|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
47-522 |
0e+00 |
|
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: 604.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 47 AQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSI 126
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 127 TRPNIIFCDGDEFEKVRSATAQL--DVKIITMRNHPSGSIRIDQVLSTP--IEKNFQPVRLEQGNDQTLAILCSSGTTGI 202
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELgpKDKIIVLDDKPDGVLSIEDLLSPTlgEEDEDLPPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 203 PKAVTITNSRQILNSSHSLTT-------NDVQYSHSTLDWITGLLTTVTSGVFSTKRIIaDNIFDPEFFMRLVEEHQITW 275
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQTFlygndgsNDVILGFLPLYHIYGLFTTLASLLNGATVII-MPKFDSELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 276 IIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTELGSMAALNLHFDEKPNSVGR 355
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 356 LVAGLKLKVICEKG-ESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKF 434
Cdd:cd05911 320 LLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 435 QNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYKQLNGGAIIVEDLV 514
Cdd:cd05911 400 KGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKV-ASYKQLRGGVVFVDEIP 478
|
....*...
gi 21356441 515 RSPNGKTN 522
Cdd:cd05911 479 KSASGKIL 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
31-537 |
2.81e-89 |
|
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: 281.70 E-value: 2.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 31 IGEIIFNEMRRHPQLIAqISATENTiLTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHS 110
Cdd:COG0318 1 LADLLRRAAARHPDRPA-LVFGGRR-LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 111 LNISYEQSTIEKLFSITRPNIIFcdgdefekvrsataqldvkiitmrnhpsgsiridqvlstpieknfqpvrleqgndqT 190
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALV--------------------------------------------------------T 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 191 LAILCSSGTTGIPKAVTIT------NSRQILnSSHSLTTNDVQYSHSTLDWITGLLTTVTSGVFS-TKRIIADNiFDPEF 263
Cdd:COG0318 103 ALILYTSGTTGRPKGVMLThrnllaNAAAIA-AALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAgATLVLLPR-FDPER 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 264 FMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTELGSMAALN 343
Cdd:COG0318 181 VLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVE-GYGLTETSPVVTVN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 344 L--HFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK-MRDhhNWFHTGDLGYVDDDG 420
Cdd:COG0318 260 PedPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEaFRD--GWLRTGDLGRLDEDG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 421 FIYIVERKKDMLKF--QNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdA 498
Cdd:COG0318 338 YLYIVGRKKDMIISggENV--YPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERL-A 414
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 21356441 499 KYK---QLnggaIIVEDLVRSPNGKTNRMANKAFFLEAKSSA 537
Cdd:COG0318 415 RYKvprRV----EFVDELPRTASGKIDRRALRERYAAGALEA 452
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
189-520 |
2.12e-77 |
|
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: 247.20 E-value: 2.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 189 QTLAILCSSGTTGIPKAVTITNSR-----QILNSSHSLTTNDVQYSHSTLDWItGLLTTVTSGVFSTKRIIADNIFDPEF 263
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNllaaaAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 264 FMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTELGSMAALN 343
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVN-GYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 344 L--HFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKmRDHHNWFHTGDLGYVDDDGF 421
Cdd:cd04433 159 PpdDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAA-VDEDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 422 IYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYK 501
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERL-APYK 316
|
330
....*....|....*....
gi 21356441 502 QLnGGAIIVEDLVRSPNGK 520
Cdd:cd04433 317 VP-RRVVFVDALPRTASGK 334
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
40-520 |
3.44e-74 |
|
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: 241.75 E-value: 3.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQIsaTENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNisyeqst 119
Cdd:cd17631 6 RRHPDRTALV--FGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 ieklFSITRPNIIFCDGDefekvrsataqldvkiitmrnhpSGSiridqvlstpieknfqPVRLEQgndqtLAILC-SSG 198
Cdd:cd17631 77 ----FRLTPPEVAYILAD-----------------------SGA----------------KVLFDD-----LALLMyTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 199 TTGIPKAVTITNsRQILNSSHS------LTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQ 272
Cdd:cd17631 109 TTGRPKGAMLTH-RNLLWNAVNalaaldLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 273 ITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKdcLHFAYGFTELGSMAALNLHFD--EKP 350
Cdd:cd17631 188 VTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVK--FVQGYGMTETSPGVTFLSPEDhrRKL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 351 NSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK-MRDhhNWFHTGDLGYVDDDGFIYIVERKK 429
Cdd:cd17631 266 GSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAaFRD--GWFHTGDLGRLDEDGYLYIVDRKK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 430 DMLKF--QNImyYPNEIESVISKMPDVVEVCVFGV----WNEIngdeATAAVVKKRGSALTAQDIVDYVETHIdAKYK-- 501
Cdd:cd17631 344 DMIISggENV--YPAEVEDVLYEHPAVAEVAVIGVpdekWGEA----VVAVVVPRPGAELDEDELIAHCRERL-ARYKip 416
|
490 500
....*....|....*....|
gi 21356441 502 -QLnggaIIVEDLVRSPNGK 520
Cdd:cd17631 417 kSV----EFVDALPRNATGK 432
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
17-523 |
4.76e-70 |
|
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: 233.96 E-value: 4.76e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 17 SGDQLEYYFDPHLSIgeiifnemrrhPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISA 96
Cdd:cd17642 16 AGEQLHKAMKRYASV-----------PGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 97 VAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDGDEFEKVRSATAQLDV--KIITM--RNHPSGSIRIDQVLST 172
Cdd:cd17642 85 PVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIikTIIILdsKEDYKGYQCLYTFITQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 173 PI-----EKNFQPVRLEQgNDQTLAILCSSGTTGIPKAVTITNSRQILNSSHS---LTTNDVQYSHSTLDWIT-----GL 239
Cdd:cd17642 165 NLppgfnEYDFKPPSFDR-DEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHArdpIFGNQIIPDTAILTVIPfhhgfGM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 240 LTTVTSGVFSTkRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIR 319
Cdd:cd17642 244 FTTLGYLICGF-RVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 320 SRLSKDCLHFAYGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKVI-CEKGESLGPDEVGELCLWNGQYWAGYYGNPEET 398
Cdd:cd17642 323 KRFKLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVdLDTGKTLGPNERGELCVKGPMIMKGYVNNPEAT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 399 HKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKK 478
Cdd:cd17642 403 KALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLE 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 21356441 479 RGSALTAQDIVDYVETHIDAKyKQLNGGAIIVEDLVRSPNGKTNR 523
Cdd:cd17642 483 AGKTMTEKEVMDYVASQVSTA-KRLRGGVKFVDEVPKGLTGKIDR 526
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
40-433 |
5.09e-70 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 230.28 E-value: 5.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAqISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQST 119
Cdd:pfam00501 6 ARTPDKTA-LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 IEKLFSITRPNIIFCDGD-EFEKVRSATAQLDVKIITMRNHPSGSIRIDQVLSTPIEKNFQPVRLEQGNDQTLAILC-SS 197
Cdd:pfam00501 85 LAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIyTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 198 GTTGIPKAVTIT---------NSRQILNSSHSLTTNDVQYSHSTLDWITG----LLTTVTSG---VFSTKriiaDNIFDP 261
Cdd:pfam00501 165 GTTGKPKGVMLThrnlvanvlSIKRVRPRGFGLGPDDRVLSTLPLFHDFGlslgLLGPLLAGatvVLPPG----FPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 262 EFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTELGSMAA 341
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVN-GYGLTETTGVVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 342 LNLHFDEK---PNSVGRLVAGLKLKVI-CEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVD 417
Cdd:pfam00501 320 TPLPLDEDlrsLGSVGRPLPGTEVKIVdDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRD 399
|
410
....*....|....*.
gi 21356441 418 DDGFIYIVERKKDMLK 433
Cdd:pfam00501 400 EDGYLEIVGRKKDQIK 415
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
27-520 |
5.90e-70 |
|
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: 232.90 E-value: 5.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 27 PHLSIGEIIFNEMRRHPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGI 106
Cdd:cd05904 3 TDLPLDSVSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 107 AFHSLNISYEQSTIEKLFSITRPNIIFCDGDEFEKVRSataqLDVKIITMRNHPSGSIRIDQVLSTPIEKNFQPVRLEQg 186
Cdd:cd05904 83 VVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLAS----LALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQ- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 nDQTLAILCSSGTTGIPKAVTIT------NSRQILNSSHSLTTNDVQY------SHstldwITGLLTTVTSGVFSTKRII 254
Cdd:cd05904 158 -DDVAALLYSSGTTGRSKGVMLThrnliaMVAQFVAGEGSNSDSEDVFlcvlpmFH-----IYGLSSFALGLLRLGATVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 255 ADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFT 334
Cdd:cd05904 232 VMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 335 ELGSMAALNLHFDE---KPNSVGRLVAGLKLKVI-CEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHT 410
Cdd:cd05904 312 ESTGVVAMCFAPEKdraKYGSVGRLVPNVEAKIVdPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 411 GDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVD 490
Cdd:cd05904 392 GDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMD 471
|
490 500 510
....*....|....*....|....*....|
gi 21356441 491 YVETHIdAKYKQLNGGAiIVEDLVRSPNGK 520
Cdd:cd05904 472 FVAKQV-APYKKVRKVA-FVDAIPKSPSGK 499
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
57-523 |
1.39e-68 |
|
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: 228.22 E-value: 1.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDg 136
Cdd:cd05936 25 LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVA- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 137 DEFEKVRSATAQLDVKIItmrNHPsgsiridqvlstpieknfqpvrleqgnDQTLAILCSSGTTGIPKAVTIT------N 210
Cdd:cd05936 104 VSFTDLLAAGAPLGERVA---LTP---------------------------EDVAVLQYTSGTTGVPKGAMLThrnlvaN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 211 SRQILN-SSHSLTTNDV-----QYSHsTLDWITGLLTTVTSGVFStkrIIADNiFDPEFFMRLVEEHQITWIIQAPAHMA 284
Cdd:cd05936 154 ALQIKAwLEDLLEGDDVvlaalPLFH-VFGLTVALLLPLALGATI---VLIPR-FRPIGVLKEIRKHRVTIFPGVPTMYI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 285 MMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTELGSMAALN-LHFDEKPNSVGRLVAGLKLK 363
Cdd:cd05936 229 ALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVE-GYGLTETSPVVAVNpLDGPRKPGSIGIPLPGTEVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 364 VICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK-MRDhhNWFHTGDLGYVDDDGFIYIVERKKDML--KFQNImyY 440
Cdd:cd05936 308 IVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEaFVD--GWLRTGDIGYMDEDGYFFIVDRKKDMIivGGFNV--Y 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 441 PNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYK---QLnggaIIVEDLVRSP 517
Cdd:cd05936 384 PREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQL-AGYKvprQV----EFRDELPKSA 458
|
....*.
gi 21356441 518 NGKTNR 523
Cdd:cd05936 459 VGKILR 464
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
25-523 |
3.25e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 225.84 E-value: 3.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 25 FDPHLSIGEIIFNEMRRHPQliAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHisavAYACFFn 104
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPD--KEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHE----YLEAYF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 105 GIA-----FHSLNISYEQSTIEKLFSITRPNIIFCDgDEFEK-VRSATAQLDV--KIITM-----RNHPSGSIRIDQVLS 171
Cdd:PRK06187 75 AVPkigavLHPINIRLKPEEIAYILNDAEDRVVLVD-SEFVPlLAAILPQLPTvrTVIVEgdgpaAPLAPEVGEYEELLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 172 T-PIEKNFQPVRLeqgNDqtLAILC-SSGTTGIPKAVTITNsRQILnsSHS--------LTTNDVQ-------YSHStld 234
Cdd:PRK06187 154 AaSDTFDFPDIDE---ND--AAAMLyTSGTTGHPKGVVLSH-RNLF--LHSlavcawlkLSRDDVYlvivpmfHVHA--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 235 WITGLLTTVtSGVfstKRIIADNiFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVET 314
Cdd:PRK06187 223 WGLPYLALM-AGA---KQVIPRR-FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 315 QHRIRSRLSKDCLHfAYGFTE---LGSMAALNLHFD---EKPNSVGRLVAGLKLKVICEKGESLGPD--EVGELCL---W 383
Cdd:PRK06187 298 LREFKEKFGIDLVQ-GYGMTEtspVVSVLPPEDQLPgqwTKRRSAGRPLPGVEARIVDDDGDELPPDggEVGEIIVrgpW 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 384 NGQywaGYYGNPEETHKMRDHhNWFHTGDLGYVDDDGFIYIVERKKDMLKF--QNImyYPNEIESVISKMPDVVEVCVFG 461
Cdd:PRK06187 377 LMQ---GYWNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIISggENI--YPRELEDALYGHPAVAEVAVIG 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356441 462 VWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYKqLNGGAIIVEDLVRSPNGKTNR 523
Cdd:PRK06187 451 VPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRL-AKFK-LPKRIAFVDELPRTSVGKILK 510
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
40-520 |
4.95e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 222.47 E-value: 4.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQST 119
Cdd:PRK07656 16 RRFGDKEAYVFGDQR--LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 IEKLFSITRPNIIFCDGD---EFEKVRSATAQLDVKII----TMRNHPSGSIRIDQVLSTPIEKNFQPvrlEQGNDQTLA 192
Cdd:PRK07656 94 AAYILARGDAKALFVLGLflgVDYSATTRLPALEHVVIceteEDDPHTEKMKTFTDFLAAGDPAERAP---EVDPDDVAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 193 ILCSSGTTGIPKAVTITNsRQILNSSHS------LTTND-----VQYSHS---TLDWITGLLTTVTsgvfstkrIIADNI 258
Cdd:PRK07656 171 ILFTSGTTGRPKGAMLTH-RQLLSNAADwaeylgLTEGDrylaaNPFFHVfgyKAGVNAPLMRGAT--------ILPLPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 259 FDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTELGS 338
Cdd:PRK07656 242 FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 339 MAALN-LHFDEK--PNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGY 415
Cdd:PRK07656 322 VTTFNrLDDDRKtvAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 416 VDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETH 495
Cdd:PRK07656 402 LDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREH 481
|
490 500
....*....|....*....|....*.
gi 21356441 496 IdAKYKQlnGGAI-IVEDLVRSPNGK 520
Cdd:PRK07656 482 L-AKYKV--PRSIeFLDELPKNATGK 504
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
30-520 |
8.23e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 206.32 E-value: 8.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 30 SIGEIIFNEMRRHPQLIAQISatENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFH 109
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVF--GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 110 SLNISYEQSTIEKLFSITRPNIIFCDGDEFEKVRSATAQLDVK------IITMRNHPSGSIRIDQVLSTpiEKNFQP-VR 182
Cdd:PRK08316 90 PVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDtlilslVLGGREAPGGWLDFADWAEA--GSVAEPdVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 183 LeqgNDQTLA-ILCSSGTTGIPKAVTITNsRQILNSSHS------LTTNDVQ------YSHSTLDwiTGLLTTVTSGvfS 249
Cdd:PRK08316 168 L---ADDDLAqILYTSGTESLPKGAMLTH-RALIAEYVScivagdMSADDIPlhalplYHCAQLD--VFLGPYLYVG--A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 250 TKRIIADNifDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLR--YYlfGGSRASVETQHRIRSRLSKDCL 327
Cdd:PRK08316 240 TNVILDAP--DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRkgYY--GASIMPVEVLKELRERLPGLRF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 328 HFAYGFTELGSMA-ALNLH-FDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK-MRDh 404
Cdd:PRK08316 316 YNCYGQTEIAPLAtVLGPEeHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEaFRG- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 405 hNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALT 484
Cdd:PRK08316 395 -GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVT 473
|
490 500 510
....*....|....*....|....*....|....*.
gi 21356441 485 AQDIVDYVETHIdAKYKqLNGGAIIVEDLVRSPNGK 520
Cdd:PRK08316 474 EDELIAHCRARL-AGFK-VPKRVIFVDELPRNPSGK 507
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
40-520 |
4.57e-55 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 193.15 E-value: 4.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQIsaTENTILTRAELQANAMHIASYMR-SLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQS 118
Cdd:PRK06839 13 YLHPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 119 TIEKLFSITRPNIIFCdgdefEKVRSATAQLDVKIITMRnHPsgsIRIDQVLSTpieKNFQPVRLEQGNDQTLAILC-SS 197
Cdd:PRK06839 91 ELIFQLKDSGTTVLFV-----EKTFQNMALSMQKVSYVQ-RV---ISITSLKEI---EDRKIDNFVEKNESASFIICyTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 198 GTTGIPKAVTITNSRQILNSSHS-----LTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQ 272
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNtfaidLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 273 ITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRlskdCLHFA--YGFTELGSMAALNLHFD--E 348
Cdd:PRK06839 239 VTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR----GFLFGqgFGMTETSPTVFMLSEEDarR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 349 KPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK-MRDhhNWFHTGDLGYVDDDGFIYIVER 427
Cdd:PRK06839 315 KVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEEtIQD--GWLCTGDLARVDEDGFVYIVGR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 428 KKDML--KFQNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYKqLNG 505
Cdd:PRK06839 393 KKEMIisGGENI--YPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFL-AKYK-IPK 468
|
490
....*....|....*
gi 21356441 506 GAIIVEDLVRSPNGK 520
Cdd:PRK06839 469 EIVFLKELPKNATGK 483
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
49-523 |
2.52e-54 |
|
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: 190.99 E-value: 2.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 49 ISATENTI-LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTthisaVAYACFFNGIAF-----HSLNISYEQSTIEK 122
Cdd:cd05926 6 LVVPGSTPaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNG-----LEFVVAFLAAARagavvAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 123 LFSITRPNIIFCDGDEFEKVRSATAQLDVKIITMRNHPSGSIRIDQ----VLSTPIEKNFQPVRLEQGNDQTLaILCSSG 198
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPASRAASKLGLAILELALDVGVLIRAPSaeslSNLLADKKNAKSEGVPLPDDLAL-ILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 199 TTGIPKAVTITNsRQILNS------SHSLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQ 272
Cdd:cd05926 160 TTGRPKGVPLTH-RNLAASatnitnTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 273 ITWIIQAPA-HMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTELGSMAALN--LHFDEK 349
Cdd:cd05926 239 ATWYTAVPTiHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLE-AYGMTEAAHQMTSNplPPGPRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 350 PNSVGRLVaGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKK 429
Cdd:cd05926 318 PGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 430 DML-----KFQnimyyPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYKqLN 504
Cdd:cd05926 397 ELInrggeKIS-----PLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHL-AAFK-VP 469
|
490
....*....|....*....
gi 21356441 505 GGAIIVEDLVRSPNGKTNR 523
Cdd:cd05926 470 KKVYFVDELPKTATGKIQR 488
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
28-523 |
1.44e-53 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 189.81 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 28 HLSIGEIIFNEMRRHPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIA 107
Cdd:PLN02246 22 HLPLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 108 FHSLNISYEQSTIEKLFSITRPNIIFCDGDEFEKVRSATAQLDVKIITMRNHPSGSIRIdQVLSTPIEKNFQPVRLEQgn 187
Cdd:PLN02246 102 TTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHF-SELTQADENELPEVEISP-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 188 DQTLAILCSSGTTGIPKAVTITNSRQIL---------NSSHSLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNI 258
Cdd:PLN02246 179 DDVVALPYSSGTTGLPKGVMLTHKGLVTsvaqqvdgeNPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 259 FDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTELGS 338
Cdd:PLN02246 259 FEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAGP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 339 MAALNLHF-----DEKPNSVGRLVAGLKLKVI-CEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGD 412
Cdd:PLN02246 339 VLAMCLAFakepfPVKSGSCGTVVRNAELKIVdPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 413 LGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYV 492
Cdd:PLN02246 419 IGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFV 498
|
490 500 510
....*....|....*....|....*....|....*
gi 21356441 493 ethidAK----YKQLNgGAIIVEDLVRSPNGKTNR 523
Cdd:PLN02246 499 -----AKqvvfYKRIH-KVFFVDSIPKAPSGKILR 527
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
40-524 |
4.44e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 188.33 E-value: 4.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQISATENTilTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQST 119
Cdd:PRK07470 18 RRFPDRIALVWGDRSW--TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 IEKLFSITRPNIIFCDGDEFEKVRSATAQ-LDVKIITMRNHPSGSIRIDQVLSTPIEKNFQPVRLEQgnDQTLAILCSSG 198
Cdd:PRK07470 96 VAYLAEASGARAMICHADFPEHAAAVRAAsPDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDH--DDPCWFFFTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 199 TTGIPKAVTITNSRQ---ILNssH------SLTTNDVQYSHSTLDWITG--LLTTVTSGVfsTKRIIADNIFDPEFFMRL 267
Cdd:PRK07470 174 TTGRPKAAVLTHGQMafvITN--HladlmpGTTEQDASLVVAPLSHGAGihQLCQVARGA--ATVLLPSERFDPAEVWAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 268 VEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFaYGFTEL-GSMAALNLHF 346
Cdd:PRK07470 250 VERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQY-FGLGEVtGNITVLPPAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 347 ---DEKPN----SVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK-MRDhhNWFHTGDLGYVDD 418
Cdd:PRK07470 329 hdaEDGPDarigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKaFRD--GWFRTGDLGHLDA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 419 DGFIYIVERKKDML--KFQNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHI 496
Cdd:PRK07470 407 RGFLYITGRASDMYisGGSNV--YPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKV 484
|
490 500
....*....|....*....|....*....
gi 21356441 497 dAKYKqLNGGAIIVEDLVRSPNGK-TNRM 524
Cdd:PRK07470 485 -ARYK-LPKRFFFWDALPKSGYGKiTKKM 511
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-501 |
3.50e-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: 3.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 188 DQTLAILCSSGTTGIPKAVTITNsRQILNSSHS------LTTND-----VQYSHStLDWITGLLTTVTSGvfsTKRIIAD 256
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTH-HNIVNNGYFigerlgLTEQDrlcipVPLFHC-FGSVLGVLACLTHG---ATMVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 257 NIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTE- 335
Cdd:cd05917 77 PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTEt 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 336 --LGSMAALNLHFDEKPNSVGRLVAGLKLKVI-CEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGD 412
Cdd:cd05917 157 spVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVdPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 413 LGYVDDDGFIYIVERKKDML--KFQNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVD 490
Cdd:cd05917 237 LAVMDEDGYCRIVGRIKDMIirGGENI--YPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKA 314
|
330
....*....|.
