQMlheRPDTVGMPSANVDVKVKN 340
Cdd:cd17641 314 FRPlrdrlgfSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAgAYTVHRDGDV---DPDTVGVPFPGTEVRIDE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 341 pnkegHGELMIKGANVMNGYLYPTDLT--DTFENGYFNTGDIAEIDHEGYVMIYDRRKDL-IISGGENIYPYQIETVAKQ 417
Cdd:cd17641 391 -----VGEILVRSPGVFVGYYKNPEATaeDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKF 465
|
330
....*....|..
gi 1853634356 418 FPGISDAVCIGH 429
Cdd:cd17641 466 SPYIAEAVVLGA 477
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
411-483 |
2.78e-14 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 67.57 E-value: 2.78e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 411 IETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV--SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGK 483
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
161-489 |
7.57e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 73.91 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIG-CKESLGFDHDTNWLSVLPIYHISGL--SVLLRAVIEGFTVRIVDKFN 237
Cdd:PRK06060 145 DALAYATYTSGTTGPPKAAIHRHADPLTFVDAmCRKALRLTPEDTGLCSARMYFAYGLgnSVWFPLATGGSAVINSAPVT 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLVPQTLNWLMqqGLHEP---HDLQKILLGGAKLSATMIETALQY--NLPIYNSFGMTETCSQF 312
Cdd:PRK06060 225 PEAAAILSARFGPSVLYGVPNFFARVI--DSCSPdsfRSLRCVVSAGEALELGLAERLMEFfgGIPILDGIGSTEVGQTF 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 313 LTATPQmlHERPDTVGMPSANVDVKVKNPNKE-----GHGELMIKGANVMNGYL-YPTDLTDtfENGYFNTGDIAEIDHE 386
Cdd:PRK06060 303 VSNRVD--EWRLGTLGRVLPPYEIRVVAPDGTtagpgVEGDLWVRGPAIAKGYWnRPDSPVA--NEGWLDTRDRVCIDSD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 387 GYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSES----DISKAQLI-AYLSQHL 461
Cdd:PRK06060 379 GWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSgatiDGSVMRDLhRGLLNRL 458
|
330 340
....*....|....*....|....*...
gi 1853634356 462 AKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK06060 459 SAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
159-489 |
1.58e-13 |
|
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: 72.46 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 159 NIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVI-EGFTVRIVDKFN 237
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLmSGGTLALSRKFS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 238 AEQILTMIKNERITHISLVPQTLNWLMqQGLHEPHDLQK--ILLGGAKLSATMIETALQ-YNLPI----YNS----FGMT 306
Cdd:cd05937 165 ASQFWKDVRDSGATIIQYVGELCRYLL-STPPSPYDRDHkvRVAWGNGLRPDIWERFRErFNVPEigefYAAtegvFALT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 307 ETCSQFLTA------------------TP-QMLHERPDTVGMPSANVDVKVknPNKEGhGELM--IKGANV--MNGYLYP 363
Cdd:cd05937 244 NHNVGDFGAgaighhglirrwkfenqvVLvKMDPETDDPIRDPKTGFCVRA--PVGEP-GEMLgrVPFKNReaFQGYLHN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 364 TD------LTDTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIG----HPD 431
Cdd:cd05937 321 EDatesklVRDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvpGHD 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1853634356 432 dtwGQVPKLYF------VSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05937 401 ---GRAGCAAItleessAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
14-489 |
1.62e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 72.75 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 14 HHIAITDGQESYTYQNLYCEASLLARRLKAYQQS----RVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQM 89
Cdd:PRK13388 16 DTIAVRYGDRTWTWREVLAEAAARAAALIALADPdrplHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 90 RSIDVQLIFCT---LPLelrgfqivsLDDIEFAGTDItmndlmdntLDIQYDTLNETVvpKDSPSNILNTSFNIDDIASI 166
Cdd:PRK13388 96 RRADCQLLVTDaehRPL---------LDGLDLPGVRV---------LDVDTPAYAELV--AAAGALTPHREVDAMDPFML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 167 MFTSGTTGPQKAVPQT-FRnhyASAIGCKESLGFDH---DTNWLSvLPIYH----ISGLSVllrAVIEGFTVRIVDKFNA 238
Cdd:PRK13388 156 IFTSGTTGAPKAVRCShGR---LAFAGRALTERFGLtrdDVCYVS-MPLFHsnavMAGWAP---AVASGAAVALPAKFSA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 EQILTMIKNERITHISLVPQTLNWLMQQGLHePHDLQKILLGGAKLSAT---MIETALQYNLPIYNSFGMTETCSQFLT- 314
Cdd:PRK13388 229 SGFLDDVRRYGATYFNYVGKPLAYILATPER-PDDADNPLRVAFGNEASprdIAEFSRRFGCQVEDGYGSSEGAVIVVRe 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 315 -ATPqmlherPDTVGMPSANVDV------------------KVKNPNkEGHGELMIK-GANVMNGYLYPTDLT-DTFENG 373
Cdd:PRK13388 308 pGTP------PGSIGRGAPGVAIynpetltecavarfdahgALLNAD-EAIGELVNTaGAGFFEGYYNNPEATaERMRHG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 374 YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWG-QVPKLYFVSE-SDISKA 451
Cdd:PRK13388 381 MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGdQVMAALVLRDgATFDPD 460
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1853634356 452 QLIAYLS--QHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK13388 461 AFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
161-464 |
2.60e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 72.24 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYA--SAIgcKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNA 238
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFEAqiEAL--REDYGIEPGEIDLPTFPLFALFGPALGMTSVIPDMDPTRPATVDP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 EQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDL---QKILLGGAKLSATMIE---TALQYNLPIYNSFGMTE----- 307
Cdd:PRK09274 252 AKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLpslRRVISAGAPVPIAVIErfrAMLPPDAEILTPYGATEalpis 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 308 --TCSQFLTATPQMLHERPDT-VGMPSANVDVKV----KNPNKEGH----------GELMIKGANVMNGYLYPTDLT--- 367
Cdd:PRK09274 332 siESREILFATRAATDNGAGIcVGRPVDGVEVRIiaisDAPIPEWDdalrlatgeiGEIVVAGPMVTRSYYNRPEATrla 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 ---DTFENGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTwGQVPKLyfVS 444
Cdd:PRK09274 412 kipDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPG-AQRPVL--CV 488
|
330 340
....*....|....*....|....