gi 21356441 491 YVETHIdAKYK 501
Cdd:cd05917 315 YCKGKI-AHYK 324
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
30-532 |
2.57e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 169.78 E-value: 2.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 30 SIGEIIFNEMRRHPQLIAqiSATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARN---TTHISAVAYACFFNGI 106
Cdd:PRK06188 13 TYGHLLVSALKRYPDRPA--LVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNrpeVLMAIGAAQLAGLRRT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 107 AFHSLNiSYEqstiEKLFSITRPNI---IFCDGDEFEKVRSATAQLD--VKIITMrnhpsGSIRIDQVLSTPIEKnFQPV 181
Cdd:PRK06188 91 ALHPLG-SLD----DHAYVLEDAGIstlIVDPAPFVERALALLARVPslKHVLTL-----GPVPDGVDLLAAAAK-FGPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 182 RLEQGNDQT--LAILCSSGTTGIPKAVTITNsRQILnsshslTTNDVQYShsTLDW---ITGLLTTVTSGVFSTK----- 251
Cdd:PRK06188 160 PLVAAALPPdiAGLAYTGGTTGKPKGVMGTH-RSIA------TMAQIQLA--EWEWpadPRFLMCTPLSHAGGAFflptl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 252 ----RIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRAS----VETQHRIRSRLS 323
Cdd:PRK06188 231 lrggTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSpvrlAEAIERFGPIFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 324 KdclhfAYGFTELGsMAALNL----HFDEKPN---SVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPE 396
Cdd:PRK06188 311 Q-----YYGQTEAP-MVITYLrkrdHDPDDPKrltSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 397 ETHK-MRDhhNWFHTGDLGYVDDDGFIYIVERKKDML---KFqNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEAT 472
Cdd:PRK06188 385 ETAEaFRD--GWLHTGDVAREDEDGFYYIVDRKKDMIvtgGF-NV--FPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVT 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356441 473 AAVVKKRGSALTAQDIVDYVETHIDAKY--KQLnggaIIVEDLVRSPNGKTNRMANKAFFLE 532
Cdd:PRK06188 460 AVVVLRPGAAVDAAELQAHVKERKGSVHapKQV----DFVDSLPLTALGKPDKKALRARYWE 517
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
53-523 |
2.41e-44 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 164.90 E-value: 2.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 53 ENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGiAFHS-LNISYEQSTIEKLFSITRPNI 131
Cdd:COG0365 36 EERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIG-AVHSpVFPGFGAEALADRIEDAEAKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 132 IFCDG------------DEFEKVRSATAQLDVKIITMRN----HPSGSIRIDQVLSTPiEKNFQPVRLEqgNDQTLAILC 195
Cdd:COG0365 115 LITADgglrggkvidlkEKVDEALEELPSLEHVIVVGRTgadvPMEGDLDWDELLAAA-SAEFEPEPTD--ADDPLFILY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 196 SSGTTGIPKAV----------TITNSRQILNsshsLTTNDVQYSHSTLDWITG--------LLTTVTSGVFSTKRIiadn 257
Cdd:COG0365 192 TSGTTGKPKGVvhthggylvhAATTAKYVLD----LKPGDVFWCTADIGWATGhsyivygpLLNGATVVLYEGRPD---- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 258 iF-DPEFFMRLVEEHQITWIIQAP-AHMAMMVNSPSFTTS-DLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFaYGFT 334
Cdd:COG0365 264 -FpDPGRLWELIEKYGVTVFFTAPtAIRALMKAGDEPLKKyDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDG-WGQT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 335 ELGSMAALNLHFDE-KPNSVGRLVAGLKLKVICEKGESLGPDEVGELCL---WNGQyWAGYYGNPEETHK-MRDHH-NWF 408
Cdd:COG0365 342 ETGGIFISNLPGLPvKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIkgpWPGM-FRGYWNDPERYREtYFGRFpGWY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 409 HTGDLGYVDDDGFIYIVERKKDMLKF--QNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALT-- 484
Cdd:COG0365 421 RTGDGARRDEDGYFWILGRSDDVINVsgHRI--GTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSde 498
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 21356441 485 -AQDIVDYVETHIdAKYKQLnggAII--VEDLVRSPNGKTNR 523
Cdd:COG0365 499 lAKELQAHVREEL-GPYAYP---REIefVDELPKTRSGKIMR 536
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
31-501 |
2.72e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 164.95 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 31 IGEIIFNEMRRHPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHS 110
Cdd:PRK12583 20 IGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 111 LNISYEQSTIEKLFSITRPNIIFCdGDEFeKVRSATAQLDVKIITMRNHPSGSI------RIDQVLS-----TPIEKNFQ 179
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVIC-ADAF-KTSDYHAMLQELLPGLAEGQPGALacerlpELRGVVSlapapPPGFLAWH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 180 PV----------RLEQGN-----DQTLAILCSSGTTGIPKAVTITNSrQILNS------SHSLTTND-----VQYSHStL 233
Cdd:PRK12583 178 ELqargetvsreALAERQasldrDDPINIQYTSGTTGFPKGATLSHH-NILNNgyfvaeSLGLTEHDrlcvpVPLYHC-F 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 234 DWITGLLTTVTSGvfsTKRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVE 313
Cdd:PRK12583 256 GMVLANLGCMTVG---ACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 314 TQHRIRSRLSKDCLHFAYGFTELGSMAALNLHFDEKP---NSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAG 390
Cdd:PRK12583 333 VMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLErrvETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 391 YYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDML--KFQNImyYPNEIESVISKMPDVVEVCVFGVWNEING 468
Cdd:PRK12583 413 YWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIirGGENI--YPREIEEFLFTHPAVADVQVFGVPDEKYG 490
|
490 500 510
....*....|....*....|....*....|...
gi 21356441 469 DEATAAVVKKRGSALTAQDIVDYVETHIdAKYK 501
Cdd:PRK12583 491 EEIVAWVRLHPGHAASEEELREFCKARI-AHFK 522
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
191-523 |
7.87e-44 |
|
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: 160.72 E-value: 7.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 191 LAIL-CSSGTTGIPKAVTITNSRQILNSSHS-----LTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFF 264
Cdd:cd05935 86 LALIpYTSGTTGLPKGCMHTHFSAAANALQSavwtgLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 265 MRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRyyLFGGSRASVETQ--HRIRSRLSKDCLHfAYGFTELGSMAAL 342
Cdd:cd05935 166 LELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLK--VLTGGGAPMPPAvaEKLLKLTGLRFVE-GYGLTETMSQTHT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 343 NLHFDEKPNSVGRLVAGLKLKVI-CEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKM---RDHHNWFHTGDLGYVDD 418
Cdd:cd05935 243 NPPLRPKLQCLGIP*FGVDARVIdIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMDE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 419 DGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKK---RGSAlTAQDIVDYVETH 495
Cdd:cd05935 323 EGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRpeyRGKV-TEEDIIEWAREQ 401
|
330 340
....*....|....*....|....*...
gi 21356441 496 IdAKYKQLNgGAIIVEDLVRSPNGKTNR 523
Cdd:cd05935 402 M-AAYKYPR-EVEFVDELPRSASGKILW 427
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
46-520 |
5.48e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 160.07 E-value: 5.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 46 IAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFS 125
Cdd:PRK08276 1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 126 ITRPNIIFCDGDEFEKVRSATAQL--DVKIITM-RNHPSGSIRIDQVLS----TPIEknfqpvrleqgnDQTL--AILCS 196
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELpaGVPLLLVvAGPVPGFRSYEEALAaqpdTPIA------------DETAgaDMLYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 197 SGTTGIPKAV-----------TITNSRQILNSSHSLTTNDVQYS-----HST-LDWITGLLT---TVtsgVFSTKriiad 256
Cdd:PRK08276 149 SGTTGRPKGIkrplpgldpdeAPGMMLALLGFGMYGGPDSVYLSpaplyHTApLRFGMSALAlggTV---VVMEK----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 257 niFDPEFFMRLVEEHQIT---WIiqaPAHMAMMVNSPSFTTS--DLSSLRYYLFGGSRASVETQHRIRSRLSkDCLHFAY 331
Cdd:PRK08276 221 --FDAEEALALIERYRVThsqLV---PTMFVRMLKLPEEVRAryDVSSLRVAIHAAAPCPVEVKRAMIDWWG-PIIHEYY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 332 GFTELGSMAALNLH-FDEKPNSVGRLVAGlKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHT 410
Cdd:PRK08276 295 ASSEGGGVTVITSEdWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 411 GDLGYVDDDGFIYIVERKKDML--KFQNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALT---A 485
Cdd:PRK08276 374 GDVGYLDEDGYLYLTDRKSDMIisGGVNI--YPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGdalA 451
|
490 500 510
....*....|....*....|....*....|....*...
gi 21356441 486 QDIVDYVETHIdAKYK---QLNggaiIVEDLVRSPNGK 520
Cdd:PRK08276 452 AELIAWLRGRL-AHYKcprSID----FEDELPRTPTGK 484
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
58-523 |
1.12e-42 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 159.91 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 58 TRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDG- 136
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 137 -------DEFEKVRSATAQLDVKIITMRNHPSGS-IRIDQVLS--TPIEknfQPVRLEqgNDQTLAILCSSGTTGIPKAV 206
Cdd:PRK06087 131 fkqtrpvDLILPLQNQLPQLQQIVGVDKLAPATSsLSLSQIIAdyEPLT---TAITTH--GDELAAVLFTSGTEGLPKGV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 207 TITN-----SRQILNSSHSLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQITWIIQAPA 281
Cdd:PRK06087 206 MLTHnnilaSERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 282 HMAMMVNSPSFTTSDLSSLRYYLFGGSRasvetqhrIRSRLSKDCLHF------AYGFTELGSMAALNLhfdEKP----- 350
Cdd:PRK06087 286 FIYDLLNLLEKQPADLSALRFFLCGGTT--------IPKKVARECQQRgikllsVYGSTESSPHAVVNL---DDPlsrfm 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 351 NSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKD 430
Cdd:PRK06087 355 HTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 431 ML--KFQNIMyyPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVV-KKRGSALTAQDIVDYVETHIDAKYKQLNGGA 507
Cdd:PRK06087 435 IIvrGGENIS--SREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlKAPHHSLTLEEVVAFFSRKRVAKYKYPEHIV 512
|
490
....*....|....*.
gi 21356441 508 IIvEDLVRSPNGKTNR 523
Cdd:PRK06087 513 VI-DKLPRTASGKIQK 527
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
29-523 |
5.55e-42 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 158.22 E-value: 5.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 29 LSIGEIIFNEMRRHPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAF 108
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 109 HSLNISYEQSTIEKLFSITRPNIIFCDGDEFEKVRSataqLDVKIITM-RNHPSGSIRIDQVLSTPIEKNFQPVRLEQGN 187
Cdd:PLN02330 108 SGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKG----LGLPVIVLgEEKIEGAVNWKELLEAADRAGDTSDNEEILQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 188 DQTLAILCSSGTTGIPKAVTITNSRQILNSSHSL------------TTNDVQYSHstldwITGLLTTVTSGVFSTKRIIA 255
Cdd:PLN02330 184 TDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLfsvgpemigqvvTLGLIPFFH-----IYGITGICCATLRNKGKVVV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 256 DNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSL--RYYLFGGSRASVETQHRIRSRLSKDCLHFAYGF 333
Cdd:PLN02330 259 MSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLklQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 334 TELGSMAALnlHFD-------EKPNSVGRLVAGLKLKVI-CEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHH 405
Cdd:PLN02330 339 TEHSCITLT--HGDpekghgiAKKNSVGFILPNLEVKFIdPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDED 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 406 NWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTA 485
Cdd:PLN02330 417 GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE 496
|
490 500 510
....*....|....*....|....*....|....*...
gi 21356441 486 QDIVDYVETHIdAKYKQLNgGAIIVEDLVRSPNGKTNR 523
Cdd:PLN02330 497 EDILNFVAANV-AHYKKVR-VVQFVDSIPKSLSGKIMR 532
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
193-520 |
1.05e-41 |
|
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: 152.66 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 193 ILCSSGTTGIPKAVtITNSRQILNSSHS------LTTNDV-----QYSHS---TLDWITGLLTTVTsgvfstkrIIADNI 258
Cdd:cd17638 5 IMFTSGTTGRSKGV-MCAHRQTLRAAAAwadcadLTEDDRyliinPFFHTfgyKAGIVACLLTGAT--------VVPVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 259 FDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTE--L 336
Cdd:cd17638 76 FDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEagV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 337 GSMAALNLHFDEKPNSVGRLVAGLKLKvICEKGESL--GPDEVgelclwngqywAGYYGNPEETHKMRDHHNWFHTGDLG 414
Cdd:cd17638 156 ATMCRPGDDAETVATTCGRACPGFEVR-IADDGEVLvrGYNVM-----------QGYLDDPEATAEAIDADGWLHTGDVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 415 YVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVET 494
Cdd:cd17638 224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRE 303
|
330 340
....*....|....*....|....*.
gi 21356441 495 HIdAKYKqLNGGAIIVEDLVRSPNGK 520
Cdd:cd17638 304 RL-ANYK-VPRFVRFLDELPRNASGK 327
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
58-520 |
3.65e-41 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 153.22 E-value: 3.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 58 TRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDgd 137
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 138 efekvrsataqldvkiitmrnhpsgsiridqvlstpieknfqpvrleqgndqTLAILCSSGTTGIPKAVTITNsRQILNS 217
Cdd:cd05934 83 ----------------------------------------------------PASILYTSGTTGPPKGVVITH-ANLTFA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 218 SHS------LTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAM-MVNSP 290
Cdd:cd05934 110 GYYsarrfgLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYlLAQPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 291 SFTTSDlSSLRyyLFGGSRASVETQHRIRSRlskdclhF------AYGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKV 364
Cdd:cd05934 190 SPDDRA-HRLR--AAYGAPNPPELHEEFEER-------FgvrlleGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 365 ICEKGESLGPDEVGELCLWNGQYWA---GYYGNPEETHKMRdHHNWFHTGDLGYVDDDGFIYIVERKKDMLKF--QNIMY 439
Cdd:cd05934 260 VDDDGQELPAGEPGELVIRGLRGWGffkGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRrgENISS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 440 YpnEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIDakYKQLNGGAIIVEDLVRSPNG 519
Cdd:cd05934 339 A--EVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLA--YFKVPRYIRFVDDLPKTPTE 414
|
.
gi 21356441 520 K 520
Cdd:cd05934 415 K 415
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
26-536 |
4.24e-41 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 155.77 E-value: 4.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 26 DPHLSIGEIIFNEmRRHPQLIAQISATENTILTRAELQANAMHIASYM-RSLGLLQMDIVGIIARNTTHISAVAYACFFN 104
Cdd:PLN02574 37 DPNLDAVSFIFSH-HNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 105 GIAFHSLNISYEQSTIEKLFSITRPNIIFCDGDEFEKVRSataqLDVKIITMR---NHPSGSIRIDQVLSTPIEKNFQPV 181
Cdd:PLN02574 116 GGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSP----LGVPVIGVPenyDFDSKRIEFPKFYELIKEDFDFVP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 182 RLEQGNDQTLAILCSSGTTGIPKAVTITNSRQILNSSHSLTTNDVQYSHSTLD-----------------WITGLLTtVT 244
Cdd:PLN02574 192 KPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDnvylaalpmfhiyglslFVVGLLS-LG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 245 SGVFSTKRiiadniFDPEFFMRLVEEHQIT-WIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLS 323
Cdd:PLN02574 271 STIVVMRR------FDASDMVKVIDRFKVThFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 324 KDCLHFAYGFTELGSMA--ALNLHFDEKPNSVGRLVAGLKLKVI-CEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK 400
Cdd:PLN02574 345 HVDFIQGYGMTESTAVGtrGFNTEKLSKYSSVGLLAPNMQAKVVdWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 401 MRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRG 480
Cdd:PLN02574 425 TIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 21356441 481 SALTAQDIVDYVETHIdAKYKQLNgGAIIVEDLVRSPNGKTNRMANKAFFLEAKSS 536
Cdd:PLN02574 505 STLSQEAVINYVAKQV-APYKKVR-KVVFVQSIPKSPAGKILRRELKRSLTNSVSS 558
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
28-501 |
6.67e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 155.35 E-value: 6.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 28 HLSIGEIIFNEMRRHPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIA 107
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 108 FHSLNISY---------EQSTIEKLFSITRpniiFCDGDEFEKVRS-----ATAQL------------DVKIITMRNHPs 161
Cdd:PRK08315 95 LVTINPAYrlseleyalNQSGCKALIAADG----FKDSDYVAMLYElapelATCEPgqlqsarlpelrRVIFLGDEKHP- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 162 GSIRIDQVLSTPieKNFQPVRLEQ-----GNDQTLAILCSSGTTGIPKAVTITnSRQILNSSHS------LTTND----- 225
Cdd:PRK08315 170 GMLNFDELLALG--RAVDDAELAArqatlDPDDPINIQYTSGTTGFPKGATLT-HRNILNNGYFigeamkLTEEDrlcip 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 226 VQYSH---STLdwitGLLTTVTSGvfSTKRIIADnIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRY 302
Cdd:PRK08315 247 VPLYHcfgMVL----GNLACVTHG--ATMVYPGE-GFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 303 YLFGGSRASVETQHRIRSRLSKDCLHFAYGFTElGS----MAALNLHFDEKPNSVGRLVAGLKLKVI-CEKGESLGPDEV 377
Cdd:PRK08315 320 GIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTE-TSpvstQTRTDDPLEKRVTTVGRALPHLEVKIVdPETGETVPRGEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 378 GELC-------LwngqywaGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDML--KFQNImyYPNEIESVI 448
Cdd:PRK08315 399 GELCtrgysvmK-------GYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIirGGENI--YPREIEEFL 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 21356441 449 SKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYK 501
Cdd:PRK08315 470 YTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKI-AHYK 521
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
191-523 |
1.43e-40 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 149.34 E-value: 1.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 191 LAILCSSGTTGIPKAVTITNSRQILNSSH-----SLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNiFDPEFFM 265
Cdd:cd17637 3 FVIIHTAAVAGRPRGAVLSHGNLIAANLQlihamGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEK-FDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 266 RLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLfggsraSVETQHRIRsRLSKDC---LHFAYGFTELGSMAAL 342
Cdd:cd17637 82 ELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVL------GLDAPETIQ-RFEETTgatFWSLYGQTETSGLVTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 343 NLhFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEET-HKMRDhhNWFHTGDLGYVDDDGF 421
Cdd:cd17637 155 SP-YRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTaYTFRN--GWHHTGDLGRFDEDGY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 422 IYIVERK--KDMLK--FQNImyYPNEIESVISKMPDVVEVCVFGV----WNeingdEATAAV-VKKRGSALTAQDIVDYV 492
Cdd:cd17637 232 LWYAGRKpeKELIKpgGENV--YPAEVEKVILEHPAIAEVCVIGVpdpkWG-----EGIKAVcVLKPGATLTADELIEFV 304
|
330 340 350
....*....|....*....|....*....|.
gi 21356441 493 ETHIdAKYKQlNGGAIIVEDLVRSPNGKTNR 523
Cdd:cd17637 305 GSRI-ARYKK-PRYVVFVEALPKTADGSIDR 333
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
40-520 |
1.92e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 153.93 E-value: 1.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQISatENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNttHISAV--AYACFFNGIAFHSLNISYEQ 117
Cdd:PRK07788 60 RRAPDRAALID--ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARN--HRGFVlaLYAAGKVGARIILLNTGFSG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 118 STIEKLFSITRPNIIFCDgDEFEKVRSATAQLDVKIITMRNHP-------SGSIRIDQVL----STPIEKNFQPVRLeqg 186
Cdd:PRK07788 136 PQLAEVAAREGVKALVYD-DEFTDLLSALPPDLGRLRAWGGNPdddepsgSTDETLDDLIagssTAPLPKPPKPGGI--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 ndqtlaILCSSGTTGIPKAV------TITNSRQILnSSHSLTTNDVQ-----------YSHSTLdwITGLLTTVTsgvfs 249
Cdd:PRK07788 212 ------VILTSGTTGTPKGAprpepsPLAPLAGLL-SRVPFRAGETTllpapmfhatgWAHLTL--AMALGSTVV----- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 250 TKRIiadniFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTS--DLSSLRYYLFGGSRASVETQHRIRSRLSkDCL 327
Cdd:PRK07788 278 LRRR-----FDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAkyDTSSLKIIFVSGSALSPELATRALEAFG-PVL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 328 HFAYGFTELGSMA-ALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYG--NPEETHKMRDh 404
Cdd:PRK07788 352 YNLYGSTEVAFATiATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDgrDKQIIDGLLS- 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 405 hnwfhTGDLGYVDDDGFIYIVERKKDMLKF--QNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSA 482
Cdd:PRK07788 431 -----SGDVGYFDEDGLLFVDGRDDDMIVSggENV--FPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAA 503
|
490 500 510
....*....|....*....|....*....|....*...