gi 1853634356 445 ESD----ISKAQLIAYLSQHLAKY 464
Cdd:PRK09274 489 ELEpgvaCSKSALYQELRALAAAH 512
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
166-492 |
5.15e-13 |
|
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: 71.19 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 166 IMFTSGTTGPQK-----------AVPQTFRNHYasaiGCKESLGF--DHDTNW-----LSVL-PIYHisGLSVLLravIE 226
Cdd:cd05967 235 ILYTSGTTGKPKgvvrdngghavALNWSMRNIY----GIKPGDVWwaASDVGWvvghsYIVYgPLLH--GATTVL---YE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 227 GFTVRIVDkfnAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPH-------DLQKILLGGAKLSATMIETALQ-YNLP 298
Cdd:cd05967 306 GKPVGTPD---PGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYikkydlsSLRTLFLAGERLDPPTLEWAENtLGVP 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 299 IYNSFGMTETCSQfLTATPQMLHERP-----DTVGMPSANVDVKVKNPNKEGHGELmikGANVMNGYLYPTDLT------ 367
Cdd:cd05967 383 VIDHWWQTETGWP-ITANPVGLEPLPikagsPGKPVPGYQVQVLDEDGEPVGPNEL---GNIVIKLPLPPGCLLtlwknd 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 DTFENGYFN-------TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKL 440
Cdd:cd05967 459 ERFKKLYLSkfpgyydTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLG 538
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1853634356 441 YFVSESDISKA------QLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRN---KLYRG 492
Cdd:cd05967 539 LVVLKEGVKITaeelekELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRtlrKIADG 599
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
161-464 |
9.99e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 69.80 E-value: 9.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQ 240
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLTSVIPDMDPTRPARADPQK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 241 ILTMIKNERITHISLVPQTLN----WLMQQGLHEPhDLQKILLGGAKLSATMIET---ALQYNLPIYNSFGMTETC---- 309
Cdd:cd05910 165 LVGAIRQYGVSIVFGSPALLErvarYCAQHGITLP-SLRRVLSAGAPVPIALAARlrkMLSDEAEILTPYGATEALpvss 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 310 --SQFLTATPQMLHERPD--TVGMPSANVDVKV--------------KNPNKEGHGELMIKGANVMNGYLYPTDLT---- 367
Cdd:cd05910 244 igSRELLATTTAATSGGAgtCVGRPIPGVRVRIieiddepiaewddtLELPRGEIGEITVTGPTVTPTYVNRPVATalak 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 -DTFENGYFN-TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGI--SDAVCIGHPDdtwGQVPKLYFV 443
Cdd:cd05910 324 iDDNSEGFWHrMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVrrSALVGVGKPG---CQLPVLCVE 400
|
330 340
....*....|....*....|...
gi 1853634356 444 SESDISK--AQLIAYLSQHLAKY 464
Cdd:cd05910 401 PLPGTITprARLEQELRALAKDY 423
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
21-489 |
1.43e-12 |
|
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: 69.63 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 21 GQESYTYQNLYCEASLLARRLKAYQQSR----VGLYIDNSIQSIilihACWLA----NIEIAMINTRLTPNEMKNQMRS- 91
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAGLRpgdtVALLLGNEPAFL----WIWLGlaklGCPVAFLNTNIRSKSLLHCFRCc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 92 ------IDVQL---IFCTLPlELRGfQIVSLddieFAGTDITMNDLMDNTLDiQYDTLNETVVPKDSPSNIlntsfNIDD 162
Cdd:cd05938 78 gakvlvVAPELqeaVEEVLP-ALRA-DGVSV----WYLSHTSNTEGVISLLD-KVDAASDEPVPASLRAHV-----TIKS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 163 IASIMFTSGTTG-PQKAVPQTFRNHYASAIgcKESLGFDHDTNWLSVLPIYHISGLSVLLRAVIE-GFTVRIVDKFNAEQ 240
Cdd:cd05938 146 PALYIYTSGTTGlPKAARISHLRVLQCSGF--LSLCGVTADDVIYITLPLYHSSGFLLGIGGCIElGATCVLKPKFSASQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 241 ILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKILLG-GAKLSATMIETALQY--NLPIYNSFGMTETCSQFLTATp 317
Cdd:cd05938 224 FWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAiGNGLRADVWREFLRRfgPIRIREFYGSTEGNIGFFNYT- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 318 qmlhERPDTVGMPSA-----------NVDVKVKNP--NKEGH------GE--LMIKGANVMN---GYLYPTDLT------ 367
Cdd:cd05938 303 ----GKIGAVGRVSYlykllfpfeliKFDVEKEEPvrDAQGFcipvakGEpgLLVAKITQQSpflGYAGDKEQTekkllr 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 DTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDA----VCI-GHPddtwGQVP-- 438
Cdd:cd05938 379 DVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVnvygVTVpGHE----GRIGma 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1853634356 439 --KLYFVSESDISKaqLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd05938 455 avKLKPGHEFDGKK--LYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
276-421 |
2.71e-12 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 69.28 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 276 KILLGGAKLSATMIETALQY--NLPIYNSFGMTETCSQFLTATPQMLhERPDTVGMPSANVDVKVKN-PNKE-------G 345
Cdd:PLN02614 389 RIILSGAAPLASHVESFLRVvaCCHVLQGYGLTESCAGTFVSLPDEL-DMLGTVGPPVPNVDIRLESvPEMEydalastP 467
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1853634356 346 HGELMIKGANVMNGYLYPTDLT-DTFENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETVAKQFPGI 421
Cdd:PLN02614 468 RGEICIRGKTLFSGYYKREDLTkEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAV 545
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
161-489 |
2.82e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 69.30 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQK--AVPQT--------FRNHY----ASAIGCKESLGFDhdtnwLSV----LPIyhISGlSVLLR 222
Cdd:PRK10252 598 HHTAYIIFTSGSTGRPKgvMVGQTaivnrllwMQNHYpltaDDVVLQKTPCSFD-----VSVweffWPF--IAG-AKLVM 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 223 AVIEGFTvrivdkfNAEQILTMIKNERITHISLVPQTL----NWLMQQGLHEPH-DLQKILLGGAKLSATMIETALQ-YN 296
Cdd:PRK10252 670 AEPEAHR-------DPLAMQQFFAEYGVTTTHFVPSMLaafvASLTPEGARQSCaSLRQVFCSGEALPADLCREWQQlTG 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 297 LPIYNSFGMTE---------TCSQFLTATPQmlheRPDTVGMPSANVDVKV----KNPNKEG-HGELMIKGANVMNGYLY 362
Cdd:PRK10252 743 APLHNLYGPTEaavdvswypAFGEELAAVRG----SSVPIGYPVWNTGLRIldarMRPVPPGvAGDLYLTGIQLAQGYLG 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 363 PTDLT------DTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGI----SDAVCIGHP 430
Cdd:PRK10252 819 RPDLTasrfiaDPFAPGerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVeqavTHACVINQA 898
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1853634356 431 DDTWGQVPKL--YFVSESD--ISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK10252 899 AATGGDARQLvgYLVSQSGlpLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
34-489 |
5.84e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 67.78 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 34 ASLLARRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFC------TLPLELRG 107
Cdd:PRK07867 42 AAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTesahaeLLDGLDPG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 108 FQIVSLDDIEFAgtditmnDLMDNTLDiqydtlNETVVPKDSPsnilntsfniDDIASIMFTSGTTGPQKAVPQTFRNHY 187
Cdd:PRK07867 122 VRVINVDSPAWA-------DELAAHRD------AEPPFRVADP----------DDLFMLIFTSGTSGDPKAVRCTHRKVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 188 ASAIGCKE--SLGFDhDTNWLSvLPIYH----ISGLSVllrAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLN 261
Cdd:PRK07867 179 SAGVMLAQrfGLGPD-DVCYVS-MPLFHsnavMAGWAV---ALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 262 WLMQQGlHEPHDLQ---KILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFlTATP--------------QMLHerP 324
Cdd:PRK07867 254 YVLATP-ERPDDADnplRIVYGNEGAPGDIARFARRFGCVVVDGFGSTEGGVAI-TRTPdtppgalgplppgvAIVD--P 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 325 DTVG-MPSANVDVKVKNPNKEGHGELM-IKGANVMNGYlY--PTDLTDTFENGYFNTGDIAEIDHEGYVMIYDRRKDLII 400
Cdd:PRK07867 330 DTGTeCPPAEDADGRLLNADEAIGELVnTAGPGGFEGY-YndPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 401 SGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWG-QV-PKLYFVSESDISKAQLIAYLSQH--LAKYKVPKHFEKVDTL 476
Cdd:PRK07867 409 VDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGdQVmAALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAEL 488
|
490
....*....|...