gi 21356441 483 LTAQDIVDYVETHIdAKYKqLNGGAIIVEDLVRSPNGK 520
Cdd:PRK07788 504 LDEDAIKDYVRDNL-ARYK-VPRDVVFLDELPRNPTGK 539
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
151-502 |
5.95e-40 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 152.72 E-value: 5.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 151 VKIITMRNHPSGSIRIDQVLSTPIEKNFQPVRLEQgnDQTLAILCSSGTTGIPKAVTITNSRQILN---SSHSL-TTNDV 226
Cdd:PRK08751 173 VKKLVPEYRINGAIRFREALALGRKHSMPTLQIEP--DDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLaGTGKL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 227 QYSHSTLdwITGL------LTTVTSGVF----STKRIIAdNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSD 296
Cdd:PRK08751 251 EEGCEVV--ITALplyhifALTANGLVFmkigGCNHLIS-NPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQID 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 297 LSSLRYYLFGGSRASVETQHRIRsRLSKDCLHFAYGFTELGSMAALN-LHFDEKPNSVGRLVAGLKLKVICEKGESLGPD 375
Cdd:PRK08751 328 FSSLKMTLGGGMAVQRSVAERWK-QVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIG 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 376 EVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVV 455
Cdd:PRK08751 407 EIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 21356441 456 EVCVFGVWNEINGdEATAAVVKKRGSALTAQDIVDYVETHIDAkYKQ 502
Cdd:PRK08751 487 EVAAVGVPDEKSG-EIVKVVIVKKDPALTAEDVKAHARANLTG-YKQ 531
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
57-520 |
2.53e-39 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 148.68 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFcdg 136
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 137 defekvrsataqldvkiitmrnhpsgsiridqvlstpIEKNFQPVRLEQGNDQTLAILCSSGTTGIPKAVtITNSRQILN 216
Cdd:cd05903 79 -------------------------------------VPERFRQFDPAAMPDAVALLLFTSGTTGEPKGV-MHSHNTLSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 217 SSHSLTTN------DVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSP 290
Cdd:cd05903 121 SIRQYAERlglgpgDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 291 SFTTSDLSSLRYYLFGGSrasveTQHRIRSRLSKDCLHF----AYGFTELGSmAALNLHFDEKPNSV---GRLVAGLKLK 363
Cdd:cd05903 201 EEAGEPLSRLRTFVCGGA-----TVPRSLARRAAELLGAkvcsAYGSTECPG-AVTSITPAPEDRRLytdGRPLPGVEIK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 364 VICEKGESLGPDEVGELCLWNGQYWAGYYGNPEEThKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDML--KFQNIMyyP 441
Cdd:cd05903 275 VVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLT-ADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIirGGENIP--V 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 442 NEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIDAKYK---QLnggaIIVEDLVRSPN 518
Cdd:cd05903 352 LEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYwpeRL----VHVDDLPRTPS 427
|
..
gi 21356441 519 GK 520
Cdd:cd05903 428 GK 429
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
57-501 |
9.35e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 146.33 E-value: 9.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDG 136
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 137 DEFEKVRS--ATAQLDVKIITmrnhpsgsiRIDQVLSTPIEKNFQPVRLEQGN---------------------DQTLAI 193
Cdd:PRK06710 130 LVFPRVTNvqSATKIEHVIVT---------RIADFLPFPKNLLYPFVQKKQSNlvvkvsesetihlwnsvekevNTGVEV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 194 LC-----------SSGTTGIPKAVTITNSRQILNsshslTTNDVQYSHSTLD------------WITGLLTTVTSGVFST 250
Cdd:PRK06710 201 PCdpendlallqyTGGTTGFPKGVMLTHKNLVSN-----TLMGVQWLYNCKEgeevvlgvlpffHVYGMTAVMNLSIMQG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 251 KRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRsRLSKDCLHFA 330
Cdd:PRK06710 276 YKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFE-TVTGGKLVEG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 331 YGFTELGSMAALNLHFDEK-PNSVGRLVAGLKLKVIC-EKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRdHHNWF 408
Cdd:PRK06710 355 YGLTESSPVTHSNFLWEKRvPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 409 HTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDI 488
Cdd:PRK06710 434 HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEEL 513
|
490
....*....|...
gi 21356441 489 VDYVETHIdAKYK 501
Cdd:PRK06710 514 NQFARKYL-AAYK 525
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
30-470 |
9.49e-37 |
|
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: 143.19 E-value: 9.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 30 SIGEIIFNEMRRHP-QLIAQISATEN-TILTRAELQANAMHIASYMRSLGLLQMD-IVGIIARNTTHISAVaYACFFNGI 106
Cdd:cd05906 11 TLLELLLRAAERGPtKGITYIDADGSeEFQSYQDLLEDARRLAAGLRQLGLRPGDsVILQFDDNEDFIPAF-WACVLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 107 ------AFHslNISYEQSTIEKLFSI----TRPnIIFCDGDEFEKVRSATAQLDVKIITMrnhpsgsIRIDQVLSTPIEK 176
Cdd:cd05906 90 vpapltVPP--TYDEPNARLRKLRHIwqllGSP-VVLTDAELVAEFAGLETLSGLPGIRV-------LSIEELLDTAADH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 177 NFQPVRleqgNDQTLAILCSSGTTGIPKAVTITnSRQILNSS------HSLTTNDVQYSHSTLDWITGLlttVTSGVFST 250
Cdd:cd05906 160 DLPQSR----PDDLALLMLTSGSTGFPKAVPLT-HRNILARSagkiqhNGLTPQDVFLNWVPLDHVGGL---VELHLRAV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 251 KR------IIADNIF-DPEFFMRLVEEHQI--TWiiqAP----AHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHR 317
Cdd:cd05906 232 YLgcqqvhVPTEEILaDPLRWLDLIDRYRVtiTW---APnfafALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 318 IRSRLSK-----DCLHFAYGFTELGSMAALNLHFDEKPN-------SVGRLVAGLKLKVICEKGESLGPDEVGELCLWNG 385
Cdd:cd05906 309 LLRLLEPyglppDAIRPAFGMTETCSGVIYSRSFPTYDHsqalefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 386 QYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDdGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVE--VCVFGVW 463
Cdd:cd05906 389 VVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVR 467
|
....*..
gi 21356441 464 NEINGDE 470
Cdd:cd05906 468 DPGAETE 474
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
188-523 |
1.06e-36 |
|
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: 140.94 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 188 DQTLAILCSSGTTGIPKAVTITNS---RQILNSS--HSLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNI--FD 260
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAywLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGprFD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 261 PEFFMRLVEEHQITWIIQAPAHMAMM--VNSPSFttsDLSSLRYYLFGGSRASVETQHRIRSRLSKDcLHFAYGFTELGS 338
Cdd:cd05972 161 AERILELLERYGVTSFCGPPTAYRMLikQDLSSY---KFSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 339 MAALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCL---WNGQYwAGYYGNPEEThKMRDHHNWFHTGDLGY 415
Cdd:cd05972 237 TVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIklpPPGLF-LGYVGDPEKT-EASIRGDYYLTGDRAY 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 416 VDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRG---SALTAQDIVDYV 492
Cdd:cd05972 315 RDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGyepSEELAEELQGHV 394
|
330 340 350
....*....|....*....|....*....|....
gi 21356441 493 ETHIDA-KYKQlnggaII--VEDLVRSPNGKTNR 523
Cdd:cd05972 395 KKVLAPyKYPR-----EIefVEELPKTISGKIRR 423
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
40-520 |
1.44e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 141.95 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQST 119
Cdd:PRK06145 13 RRTPDRAALVYRDQE--ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 IEKLFSITRPNIIFCDgDEFEkvrsATAQLDVKIITMRNHPSGSIRidqVLSTP-IEKNFQPVRLEqgnDQTLAILCSSG 198
Cdd:PRK06145 91 VAYILGDAGAKLLLVD-EEFD----AIVALETPKIVIDAAAQADSR---RLAQGgLEIPPQAAVAP---TDLVRLMYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 199 TTGIPKAVTIT-------NSRQI----LNSSHSLTTNDVQYSHSTLDwITGLLTTVTSGvfsTKRIIADniFDPEFFMRL 267
Cdd:PRK06145 160 TTDRPKGVMHSygnlhwkSIDHVialgLTASERLLVVGPLYHVGAFD-LPGIAVLWVGG---TLRIHRE--FDPEAVLAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 268 VEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASvetQHRIR--SRLSKDCLHF-AYGFTELGSMAALNL 344
Cdd:PRK06145 234 IERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTP---ESRIRdfTRVFTRARYIdAYGLTETCSGDTLME 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 345 HFDE--KPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRdHHNWFHTGDLGYVDDDGFI 422
Cdd:PRK06145 311 AGREieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 423 YIVERKKDML--KFQNIMyyPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTaqdiVDYVETHIDAKY 500
Cdd:PRK06145 390 YLTDRKKDMIisGGENIA--SSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT----LEALDRHCRQRL 463
|
490 500
....*....|....*....|....*.
gi 21356441 501 ------KQLnggaIIVEDLVRSPNGK 520
Cdd:PRK06145 464 asfkvpRQL----KVRDELPRNPSGK 485
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
57-461 |
2.12e-36 |
|
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: 140.81 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIafhsLNIS-YEQSTIEKLFSItrpniifcd 135
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGA----VPVPiYPTSSAEQIAYI--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 136 gdefekVRSAtaqlDVKIItmrnhpsgsiridqVLSTPieknfqpvrleqgnDQTLAILCSSGTTGIPKAVTITNS---R 212
Cdd:cd05907 73 ------LNDS----EAKAL--------------FVEDP--------------DDLATIIYTSGTTGRPKGVMLSHRnilS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 213 QILNSSHSL-TTNDVQY------SHStLDWITG----LLTTVTSGVFSTKRIIADNI--FDPEFFM---RLVEEHQITWI 276
Cdd:cd05907 115 NALALAERLpATEGDRHlsflplAHV-FERRAGlyvpLLAGARIYFASSAETLLDDLseVRPTVFLavpRVWEKVYAAIK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 277 IQA-PAHMAMMvnspsFTTSDLSSLRYYLFGGSRASVETQHRIRsrlsKDCLHF--AYGFTELGSMAALNLHFDEKPNSV 353
Cdd:cd05907 194 VKAvPGLKRKL-----FDLAVGGRLRFAASGGAPLPAELLHFFR----ALGIPVyeGYGLTETSAVVTLNPPGDNRIGTV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 354 GRLVAGLKLKVicekgeslgpDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLK 433
Cdd:cd05907 265 GKPLPGVEVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLII 334
|
410 420 430
....*....|....*....|....*....|.
gi 21356441 434 F---QNImyYPNEIESVISKMPDVVEVCVFG 461
Cdd:cd05907 335 TsggKNI--SPEPIENALKASPLISQAVVIG 363
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
40-520 |
8.60e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 139.56 E-value: 8.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQST 119
Cdd:PRK09088 6 RLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 IEKLFSITRPNIIFCDgDEFEKVRSATAQLDVKIITMRNH-PSGSIRIDQvlstpieknfqpvrleqgnDQTLAILCSSG 198
Cdd:PRK09088 86 LDALLQDAEPRLLLGD-DAVAAGRTDVEDLAAFIASADALePADTPSIPP-------------------ERVSLILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 199 TTGIPKAVTITnSRQILNSSH--SLTTNDVQYSHSTLD----WITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQ 272
Cdd:PRK09088 146 TSGQPKGVMLS-ERNLQQTAHnfGVLGRVDAHSSFLCDapmfHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 273 --ITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETqhrIRSRLSKDC-LHFAYGFTELGS---MAALNLHF 346
Cdd:PRK09088 225 lgITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAED---ILGWLDDGIpMVDGFGMSEAGTvfgMSVDCDVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 347 DEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVE 426
Cdd:PRK09088 302 RAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 427 RKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYKqLNGG 506
Cdd:PRK09088 382 RKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRL-AKYK-VPKH 459
|
490
....*....|....
gi 21356441 507 AIIVEDLVRSPNGK 520
Cdd:PRK09088 460 LRLVDALPRTASGK 473
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
57-523 |
1.72e-35 |
|
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: 137.48 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIafhslnisyeqstiEKLFSITRpniifcdg 136
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGA--------------EAVLLNTR-------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 137 defekvrsataqldvkiitmrnhpsgsiridqvlSTPIEKNFQPVRLEQGNDQTLAILCSSGTTGIPKAVTITnSRQILN 216
Cdd:cd05912 60 ----------------------------------LTPNELAFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQT-FGNHWW 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 217 SSHS------LTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNiFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSP 290
Cdd:cd05912 105 SAIGsalnlgLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDK-FDAEQVLHLINSGKVTIISVVPTMLQRLLEIL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 291 SFTTSdlSSLRYYLFGGSRASvetQHRIRSRLSKDC-LHFAYGFTELGS-MAALN-LHFDEKPNSVGRLVAGLKLKVice 367
Cdd:cd05912 184 GEGYP--NNLRCILLGGGPAP---KPLLEQCKEKGIpVYQSYGMTETCSqIVTLSpEDALNKIGSAGKPLFPVELKI--- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 368 KGESLGPDEVGELCLWNGQYWAGYYGNPEEThKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDML--KFQNImyYPNEIE 445
Cdd:cd05912 256 EDDGQPPYEVGEILLKGPNVTKGYLNRPDAT-EESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIisGGENI--YPAEIE 332
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356441 446 SVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRgsALTAQDIVDYVETHIdAKYKqLNGGAIIVEDLVRSPNGKTNR 523
Cdd:cd05912 333 EVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER--PISEEELIAYCSEKL-AKYK-VPKKIYFVDELPRTASGKLLR 406
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
53-523 |
5.83e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 137.02 E-value: 5.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 53 ENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNG--IAFhsLN-------ISYEQSTIEKL 123
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGavAVL--LNtrlsreeLLWQLDDAEVK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 124 FSITrpniifcdGDEFEkvrsatAQLDVKIitmrnhpsgSIRIDQVLSTPiEKNFQPVRlEQGNDQTLAILCSSGTTGIP 203
Cdd:PRK03640 102 CLIT--------DDDFE------AKLIPGI---------SVKFAELMNGP-KEEAEIQE-EFDLDEVATIMYTSGTTGKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 204 KAVTITNSrqilNSSHS---------LTTND-----VQYSHstldwITGLLTTVTSGVFSTkRIIADNIFDPEFFMRLVE 269
Cdd:PRK03640 157 KGVIQTYG----NHWWSavgsalnlgLTEDDcwlaaVPIFH-----ISGLSILMRSVIYGM-RVVLVEKFDAEKINKLLQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 270 EHQITwIIQAPAHM--AMMVNSPSFTTSdlSSLRYYLFGGSRASVET-----QHRIRSRLSkdclhfaYGFTELGS-MAA 341
Cdd:PRK03640 227 TGGVT-IISVVSTMlqRLLERLGEGTYP--SSFRCMLLGGGPAPKPLleqckEKGIPVYQS-------YGMTETASqIVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 342 LNLHFD-EKPNSVGRLVAGLKLKvICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK-MRDhhNWFHTGDLGYVDDD 419
Cdd:PRK03640 297 LSPEDAlTKLGSAGKPLFPCELK-IEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATREtFQD--GWFKTGDIGYLDEE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 420 GFIYIVERKKDMLKF--QNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKkrGSALTAQDIVDYVETHId 497
Cdd:PRK03640 374 GFLYVLDRRSDLIISggENI--YPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKL- 448
|
490 500
....*....|....*....|....*.
gi 21356441 498 AKYKqLNGGAIIVEDLVRSPNGKTNR 523
Cdd:PRK03640 449 AKYK-VPKRFYFVEELPRNASGKLLR 473
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
55-520 |
6.53e-35 |
|
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: 137.76 E-value: 6.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 55 TILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTT-HISAVaYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIF 133
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHrHLELY-YAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 134 CDgDEF----EKVRSATAQLDVKIITMRNHPSGSIRIDQVLS--TPIEKNFQPVRLEQGNDQTLAILC-SSGTTGIPKAV 206
Cdd:cd12119 103 VD-RDFlpllEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAyeELLAAESPEYDWPDFDENTAAAICyTSGTTGNPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 207 TITNSRQILNSSHSLTTNDVQYSHStlD-------------WitGL-LTTVTSGvfsTKRIIADNIFDPEFFMRLVEEHQ 272
Cdd:cd12119 182 VYSHRSLVLHAMAALLTDGLGLSES--DvvlpvvpmfhvnaW--GLpYAAAMVG---AKLVLPGPYLDPASLAELIEREG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 273 ITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGS---RASVETQHRIRSRLskdcLHfAYGFTE---LGSMAAL---- 342
Cdd:cd12119 255 VTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSavpRSLIEAFEERGVRV----IH-AWGMTEtspLGTVARPpseh 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 343 -NLHFDEKPN---SVGRLVAGLKLKVICEKGESLGPD--EVGELCL---WngqYWAGYYGNPEEThKMRDHHNWFHTGDL 413
Cdd:cd12119 330 sNLSEDEQLAlraKQGRPVPGVELRIVDDDGRELPWDgkAVGELQVrgpW---VTKSYYKNDEES-EALTEDGWLRTGDV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 414 GYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVE 493
Cdd:cd12119 406 ATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLA 485
|
490 500
....*....|....*....|....*..
gi 21356441 494 THIdAKYkQLNGGAIIVEDLVRSPNGK 520
Cdd:cd12119 486 DKV-AKW-WLPDDVVFVDEIPKTSTGK 510
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
286-501 |
1.78e-34 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 136.72 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 286 MVNSPSFTTSDLSSLRYYLFGG---SRASVETQHRirsrLSKDCLHFAYGFTELGSMAALNLHFDEKPN-SVGRLVAGLK 361
Cdd:PRK08974 313 LLNNEEFQELDFSSLKLSVGGGmavQQAVAERWVK----LTGQYLLEGYGLTECSPLVSVNPYDLDYYSgSIGLPVPSTE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 362 LKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK-MRDhhNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYY 440
Cdd:PRK08974 389 IKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEvIKD--GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVY 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356441 441 PNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSaLTAQDIVDYVETHIDAkYK 501
Cdd:PRK08974 467 PNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPS-LTEEELITHCRRHLTG-YK 525
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
57-520 |
2.61e-34 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 136.34 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTI--------EKLFSITR 128
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELsfmlkhaeSKVLVVPK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 129 pniIFCDGDEFEKVRSATAQL-DVKIITMRNhPSGSIRIDQVLSTPI---EKNFQPV--RLEQGNDQTLAILCSSGTTGI 202
Cdd:PRK13295 136 ---TFRGFDHAAMARRLRPELpALRHVVVVG-GDGADSFEALLITPAweqEPDAPAIlaRLRPGPDDVTQLIYTSGTTGE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 203 PKAVTIT------NSRQILNSSHsLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQITWI 276
Cdd:PRK13295 212 PKGVMHTantlmaNIVPYAERLG-LGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 277 IQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGS---RASVEtqhRIRSRLSKDCLHfAYGFTELGSMAALNLHFDEK--PN 351
Cdd:PRK13295 291 MASTPFLTDLTRAVKESGRPVSSLRTFLCAGApipGALVE---RARAALGAKIVS-AWGMTENGAVTLTKLDDPDEraST 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 352 SVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKmrDHHNWFHTGDLGYVDDDGFIYIVERKKDM 431
Cdd:PRK13295 367 TDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDV 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 432 L--KFQNImyyPN-EIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIDAKyKQLNGGAI 508
Cdd:PRK13295 445 IirGGENI---PVvEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQKVAK-QYIPERLV 520
|
490
....*....|..
gi 21356441 509 IVEDLVRSPNGK 520
Cdd:PRK13295 521 VRDALPRTPSGK 532
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
64-525 |
2.91e-34 |
|
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: 134.88 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 64 ANAMHIASYMRSLGLLQMD-IVGIIARNTTHIS---AVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCD---G 136
Cdd:cd05922 1 LGVSAAASALLEAGGVRGErVVLILPNRFTYIElsfAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADagaA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 137 DEFEKVRSATAQldvkiitmrnhPSGSIRIDQVlsTPIEKNFQPVRLEqgNDQTLAILCSSGTTGIPKAVTITNsRQILN 216
Cdd:cd05922 81 DRLRDALPASPD-----------PGTVLDADGI--RAARASAPAHEVS--HEDLALLLYTSGSTGSPKLVRLSH-QNLLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 217 SSHS------LTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMvNSP 290
Cdd:cd05922 145 NARSiaeylgITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAML-TRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 291 SFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTE-LGSMAALNLH-FDEKPNSVGRLVAGLKLKVICEK 368
Cdd:cd05922 224 GFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEaTRRMTYLPPErILEKPGSIGLAIPGGEFEILDDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 369 GESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVI 448
Cdd:cd05922 304 GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 449 SKMPDVVEVCVFGVwnEINGDEATAAVVkkrgsALTAQDIVDYVethIDAKYKQLNGGAI-----IVEDLVRSPNGKTNR 523
Cdd:cd05922 384 RSIGLIIEAAAVGL--PDPLGEKLALFV-----TAPDKIDPKDV---LRSLAERLPPYKVpatvrVVDELPLTASGKVDY 453
|
..
gi 21356441 524 MA 525
Cdd:cd05922 454 AA 455
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
192-523 |
4.98e-34 |
|
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: 133.95 E-value: 4.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 192 AILCSSGTTGIPKAVTITNsRQILNSSHSL------TTNDV-------QYSHSTldwITGLLTTVTSG---VFSTKriia 255
Cdd:cd05941 93 LILYTSGTTGRPKGVVLTH-ANLAANVRALvdawrwTEDDVllhvlplHHVHGL---VNALLCPLFAGasvEFLPK---- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 256 dniFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFG-------GSRA-SVETQHRIRSRLSKDCL 327
Cdd:cd05941 165 ---FDPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAErlrlmvsGSAAlPVPTLEEWEAITGHTLL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 328 HfAYGFTELGsMAALN-LHFDEKPNSVGRLVAGLKLKVI-CEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHH 405
Cdd:cd05941 242 E-RYGMTEIG-MALSNpLDGERRPGTVGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 406 NWFHTGDLGYVDDDGFIYIVERKKDML-KFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVV-KKRGSAL 483
Cdd:cd05941 320 GWFKTGDLGVVDEDGYYWILGRSSVDIiKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVlRAGAAAL 399
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 21356441 484 TAQDIVDYVETHIdAKYKQlNGGAIIVEDLVRSPNGKTNR 523
Cdd:cd05941 400 SLEELKEWAKQRL-APYKR-PRRLILVDELPRNAMGKVNK 437
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
40-525 |
5.47e-34 |
|
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: 133.91 E-value: 5.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAqiSATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQST 119
Cdd:cd05945 2 AANPDRPA--VVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 IEKLFSITRPNIIFCDGDEfekvrsataqldvkiitmrnhpsgsiridqvlstpieknfqpvrleqgndqTLAILCSSGT 199
Cdd:cd05945 80 IREILDAAKPALLIADGDD---------------------------------------------------NAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 200 TGIPKAVTITN------SRQILnSSHSLTTNDVQYSH-------STLDWITGLLTTVTsgVFSTKRiiaDNIFDPEFFMR 266
Cdd:cd05945 109 TGRPKGVQISHdnlvsfTNWML-SDFPLGPGDVFLNQapfsfdlSVMDLYPALASGAT--LVPVPR---DATADPKQLFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 267 LVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTELgSMAALNLHF 346
Cdd:cd05945 183 FLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEA-TVAVTYIEV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 347 DEKPNS------VGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHN---WFHTGDLGYVD 417
Cdd:cd05945 262 TPEVLDgydrlpIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEgqrAYRTGDLVRLE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 418 DDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVvevcvfgvwneingdeaTAAVVKKRGSALTAQDIVDYVETHID 497
Cdd:cd05945 342 ADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGV-----------------KEAVVVPKYKGEKVTELIAFVVPKPG 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 21356441 498 AKYKQLNG----------------GAIIVEDLVRSPNGKTNRMA 525
Cdd:cd05945 405 AEAGLTKAikaelaerlppymiprRFVYLDELPLNANGKIDRKA 448
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
40-520 |
5.87e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 134.82 E-value: 5.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNiSYeqST 119
Cdd:PRK13391 8 QTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN-SH--LT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 IEKLFSI---TRPNIIFCDGDEFEKVRSATAQL-DVKIITMRNHPSGSIRID-------QVLSTPIEknfqpvrleqgnD 188
Cdd:PRK13391 85 PAEAAYIvddSGARALITSAAKLDVARALLKQCpGVRHRLVLDGDGELEGFVgyaeavaGLPATPIA------------D 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 189 QTL--AILCSSGTTGIPKAVTITNSRQILNSSHSLT---------TNDVQY------SHSTLDWITGLLTTVTSGVfstk 251
Cdd:PRK13391 153 ESLgtDMLYSSGTTGRPKGIKRPLPEQPPDTPLPLTaflqrlwgfRSDMVYlspaplYHSAPQRAVMLVIRLGGTV---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 252 rIIADNiFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTS--DLSSLRYYLFGGSRASVETQHRIRSRLSKdCLHF 329
Cdd:PRK13391 229 -IVMEH-FDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDkyDLSSLEVAIHAAAPCPPQVKEQMIDWWGP-IIHE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 330 AYGFTELGSMAALNLH-FDEKPNSVGRLVAGlKLKVICEKGESLGPDEVGELclwngqYWAG-----YYGNPEETHKMRD 403
Cdd:PRK13391 306 YYAATEGLGFTACDSEeWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTI------WFEGgrpfeYLNDPAKTAEARH 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 404 -HHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSA 482
Cdd:PRK13391 379 pDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVD 458
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 21356441 483 LT---AQDIVDYVETHIdAKYKQLNggAIIVED-LVRSPNGK 520
Cdd:PRK13391 459 PGpalAAELIAFCRQRL-SRQKCPR--SIDFEDeLPRLPTGK 497
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
55-520 |
2.14e-33 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 133.73 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 55 TILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFC 134
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 135 DGDEFEKVRSA----TAQLDVKIITMRNHPSGSIRIDQVLSTPIEKNFQPVRLEQGNdqTLAILCSSGTTGIPKAVTITN 210
Cdd:PRK06155 125 EAALLAALEAAdpgdLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAVQPGD--TAAILYTSGTTGPSKGVCCPH 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 211 SRQI---LNSSHSL--TTNDVQYSHSTLdWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQ--ITWIIQAPAHM 283
Cdd:PRK06155 203 AQFYwwgRNSAEDLeiGADDVLYTTLPL-FHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRRHGatVTYLLGAMVSI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 284 amMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSkdcLHFAYGFTELGSMAALNlHFDEKPNSVGRLVAGLKLK 363
Cdd:PRK06155 282 --LLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVD---LLDGYGSTETNFVIAVT-HGSQRPGSMGRLAPGFEAR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 364 VICEKGESLGPDEVGELCLWNGQYWA---GYYGNPEETHKM-RDHhnWFHTGDLGYVDDDGFIYIVERKKDMLKF--QNI 437
Cdd:PRK06155 356 VVDEHDQELPDGEPGELLLRADEPFAfatGYFGMPEKTVEAwRNL--WFHTGDRVVRDADGWFRFVDRIKDAIRRrgENI 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 438 MYYpnEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdaKYKQLNGGAIIVEDLVRSP 517
Cdd:PRK06155 434 SSF--EVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRL--AYFAVPRYVEFVAALPKTE 509
|
...
gi 21356441 518 NGK 520
Cdd:PRK06155 510 NGK 512
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
58-459 |
2.31e-33 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 131.23 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 58 TRAEL--QANAmhIASYMRSLGLLQM-DIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFC 134
Cdd:TIGR01733 1 TYRELdeRANR--LARHLRAAGGVGPgDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 135 DgdefEKVRSATAQLDVKIITmrnhpsgsIRIDQVLSTPIEKNFQPVRLEQGNDQTLAILCSSGTTGIPKAVTITNsRQI 214
Cdd:TIGR01733 79 D----SALASRLAGLVLPVIL--------LDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTH-RSL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 215 LNSSHSLTT------NDVQYSHSTLDW---ITGLLTTVTSG---VFSTKRIIADnifDPEFFMRLVEEHQITWIIQAPAH 282
Cdd:TIGR01733 146 VNLLAWLARrygldpDDRVLQFASLSFdasVEEIFGALLAGatlVVPPEDEERD---DAALLAALIAEHPVTVLNLTPSL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 283 MAMMVNSPSfttSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTE--LGSMAALNLH---FDEKPNSVGRLV 357
Cdd:TIGR01733 223 LALLAAALP---PALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTEttVWSTATLVDPddaPRESPVPIGRPL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 358 AGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEET--------HKMRDHHNWFHTGDLGYVDDDGFIYIVERKK 429
Cdd:TIGR01733 300 ANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTaerfvpdpFAGGDGARLYRTGDLVRYLPDGNLEFLGRID 379
|
410 420 430
....*....|....*....|....*....|
gi 21356441 430 DMLKFQNIMYYPNEIESVISKMPDVVEVCV 459
Cdd:TIGR01733 380 DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
190-523 |
3.46e-33 |
|
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: 129.30 E-value: 3.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 190 TLAILCSSGTTGIPKAVTITNSRQILNSSH------SLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEF 263
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDIlqkeglNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 264 FMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRAsVETQHRIRSRLSKDCLHFAYGFTELGSMAALN 343
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRA-IAADVRFIEATGLTNTAQVYGLSETGTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 344 LHFDEKP-NSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEET-HKMRDhhNWFHTGDLGYVDDDGF 421
Cdd:cd17635 162 TDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTaEVLID--GWVNTGDLGERREDGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 422 IYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVK---KRGSALTAQDIVDYVETHIDA 498
Cdd:cd17635 240 LFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeLDENAIRALKHTIRRELEPYA 319
|
330 340
....*....|....*....|....*
gi 21356441 499 KYKQLnggaIIVEDLVRSPNGKTNR 523
Cdd:cd17635 320 RPSTI----VIVTDIPRTQSGKVKR 340
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
57-501 |
4.34e-33 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 132.13 E-value: 4.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDG 136
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 137 DEFEKVRSATAQlDVKIITMRNHPS--GSIRIDQVLSTPIE---------KNFQPVRLEQGnDQTLAILCSSGTTGIPKA 205
Cdd:PRK12406 92 DLLHGLASALPA-GVTVLSVPTPPEiaAAYRISPALLTPPAgaidwegwlAQQEPYDGPPV-PQPQSMIYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 206 VTITN--------SRQILNSSHSLTTNDVqyshsTLdwITGLLTTVTSGVFSTKRI-IADNI-----FDPEFFMRLVEEH 271
Cdd:PRK12406 170 VRRAAptpeqaaaAEQMRALIYGLKPGIR-----AL--LTGPLYHSAPNAYGLRAGrLGGVLvlqprFDPEELLQLIERH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 272 QITWIIQAPAHMAMMVNSPSFTTS--DLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFaYGFTELGSMA------ALN 343
Cdd:PRK12406 243 RITHMHMVPTMFIRLLKLPEEVRAkyDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEY-YGSTESGAVTfatsedALS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 344 lhfdeKPNSVGRLVAGLKLKVICEKGESLGPDEVGEL-CLWNGQYWAGYYGNPEETHKMrDHHNWFHTGDLGYVDDDGFI 422
Cdd:PRK12406 322 -----HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIySRIAGNPDFTYHNKPEKRAEI-DRGGFITSGDVGYLDADGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 423 YIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGdEATAAVVKKR-GSALTAQDIVDYVETHIdAKYK 501
Cdd:PRK12406 396 FLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFG-EALMAVVEPQpGATLDEADIRAQLKARL-AGYK 473
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
194-525 |
8.28e-33 |
|
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: 131.34 E-value: 8.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 194 LCSSGTTGIPKAVTITNS----------RQILnsshSLTTNDVQYSHSTLDWITGLLTTVT-------SGVFSTKRIIAD 256
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHAdiywtaelyaRNVL----GIREDDVCFSAAKLFFAYGLGNSLTfplsvgaTTVLMPERPTPA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 257 NIFDpeffmrLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTEL 336
Cdd:cd05959 245 AVFK------RIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILD-GIGSTEM 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 337 GSMAALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHnWFHTGDLGYV 416
Cdd:cd05959 318 LHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE-WTRTGDKYVR 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 417 DDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRG---SALTAQDIVDYVE 493
Cdd:cd05959 397 DDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGyedSEALEEELKEFVK 476
|
330 340 350
....*....|....*....|....*....|...
gi 21356441 494 THIDA-KYKQlngGAIIVEDLVRSPNGKTNRMA 525
Cdd:cd05959 477 DRLAPyKYPR---WIVFVDELPKTATGKIQRFK 506
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
174-520 |
2.15e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 130.85 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 174 IEKNFQPVRLEQGNDqTLAIL-CSSGTTGIPKAVTITNSR---QILNSSH--SLTTNDVQYSHSTLDWITGLLTTVTSGV 247
Cdd:PRK08314 176 LAAGLAPPPHTAGPD-DLAVLpYTSGTTGVPKGCMHTHRTvmaNAVGSVLwsNSTPESVVLAVLPLFHVTGMVHSMNAPI 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 248 FSTKRIIADNIFDPEFFMRLVEEHQIT-WiiQAPAhmAMMVN---SPSFTTSDLSSLRYylFGGSRASVETQhrIRSRLS 323
Cdd:PRK08314 255 YAGATVVLMPRWDREAAARLIERYRVThW--TNIP--TMVVDflaSPGLAERDLSSLRY--IGGGGAAMPEA--VAERLK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 324 KDC-LHF--AYGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKVI-CEKGESLGPDEVGELCLWNGQYWAGYYGNPEETH 399
Cdd:PRK08314 327 ELTgLDYveGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIdPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 400 KM---RDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVV 476
Cdd:PRK08314 407 EAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVV 486
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 21356441 477 KK---RGSAlTAQDIVDYVETHIDA-KYKQLnggAIIVEDLVRSPNGK 520
Cdd:PRK08314 487 LRpeaRGKT-TEEEIIAWAREHMAAyKYPRI---VEFVDSLPKSGSGK 530
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
41-523 |
3.18e-32 |
|
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: 129.55 E-value: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 41 RHPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTI 120
Cdd:cd05923 13 RAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 121 EKLfsITRPNI---IFCDGDEfekVRSATAQLDVKIITMRNHPSgsIRIDQVLSTPIEknFQPVRLEQgndqTLAILCSS 197
Cdd:cd05923 93 AEL--IERGEMtaaVIAVDAQ---VMDAIFQSGVRVLALSDLVG--LGEPESAGPLIE--DPPREPEQ----PAFVFYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 198 GTTGIPKAVTItnSRQILNSSHSLTTNDVQYSHSTLDWITGLLTTV-TSGVFST--------KRIIADNIFDPEFFMRLV 268
Cdd:cd05923 160 GTTGLPKGAVI--PQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYhVIGFFAVlvaalaldGTYVVVEEFDPADALKLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 269 EEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFaYGFTElgsmaALNLHFDE 348
Cdd:cd05923 238 EQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI-YGTTE-----AMNSLYMR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 349 KPNSVGRLVAGLKLKV-ICEKGES----LGPDEVGELC--LWNGQYWAGYYGNPEETHKmRDHHNWFHTGDLGYVDDDGF 421
Cdd:cd05923 312 DARTGTEMRPGFFSEVrIVRIGGSpdeaLANGEEGELIvaAAADAAFTGYLNQPEATAK-KLQDGWYRTGDVGYVDPSGD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 422 IYIVERKKDMLKF--QNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSaLTAQDIVDYVETHIDAK 499
Cdd:cd05923 391 VRILGRVDDMIISggENI--HPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGT-LSADELDQFCRASELAD 467
|
490 500
....*....|....*....|....
gi 21356441 500 YKQLNgGAIIVEDLVRSPNGKTNR 523
Cdd:cd05923 468 FKRPR-RYFFLDELPKNAMNKVLR 490
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
151-501 |
3.92e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 130.27 E-value: 3.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 151 VKIITMRNHPSGSIRIDQVLSTPIEKNFQPVRLeQGNDqtLAIL-CSSGTTGIPKAVTITNSRQILN--SSHSLTTNDVQ 227
Cdd:PRK05677 172 VKKMVPAYHLPQAVKFNDALAKGAGQPVTEANP-QADD--VAVLqYTGGTTGVAKGAMLTHRNLVANmlQCRALMGSNLN 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 228 YSHSTLdwITGL----LTTVTSGVFSTKRIIADNIF-----DPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLS 298
Cdd:PRK05677 249 EGCEIL--IAPLplyhIYAFTFHCMAMMLIGNHNILisnprDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFS 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 299 SLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVG 378
Cdd:PRK05677 327 ALKLTLSGGMALQLATAERWKEVTGCAICE-GYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVG 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 379 ELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVC 458
Cdd:PRK05677 406 ELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCA 485
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 21356441 459 VFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIDAkYK 501
Cdd:PRK05677 486 AIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTG-YK 527
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
26-461 |
2.58e-31 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 127.91 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 26 DPHLSIGEIIFNEMRRHPQLIAQISATEN--TILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFF 103
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 104 NGiAfhslnIS---YEQSTIEKLFSI---TRPNIIFCDGDE-FEKVRSATAQLD--VKIITM----RNHPSGSIRIDQVL 170
Cdd:COG1022 88 AG-A-----VTvpiYPTSSAEEVAYIlndSGAKVLFVEDQEqLDKLLEVRDELPslRHIVVLdprgLRDDPRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 171 STPIEKNFQPV---RLEQGNDQTLAILC-SSGTTGIPKAVTIT------NSRQILnSSHSLTTNDVQYSHSTLDWI---T 237
Cdd:COG1022 162 ALGREVADPAEleaRRAAVKPDDLATIIyTSGTTGRPKGVMLThrnllsNARALL-ERLPLGPGDRTLSFLPLAHVferT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 238 GLLTTVTSGV---FSTK-RIIADNI--FDPEFFM---RLVE----------EHQiTWIIQAPAHMAMMV----------- 287
Cdd:COG1022 241 VSYYALAAGAtvaFAESpDTLAEDLreVKPTFMLavpRVWEkvyagiqakaEEA-GGLKRKLFRWALAVgrryararlag 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 288 NSPSFttsdLSSLRYYL------------FGGsrasvetqhRIR------SRLSKDCLHF----------AYGFTELGSM 339
Cdd:COG1022 320 KSPSL----LLRLKHALadklvfsklreaLGG---------RLRfavsggAALGPELARFfralgipvleGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 340 AALNLHFDEKPNSVGRLVAGLKLKVicekgeslgpDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDD 419
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDED 456
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 21356441 420 GFIYIVERKKDMLKFQN-IMYYPNEIESVISKMPDVVEVCVFG 461
Cdd:COG1022 457 GFLRITGRKKDLIVTSGgKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
142-520 |
3.97e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 126.82 E-value: 3.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 142 VRSATAQLDVKIITMRNHPSGSIRIDQVLSTPIEkNFQPVRLEqgNDQTLAILCSSGTTGIPKAVTITNSR------QIL 215
Cdd:PRK07786 131 VRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGP-AHAPVDIP--NDSPALIMYTSGTTGRPKGAVLTHANltgqamTCL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 216 NSSHSLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIAD-NIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTT 294
Cdd:PRK07786 208 RTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPlGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARP 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 295 SDLSsLRYYLFGGSRASvETQHRIRSRLSKDCLHFA-YGFTELGSMAALNLHFD--EKPNSVGRLVAGLKLKVICEKGES 371
Cdd:PRK07786 288 RDLA-LRVLSWGAAPAS-DTLLRQMAATFPEAQILAaFGQTEMSPVTCMLLGEDaiRKLGSVGKVIPTVAARVVDENMND 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 372 LGPDEVGELCLWNGQYWAGYYGNPEETHKMRdHHNWFHTGDLGYVDDDGFIYIVERKKDML--KFQNImyYPNEIESVIS 449
Cdd:PRK07786 366 VPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKDMIisGGENI--YCAEVENVLA 442
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356441 450 KMPDVVEVCVFGVWNEINGDEATA-AVVKKRGSALTAQDIVDYVETHIdAKYKQLNgGAIIVEDLVRSPNGK 520
Cdd:PRK07786 443 SHPDIVEVAVIGRADEKWGEVPVAvAAVRNDDAALTLEDLAEFLTDRL-ARYKHPK-ALEIVDALPRNPAGK 512
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
162-491 |
1.20e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 125.52 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 162 GSIRIDQVLSTPIEKNFQPVRLeQGNDqtLAIL-CSSGTTGIPKAVTIT------NSRQI---LNSSHSLTTNDVQYS-- 229
Cdd:PRK07059 180 GHVRFNDALAEGARQTFKPVKL-GPDD--VAFLqYTGGTTGVSKGATLLhrnivaNVLQMeawLQPAFEKKPRPDQLNfv 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 230 ------HSTLDWITGLLTTVTSGVfstkRIIADNIFDPEFFMRLVEEHQITWIiqaPA----HMAMMvNSPSFTTSDLSS 299
Cdd:PRK07059 257 calplyHIFALTVCGLLGMRTGGR----NILIPNPRDIPGFIKELKKYQVHIF---PAvntlYNALL-NNPDFDKLDFSK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 300 LRYYLFGGsrasVETQHRIRSRLSK--DC-LHFAYGFTELGSMAALN-LHFDEKPNSVGRLVAGLKLKVICEKGESLGPD 375
Cdd:PRK07059 329 LIVANGGG----MAVQRPVAERWLEmtGCpITEGYGLSETSPVATCNpVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLG 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 376 EVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVV 455
Cdd:PRK07059 405 EPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVL 484
|
330 340 350
....*....|....*....|....*....|....*.