gi 1853634356 477 PYTSTGKLQRNKL 489
Cdd:PRK07867 489 PRTATFKVLKRQL 501
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
327-486 |
6.92e-12 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 67.48 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 327 VGMPSANVDVKVKNP------NKEGHGELMIKGANVMNGYLYPTDLTdtfENGYFNTGDIAEIDHEGYVmIYDRRKDLII 400
Cdd:PRK05851 347 LGNPIPGMEVRISPGdgaagvAGREIGEIEIRGASMMSGYLGQAPID---PDDWFPTGDLGYLVDGGLV-VCGRAKELIT 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 401 SGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSE---SDISKAQliAYLSQHLAKY--KVPKH--FEKV 473
Cdd:PRK05851 423 VAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEfrgPDEAGAR--SEVVQRVASEcgVVPSDvvFVAP 500
|
170
....*....|...
gi 1853634356 474 DTLPYTSTGKLQR 486
Cdd:PRK05851 501 GSLPRTSSGKLRR 513
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
159-491 |
1.13e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 66.74 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 159 NIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGL-SVLLRAVIEG---------- 227
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLiAFHLAPLIAGmnqylmptrl 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 228 FTVR------IVDKFNAEQI----------LTMIKNERITHISLvpQTLNWLMQQGlhEPHDLQKILLGGAKLSA-TMIE 290
Cdd:cd05908 184 FIRRpilwlkKASEHKATIVsspnfgykyfLKTLKPEKANDWDL--SSIRMILNGA--EPIDYELCHEFLDHMSKyGLKR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 291 TALqynLPIY----NSFGMTETCSQFLTATPQMLHE------------RPDT-------VGMPSANVDVKVKNPNKEG-- 345
Cdd:cd05908 260 NAI---LPVYglaeASVGASLPKAQSPFKTITLGRRhvthgepepevdKKDSecltfveVGKPIDETDIRICDEDNKIlp 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 346 ---HGELMIKGANVMNGYLYPTDLTDTF--ENGYFNTGDIAEIdHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPG 420
Cdd:cd05908 337 dgyIGHIQIRGKNVTPGYYNNPEATAKVftDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEG 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 421 ISD---AVCIGHPDDTwgqvpklyfvSESDISKAQLIAYLSQHLAKY--KVPKHFEK-----------VDTLPYTSTGKL 484
Cdd:cd05908 416 VELgrvVACGVNNSNT----------RNEEIFCFIEHRKSEDDFYPLgkKIKKHLNKrggwqinevlpIRRIPKTTSGKV 485
|
....*..
gi 1853634356 485 QRNKLYR 491
Cdd:cd05908 486 KRYELAQ 492
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
161-379 |
1.34e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 66.83 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDT-----NWLsvlPIYHISGLSVLLRAVIE-GFTVRIVD 234
Cdd:PRK08180 209 DTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppvlvDWL---PWNHTFGGNHNLGIVLYnGGTLYIDD 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 235 -KFNAEQILTMIKNERitHIS-----LVPQtlNWLM-QQGLHEPHDLQKILL--------GGAKLSAT-------MIETA 292
Cdd:PRK08180 286 gKPTPGGFDETLRNLR--EISptvyfNVPK--GWEMlVPALERDAALRRRFFsrlkllfyAGAALSQDvwdrldrVAEAT 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 293 LQYNLPIYNSFGMTETCSQFLTATPQMlhERPDTVGMPSANVDVK-VknPNkEGHGELMIKGANVMNGYLYPTDLT-DTF 370
Cdd:PRK08180 362 CGERIRMMTGLGMTETAPSATFTTGPL--SRAGNIGLPAPGCEVKlV--PV-GGKLEVRVKGPNVTPGYWRAPELTaEAF 436
|
250
....*....|
gi 1853634356 371 -ENGYFNTGD 379
Cdd:PRK08180 437 dEEGYYRSGD 446
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
96-489 |
2.69e-11 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 65.69 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 96 LIFCT--LPLELRGFQIVSLDDIE---FAGTDITMNDLMDNtldiqydtlnetvvpkdspsnilntsfniDDIASIMFTS 170
Cdd:PRK04813 102 LIIATeeLPLEILGIPVITLDELKdifATGNPYDFDHAVKG-----------------------------DDNYYIIFTS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 171 GTTGPQKAVP------QTFRNHYASAIGCKES--------LGFDhdtnwLSVLPIYhisglsvllRAVIEGFTVRIVDKf 236
Cdd:PRK04813 153 GTTGKPKGVQishdnlVSFTNWMLEDFALPEGpqflnqapYSFD-----LSVMDLY---------PTLASGGTLVALPK- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 237 naeqilTMIKNERITHISLVPQTLN-W----------LMQQGLHEPH--DLQKILLGGAKLSAtmiETA--LQYNLP--- 298
Cdd:PRK04813 218 ------DMTANFKQLFETLPQLPINvWvstpsfadmcLLDPSFNEEHlpNLTHFLFCGEELPH---KTAkkLLERFPsat 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 299 IYNSFGMTETCSQfLTA---TPQMLHE---------RPDTVGMPSANVDVKVKNPNKeghGELMIKGANVMNGYLYPTDL 366
Cdd:PRK04813 289 IYNTYGPTEATVA-VTSieiTDEMLDQykrlpigyaKPDSPLLIIDEEGTKLPDGEQ---GEIVISGPSVSKGYLNNPEK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 367 TD---TFENGY--FNTGDIAEIDHEgyVMIYDRRKDLIIS-GGENIYPYQIETVAKQFPGISDAVCIghPDDTWGQVPKL 440