gi 21356441 456 EVCVFGVWNEINGdEATAAVVKKRGSALTAQDIVDY 491
Cdd:PRK07059 485 EVAAVGVPDEHSG-EAVKLFVVKKDPALTEEDVKAF 519
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
183-523 |
1.41e-30 |
|
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: 123.79 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 183 LEQGNDqtLA-ILCSSGTTGIPKAVTITNsRQILN------SSHSLTTNDVQYSHSTLDW---ITGLLTTVTSGvfSTKR 252
Cdd:cd05930 89 LTDPDD--LAyVIYTSGSTGKPKGVMVEH-RGLVNlllwmqEAYPLTPGDRVLQFTSFSFdvsVWEIFGALLAG--ATLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 253 IIA-DNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFttSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAY 331
Cdd:cd05930 164 VLPeEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL--AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 332 GFTELGSMAAL----NLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLwNGQYWA-GYYGNPEETHKmRDHHN 406
Cdd:cd05930 242 GPTEATVDATYyrvpPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYI-GGAGLArGYLNRPELTAE-RFVPN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 407 WFH-------TGDLGYVDDDGFIYIVERKKDMLKfqnIMYY---PNEIESVISKMPDVVEVCVFgVWNEINGDEATAA-V 475
Cdd:cd05930 320 PFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVK---IRGYrieLGEIEAALLAHPGVREAAVV-AREDGDGEKRLVAyV 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 21356441 476 VKKRGSALTAQDIVDYVETH-----IDAKYkqlnggaIIVEDLVRSPNGKTNR 523
Cdd:cd05930 396 VPDEGGELDEEELRAHLAERlpdymVPSAF-------VVLDALPLTPNGKVDR 441
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
188-529 |
1.81e-30 |
|
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: 125.51 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 188 DQTLAILCSSGTTGIPKAVTITNSRQILNSSHSLTT------NDVQYSHSTLDWITG--------LLTTVTSGVFSTKri 253
Cdd:cd05967 230 TDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNiygikpGDVWWAASDVGWVVGhsyivygpLLHGATTVLYEGK-- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 254 iADNIFDPEFFMRLVEEHQITWIIQAP-AHMAMMVNSPS---FTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCL-H 328
Cdd:cd05967 308 -PVGTPDPGAFWRVIEKYQVNALFTAPtAIRAIRKEDPDgkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIdH 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 329 faYGFTELGSMAALNL----HFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELC------------LWNGQ------ 386
Cdd:cd05967 387 --WWQTETGWPITANPvglePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIViklplppgclltLWKNDerfkkl 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 387 YWA---GYYgnpeethkmrdhhnwfHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVW 463
Cdd:cd05967 465 YLSkfpGYY----------------DTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVR 528
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356441 464 NEINGDEATAAVVKKRGSALTAQDIVDYVETHID------AKYKQlnggAIIVEDLVRSPNGKTNRMANKAF 529
Cdd:cd05967 529 DELKGQVPLGLVVLKEGVKITAEELEKELVALVReqigpvAAFRL----VIFVKRLPKTRSGKILRRTLRKI 596
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
187-528 |
3.76e-30 |
|
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: 122.61 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 NDQTLaILCSSGTTGIPKAVTITNSRQIlnsSHSLTT--------NDVQYSHSTLDWITGLLTTV-TSGVFSTKRIIADN 257
Cdd:cd05969 89 EDPTL-LHYTSGTTGTPKGVLHVHDAMI---FYYFTGkyvldlhpDDIYWCTADPGWVTGTVYGIwAPWLNGVTNVVYEG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 258 IFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTS--DLSSLRYYLFGGSRASVETQHRIRSRLSKDcLHFAYGFTE 335
Cdd:cd05969 165 RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARkyDLSSLRFIHSVGEPLNPEAIRWGMEVFGVP-IHDTWWQTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 336 LGSMAALN-LHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNG--QYWAGYYGNpEETHKMRDHHNWFHTGD 412
Cdd:cd05969 244 TGSIMIANyPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGwpSMFRGIWND-EERYKNSFIDGWYLTGD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 413 LGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRG---SALTAQDIV 489
Cdd:cd05969 323 LAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGfepSDELKEEII 402
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 21356441 490 DYVETHIDAKY--KQLNggaiIVEDLVRSPNGKTNRMANKA 528
Cdd:cd05969 403 NFVRQKLGAHVapREIE----FVDNLPKTRSGKIMRRVLKA 439
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
40-520 |
4.28e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 123.58 E-value: 4.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNisyeqst 119
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAIN------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 ieklFSITRPNIIFCDGDEFEKVRSATAQLDVKI------ITMRNHPSGsiRIDQVLStpIEKNFQ---PVRLEQGNDQT 190
Cdd:PRK13390 81 ----HHLTAPEADYIVGDSGARVLVASAALDGLAakvgadLPLRLSFGG--EIDGFGS--FEAALAgagPRLTEQPCGAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 191 LaiLCSSGTTGIPKAVTITNSRQ-----------ILNSSHSLTTNDVQYS-----HST-LDWiTGLLTTVTSGVFSTKRi 253
Cdd:PRK13390 153 M--LYSSGTTGFPKGIQPDLPGRdvdapgdpivaIARAFYDISESDIYYSsapiyHAApLRW-CSMVHALGGTVVLAKR- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 254 iadniFDPEFFMRLVEEHQITWIIQAPAHMAMMV--NSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFaY 331
Cdd:PRK13390 229 -----FDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEY-Y 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 332 GFTELGSMAALNL-HFDEKPNSVGRLVAGlKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRD--HHNWF 408
Cdd:PRK13390 303 SSTEAHGMTFIDSpDWLAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHpaHPFWT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 409 HTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAV---VKKRGSALTA 485
Cdd:PRK13390 382 TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIqlvEGIRGSDELA 461
|
490 500 510
....*....|....*....|....*....|....*
gi 21356441 486 QDIVDYVETHIdAKYKQLNgGAIIVEDLVRSPNGK 520
Cdd:PRK13390 462 RELIDYTRSRI-AHYKAPR-SVEFVDELPRTPTGK 494
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
192-475 |
9.57e-30 |
|
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: 122.10 E-value: 9.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 192 AILCSSGTTGIPKAVtitnsRQilNSSHSLTTNDVQYSHSTLDWITGLLTTVTSG----------VFSTKR-----IIAD 256
Cdd:cd05929 129 KMLYSGGTTGRPKGI-----KR--GLPGGPPDNDTLMAAALGFGPGADSVYLSPAplyhaapfrwSMTALFmggtlVLME 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 257 NiFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTS--DLSSLRYYLFGGSRASVETQHRIrSRLSKDCLHFAYGFT 334
Cdd:cd05929 202 K-FDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNayDLSSLKRVIHAAAPCPPWVKEQW-IDWGGPIIWEYYGGT 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 335 ELGSMAALN-----LHfdekPNSVGRLVAGlKLKVICEKGESLGPDEVGELCLWNGQYWAgYYGNPEETHKMRDHHNWFH 409
Cdd:cd05929 280 EGQGLTIINgeewlTH----PGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWST 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356441 410 TGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAV 475
Cdd:cd05929 354 LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVV 419
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
259-501 |
1.30e-29 |
|
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: 118.94 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 259 FDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASV--ETQHRIRSRLskdclhFAYGFTEL 336
Cdd:cd17636 75 VDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMatVDTSPWGRKP------GGYGQTEV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 337 GSMAALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEET-HKMRDhhNWFHTGDLGY 415
Cdd:cd17636 149 MGLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNaRRTRG--GWHHTNDLGR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 416 VDDDGFIYIVERKKDMLK--FQNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVE 493
Cdd:cd17636 227 REPDGSLSFVGPKTRMIKsgAENI--YPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCR 304
|
....*...
gi 21356441 494 THIdAKYK 501
Cdd:cd17636 305 ARI-ASYK 311
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
57-520 |
3.93e-29 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 120.75 E-value: 3.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDG 136
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 137 DEFEKVRSATAQLDVKII-TMRNHPSGSIrIDQVLSTPIEknFQPVRleQGNDQTLAILCSSGTTGIPKAVTIT------ 209
Cdd:PRK07514 109 ANFAWLSKIAAAAGAPHVeTLDADGTGSL-LEAAAAAPDD--FETVP--RGADDLAAILYTSGTTGRSKGAMLShgnlls 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 210 NSrQILNSSHSLTTNDVqyshstldWITGLLTTVTSGVFstkriIADN---------IFDPEFFMRLVeehqITWIIQAP 280
Cdd:PRK07514 184 NA-LTLVDYWRFTPDDV--------LIHALPIFHTHGLF-----VATNvallagasmIFLPKFDPDAV----LALMPRAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 281 AHMAM------MVNSPSFTTSDLSSLRyyLF-GGS--------RASVE-TQHRIRSRlskdclhfaYGFTELGsMAALN- 343
Cdd:PRK07514 246 VMMGVptfytrLLQEPRLTREAAAHMR--LFiSGSapllaethREFQErTGHAILER---------YGMTETN-MNTSNp 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 344 LHFDEKPNSVGRLVAGLKLKVIC-EKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFI 422
Cdd:PRK07514 314 YDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 423 YIVERKKDML---KFqNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAK 499
Cdd:PRK07514 394 HIVGRGKDLIisgGY-NV--YPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRL-AR 469
|
490 500
....*....|....*....|.
gi 21356441 500 YKQLNgGAIIVEDLVRSPNGK 520
Cdd:PRK07514 470 FKQPK-RVFFVDELPRNTMGK 489
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
196-523 |
6.94e-29 |
|
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: 119.10 E-value: 6.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 196 SSGTTGIPKAV------TITNSRQILNSSHSLTTNDVQYSHSTLDWITGLLTTVTSGVFS-TKRIIADNIFDPEFFMRLV 268
Cdd:cd05919 99 SSGTTGPPKGVmhahrdPLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVgASAVLNPGWPTAERVLATL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 269 EEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTELGSMAALNLHFDE 348
Cdd:cd05919 179 ARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILD-GIGATEVGHIFLSNRPGAW 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 349 KPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKmRDHHNWFHTGDLGYVDDDGFIYIVERK 428
Cdd:cd05919 258 RLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRA-TFNGGWYRTGDKFCRDADGWYTHAGRA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 429 KDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSA---LTAQDIVDYVETHIdAKYKqLNG 505
Cdd:cd05919 337 DDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAApqeSLARDIHRHLLERL-SAHK-VPR 414
|
330
....*....|....*...
gi 21356441 506 GAIIVEDLVRSPNGKTNR 523
Cdd:cd05919 415 RIAFVDELPRTATGKLQR 432
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
283-523 |
1.76e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 119.16 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 283 MAMMvNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSrLSKDCLHFAYGFTELGSMAALNLHFDE-KPNSVGRLVAGLK 361
Cdd:PRK12492 319 VALM-DHPGFKDLDFSALKLTNSGGTALVKATAERWEQ-LTGCTIVEGYGLTETSPVASTNPYGELaRLGTVGIPVPGTA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 362 LKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYP 441
Cdd:PRK12492 397 LKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYP 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 442 NEIESVISKMPDVVEVCVFGVWNEINGdEATAAVVKKRGSALTAQDIVDYVETHIDAkYKqLNGGAIIVEDLVRSPNGKT 521
Cdd:PRK12492 477 NEIEDVVMAHPKVANCAAIGVPDERSG-EAVKLFVVARDPGLSVEELKAYCKENFTG-YK-VPKHIVLRDSLPMTPVGKI 553
|
..
gi 21356441 522 NR 523
Cdd:PRK12492 554 LR 555
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
51-525 |
2.17e-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: 118.75 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 51 ATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTthisavaYACFFNGIAFHSLNI-----SYEQSTIEKLFS 125
Cdd:cd05970 42 AGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRR-------YEFWYSLLALHKLGAiaipaTHQLTAKDIVYR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 126 ITRPNI--IFCDG-----DEFEKVRSATAQLDVKIITMRNHPSGSIRIDQVL--STPIeknFQPVR--LEQGNDQTLAIL 194
Cdd:cd05970 115 IESADIkmIVAIAednipEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKLIknASPD---FERPTanSYPCGEDILLVY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 195 CSSGTTGIPKAVTITNSR---QILNSS--HSLTTNDVQYSHSTLDWITGLLttvtsGVFSTKRIIADNI-------FDPE 262
Cdd:cd05970 192 FSSGTTGMPKMVEHDFTYplgHIVTAKywQNVREGGLHLTVADTGWGKAVW-----GKIYGQWIAGAAVfvydydkFDPK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 263 FFMRLVEEHQITWIIQAPAHMAMMVNSpSFTTSDLSSLRYYLFGGSRASVETQHRIRsRLSKDCLHFAYGFTELGSMAAL 342
Cdd:cd05970 267 ALLEKLSKYGVTTFCAPPTIYRFLIRE-DLSRYDLSSLRYCTTAGEALNPEVFNTFK-EKTGIKLMEGFGQTETTLTIAT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 343 NLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQ-----YWAGYYGNPEETHKMRdHHNWFHTGDLGYVD 417
Cdd:cd05970 345 FPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 418 DDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRG---SALTAQDIVDYVEt 494
Cdd:cd05970 424 EDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGyepSEELKKELQDHVK- 502
|
490 500 510
....*....|....*....|....*....|...
gi 21356441 495 HIDAKYKQLNggaII--VEDLVRSPNGKTNRMA 525
Cdd:cd05970 503 KVTAPYKYPR---IVefVDELPKTISGKIRRVE 532
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
196-477 |
7.08e-28 |
|
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: 113.65 E-value: 7.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 196 SSGTTGIPKAVTITNSRQIlnssHSLTTNDVQYSHSTLDWI--------TGLLTTVTSGVFSTKRIIADNIFDPEFFMRL 267
Cdd:cd17633 8 TSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAIlapgplshSLFLYGAISALYLGGTFIGQRKFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 268 VEEHQITWIIQAPAHMAMMVNspsfTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTELGSMAALNLHFD 347
Cdd:cd17633 84 INQYNATVIYLVPTMLQALAR----TLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 348 EKPNSVGRLVAGLKLKVICEKGeslgpDEVGELCLWNGQYWAGYYGNPEETHkmrdhHNWFHTGDLGYVDDDGFIYIVER 427
Cdd:cd17633 160 RPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGR 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 21356441 428 KKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGV----WNEI-----NGDEATAAVVK 477
Cdd:cd17633 230 ESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdarFGEIavalySGDKLTYKQLK 288
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
186-498 |
7.13e-28 |
|
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: 115.99 E-value: 7.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 186 GNDQTLAILCSSGTTGIPKAVtITNSRQILNS------SHSL--TTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADN 257
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGA-LHAHRVLLGHlpgvqfPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 258 I--FDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDcLHFAYGFTE 335
Cdd:cd05971 165 MtkFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVE-VNEFYGQTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 336 ----LGSMAALnlhFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLW--NGQYWAGYYGNPEETHKmRDHHNWFH 409
Cdd:cd05971 244 cnlvIGNCSAL---FPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEK-KMAGDWLL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 410 TGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRG---SALTAQ 486
Cdd:cd05971 320 TGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGetpSDALAR 399
|
330
....*....|..
gi 21356441 487 DIVDYVETHIDA 498
Cdd:cd05971 400 EIQELVKTRLAA 411
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
27-501 |
7.51e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 117.45 E-value: 7.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 27 PHLSIGEIIFNEMRRH-----PQLIAQISAteNTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYAC 101
Cdd:PRK06178 26 PEYPHGERPLTEYLRAwarerPQRPAIIFY--GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 102 FFNGIAFHSLN-ISYEQSTIEKLfSITRPNIIFCDgDEF----EKVRSATAQLDVKIITM-------------------R 157
Cdd:PRK06178 104 LKLGAVHVPVSpLFREHELSYEL-NDAGAEVLLAL-DQLapvvEQVRAETSLRHVIVTSLadvlpaeptlplpdslrapR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 158 NHPSGSIRIDQVLSTPIeknfQPVRLEQGNDQTLAIL-CSSGTTGIPKAVTITNSRQILNS------SHSLTTNDVQYSH 230
Cdd:PRK06178 182 LAAAGAIDLLPALRACT----APVPLPPPALDALAALnYTGGTTGMPKGCEHTQRDMVYTAaaayavAVVGGEDSVFLSF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 231 STLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQITwiiqapaHMAMMVNS-------PSFTTSDLSSLRYy 303
Cdd:PRK06178 258 LPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVT-------RTVMLVDNavelmdhPRFAEYDLSSLRQ- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 304 lfggSRAS-------VETQHRIRSRLSKDCLHFAYGFTELGSMAALNLHFDE-------KPNSVGRLVAGLKLKvIC--E 367
Cdd:PRK06178 330 ----VRVVsfvkklnPDYRQRWRALTGSVLAEAAWGMTETHTCDTFTAGFQDddfdllsQPVFVGLPVPGTEFK-ICdfE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 368 KGESLGPDEVGELCLWNGQYWAGYYGNPEET-HKMRDhhNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIES 446
Cdd:PRK06178 405 TGELLPLGAEGEIVVRTPSLLKGYWNKPEATaEALRD--GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEA 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 21356441 447 VISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYK 501
Cdd:PRK06178 483 LLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENM-AVYK 536
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
42-523 |
1.11e-27 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 116.78 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 42 HPQLIaqisaTENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNttHISAVAYACFFNGIAFHS--LNISYEQST 119
Cdd:PRK13382 59 RPGLI-----DELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRN--HRGFVEALLAANRIGADIllLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 IEKLFSITRPNIIFCDgDEF-EKVRSATAQLD--VKIITMRNHPsGSIRIDQVLSTPIEKnfQPVRLEQgndQTLAILCS 196
Cdd:PRK13382 132 LAEVVTREGVDTVIYD-EEFsATVDRALADCPqaTRIVAWTDED-HDLTVEVLIAAHAGQ--RPEPTGR---KGRVILLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 197 SGTTGIPKAVTITNSRQILNSShslttndvqyshSTLD---WITGLLTTVTSGVFST-------------KRIIADNIFD 260
Cdd:PRK13382 205 SGTTGTPKGARRSGPGGIGTLK------------AILDrtpWRAEEPTVIVAPMFHAwgfsqlvlaaslaCTIVTRRRFD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 261 PEFFMRLVEEHQITWIIQAPAHMAMMVNSPS--FTTSDLSSLRYYLFGGSRAS----VETQHRIrsrlsKDCLHFAYGFT 334
Cdd:PRK13382 273 PEATLDLIDRHRATGLAVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRpdvvIAFMDQF-----GDVIYNNYNAT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 335 ELGsMAALNLHFDEK--PNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYygnpeETHKMRDHHNWF-HTG 411
Cdd:PRK13382 348 EAG-MIATATPADLRaaPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY-----TSGSTKDFHDGFmASG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 412 DLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDY 491
Cdd:PRK13382 422 DVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQH 501
|
490 500 510
....*....|....*....|....*....|..
gi 21356441 492 VETHIdAKYKqLNGGAIIVEDLVRSPNGKTNR 523
Cdd:PRK13382 502 VRDNL-ANYK-VPRDIVVLDELPRGATGKILR 531
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
162-523 |
2.41e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 115.87 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 162 GSIRIDQVLSTPIEKNFQPVRLEQGNDQTLA-ILCSSGTTGIPKAVTITNSrqilnsshSLTTNDVQYSHstldWITGL- 239
Cdd:PRK05605 192 GTVPWETLVDAAIGGDGSDVSHPRPTPDDVAlILYTSGTTGKPKGAQLTHR--------NLFANAAQGKA----WVPGLg 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 240 -----------------LT-TVTSGVFSTKRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLR 301
Cdd:PRK05605 260 dgpervlaalpmfhaygLTlCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 302 YYLFGGSRASVETQHRIRSrLSKDCLHFAYGFTELGSMAALN-LHFDEKPNSVG--------RLVAGLKLkvicekGESL 372
Cdd:PRK05605 340 NAFSGAMALPVSTVELWEK-LTGGLLVEGYGLTETSPIIVGNpMSDDRRPGYVGvpfpdtevRIVDPEDP------DETM 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 373 GPDEVGELCLWNGQYWAGYYGNPEETHKMRdHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMP 452
Cdd:PRK05605 413 PDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHP 491
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356441 453 DVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYKqLNGGAIIVEDLVRSPNGKTNR 523
Cdd:PRK05605 492 GVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHL-TRYK-VPRRFYHVDELPRDQLGKVRR 560
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
58-501 |
4.52e-27 |
|
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: 113.70 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 58 TRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDgd 137
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 138 efekvrsatAQLDVKIITmrnhpsgSIRIDQVLS-----TPIEKNFQpvrleqgNDQTLAILCSSGTTGIPKAVTITNsR 212
Cdd:TIGR01923 79 ---------SLLEEKDFQ-------ADSLDRIEAagryeTSLSASFN-------MDQIATLMFTSGTTGKPKAVPHTF-R 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 213 QILNSSHSL------TTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDpefFMRLVEEHQITWIIQAPAHMAMM 286
Cdd:TIGR01923 135 NHYASAVGSkenlgfTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ---LLEMIANERVTHISLVPTQLNRL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 287 VNSpsftTSDLSSLRYYLFGGSRASVEtqhrirsrLSKDC------LHFAYGFTELGS-MAALNLHFDEKPNSVGRLVAG 359
Cdd:TIGR01923 212 LDE----GGHNENLRKILLGGSAIPAP--------LIEEAqqyglpIYLSYGMTETCSqVTTATPEMLHARPDVGRPLAG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 360 LKLKVICEKGESLGPDEVGELCLWNGqYWagyygNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDML--KFQNI 437
Cdd:TIGR01923 280 REIKIKVDNKEGHGEIMVKGANLMKG-YL-----YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIisGGENI 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356441 438 myYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKrgSALTAQDIVDYVETHIdAKYK 501
Cdd:TIGR01923 354 --YPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKL-AKYK 412
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
176-520 |
9.80e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 113.62 E-value: 9.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 176 KNFQPVRLEQ----GNDQTLAILCSSGTTGIPKAVTITNSrQILNSSH------SLTTNDVQYS-----HSTLDwITGLL 240
Cdd:PRK08008 157 KAQQPATLCYapplSTDDTAEILFTSGTTSRPKGVVITHY-NLRFAGYysawqcALRDDDVYLTvmpafHIDCQ-CTAAM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 241 TTVTSGV-------FSTKRiiadnifdpefFMRLVEEHQITwIIQApahMAMMVNS----PSFTTSDLSSLRYYLFGGSR 309
Cdd:PRK08008 235 AAFSAGAtfvllekYSARA-----------FWGQVCKYRAT-ITEC---IPMMIRTlmvqPPSANDRQHCLREVMFYLNL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 310 ASVETQ---HRIRSRLSKdclhfAYGFTELGSMAALNLHFDEK--PnSVGRLVAGLKLKVICEKGESLGPDEVGELCLwN 384
Cdd:PRK08008 300 SDQEKDafeERFGVRLLT-----SYGMTETIVGIIGDRPGDKRrwP-SIGRPGFCYEAEIRDDHNRPLPAGEIGEICI-K 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 385 G----QYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKF--QNIMyyPNEIESVISKMPDVVEVC 458
Cdd:PRK08008 373 GvpgkTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRggENVS--CVELENIIATHPKIQDIV 450
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356441 459 VFGVWNEINgDEATAA-VVKKRGSALTAQDIVDYVETHIdAKYKqLNGGAIIVEDLVRSPNGK 520
Cdd:PRK08008 451 VVGIKDSIR-DEAIKAfVVLNEGETLSEEEFFAFCEQNM-AKFK-VPSYLEIRKDLPRNCSGK 510
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
57-520 |
4.52e-26 |
|
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: 111.24 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTthisAVAYACFFN----GIAFHSLNISYEQSTIEKLFSITRPNII 132
Cdd:cd12118 30 YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNT----PAMYELHFGvpmaGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 133 FCDgDEFEkvrsataqldvkiitmrnhpsgsirIDQVLSTPiEKNFQPVRlEQGNDQTLAILCSSGTTGIPKAVTITNSR 212
Cdd:cd12118 106 FVD-REFE-------------------------YEDLLAEG-DPDFEWIP-PADEWDPIALNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 213 QILNSSHSLTTNDVQySHSTLDWI------TGLLTTVTSGVFSTKRIIADNIFDPEFFmRLVEEHQITWIIQAPAHMAMM 286
Cdd:cd12118 158 AYLNALANILEWEMK-QHPVYLWTlpmfhcNGWCFPWTVAAVGGTNVCLRKVDAKAIY-DLIEKHKVTHFCGAPTVLNML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 287 VNSPSFTTSDLSSLRYYLFGGSRASVETQHRIrSRLSKDCLHfAYGFTE---LGSMAALNLHFDEKPNSvgrLVAGLKLK 363
Cdd:cd12118 236 ANAPPSDARPLPHRVHVMTAGAPPPAAVLAKM-EELGFDVTH-VYGLTEtygPATVCAWKPEWDELPTE---ERARLKAR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 364 -----VICEKGESLGPD----------EVGELCLWNGQYWAGYYGNPEETHK-MRDhhNWFHTGDLGYVDDDGFIYIVER 427
Cdd:cd12118 311 qgvryVGLEEVDVLDPEtmkpvprdgkTIGEIVFRGNIVMKGYLKNPEATAEaFRG--GWFHSGDLAVIHPDGYIEIKDR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 428 KKDML--KFQNIMYYpnEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYKQLNg 505
Cdd:cd12118 389 SKDIIisGGENISSV--EVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHL-AGFMVPK- 464
|
490
....*....|....*
gi 21356441 506 gAIIVEDLVRSPNGK 520
Cdd:cd12118 465 -TVVFGELPKTSTGK 478
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
188-494 |
6.80e-26 |
|
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: 110.88 E-value: 6.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 188 DQTLAILCSSGTTGIPKAVTIT------NSRQILNSShSLTTNDVQYS-----HStLDWITGLLTTVTSGVfstKRIIAD 256
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLShknllaNVEQITAIF-DPNPEDVVFGalpffHS-FGLTGCLWLPLLSGI---KVVFHP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 257 NIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPsfTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTEL 336
Cdd:cd05909 222 NPLDYKKIPELIYDKKATILLGTPTFLRGYARAA--HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILE-GYGTTEC 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 337 GSMAALNL-HFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNG-QYWAGYYGNPEEThKMRDHHNWFHTGDLG 414
Cdd:cd05909 299 SPVISVNTpQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGpNVMLGYLNEPELT-SFAFGDGWYDTGDIG 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 415 YVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISK-MPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVE 493
Cdd:cd05909 378 KIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEiLPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNAG 457
|
.
gi 21356441 494 T 494
Cdd:cd05909 458 I 458
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
187-523 |
1.19e-25 |
|
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: 109.84 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 NDQTLAILCSSGTTGIPKAVTITNsRQILNSSHS------LTTNDVQYS----HSTLDWITGLLTTVTSG---VFSTKrI 253
Cdd:cd05914 88 EDDVALINYTSGTTGNSKGVMLTY-RNIVSNVDGvkevvlLGKGDKILSilplHHIYPLTFTLLLPLLNGahvVFLDK-I 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 254 IADNIFDPEFF---MRL-------VEEHQITWIIQ--APAHMAMMVNSPSFTTSDLSSLRYYL---FGGsrasvetqhRI 318
Cdd:cd05914 166 PSAKIIALAFAqvtPTLgvpvplvIEKIFKMDIIPklTLKKFKFKLAKKINNRKIRKLAFKKVheaFGG---------NI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 319 R------SRLSKDCLHF----------AYGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKVICEKGESlgpdEVGELCL 382
Cdd:cd05914 237 KefviggAKINPDVEEFlrtigfpytiGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPAT----GEGEIIV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 383 WNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKF---QNImyYPNEIESVISKMPDVVEVCV 459
Cdd:cd05914 313 RGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLssgKNI--YPEEIEAKINNMPFVLESLV 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356441 460 FgvwnEINGDEATAAVV---KKRGSALTAQDIVDYV-ETHID------AKYKQLNGGAIIVEDLVRSPNGKTNR 523
Cdd:cd05914 391 V----VQEKKLVALAYIdpdFLDVKALKQRNIIDAIkWEVRDkvnqkvPNYKKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
188-523 |
1.71e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 110.43 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 188 DQTLAILCSSGTTGIPKAVTITNSRQI-----LNSSHSLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRII-------- 254
Cdd:PRK07529 213 DDVAAYFHTGGTTGMPKLAQHTHGNEVanawlGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVlatpqgyr 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 255 ADNIFDPefFMRLVEEHQITWIIQAPAHMAMMVNSPSfTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFT 334
Cdd:PRK07529 293 GPGVIAN--FWKIVERYRINFLSGVPTVYAALLQVPV-DGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVE-GYGLT 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 335 ELGSMAALN-LHFDEKPNSVGRLVAGLKLKVI--CEKGESL---GPDEVGELCLWNGQYWAGYYgNPEETHKMRDHHNWF 408
Cdd:PRK07529 369 EATCVSSVNpPDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWL 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 409 HTGDLGYVDDDGFIYIVERKKDML--KFQNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQ 486
Cdd:PRK07529 448 NTGDLGRIDADGYFWLTGRAKDLIirGGHNI--DPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEA 525
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 21356441 487 DIVDYVETHID---AKYKQLnggaIIVEDLVRSPNGKTNR 523
Cdd:PRK07529 526 ELLAFARDHIAeraAVPKHV----RILDALPKTAVGKIFK 561
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-496 |
3.88e-25 |
|
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: 106.80 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 188 DQTLAILCSSGTTGIPKAVTITNSRQI-----LNSSHSLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRII-------- 254
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVynawmLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVlagpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 255 ADNIFDPefFMRLVEEHQITWIIQAPAHMAMMVNSPsfTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFT 334
Cdd:cd05944 82 NPGLFDN--FWKLVERYRITSLSTVPTVYAALLQVP--VNADISSLRFAMSGAAPLPVELRARFEDATGLPVVE-GYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 335 ELGSMAALNLHFDE-KPNSVGRLVAGLKLKVICEKGES-----LGPDEVGELCLWNGQYWAGY-YGNPEETHKMRDhhNW 407
Cdd:cd05944 157 EATCLVAVNPPDGPkRPGSVGLRLPYARVRIKVLDGVGrllrdCAPDEVGEICVAGPGVFGGYlYTEGNKNAFVAD--GW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 408 FHTGDLGYVDDDGFIYIVERKKDML--KFQNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTA 485
Cdd:cd05944 235 LNTGDLGRLDADGYLFITGRAKDLIirGGHNI--DPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEE 312
|
330
....*....|.
gi 21356441 486 QDIVDYVETHI 496
Cdd:cd05944 313 EELLAWARDHV 323
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
35-525 |
5.11e-25 |
|
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: 108.06 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 35 IFNEM-RRHPQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTH----ISAVAYAcffnGIAFH 109
Cdd:cd12117 2 LFEEQaARTPDAVAVVYGDRS--LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPElvvaLLAVLKA----GAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 110 SLNISYEQSTIEKLFSITRPNIIFCDgdefekvRSATAQLDvkiitmrnhpsGSIRIDQVLSTPIEKNFQPVRLEQGNDQ 189
Cdd:cd12117 76 PLDPELPAERLAFMLADAGAKVLLTD-------RSLAGRAG-----------GLEVAVVIDEALDAGPAGNPAVPVSPDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 190 TLAILCSSGTTGIPKAVTITNS---RQILNSSH-SLTTNDVQYSHSTLDW------ITGLLTTVTSGVFSTKriiaDNIF 259
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRgvvRLVKNTNYvTLGPDDRVLQTSPLAFdastfeIWGALLNGARLVLAPK----GTLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 260 DPEFFMRLVEEHQITwiiqapahmAMMVNSPSFTT------SDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYG- 332
Cdd:cd12117 214 DPDALGALIAEEGVT---------VLWLTAALFNQladedpECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGp 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 333 -----FTELGSMAALNLHFDEKPnsVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEET------HKM 401
Cdd:cd12117 285 tenttFTTSHVVTELDEVAGSIP--IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTaerfvaDPF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 402 RDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVfGVWNEINGDEATAAVVKKRGs 481
Cdd:cd12117 363 GPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVV-VVREDAGGDKRLVAYVVAEG- 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 21356441 482 ALTAQDIVDYVEthidakyKQLNGGAI-----IVEDLVRSPNGKTNRMA 525
Cdd:cd12117 441 ALDAAELRAFLR-------ERLPAYMVpaafvVLDELPLTANGKVDRRA 482
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
40-525 |
5.92e-25 |
|
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: 108.20 E-value: 5.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQISatENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIA-RNTTHISAVaYACFFNGIAFHSLNISYEQS 118
Cdd:cd17651 6 ARTPDAPALVA--EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCArRSAELVVAL-LAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 119 TIEKLFSITRPNIIFC---DGDEFEKVRSATAQLDvkiitmrnhpsgsiriDQVLSTPIEknfQPVRLEQGNDQTLAILC 195
Cdd:cd17651 83 RLAFMLADAGPVLVLThpaLAGELAVELVAVTLLD----------------QPGAAAGAD---AEPDPALDADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 196 SSGTTGIPKAVTITnsrqilnssHSLTTNDVQYSHSTLDWITGLLTTVTSG---------VFS------TKRIIADNI-F 259
Cdd:cd17651 144 TSGSTGRPKGVVMP---------HRSLANLVAWQARASSLGPGARTLQFAGlgfdvsvqeIFStlcagaTLVLPPEEVrT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 260 DPEFFMRLVEEHQITwIIQAPAHMA-MMVNSPSFTTSDLSSLRYYLFGGSRASVETQHR-IRSRLSKDCLHFAYGFTELG 337
Cdd:cd17651 215 DPPALAAWLDEQRIS-RVFLPTVALrALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLReFCAGLPGLRLHNHYGPTETH 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 338 SMAALNLHFD----EKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKmRDHHNWF----- 408
Cdd:cd17651 294 VVTALSLPGDpaawPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAE-RFVPDPFvpgar 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 409 --HTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQ 486
Cdd:cd17651 373 myRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAA 452
|
490 500 510
....*....|....*....|....*....|....*....
gi 21356441 487 DIVDYVETHIDAkYkQLNGGAIIVEDLVRSPNGKTNRMA 525
Cdd:cd17651 453 ELRAALATHLPE-Y-MVPSAFVLLDALPLTPNGKLDRRA 489
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
16-476 |
3.81e-24 |
|
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: 107.25 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 16 WSGDQLEYyfDPHLSIGEIIFNEMRRHPQLIAQISatENTILTRAELQANAMHIASYMRSLGLLQMDIVGI-IARNTTHI 94
Cdd:COG1020 465 WNATAAPY--PADATLHELFEAQAARTPDAVAVVF--GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVcLERSLEMV 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 95 SAVaYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDGDEFEKVRSATAQLdvkiitmrnhpsgsIRIDQ--VLST 172
Cdd:COG1020 541 VAL-LAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPV--------------LALDAlaLAAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 173 PIEKNFQPVRLEQgndqtLA-ILCSSGTTGIPKAVTITNsRQILNSSHS------LTTNDV-----QYSH--STLDWITG 238
Cdd:COG1020 606 PATNPPVPVTPDD-----LAyVIYTSGSTGRPKGVMVEH-RALVNLLAWmqrrygLGPGDRvlqfaSLSFdaSVWEIFGA 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 239 LLT--TVtsgvfstkrIIADN--IFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPsftTSDLSSLRYYLFGGSRASVET 314
Cdd:COG1020 680 LLSgaTL---------VLAPPeaRRDPAALAELLARHRVTVLNLTPSLLRALLDAA---PEALPSLRLVLVGGEALPPEL 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 315 QHRIRSRLSKDCLHFAYGFTE--LGSMAALNLHFDEKPNSV--GRLVAGLKLKVICEKGESLGPDEVGELCLwNGQYWA- 389
Cdd:COG1020 748 VRRWRARLPGARLVNLYGPTEttVDSTYYEVTPPDADGGSVpiGRPIANTRVYVLDAHLQPVPVGVPGELYI-GGAGLAr 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 390 GYYGNPEET-------HKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKfqnIMYY---PNEIESVISKMPDVVEVCV 459
Cdd:COG1020 827 GYLNRPELTaerfvadPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVK---IRGFrieLGEIEAALLQHPGVREAVV 903
|
490
....*....|....*..
gi 21356441 460 FgVWNEINGDEATAAVV 476
Cdd:COG1020 904 V-AREDAPGDKRLVAYV 919
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
196-523 |
4.83e-24 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 105.61 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 196 SSGTTGIPKAVTITNSRQILNSSHS-----LTTNDVQ---------YSHStldwITGLLttvtsGVFST--KRIIADNiF 259
Cdd:COG1021 192 SGGTTGLPKLIPRTHDDYLYSVRASaeicgLDADTVYlaalpaahnFPLS----SPGVL-----GVLYAggTVVLAPD-P 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 260 DPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLskDC-LHFAYG------ 332
Cdd:COG1021 262 SPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPAL--GCtLQQVFGmaeglv 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 333 -FTELGSMAALNLHfdekpnSVGR-LVAGLKLKVICEKGESLGPDEVGELcLWNGQY-WAGYYGNPEethkmrdhHN--- 406
Cdd:COG1021 340 nYTRLDDPEEVILT------TQGRpISPDDEVRIVDEDGNPVPPGEVGEL-LTRGPYtIRGYYRAPE--------HNara 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 407 -----WFHTGDLGYVDDDGFIYIVERKKDMLKF--QNImyYPNEIESVISKMPDVVEVCVFGVWNEINGdEATAAVVKKR 479
Cdd:COG1021 405 ftpdgFYRTGDLVRRTPDGYLVVEGRAKDQINRggEKI--AAEEVENLLLAHPAVHDAAVVAMPDEYLG-ERSCAFVVPR 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 21356441 480 GSALTAQDIVDYVETHIDAKYK---QLnggaIIVEDLVRSPNGKTNR 523
Cdd:COG1021 482 GEPLTLAELRRFLRERGLAAFKlpdRL----EFVDALPLTAVGKIDK 524
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
187-523 |
1.28e-23 |
|
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: 103.37 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 NDQTLAILCSSGTTGIPKAV-----TITNSRQILNSSHSLTTNDVQYSHSTLDWITGLLTTVTSGV-FSTKRIIADNIFD 260
Cdd:cd05973 87 DSDPFVMMFTSGTTGLPKGVpvplrALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLaLGHPTILLEGGFS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 261 PEFFMRLVEEHQITWIIQAP-AHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKdCLHFAYGFTELGsM 339
Cdd:cd05973 167 VESTWRVIERLGVTNLAGSPtAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGV-PIHDHYGQTELG-M 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 340 AALNLHFDEKP---NSVGRLVAGLKLKVICEKGESLGPDEVGELC--------LWngqyWAGYYGNPEETHKMRdhhnWF 408
Cdd:cd05973 245 VLANHHALEHPvhaGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAidiansplMW----FRGYQLPDTPAIDGG----YY 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 409 HTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTaQDI 488
Cdd:cd05973 317 LTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGT-PAL 395
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 21356441 489 VDYVETHIDAKY------KQLNggaiIVEDLVRSPNGKTNR 523
Cdd:cd05973 396 ADELQLHVKKRLsahaypRTIH----FVDELPKTPSGKIQR 432
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
41-523 |
1.67e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 103.92 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 41 RHPQLIAQISatENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTI 120
Cdd:PRK13383 47 RWPGRTAIID--DDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 121 EKLFSITRPNIIFCDGDEFEKVRSATAQLDVkiitmrnhpsgsirIDQVLSTPIEKNFQPVRLEQGNdqtlAILCSSGTT 200
Cdd:PRK13383 125 AAALRAHHISTVVADNEFAERIAGADDAVAV--------------IDPATAGAEESGGRPAVAAPGR----IVLLTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 201 GIPKAV--------TITNSRQILNSSHSLTTNDVQYSHST---LDWITGLLTTVTSGVFSTKRIiadniFDPEFFMRLVE 269
Cdd:PRK13383 187 GKPKGVprapqlrsAVGVWVTILDRTRLRTGSRISVAMPMfhgLGLGMLMLTIALGGTVLTHRH-----FDAEAALAQAS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 270 EHQITWIIQAPAHMAMMVNSPSFTTS--DLSSLRYYLFGGSRASVETQHRIRSRLSkDCLHFAYGFTELGSMA-ALNLHF 346
Cdd:PRK13383 262 LHRADAFTAVPVVLARILELPPRVRArnPLPQLRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGSTEVGIGAlATPADL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 347 DEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYY--GNPEETHKMRDhhnwfhTGDLGYVDDDGFIYI 424
Cdd:PRK13383 341 RDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTdgGGKAVVDGMTS------TGDMGYLDNAGRLFI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 425 VERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYKQ-- 502
Cdd:PRK13383 415 VGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRV-SRFEQpr 493
|
490 500
....*....|....*....|..
gi 21356441 503 -LNggaiIVEDLVRSPNGKTNR 523
Cdd:PRK13383 494 dIN----IVSSIPRNPTGKVLR 511
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
196-525 |
2.80e-23 |
|
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: 102.56 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 196 SSGTTGIPKA----------VTITNSRQILNsshsLTTNDVQYSHSTLDWITGL-------LTTVTSGVFSTKRIiADNI 258
Cdd:cd05958 105 TSGTTGAPKAtmhfhrdplaSADRYAVNVLR----LREDDRFVGSPPLAFTFGLggvllfpFGVGASGVLLEEAT-PDLL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 259 FDpeffmrLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTELGS 338
Cdd:cd05958 180 LS------AIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIID-GIGSTEMFH 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 339 MAALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLwngQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDD 418
Cdd:cd05958 253 IFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAV---RGPTGCRYLADKRQRTYVQGGWNITGDTYSRDP 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 419 DGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRG---SALTAQDIVDYVETH 495
Cdd:cd05958 330 DGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGvipGPVLARELQDHAKAH 409
|
330 340 350
....*....|....*....|....*....|.
gi 21356441 496 IdAKYKQLNggAI-IVEDLVRSPNGKTNRMA 525
Cdd:cd05958 410 I-APYKYPR--AIeFVTELPRTATGKLQRFA 437
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
111-527 |
3.35e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 102.55 E-value: 3.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 111 LNISYEQSTIEKLFSITRPNIIFCDGDEFEKVRSATAQLdvkiitmrnhpsgsIRIDQVLSTpIEKNFQpvRLEQGNDQT 190
Cdd:PRK07638 80 LDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRV--------------IEIDEWKRM-IEKYLP--TYAPIENVQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 191 LAIL---CSSGTTGIPKAVTITNSRQIlnssHSLTTNDVQYSHSTLDWITGLLTTVTS----GVFSTKRIIADNIFDPEF 263
Cdd:PRK07638 143 NAPFymgFTSGSTGKPKAFLRAQQSWL----HSFDCNVHDFHMKREDSVLIAGTLVHSlflyGAISTLYVGQTVHLMRKF 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 264 F----MRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDL---SSlryylfgGSRASVETQHRIRSRLSKDCLHFAYGFTEL 336
Cdd:PRK07638 219 IpnqvLDKLETENISVMYTVPTMLESLYKENRVIENKMkiiSS-------GAKWEAEAKEKIKNIFPYAKLYEFYGASEL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 337 GSMAAL-NLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMrDHHNWFHTGDLGY 415
Cdd:PRK07638 292 SFVTALvDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAREL-NADGWMTVRDVGY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 416 VDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGV----WNEIngdeaTAAVVKkrGSAlTAQDIVDY 491
Cdd:PRK07638 371 EDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVpdsyWGEK-----PVAIIK--GSA-TKQQLKSF 442
|
410 420 430
....*....|....*....|....*....|....*.
gi 21356441 492 VETHIdAKYKqLNGGAIIVEDLVRSPNGKTNRMANK 527
Cdd:PRK07638 443 CLQRL-SSFK-IPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
57-490 |
8.21e-23 |
|
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: 101.93 E-value: 8.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLlQMDIVGIIARNTTHISAVAYACFFNG-IA--FHSLNISYEQSTIEKLFSITRPNIIF 133
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGaIAvpLPPPTPGRHAERLAAILADAGPRVVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 134 CDGDEFEKVRsATAQLDVKIITMRnhpsgSIRIDQVLSTPIEkNFQPVRLEQGndqTLAIL-CSSGTTGIPKAVTIT--- 209
Cdd:cd05931 104 TTAAALAAVR-AFAASRPAAGTPR-----LLVVDLLPDTSAA-DWPPPSPDPD---DIAYLqYTSGSTGTPKGVVVThrn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 210 ---NSRQILNSSHsLTTNDVqyshsTLDW---------ITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEEHQITwII 277
Cdd:cd05931 174 llaNVRQIRRAYG-LDPGDV-----VVSWlplyhdmglIGGLLTPLYSGGPSVLMSPAAFLRRPLRWLRLISRYRAT-IS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 278 QAP----AHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSR-----LSKDCLHFAYG---------FTELGS- 338
Cdd:cd05931 247 AAPnfayDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAfapfgFRPEAFRPSYGlaeatlfvsGGPPGTg 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 339 -------MAALNLHFDEKPN---------SVGRLVAGLKLKVIC-EKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKM 401
Cdd:cd05931 327 pvvlrvdRDALAGRAVAVAAddpaarelvSCGRPLPDQEVRIVDpETGRELPDGEVGEIWVRGPSVASGYWGRPEATAET 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 402 ------RDHHNWFHTGDLGYVdDDGFIYIVERKKDMLkfqnIM----YYPNEIESVISKMPDVVE---VCVFGVWNEING 468
Cdd:cd05931 407 fgalaaTDEGGWLRTGDLGFL-HDGELYITGRLKDLI----IVrgrnHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEE 481
|
490 500
....*....|....*....|..
gi 21356441 469 DEATAAVVKKRGSALTAQDIVD 490
Cdd:cd05931 482 RLVVVAEVERGADPADLAAIAA 503
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
167-480 |
9.62e-23 |
|
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: 101.88 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 167 DQVLSTPIEknFQPVRLEQgnDQTLAILCSSGTTGIPKAVTITNSRQILNSSHSLT------TNDVQYSHSTLDWITG-- 238
Cdd:cd17634 215 DLIAKASPE--HQPEAMNA--EDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKyvfdygPGDIYWCTADVGWVTGhs 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 239 ------LLTTVTSGVFSTKriiaDNIFDPEFFMRLVEEHQITWIIQAP-AHMAMMVNSP-SFTTSDLSSLRYYLFGGSRA 310
Cdd:cd17634 291 yllygpLACGATTLLYEGV----PNWPTPARMWQVVDKHGVNILYTAPtAIRALMAAGDdAIEGTDRSSLRILGSVGEPI 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 311 SVETQHRIRSRLSKD-CLHFAY-GFTELGSMAALNLHFDE--KPNSVGRLVAGLKLKVICEKGESLGPDEVGELCL---W 383
Cdd:cd17634 367 NPEAYEWYWKKIGKEkCPVVDTwWQTETGGFMITPLPGAIelKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVItdpW 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 384 NGQYWAGYYGNPE--ETHKMRDHHNWFHtGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFG 461
Cdd:cd17634 447 PGQTRTLFGDHERfeQTYFSTFKGMYFS-GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVG 525
|
330
....*....|....*....