Cdd:PRK04813 365 TAeafFTFDGQpaYHTGDAGYLEDG--LLFYQGRIDFQIKlNGYRIELEEIEQNLRQSSYVESAVVV--PYNKDHKVQYL 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1853634356 441 Y---------FVSESDISKAqLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PRK04813 441 IayvvpkeedFEREFELTKA-IKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
161-491 |
6.91e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.36 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVP--------------QTFRNHYASAIGCKESLGFD--HDtNWLSVLpiyhISGLSVLLRAV 224
Cdd:PRK12316 2146 ENLAYVIYTSGSTGLPKGVAvshgalvahcqaagERYELSPADCELQFMSFSFDgaHE-QWFHPL----LNGARVLIRDD 2220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 225 iegftvrivDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHE--PHDLQKILLGGAKLSATMIETALQYNLPIY-- 300
Cdd:PRK12316 2221 ---------ELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDgrPPAVRVYCFGGEAVPAASLRLAWEALRPVYlf 2291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 301 NSFGMTETcsqflTATPQMLHERPDT--------VGMPSAN-----VDVKVKNPNKEGHGELMIKGANVMNGYLYPTDLT 367
Cdd:PRK12316 2292 NGYGPTEA-----VVTPLLWKCRPQDpcgaayvpIGRALGNrrayiLDADLNLLAPGMAGELYLGGEGLARGYLNRPGLT 2366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 368 ------DTFENG---YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHpDDTWGQVP 438
Cdd:PRK12316 2367 aerfvpDPFSASgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQL 2445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 439 KLYFVSES--DISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:PRK12316 2446 VAYVVPDDaaEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
296-486 |
1.81e-10 |
|
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: 63.35 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 296 NLPIYNSFGMTETCSQFLTATPQMLHERPDTVGMPSANVDVKVKNPN-----KEGHGELMIKGAnvmngylYPTDL---- 366
Cdd:cd05966 381 RCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEgneveGEVEGYLVIKRP-------WPGMArtiy 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 367 --TDTFENGYFN-------TGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQV 437
Cdd:cd05966 454 gdHERYEDTYFSkfpgyyfTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEA 533
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1853634356 438 PKLYFV-----SESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:cd05966 534 IYAFVTlkdgeEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMR 587
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
153-398 |
4.08e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 58.83 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 153 ILNTSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESL-----GFDHDTNWLSVLPIYHISGLSV----LLRA 223
Cdd:PTZ00216 256 PLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLndligPPEEDETYCSYLPLAHIMEFGVtnifLARG 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 224 VIEGF-TVR-IVDKF----------------NAEQILTMIKneRITHISLVP-------------QT-LNWLMqQGLHEP 271
Cdd:PTZ00216 336 ALIGFgSPRtLTDTFarphgdltefrpvfliGVPRIFDTIK--KAVEAKLPPvgslkrrvfdhayQSrLRALK-EGKDTP 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 272 HDLQK---------------ILLGGAKLSAtmiETALQYNL---PIYNSFGMTETCSqflTATPQMLHE-RPDTVGMPSA 332
Cdd:PTZ00216 413 YWNEKvfsapravlggrvraMLSGGGPLSA---ATQEFVNVvfgMVIQGWGLTETVC---CGGIQRTGDlEPNAVGQLLK 486
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 333 NVDVKV------KNPNK-EGHGELMIKGANVMNGYLYPTDLTDTF--ENGYFNTGDIAEIDHEGYVMIYDRRKDL 398
Cdd:PTZ00216 487 GVEMKLldteeyKHTDTpEPRGEILLRGPFLFKGYYKQEELTREVldEDGWFHTGDVGSIAANGTLRIIGRVKAL 561
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
161-422 |
4.76e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 58.70 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESL-----GFDHDTNWLSVLPIYHI-----------SGLSV----- 219
Cdd:PLN02861 220 TDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLkvtdrVATEEDSYFSYLPLAHVydqvietycisKGASIgfwqg 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 220 LLRAVIEGFTV----------RIVDKFNAeQILTMIKNERITHISLVPQTLNWL---MQQGL--HEPHDL---------- 274
Cdd:PLN02861 300 DIRYLMEDVQAlkptifcgvpRVYDRIYT-GIMQKISSGGMLRKKLFDFAYNYKlgnLRKGLkqEEASPRldrlvfdkik 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 275 ------QKILLGGAKLSATMIETALQYN--LPIYNSFGMTETCSQFLTATPQMLhERPDTVGMPSANVDVKVKNPNKEGH 346
Cdd:PLN02861 379 eglggrVRLLLSGAAPLPRHVEEFLRVTscSVLSQGYGLTESCGGCFTSIANVF-SMVGTVGVPMTTIEARLESVPEMGY 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 347 --------GELMIKGANVMNGYLYPTDLTD-TFENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETVAK 416
Cdd:PLN02861 458 dalsdvprGEICLRGNTLFSGYHKRQDLTEeVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYS 537
|
....*.
gi 1853634356 417 QFPGIS 422
Cdd:PLN02861 538 RCPLIA 543
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
45-399 |
6.50e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 58.20 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 45 QQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFCTlPLELRGFQIVSlDDIEFAGTDIT 124
Cdd:PLN02387 130 KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICD-SKQLKKLIDIS-SQLETVKRVIY 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 125 MNDLMDNTLDIQYDTLNETV-----VPKDSPSNILNTSF-NIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESL- 197
Cdd:PLN02387 208 MDDEGVDSDSSLSGSSNWTVssfseVEKLGKENPVDPDLpSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVp 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 198 GFDHDTNWLSVLPIYHISGL---SVLLR---AVIEGFTVRIVD-----KFNAEQILTMIKNeriTHISLVPQTL------ 260
Cdd:PLN02387 288 KLGKNDVYLAYLPLAHILELaaeSVMAAvgaAIGYGSPLTLTDtsnkiKKGTKGDASALKP---TLMTAVPAILdrvrdg 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 261 -----------------------------NWLMQQGLHE---------------PHDLQKILLGGAKLSA-TMIETALQY 295
Cdd:PLN02387 365 vrkkvdakgglakklfdiaykrrlaaiegSWFGAWGLEKllwdalvfkkiravlGGRIRFMLSGGAPLSGdTQRFINICL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 296 NLPIYNSFGMTETCSqflTATpqmLHERPDT----VGMPSANVDVKVKNPNKEGH---------GELMIKGANVMNGYLY 362
Cdd:PLN02387 445 GAPIGQGYGLTETCA---GAT---FSEWDDTsvgrVGPPLPCCYVKLVSWEEGGYlisdkpmprGEIVIGGPSVTLGYFK 518
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1853634356 363 PTDLTD----TFENG--YFNTGDIAEIDHEGYVMIYDRRKDLI 399
Cdd:PLN02387 519 NQEKTDevykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIV 561
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
45-414 |
8.78e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 57.80 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 45 QQSRVGLYIDNSIQSIILIHACW-LANIEIAMINTrLTPNEMKNQMRSIDVQLIFC---TLPLELrGF--QIVSLDDIEF 118
Cdd:PLN02736 102 KGACVGLYFINRPEWLIVDHACSaYSYVSVPLYDT-LGPDAVKFIVNHAEVAAIFCvpqTLNTLL-SClsEIPSVRLIVV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 119 AGTDitmNDLMDNTLD------IQYDTL----NETVVPKDSPSNilntsfniDDIASIMFTSGTTGPQKAVPQTFRNHYA 188
Cdd:PLN02736 180 VGGA---DEPLPSLPSgtgveiVTYSKLlaqgRSSPQPFRPPKP--------EDVATICYTSGTTGTPKGVVLTHGNLIA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 189 SAIGCKESLGFDHDTNWLSVLPIYHI----SGLSVLLRAVIEGF-----------------TV---------RIVDKfna 238
Cdd:PLN02736 249 NVAGSSLSTKFYPSDVHISYLPLAHIyervNQIVMLHYGVAVGFyqgdnlklmddlaalrpTIfcsvprlynRIYDG--- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 239 eqILTMIKN-----ERITHISLVPQtlnwlmQQGLHEPHDLQKIL-----------LGG---------AKLSATMIE-TA 292
Cdd:PLN02736 326 --ITNAVKEsgglkERLFNAAYNAK------KQALENGKNPSPMWdrlvfnkikakLGGrvrfmssgaSPLSPDVMEfLR 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 293 LQYNLPIYNSFGMTETcSQFLTATpqmlHERPDT---VGMPSANVDVK-VKNPNKE--------GHGELMIKGANVMNGY 360
Cdd:PLN02736 398 ICFGGRVLEGYGMTET-SCVISGM----DEGDNLsghVGSPNPACEVKlVDVPEMNytsedqpyPRGEICVRGPIIFKGY 472
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1853634356 361 LYPTDLTDTF--ENGYFNTGDIAEIDHEGYVMIYDRRKDLI-ISGGENIYPYQIETV 414
Cdd:PLN02736 473 YKDEVQTREVidEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 529
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
159-491 |
8.98e-09 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 57.43 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 159 NIDDIASIMFTSGTTG-PQKAVPQTFRnHYASAIGCKESLGFDHDTNWLSVLPIYHISGLSVLL-RAVIEGFTVRIVDKF 236
Cdd:cd05939 102 NFRDKLFYIYTSGTTGlPKAAVIVHSR-YYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVgQALLHGSTVVIRKKF 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 237 NAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPHDLQKI-LLGGAKLSATMIETALQ-YNLP-IYNSFGMTE-TCS-- 310
Cdd:cd05939 181 SASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVrLAVGNGLRPQIWEQFVRrFGIPqIGEFYGATEgNSSlv 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 311 ---------QFLTATPQMLHE------RPDTV---------------GMPSANVD-VKVKNPNKEGHGELMiKGANvmNG 359
Cdd:cd05939 261 nidnhvgacGFNSRILPSVYPirlikvDEDTGelirdsdglcipcqpGEPGLLVGkIIQNDPLRRFDGYVN-EGAT--NK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 360 YLYptdlTDTFENG--YFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHpddtwgQV 437
Cdd:cd05939 338 KIA----RDVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV------EV 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1853634356 438 P----KLYFVSESDISKAQLIAYLSQHLAK----YKVPKHFEKVDTLPYTSTGKLQRNKLYR 491