gi 21356441 462 VWNEINGDEATAAVVKKRG 480
Cdd:cd17634 526 IPHAIKGQAPYAYVVLNHG 544
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
183-476 |
2.91e-22 |
|
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: 100.23 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 183 LEQGNDQTLAILCSSGTTGIPKAVTITNSRQILNSS------HSLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIAD 256
Cdd:cd05928 169 VETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKvngrywLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVH 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 257 NI--FDPEFFMRLVEEHQITWIIQAPAHMAMMVNSpSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDcLHFAYGFT 334
Cdd:cd05928 249 HLprFDPLVILKTLSSYPITTFCGAPTVYRMLVQQ-DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD-IYEGYGQT 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 335 ELGSMAALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGEL----------CLWNGqywagYYGNPEETHKMRdH 404
Cdd:cd05928 327 ETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIgirvkpirpfGLFSG-----YVDNPEKTAATI-R 400
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356441 405 HNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVV 476
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVV 472
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
183-482 |
4.25e-22 |
|
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: 99.48 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 183 LEQGNDQTLAILCSSGTTGIPKAVTITNSRQILNSSHSLTTNDVQYSHSTLDW---------ITGLLTTVTSGvfstkri 253
Cdd:cd05908 101 LCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWmplthdmglIAFHLAPLIAG------- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 254 IADNIFDPEFFMRlveeHQITWIIQAPAHMAMMVNSPSF-----------TTS---DLSSLRYYLFGGSRASVETQHRIR 319
Cdd:cd05908 174 MNQYLMPTRLFIR----RPILWLKKASEHKATIVSSPNFgykyflktlkpEKAndwDLSSIRMILNGAEPIDYELCHEFL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 320 SRLS-----KDCLHFAYGFTElGSMAA----LNLHF--------------------DEKPN-----SVGRLVAGLKLKVI 365
Cdd:cd05908 250 DHMSkyglkRNAILPVYGLAE-ASVGAslpkAQSPFktitlgrrhvthgepepevdKKDSEcltfvEVGKPIDETDIRIC 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 366 CEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVdDDGFIYIVERKKDMLKFQNIMYYPNEIE 445
Cdd:cd05908 329 DEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIE 407
|
330 340 350
....*....|....*....|....*....|....*....
gi 21356441 446 SVISKMPDVV--EVCVFGVWNEINGDEATAAVVKKRGSA 482
Cdd:cd05908 408 RIAEELEGVElgRVVACGVNNSNTRNEEIFCFIEHRKSE 446
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
84-485 |
1.24e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 98.21 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 84 VGIIARNTTHISAVAYACFFNGIAFHSLNIsyeqstieklfsiTRpniifcDGDEFEK-VRSATAQLdvkIITMRNHPS- 161
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNP-------------TR------RGAALARdIAHADCQL---VLTESAHAEl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 162 -----GSIRIDQVLSTPIE------KNFQPVRLEQGNDQTLAILCSSGTTGIPKAVTITNSR-----QILNSSHSLTTND 225
Cdd:PRK07867 115 ldgldPGVRVINVDSPAWAdelaahRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKvasagVMLAQRFGLGPDD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 226 VQYS-----HST---LDWITGLLTTVTSGV---FSTKRIIADnifdpeffmrlVEEHQITWIIQAPAHMAMMVNSPSFTT 294
Cdd:PRK07867 195 VCYVsmplfHSNavmAGWAVALAAGASIALrrkFSASGFLPD-----------VRRYGATYANYVGKPLSYVLATPERPD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 295 SDLSSLRYyLFGGSRASVETQhRIRSRLskDC-LHFAYGFTELGsmAALNLHFDEKPNSVGRLVAGLKL----------- 362
Cdd:PRK07867 264 DADNPLRI-VYGNEGAPGDIA-RFARRF--GCvVVDGFGSTEGG--VAITRTPDTPPGALGPLPPGVAIvdpdtgtecpp 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 363 KVICEKGESLGPDEVGELCLWNGQYW-AGYYGNPE-ETHKMRDhhNWFHTGDLGYVDDDGFIYIVERKKDMLKF--QNIM 438
Cdd:PRK07867 338 AEDADGRLLNADEAIGELVNTAGPGGfEGYYNDPEaDAERMRG--GVYWSGDLAYRDADGYAYFAGRLGDWMRVdgENLG 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 21356441 439 YYPneIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTA 485
Cdd:PRK07867 416 TAP--IERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDP 460
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
197-530 |
6.22e-21 |
|
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: 93.93 E-value: 6.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 197 SGTTGIPKAVTIT-----NSRQILNSSHSLTTNDVQYSHSTLDWITGLLTTVTSgvfstkrIIADNIF---DPEFFMRLV 268
Cdd:cd17630 9 SGSTGTPKAVVHTaanllASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS-------LLAGAELvllERNQALAED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 269 EEHQ-ITWIIQAPAHMAMMVNSPsFTTSDLSSLRYYLFGGSRASVE-----TQHRIRsrlskdcLHFAYGFTELGSMAAL 342
Cdd:cd17630 82 LAPPgVTHVSLVPTQLQRLLDSG-QGPAALKSLRAVLLGGAPIPPElleraADRGIP-------LYTTYGMTETASQVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 343 NLHFDEKPNSVGRLVAGLKLKVICEkgeslGPDEVGELCLWNGqYWAGyygnpeETHKMRDHHNWFHTGDLGYVDDDGFI 422
Cdd:cd17630 154 KRPDGFGRGGVGVLLPGRELRIVED-----GEIWVGGASLAMG-YLRG------QLVPEFNEDGWFTTKDLGELHADGRL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 423 YIVERKKDMLKF--QNIMyyPNEIESVISKMPDVVEVCVFGVWNEINGdEATAAVVKKRGSALTAqDIVDYVETHIdAKY 500
Cdd:cd17630 222 TVLGRADNMIISggENIQ--PEEIEAALAAHPAVRDAFVVGVPDEELG-QRPVAVIVGRGPADPA-ELRAWLKDKL-ARF 296
|
330 340 350
....*....|....*....|....*....|.
gi 21356441 501 KQLNggAI-IVEDLVRSPNGKTNRMANKAFF 530
Cdd:cd17630 297 KLPK--RIyPVPELPRTGGGKVDRRALRAWL 325
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
191-523 |
9.71e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 95.96 E-value: 9.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 191 LAILCSSGTTGIPKAVTITNSRQIL----NSSHSLTTNDVQ--YSHSTLDWIT------GLLTTVTSGVFSTKRIIaDNI 258
Cdd:PTZ00237 257 LYILYTSGTTGNSKAVVRSNGPHLVglkyYWRSIIEKDIPTvvFSHSSIGWVSfhgflyGSLSLGNTFVMFEGGII-KNK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 259 FDPEFFMRLVEEHQITWIIQAPAHMAMMV-NSPSFTT----SDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGF 333
Cdd:PTZ00237 336 HIEDDLWNTIEKHKVTHTLTLPKTIRYLIkTDPEATIirskYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSR-GYGQ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 334 TELGSMAALNLHFDEKP-NSVGRLVAGLKLKVICEKGESLGPDEVGELCL---WNGQYWAGYYGNPEETHKM-RDHHNWF 408
Cdd:PTZ00237 415 TEIGITYLYCYGHINIPyNATGVPSIFIKPSILSEDGKELNVNEIGEVAFklpMPPSFATTFYKNDEKFKQLfSKFPGYY 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 409 HTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDI 488
Cdd:PTZ00237 495 NSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDL 574
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 21356441 489 VDY-------VETHIDaKYKQLNgGAIIVEDLVRSPNGKTNR 523
Cdd:PTZ00237 575 NKLkneinniITQDIE-SLAVLR-KIIIVNQLPKTKTGKIPR 614
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
180-491 |
1.23e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 95.09 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 180 PVRlEQGNDQTLAILCSSGTTGIPKAVTITNSR-----QILNSSHSLTTNDVQYS-----HSTLdWITGLLTTVTSGV-- 247
Cdd:PRK13388 143 PHR-EVDAMDPFMLIFTSGTTGAPKAVRCSHGRlafagRALTERFGLTRDDVCYVsmplfHSNA-VMAGWAPAVASGAav 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 248 -----FSTKRIIADnifdpeffmrlVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLfgGSRASVETQHRIRSRL 322
Cdd:PRK13388 221 alpakFSASGFLDD-----------VRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAF--GNEASPRDIAEFSRRF 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 323 skDC-LHFAYGFTELGSMAALNLhfDEKPNSVGRLVAGLKL-----KVIC------EKGESLGPDE-VGELCLWNGQ-YW 388
Cdd:PRK13388 288 --GCqVEDGYGSSEGAVIVVREP--GTPPGSIGRGAPGVAIynpetLTECavarfdAHGALLNADEaIGELVNTAGAgFF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 389 AGYYGNPEET-HKMRdhHNWFHTGDLGYVDDDGFIYIVERKKDMLKF--QNIMYYPneIESVISKMPDVVEVCVFGVWNE 465
Cdd:PRK13388 364 EGYYNNPEATaERMR--HGMYWSGDLAYRDADGWIYFAGRTADWMRVdgENLSAAP--IERILLRHPAINRVAVYAVPDE 439
|
330 340
....*....|....*....|....*.
gi 21356441 466 INGDEATAAVVKKRGSALTAQDIVDY 491
Cdd:PRK13388 440 RVGDQVMAALVLRDGATFDPDAFAAF 465
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
193-498 |
1.27e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 95.34 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 193 ILCSSGTTGIPKAVTITNSrQILNSSHSLTTNdvqYSHSTLD-------------WITGLLTTVTSGvfSTKRIIADNIF 259
Cdd:PRK05852 181 IMFTGGTTGLPKMVPWTHA-NIASSVRAIITG---YRLSPRDatvavmplyhghgLIAALLATLASG--GAVLLPARGRF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 260 DPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDL--SSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTE-- 335
Cdd:PRK05852 255 SAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQTEFAAPVVC-AFGMTEat 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 336 --LGSMAALNLHFDEKPNSVGRLVA---GLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHhNWFHT 410
Cdd:PRK05852 334 hqVTTTQIEGIGQTENPVVSTGLVGrstGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD-GWLRT 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 411 GDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVD 490
Cdd:PRK05852 413 GDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQ 492
|
....*...
gi 21356441 491 YVETHIDA 498
Cdd:PRK05852 493 FCRERLAA 500
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
57-531 |
1.57e-20 |
|
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: 95.25 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGI----------IARNTTHISAVAYAcFFNGIAFHSLNISYEQSTIEKLFS- 125
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIylpmipeivpAFLAVARIGGIVVP-IFSGFGKEAAATRLQDAEAKALITa 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 126 --ITRPNIIFCDGDEFEKVRSATAQLDvKIITMRN--HPSGSIRIDQvLSTPIEKNFQPVRLEQ-GNDQTLAILCSSGTT 200
Cdd:cd05968 171 dgFTRRGREVNLKEEADKACAQCPTVE-KVVVVRHlgNDFTPAKGRD-LSYDEEKETAGDGAERtESEDPLMIIYTSGTT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 201 GIPKAVTITNS----RQILNSSH--SLTTNDVQYSHSTLDWITG-------LLTTVTSGVFSTkriiADNIFDPEFFMRL 267
Cdd:cd05968 249 GKPKGTVHVHAgfplKAAQDMYFqfDLKPGDLLTWFTDLGWMMGpwlifggLILGATMVLYDG----APDHPKADRLWRM 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 268 VEEHQITWIIQAPAHM-AMMVNSPSFT-TSDLSSLRyyLFGGSRASVETQ---HRIRSRLSKDCLHFAY-GFTEL-GSMA 340
Cdd:cd05968 325 VEDHEITHLGLSPTLIrALKPRGDAPVnAHDLSSLR--VLGSTGEPWNPEpwnWLFETVGKGRNPIINYsGGTEIsGGIL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 341 ALNLHFDEKPNSVGRLVAGLKLKVICEKGESLgPDEVGELCL---WNGQYwAGYYGNPE---ETHKMRDHHNWFHtGDLG 414
Cdd:cd05968 403 GNVLIKPIKPSSFNGPVPGMKADVLDESGKPA-RPEVGELVLlapWPGMT-RGFWRDEDrylETYWSRFDNVWVH-GDFA 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 415 YVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALT---AQDIVDY 491
Cdd:cd05968 480 YYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMER 559
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 21356441 492 VETHIDakyKQLNGGAI-IVEDLVRSPNGKTNRMANKAFFL 531
Cdd:cd05968 560 VADELG---KPLSPERIlFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
187-427 |
2.32e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 95.38 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 NDQTLAILCSSGTTGIPKAVTIT------NSRQI---LNsshsLTTNDVQYS-----HSTldwitGLltTVT------SG 246
Cdd:PRK08633 781 PDDTATIIFSSGSEGEPKGVMLShhnilsNIEQIsdvFN----LRNDDVILSslpffHSF-----GL--TVTlwlpllEG 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 247 VfstKRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDC 326
Cdd:PRK08633 850 I---KVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRI 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 327 LHfAYGFTELGSMAALNL----------HFDEKPNSVGRLVAGLKLKVI-CEKGESLGPDEVGELCLWNGQYWAGYYGNP 395
Cdd:PRK08633 927 LE-GYGATETSPVASVNLpdvlaadfkrQTGSKEGSVGMPLPGVAVRIVdPETFEELPPGEDGLILIGGPQVMKGYLGDP 1005
|
250 260 270
....*....|....*....|....*....|....*
gi 21356441 396 EETHK-MRDHHN--WFHTGDLGYVDDDGFIYIVER 427
Cdd:PRK08633 1006 EKTAEvIKDIDGigWYVTGDKGHLDEDGFLTITDR 1040
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
67-523 |
2.42e-20 |
|
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: 94.03 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 67 MHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDgDEFEKVRSAT 146
Cdd:cd05915 35 RRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD-PNLLPLVEAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 147 AQLDVKIITMRNHPSGSIRIDQVLSTPiEKNFQPVRLEQGNDqTLAILCSSGTTGIPKAVTITNSRQILNSSHSLTTNDV 226
Cdd:cd05915 114 RGELKTVQHFVVMDEKAPEGYLAYEEA-LGEEADPVRVPERA-ACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 227 QYS-----------HSTLDWITGLLTTVTSGVFSTKRIIADN--IFDPeffmrlVEEHQITWIIQAPAHMAMMVNSPSFT 293
Cdd:cd05915 192 ALSekdvvlpvvpmFHVNAWCLPYAATLVGAKQVLPGPRLDPasLVEL------FDGEGVTFTAGVPTVWLALADYLEST 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 294 TSDLSSLRYYLFGGSrASVETQHRIRsRLSKDCLHFAYGFTE---LGSMAALNLHFDEKPNSVG-RLVAGLKLKVICEKG 369
Cdd:cd05915 266 GHRLKTLRRLVVGGS-AAPRSLIARF-ERMGVEVRQGYGLTEtspVVVQNFVKSHLESLSEEEKlTLKAKTGLPIPLVRL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 370 ESLGP---------DEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYY 440
Cdd:cd05915 344 RVADEegrpvpkdgKALGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWIS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 441 PNEIESVISKMPDVVEVCVFGVWNEINGdEATAAVVKKRGSALTAQDIVDYVETHIdAKYKQLNGGAIIVEDLVRSPNGK 520
Cdd:cd05915 424 SVDLENALMGHPKVKEAAVVAIPHPKWQ-ERPLAVVVPRGEKPTPEELNEHLLKAG-FAKWQLPDAYVFAEEIPRTSAGK 501
|
...
gi 21356441 521 TNR 523
Cdd:cd05915 502 FLK 504
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
40-525 |
2.49e-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: 93.54 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQst 119
Cdd:cd12115 10 ARTPDAIALVCGDES--LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPP-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 ieklfsitrpniifcdgdefEKVRSataqldvkiiTMRNHpsgsiRIDQVLSTPieknfqpvrleqgnDQTLAILCSSGT 199
Cdd:cd12115 86 --------------------ERLRF----------ILEDA-----QARLVLTDP--------------DDLAYVIYTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 200 TGIPKAVTITnsrqilnssHSLTTNDVQYS--HSTLDWITGLLTTvTSGVF-----------ST--KRIIADNIFDPEFF 264
Cdd:cd12115 117 TGRPKGVAIE---------HRNAAAFLQWAaaAFSAEELAGVLAS-TSICFdlsvfelfgplATggKVVLADNVLALPDL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 265 MRLVEehqITWIIQAPAHMAMMVNSPSFTTSdlssLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTE---LGSMAA 341
Cdd:cd12115 187 PAAAE---VTLINTVPSAAAELLRHDALPAS----VRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEdttYSTVAP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 342 LNLHFDEKPnSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEET------HKMRDHHNWFHTGDLGY 415
Cdd:cd12115 260 VPPGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTaerflpDPFGPGARLYRTGDLVR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 416 VDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETH 495
Cdd:cd12115 339 WRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTR 418
|
490 500 510
....*....|....*....|....*....|
gi 21356441 496 IdaKYKQLNGGAIIVEDLVRSPNGKTNRMA 525
Cdd:cd12115 419 L--PAYMVPSRFVRLDALPLTPNGKIDRSA 446
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
43-525 |
3.32e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 93.49 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 43 PQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMDIVGIIA-RNTTHISAVaYACFFNGIAFHSLNISYEQSTIE 121
Cdd:cd12114 1 PDATAVICGDGT--LTYGELAERARRVAGALKAAGVRPGDLVAVTLpKGPEQVVAV-LGILAAGAAYVPVDIDQPAARRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 122 KLFSITRPN-IIFCDGDEFEKVRSATAQLDvkiitmrnhpsgsiriDQVLSTPiEKNFQPVRLEQgnDQTLAILCSSGTT 200
Cdd:cd12114 78 AILADAGARlVLTDGPDAQLDVAVFDVLIL----------------DLDALAA-PAPPPPVDVAP--DDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 201 GIPKAVTITNSRQI-----LNSSHSLTTNDVQYSHSTLDW------ITGLLTTVTSGVFSTkriiADNIFDPEFFMRLVE 269
Cdd:cd12114 139 GTPKGVMISHRAALntildINRRFAVGPDDRVLALSSLSFdlsvydIFGALSAGATLVLPD----EARRRDPAHWAELIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 270 EHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTElgsmAAL--NLH-- 345
Cdd:cd12114 215 RHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATE----ASIwsIYHpi 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 346 --FDEKPNSV--GRLVAGLKLKVICEKGESLgPDEV-GELclwngqyWA-------GYYGNPEET------HkmRDHHNW 407
Cdd:cd12114 291 deVPPDWRSIpyGRPLANQRYRVLDPRGRDC-PDWVpGEL-------WIggrgvalGYLGDPELTaarfvtH--PDGERL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 408 FHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwneiNGDEAT---AAVVKKRGSALT 484
Cdd:cd12114 361 YRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL----GDPGGKrlaAFVVPDNDGTPI 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 21356441 485 AQDIVDYVE------THIDAKYKQLnggaiivEDLVRSPNGKTNRMA 525
Cdd:cd12114 437 APDALRAFLaqtlpaYMIPSRVIAL-------EALPLTANGKVDRAA 476
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
300-461 |
1.19e-19 |
|
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: 91.89 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 300 LRYYLFGGSRASVETQHRIRSRLSkdCLHFAYGFTELGSMAALNLHFDEKPNSVGRLVAG--LKLKVICEKG-ESLGPDE 376
Cdd:cd17639 252 LRYMLSGGAPLSADTQEFLNIVLC--PVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCceIKLVDWEEGGySTDKPPP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 377 VGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNE-IESVISKMPDVV 455
Cdd:cd17639 330 RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEkLESIYRSNPLVN 409
|
....*.