Cdd:cd05939 408 PgvegRAGMAAIVDPERKVDLDRFSAVLAKslppYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
163-489 |
7.70e-08 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 54.40 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 163 IASIMFTSGTTGPQK--AVP-QTFRNHYASAigCKESLGFDHDTNWLSVLPIYHISGLSVLLrAVIEGFTVRIVD---KF 236
Cdd:cd17654 120 LAYVIHTSGTTGTPKivAVPhKCILPNIQHF--RSLFNITSEDILFLTSPLTFDPSVVEIFL-SLSSGATLLIVPtsvKV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 237 NAEQILTMI-KNERITHISLVPQTLNWLMQQGLHEP-----HDLQKILLGGAKL-SATMIETALQY--NLPIYNSFGMTE 307
Cdd:cd17654 197 LPSKLADILfKRHRITVLQATPTLFRRFGSQSIKSTvlsatSSLRVLALGGEPFpSLVILSSWRGKgnRTRIFNIYGITE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 308 TCSQFLTATPQMLhERPDTVGMPSANVDVKVK-NPNKEGHGELMIKGANVmngyLYPTDLTDTFENGYFN-TGDIAEIDh 385
Cdd:cd17654 277 VSCWALAYKVPEE-DSPVQLGSPLLGTVIEVRdQNGSEGTGQVFLGGLNR----VCILDDEVTVPKGTMRaTGDFVTVK- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 386 EGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGIsDAVCIGHPDDtwgQVPKLYFVSESdiSKAQLIAYLSQH-LAKY 464
Cdd:cd17654 351 DGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGES--SSSRIHKELQLTlLSSH 424
|
330 340
....*....|....*....|....*
gi 1853634356 465 KVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:cd17654 425 AIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
138-417 |
3.71e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 52.81 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 138 DTLNETVVPKDSpsnilntsfNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDHDTNWLSVLPIYHISGL 217
Cdd:PRK07769 166 DEVGATWVPPEA---------NEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 218 -SVLLRAVIEGFT--------VRIVDKFNAEqiLTMIKNERITHISLVPQ-TLNWLMQQGL----HEPHDLQKI--LLGG 281
Cdd:PRK07769 237 iTVLLPALLGHYItfmspaafVRRPGRWIRE--LARKPGGTGGTFSAAPNfAFEHAAARGLpkdgEPPLDLSNVkgLLNG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 282 AK--LSATM---IETALQYNLP---IYNSFGMTETcSQFLTATP---------------------QMLHERPDTVGMPSA 332
Cdd:PRK07769 315 SEpvSPASMrkfNEAFAPYGLPptaIKPSYGMAEA-TLFVSTTPmdeeptviyvdrdelnagrfvEVPADAPNAVAQVSA 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 333 N----------VDVKVKNPNKEGH-GELMIKGANVMNGYLYPTDLTD-TFEN------------------GYFNTGDIAe 382
Cdd:PRK07769 394 GkvgvsewaviVDPETASELPDGQiGEIWLHGNNIGTGYWGKPEETAaTFQNilksrlseshaegapddaLWVRTGDYG- 472
|
330 340 350
....*....|....*....|....*....|....*
gi 1853634356 383 IDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQ 417
Cdd:PRK07769 473 VYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQE 507
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
369-486 |
1.28e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 50.91 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 369 TFENGYFnTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFVSESDI 448
Cdd:PRK00174 480 TFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGE 558
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1853634356 449 SK-AQLIAYLSQHLAK----YKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PRK00174 559 EPsDELRKELRNWVRKeigpIAKPDVIQFAPGLPKTRSGKIMR 601
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
161-423 |
2.00e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.15 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 161 DDIASIMFTSGTTGPQKAVPQTFR--NHYASAIG-CKESLGFDHDTnwlsvlpIYHIS--------GLSVL--LRAVieG 227
Cdd:COG1541 83 EEIVRIHASSGTTGKPTVVGYTRKdlDRWAELFArSLRAAGVRPGD-------RVQNAfgyglftgGLGLHygAERL--G 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 228 FTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLM----QQGLhEPHD--LQKILLGGAKLSATM---IETALqyNLP 298
Cdd:COG1541 154 ATVIPAGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAevaeEEGI-DPRDlsLKKGIFGGEPWSEEMrkeIEERW--GIK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 299 IYNSFGMTETCSQFLTATPQM--LHERPD----TVgmpsanVDVKVKNPNKEGH-GELMIkganvmngylypTDLTDtfe 371
Cdd:COG1541 231 AYDIYGLTEVGPGVAYECEAQdgLHIWEDhflvEI------IDPETGEPVPEGEeGELVV------------TTLTK--- 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1853634356 372 NGY----FNTGDIAEIDHE----GYVM-----IYDRRKDLIISGGENIYPYQIETVAKQFPGISD 423
Cdd:COG1541 290 EAMplirYRTGDLTRLLPEpcpcGRTHprigrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGP 354
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
138-419 |
1.69e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 47.43 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 138 DTLNETVVPkdspsnilnTSFNIDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGF-DHDTNWLSVLPIYHISG 216
Cdd:PRK12476 179 DSAGESFVP---------VELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLlDRNTHGVSWLPLYHDMG 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 217 LSVL-LRAVIEGFTVRIVDKFNAEQILTMIK--NERITHISLVPQTLN----WLMQQGLHEPH---DLQKILL--GGAKL 284
Cdd:PRK12476 250 LSMIgFPAVYGGHSTLMSPTAFVRRPQRWIKalSEGSRTGRVVTAAPNfayeWAAQRGLPAEGddiDLSNVVLiiGSEPV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 285 SATMIET---AL-QYNLP---IYNSFGMTETCSQFLTATPQ--------------------MLHERPDTV-----GMPSA 332
Cdd:PRK12476 330 SIDAVTTfnkAFaPYGLPrtaFKPSYGIAEATLFVATIAPDaepsvvyldreqlgagravrVAADAPNAVahvscGQVAR 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 333 NVDVKVKNPNKE-----GH-GELMIKGANVMNGYL-YPTDLTDTFEN-------------------GYFNTGDIA-EIDH 385
Cdd:PRK12476 410 SQWAVIVDPDTGaelpdGEvGEIWLHGDNIGRGYWgRPEETERTFGAklqsrlaegshadgaaddgTWLRTGDLGvYLDG 489
|
330 340 350
....*....|....*....|....*....|....*
gi 1853634356 386 EGYVMiyDRRKDLIISGGENIYPYQIE-TVAKQFP 419
Cdd:PRK12476 490 ELYIT--GRIADLIVIDGRNHYPQDIEaTVAEASP 522
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
134-486 |
2.85e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 46.48 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 134 DIQYDTLNETVVPKDSPSNILNTSfnidDIASIMFTSGTTGPQKAVpQTFRNHYASAIGCKESLGFD----------HDT 203
Cdd:PRK10524 210 DVDYATLRAQHLGARVPVEWLESN----EPSYILYTSGTTGKPKGV-QRDTGGYAVALATSMDTIFGgkagetffcaSDI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 204 NWL---SVLpIYH--ISGLSVLLravIEGFTVR--------IVDKFnaeqiltmikneRITHISLVPQTLNWLMQQG--L 268
Cdd:PRK10524 285 GWVvghSYI-VYAplLAGMATIM---YEGLPTRpdagiwwrIVEKY------------KVNRMFSAPTAIRVLKKQDpaL 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 269 HEPHD---LQKILLGGAKL---SATMIETALqyNLPIYNSFGMTETCSQFLTATP--QMLHERPDTVGMPSANVDVKVKN 340
Cdd:PRK10524 349 LRKHDlssLRALFLAGEPLdepTASWISEAL--GVPVIDNYWQTETGWPILAIARgvEDRPTRLGSPGVPMYGYNVKLLN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 341 pnkEGHGELMI---KGANVMNGYLYPTDLT------DTFENGYF--------NTGDIAEIDHEGYVMIYDRRKDLIISGG 403
Cdd:PRK10524 427 ---EVTGEPCGpneKGVLVIEGPLPPGCMQtvwgddDRFVKTYWslfgrqvySTFDWGIRDADGYYFILGRTDDVINVAG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 404 ENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPkLYFVSESDISK-----------AQLIAYLSQHLAKYKVPKHFEK 472
Cdd:PRK10524 504 HRLGTREIEESISSHPAVAEVAVVGVKDALKGQVA-VAFVVPKDSDSladrearlaleKEIMALVDSQLGAVARPARVWF 582
|
410
....*....|....
gi 1853634356 473 VDTLPYTSTGKLQR 486
Cdd:PRK10524 583 VSALPKTRSGKLLR 596
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
373-486 |
8.83e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 45.12 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 373 GYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQVPKLYFV-----SESD 447
Cdd:PTZ00237 492 GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVlkqdqSNQS 571
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1853634356 448 IS----KAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQR 486
Cdd:PTZ00237 572 IDlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
298-489 |
1.06e-04 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 44.89 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 298 PIYNSFGMTETCSQFLTATPQMLHERPDTVGMP-----SANVDVKVKNPNKEGHGELMIKGA-----NVMNG--YLYPTD 365
Cdd:PLN02654 427 PISDTWWQTETGGFMITPLPGAWPQKPGSATFPffgvqPVIVDEKGKEIEGECSGYLCVKKSwpgafRTLYGdhERYETT 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 366 LTDTFEnGYFNTGDIAEIDHEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCIGHPDDTWGQ-----VPKL 440
Cdd:PLN02654 507 YFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQgiyafVTLV 585
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1853634356 441 YFVSESDISKAQLIAYLSQHLAKYKVPKHFEKVDTLPYTSTGKLQRNKL 489
Cdd:PLN02654 586 EGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
347-432 |
3.01e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 40.31 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853634356 347 GELMIKGANVMNGYLYPTDLTD-TF------------ENGYFNTGDIAEIdHEGYVMIYDRRKDLIISGGENIYPYQIET 413
Cdd:PRK05850 398 GEIWVHGDNVAAGYWQKPEETErTFgatlvdpspgtpEGPWLRTGDLGFI-SEGELFIVGRIKDLLIVDGRNHYPDDIEA 476
|
90
....*....|....*....
gi 1853634356 414 VAKQFPGiSDAVCIGHPDD 432
Cdd:PRK05850 477 TIQEITG-GRVAAISVPDD 494
|
|
| |