gi 21356441 456 EVCVFG 461
Cdd:cd17639 410 NICVYA 415
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
66-461 |
1.21e-19 |
|
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: 92.28 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 66 AMHIASYMRSLGLLQ--MDIVGIIARNTTHISAVAYACFFNGIAFHSLnisYEQS---TIEKLFSITRPNIIFCDGDefe 140
Cdd:cd05927 15 ADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPL---YDTLgpeAIEYILNHAEISIVFCDAG--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 141 kvrsataqldVKIITMRNhpsgsiridqvlstpIEK--NFQPVRLEQGNDQTLAILC-SSGTTGIPKAVTITNsRQILNS 217
Cdd:cd05927 89 ----------VKVYSLEE---------------FEKlgKKNKVPPPPPKPEDLATICyTSGTTGNPKGVMLTH-GNIVSN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 218 SHSL----------TTNDVQYS-----HS-------------------------TLDWITGLLTTVTSGVfstKRI---I 254
Cdd:cd05927 143 VAGVfkileilnkiNPTDVYISylplaHIfervvealflyhgakigfysgdirlLLDDIKALKPTVFPGV---PRVlnrI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 255 ADNIFDpeffmrlvEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYY----------LFGGsrasvetqhRIR----- 319
Cdd:cd05927 220 YDKIFN--------KVQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWdklvfnkikqALGG---------NVRlmltg 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 320 -SRLSKDCLHFA-----------YGFTELGSMAALNLHFDEKPNSVGRLV--AGLKLKVICEKG-ESLGPDEVGELCLWN 384
Cdd:cd05927 283 sAPLSPEVLEFLrvalgcpvlegYGQTECTAGATLTLPGDTSVGHVGGPLpcAEVKLVDVPEMNyDAKDPNPRGEVCIRG 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356441 385 GQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYY-PNEIESVISKMPDVVEVCVFG 461
Cdd:cd05927 363 PNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVaPEKIENIYARSPFVAQIFVYG 440
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
191-522 |
1.32e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 90.52 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 191 LAILCSSGTTGIPKAV---------TITNSRQIL--NSSHSLTTNDVQYSHSTLDWI--------TGLLTTVTSGVFSTK 251
Cdd:cd05924 6 LYILYTGGTTGMPKGVmwrqedifrMLMGGADFGtgEFTPSEDAHKAAAAAAGTVMFpapplmhgTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 252 RIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAM-MVNS-PSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHF 329
Cdd:cd05924 86 VVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMARpLIDAlRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 330 AYGFTELGSMAALnlHFDEKPNSVG-RLVAGLKLKVICEKGESL--GPDEVGELCLwNGQYWAGYYGNPE---ETHKMRD 403
Cdd:cd05924 166 AFGSSETGFTGSG--HSAGSGPETGpFTRANPDTVVLDDDGRVVppGSGGVGWIAR-RGHIPLGYYGDEAktaETFPEVD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 404 HHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEaTAAVVKKRGSA- 482
Cdd:cd05924 243 GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE-VVAVVQLREGAg 321
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 21356441 483 LTAQDIVDYVETHIdAKYKqLNGGAIIVEDLVRSPNGKTN 522
Cdd:cd05924 322 VDLEELREHCRTRI-ARYK-LPKQVVFVDEIERSPAGKAD 359
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
164-445 |
2.31e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 91.21 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 164 IRIDQVLSTPieknfqPVRLEQGNDQTLAIL-CSSGTTGIPKAVTIT------NSRQILNSSHSLTTNDVqyshsTLDWI 236
Cdd:PRK07768 133 LTVADLLAAD------PIDPVETGEDDLALMqLTSGSTGSPKAVQIThgnlyaNAEAMFVAAEFDVETDV-----MVSWL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 237 --------TGLLTT-VTSGVFSTKRIIADNIFDPEFFMRLVEEHQITwIIQAP----AHMA-MMVNSPSFTTSDLSSLRY 302
Cdd:PRK07768 202 plfhdmgmVGFLTVpMYFGAELVKVTPMDFLRDPLLWAELISKYRGT-MTAAPnfayALLArRLRRQAKPGAFDLSSLRF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 303 YLFGGSRASVETQHRI-----RSRLSKDCLHFAYGFTE--LG-SMAALN--LHFDE----------------KPN----- 351
Cdd:PRK07768 281 ALNGAEPIDPADVEDLldagaRFGLRPEAILPAYGMAEatLAvSFSPCGagLVVDEvdadllaalrravpatKGNtrrla 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 352 SVGRLVAGLKLKVICEKGESLGPDEVGELCLwNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDM 431
Cdd:PRK07768 361 TLGPPLPGLEVRVVDEDGQVLPPRGVGVIEL-RGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDV 439
|
330
....*....|....*...
gi 21356441 432 LkfqnIM----YYPNEIE 445
Cdd:PRK07768 440 I----IMagrnIYPTDIE 453
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
33-525 |
3.17e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 90.84 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 33 EIIFNEMRRHPQLIAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLN 112
Cdd:PRK05857 18 DRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 113 ISYEQSTIEKLFSITRPNIIF------CDGDEFEKVRSATAQLDVKIITMRNHPSGSIRIDQVLSTPieknfqpvrlEQG 186
Cdd:PRK05857 98 GNLPIAAIERFCQITDPAAALvapgskMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA----------DQG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 NDQTLAILCSSGTTGIPKAVTITNSR-----QILNSSH----SLTTNDVQYS-----H-STLDWI-TGLL---TTVTSGV 247
Cdd:PRK05857 168 SEDPLAMIFTSGTTGEPKAVLLANRTffavpDILQKEGlnwvTWVVGETTYSplpatHiGGLWWIlTCLMhggLCVTGGE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 248 FSTKriiadnifdpefFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRS---RLSK 324
Cdd:PRK05857 248 NTTS------------LLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEAtgvRTAQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 325 dclhfAYGFTELGSmAALNLHFDE------KPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWnGQYWA-------GY 391
Cdd:PRK05857 316 -----VYGLSETGC-TALCLPTDDgsivkiEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPSASF-GTLWIkspanmlGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 392 YGNPEETHKMRdHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFgvwnEINGDEA 471
Cdd:PRK05857 389 WNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACY----EIPDEEF 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356441 472 TAAVvkkrGSALTAQDIVD-----YVETHIDAKYKQLNGGA------IIVEDLVRSPNGKTNRMA 525
Cdd:PRK05857 464 GALV----GLAVVASAELDesaarALKHTIAARFRRESEPMarpstiVIVTDIPRTQSGKVMRAS 524
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
192-479 |
3.26e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 91.01 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 192 AILC-SSGTTGIPKAVTITNSRQILNSSHSLT-----TNDVqYSH-STLDWITGL---LTTVTSGvfstkriiADNIFDP 261
Cdd:PLN02860 175 VLICfTSGTTGRPKGVTISHSALIVQSLAKIAivgygEDDV-YLHtAPLCHIGGLssaLAMLMVG--------ACHVLLP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 262 EFFMRLV----EEHQITWIIQAPAHMA--MMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTE 335
Cdd:PLN02860 246 KFDAKAAlqaiKQHNVTSMITVPAMMAdlISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 336 -LGSMAALNLH-------------FDEKPNSVGRLVAG---------LKLKvICEKGeslgPDEVGELCLWNGQYWAGYY 392
Cdd:PLN02860 326 aCSSLTFMTLHdptlespkqtlqtVNQTKSSSVHQPQGvcvgkpaphVELK-IGLDE----SSRVGRILTRGPHVMLGYW 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 393 GNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKF--QNImyYPNEIESVISKMPDVVEVCVFGVWNEINGdE 470
Cdd:PLN02860 401 GQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTggENV--YPEEVEAVLSQHPGVASVVVVGVPDSRLT-E 477
|
....*....
gi 21356441 471 ATAAVVKKR 479
Cdd:PLN02860 478 MVVACVRLR 486
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
33-456 |
9.20e-19 |
|
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: 88.91 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 33 EIIFNEMRRHPQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMDIVGIIA-RNTTHISAVaYACFFNGIAFHSL 111
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGS--LTYGELDAASNALANRLLQLGVVPGDVVPLLSdRSLEMLVAI-LAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 112 NISYEQSTIEKLFSITRPNIIFCDGdefekvrsataqldvkiitmrnhpsgsiridqvlstpieknfqpvrleqgNDQTL 191
Cdd:cd17653 78 DAKLPSARIQAILRTSGATLLLTTD--------------------------------------------------SPDDL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 192 A-ILCSSGTTGIPKAVTITnsrqilnssHSLTTNDVQYSHSTLDwitgllttvtSGVFSTKRIIADNIFDP---EFFMRL 267
Cdd:cd17653 108 AyIIFTSGSTGIPKGVMVP---------HRGVLNYVSQPPARLD----------VGPGSRVAQVLSIAFDAcigEIFSTL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 268 -------VEEHQITWiiqapAHMAMMVN----SPSFTT----SDLSSLRYYLFGGSraSVeTQHRIRSRLSKDCLHFAYG 332
Cdd:cd17653 169 cnggtlvLADPSDPF-----AHVARTVDalmsTPSILStlspQDFPNLKTIFLGGE--AV-PPSLLDRWSPGRRLYNAYG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 333 FTELGSMAALNLHFDEKPNSVGRLVAGLKLkVICEKGESLGP-DEVGELCLWNGQYWAGYYGNPEET----HKMRDHHNW 407
Cdd:cd17653 241 PTECTISSTMTELLPGQPVTIGKPIPNSTC-YILDADLQPVPeGVVGEICISGVQVARGYLGNPALTaskfVPDPFWPGS 319
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 21356441 408 --FHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVE 456
Cdd:cd17653 320 rmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVT 370
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
57-520 |
9.82e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 89.17 E-value: 9.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCD- 135
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 136 --GDEFEKVRSATAQLDVkIITMRN-----HPSGSIRIDQVLSTPIEKnfqPVRLEQGNDQtLAILCSSGTTGIPKAVTI 208
Cdd:PRK07798 109 efAPRVAEVLPRLPKLRT-LVVVEDgsgndLLPGAVDYEDALAAGSPE---RDFGERSPDD-LYLLYTGGTTGMPKGVMW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 209 TNS---RQILNSSHSLTTNDVQYSHSTLD---------WI--------TGLLTTVTSGVFSTKRIIADNI-FDPEFFMRL 267
Cdd:PRK07798 184 RQEdifRVLLGGRDFATGEPIEDEEELAKraaagpgmrRFpapplmhgAGQWAAFAALFSGQTVVLLPDVrFDADEVWRT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 268 VEEHQITWI-----------IQAPAHMAmmvnspsftTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTEL 336
Cdd:PRK07798 264 IEREKVNVItivgdamarplLDALEARG---------PYDLSSLFAIASGGALFSPSVKEALLELLPNVVLTDSIGSSET 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 337 GSMAALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGP--DEVGELCLwNGQYWAGYYGNPE---ETHKMRDHHNWFHTG 411
Cdd:PRK07798 335 GFGGSGTVAKGAVHTGGPRFTIGPRTVVLDEDGNPVEPgsGEIGWIAR-RGHIPLGYYKDPEktaETFPTIDGVRYAIPG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 412 DLGYVDDDGFIYIVER---------KKdmlkfqnimYYPNEIESVISKMPDVVEVCVFGVWNEINGdEATAAVVKKR-GS 481
Cdd:PRK07798 414 DRARVEADGTITLLGRgsvcintggEK---------VFPEEVEEALKAHPDVADALVVGVPDERWG-QEVVAVVQLReGA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 21356441 482 ALTAQDIVDYVETHIdAKYK---QLnggaIIVEDLVRSPNGK 520
Cdd:PRK07798 484 RPDLAELRAHCRSSL-AGYKvprAI----WFVDEVQRSPAGK 520
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
197-498 |
1.42e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 88.80 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 197 SGTTGIPKAVTITNSRQILnssHSLTTNDVQYSHS------TLD--WITG--------LLTTVTSgvfstkrIIADNIFD 260
Cdd:PRK04319 214 SGSTGKPKGVLHVHNAMLQ---HYQTGKYVLDLHEddvywcTADpgWVTGtsygifapWLNGATN-------VIDGGRFS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 261 PEFFMRLVEEHQITWIIQAPA--HMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETqhrirSRLSKDCL----HFAYGFT 334
Cdd:PRK04319 284 PERWYRILEDYKVTVWYTAPTaiRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEV-----VRWGMKVFglpiHDNWWMT 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 335 ELGSMAALNLH-FDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGqyWA----GYYGNPEETHK-MRDhhNWF 408
Cdd:PRK04319 359 ETGGIMIANYPaMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKG--WPsmmrGIWNNPEKYESyFAG--DWY 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 409 HTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQ-- 486
Cdd:PRK04319 435 VSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElk 514
|
330
....*....|...
gi 21356441 487 -DIVDYVETHIDA 498
Cdd:PRK04319 515 eEIRGFVKKGLGA 527
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
322-461 |
6.63e-18 |
|
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: 87.03 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 322 LSKDCLHF----------AYGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKVICEKGeslgpDEVGELCLWNGQYWAGY 391
Cdd:cd05933 332 ISRETLEFflslnipimeLYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDA-----DGIGEICFWGRHVFMGY 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356441 392 YGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKF---QNIMYYPNEiESVISKMPDVVEVCVFG 461
Cdd:cd05933 407 LNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITaggENVPPVPIE-DAVKKELPIISNAMLIG 478
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
26-495 |
1.96e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 85.31 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 26 DPHLSIGEIIFNEMRRHPQLIAQISatENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNG 105
Cdd:PRK08279 34 DSKRSLGDVFEEAAARHPDRPALLF--EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 106 IAFHSLNISYEQSTIEKLFSITRPNIIFCDGDEFEKVRSATAQLDVKII------TMRNHPSGSIRIDQVLSTPIEKNFQ 179
Cdd:PRK08279 112 AVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRlwvaggDTLDDPEGYEDLAAAAAGAPTTNPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 180 PVRLEQGNDQTLAILcSSGTTGIPKAVTITNSRqILNSSHS------LTTNDVQYS-----HSTldwitGLLTTVTSGVF 248
Cdd:PRK08279 192 SRSGVTAKDTAFYIY-TSGTTGLPKAAVMSHMR-WLKAMGGfggllrLTPDDVLYCclplyHNT-----GGTVAWSSVLA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 249 STKRIIADNIFDPEFFMRLVEEHQIT----------WIIQAPAHmammvnspsftTSDLS-SLRYYLFGGSRASV--ETQ 315
Cdd:PRK08279 265 AGATLALRRKFSASRFWDDVRRYRATafqyigelcrYLLNQPPK-----------PTDRDhRLRLMIGNGLRPDIwdEFQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 316 HR--IrsrlsKDCLHFaYGFTElGSMAALNlhFDEKPNSVGRLVAGLK-----LKVICEKGESL----------GPDEVG 378
Cdd:PRK08279 334 QRfgI-----PRILEF-YAASE-GNVGFIN--VFNFDGTVGRVPLWLAhpyaiVKYDVDTGEPVrdadgrcikvKPGEVG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 379 ELC--LWNGQYWAGYyGNPEETHK--MRDHHN----WFHTGDLGYVDDDGFIYIVERKKDML--KFQNIMyyPNEIESVI 448
Cdd:PRK08279 405 LLIgrITDRGPFDGY-TDPEASEKkiLRDVFKkgdaWFNTGDLMRDDGFGHAQFVDRLGDTFrwKGENVA--TTEVENAL 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 21356441 449 SKMPDVVEVCVFGVwnEI---NGDEATAAVVKKRGSALTAQDIVDYVETH 495
Cdd:PRK08279 482 SGFPGVEEAVVYGV--EVpgtDGRAGMAAIVLADGAEFDLAALAAHLYER 529
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
314-496 |
7.25e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 83.12 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 314 TQHRIRSRlskdclhfaYGFTElgSMAALNLHFD--EKPNSVGRLVAGLKLKVICEKGESLGPD--EVGELCLWNGQYWA 389
Cdd:PRK07787 265 TGHRPVER---------YGMTE--TLITLSTRADgeRRPGWVGLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTLFD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 390 GYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKK-DMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEING 468
Cdd:PRK07787 334 GYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLG 413
|
170 180
....*....|....*....|....*...
gi 21356441 469 DEATAAVVKKRGSAltAQDIVDYVETHI 496
Cdd:PRK07787 414 QRIVAYVVGADDVA--ADELIDFVAQQL 439
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
196-498 |
1.08e-16 |
|
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: 82.40 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 196 SSGTTGIPKAVTITNSRQIL-----NSSHSLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFMRLVEE 270
Cdd:cd05940 89 TSGTTGLPKAAIISHRRAWRggaffAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 271 HQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASV--ETQHRIRSrlsKDCLHFaYGFTElGSMAALNlhFDE 348
Cdd:cd05940 169 YQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLRPDIweEFKERFGV---PRIAEF-YAATE-GNSGFIN--FFG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 349 KPNSVGR------LVAGLKL-KVICEKGESL----------GPDEVGELCLWNGQYWA--GYYGNPEETHKM-----RDH 404
Cdd:cd05940 242 KPGAIGRnpsllrKVAPLALvKYDLESGEPIrdaegrcikvPRGEPGLLISRINPLEPfdGYTDPAATEKKIlrdvfKKG 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 405 HNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwnEINGDE---ATAAVVKKRGS 481
Cdd:cd05940 322 DAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGV--QVPGTDgraGMAAIVLQPNE 399
|
330
....*....|....*..
gi 21356441 482 ALTAQDIVDYVETHIDA 498
Cdd:cd05940 400 EFDLSALAAHLEKNLPG 416
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
57-525 |
1.11e-16 |
|
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: 82.72 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDG 136
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 137 DEFEKvrsATAQLDVkiiTMRNHPSGSIRIDQVLSTPieknfQPvrleqgnDQTLAILCSSGTTGIPKAVTITNsRQILN 216
Cdd:cd12116 93 ALPDR---LPAGLPV---LLLALAAAAAAPAAPRTPV-----SP-------DDLAYVIYTSGSTGRPKGVVVSH-RNLVN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 217 SSHS---------------LTTndVQYSHSTLDWITGLLTTVTSGVFStkriiADNIFDPEFFMRLVEEHQITWiIQA-P 280
Cdd:cd12116 154 FLHSmrerlglgpgdrllaVTT--YAFDISLLELLLPLLAGARVVIAP-----RETQRDPEALARLIEAHSITV-MQAtP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 281 AHMAMMVNSpsfTTSDLSSLRyYLFGGSRASVETQHRIRSRLSkdCLHFAYGFTEL---GSMAALNLhfDEKPNSVGRLV 357
Cdd:cd12116 226 ATWRMLLDA---GWQGRAGLT-ALCGGEALPPDLAARLLSRVG--SLWNLYGPTETtiwSTAARVTA--AAGPIPIGRPL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 358 AGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK--MRDHHN-----WFHTGDLGYVDDDGFIYIVERKKD 430
Cdd:cd12116 298 ANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAErfVPDPFAgpgsrLYRTGDLVRRRADGRLEYLGRADG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 431 MLKFQNIMYYPNEIESVISKMPDVVEVCVFgVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIDAkYkQLNGGAIIV 510
Cdd:cd12116 378 QVKIRGHRIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPA-Y-MVPSAFVRL 454
|
490
....*....|....*
gi 21356441 511 EDLVRSPNGKTNRMA 525
Cdd:cd12116 455 DALPLTANGKLDRKA 469
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
443-520 |
2.57e-16 |
|
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: 73.73 E-value: 2.57e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356441 443 EIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYVETHIdAKYKQLNgGAIIVEDLVRSPNGK 520
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREEL-GPYAVPK-EVVFVDELPKTRSGK 76
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
22-525 |
3.42e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.52 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 22 EYYFDPHlSIGEIIFNEMRRHPQLIAQISatENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYAC 101
Cdd:PRK12467 506 ATEYAPD-CVHQLIEAQARQHPERPALVF--GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 102 FFNGIAFHSLNISYEQstiEKL-FSITRPNIIFCDGDEfekvrSATAQLDVkiitmrnhPSG--SIRIDQV--LSTPIEK 176
Cdd:PRK12467 583 LKAGGAYVPLDPEYPQ---DRLaYMLDDSGVRLLLTQS-----HLLAQLPV--------PAGlrSLCLDEPadLLCGYSG 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 177 NFQPVRLEQGNdqtLA-ILCSSGTTGIPKAVTI-----TNSRQILNSSHSLTTNDVQYSHSTLDW---ITGLLTTVTSGv 247
Cdd:PRK12467 647 HNPEVALDPDN---LAyVIYTSGSTGQPKGVAIshgalANYVCVIAERLQLAADDSMLMVSTFAFdlgVTELFGALASG- 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 248 fSTKRIIA-DNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSftTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDC 326
Cdd:PRK12467 723 -ATLHLLPpDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASR--VALPRPQRALVCGGEALQVDLLARVRALGPGAR 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 327 LHFAYGFTE------LGSMAALNLHFDEKPnsVGRLVAGLKLKVICEKGESLGPDEVGELCLwNGQYWA-GYYGNPEETH 399
Cdd:PRK12467 800 LINHYGPTEttvgvsTYELSDEERDFGNVP--IGQPLANLGLYILDHYLNPVPVGVVGELYI-GGAGLArGYHRRPALTA 876
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 400 KM-------RDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwNEINGDEAT 472
Cdd:PRK12467 877 ERfvpdpfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ-PGDAGLQLV 955
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356441 473 AAVV----------KKRGSALTA---QDIVDY-VETHIdakykqlnggaIIVEDLVRSPNGKTNRMA 525
Cdd:PRK12467 956 AYLVpaavadgaehQATRDELKAqlrQVLPDYmVPAHL-----------LLLDSLPLTPNGKLDRKA 1011
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
12-525 |
5.57e-16 |
|
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: 80.45 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 12 DRKIWSGDQLeyyfdphlsiGEIIFNEMRRHPQLIAQISAteNTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNT 91
Cdd:cd05920 8 AAGYWQDEPL----------GDLLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 92 THISAVAYACFFNGIA-FHSLNiSYEQSTIEKLFSITRPNIIFCDgDEFEKVRSATAQLDVkiitMRNHPsgsiridqvl 170
Cdd:cd05920 76 AEFVVLFFALLRLGAVpVLALP-SHRRSELSAFCAHAEAVAYIVP-DRHAGFDHRALAREL----AESIP---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 171 stpieknfqpvrleqgndQTLAILCSSGTTGIPKAVTITNSRQILNSSHS-----LTTNDVqY------SHSTLDWITGL 239
Cdd:cd05920 140 ------------------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASaevcgLDQDTV-YlavlpaAHNFPLACPGV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 240 LTTVTSGvfsTKRIIADNIfDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIR 319
Cdd:cd05920 201 LGTLLAG---GRVVLAPDP-SPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 320 SRLskDC-LHFAYG-------FTELGSMAALNLHFDEKPNSvgrlvAGLKLKVICEKGESLGPDEVGELcLWNGQY-WAG 390
Cdd:cd05920 277 PVL--GCtLQQVFGmaegllnYTRLDDPDEVIIHTQGRPMS-----PDDEIRVVDEEGNPVPPGEEGEL-LTRGPYtIRG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 391 YYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGdE 470
Cdd:cd05920 349 YYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLG-E 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 21356441 471 ATAAVVKKRGSALTAQDIVDYVETHIDAKYKqLNGGAIIVEDLVRSPNGKTNRMA 525
Cdd:cd05920 428 RSCAFVVLRDPPPSAAQLRRFLRERGLAAYK-LPDRIEFVDSLPLTAVGKIDKKA 481
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
57-419 |
1.80e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 79.32 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAF------HSLnISYEQSTIEKLFSITRPN 130
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAapvspaYSL-MSHDHAKLKHLFDLVKPR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 131 IIFC-DGDEFEKVRSATAQLDVKIITMRNHPSG--SIRIDQVLSTPIEKNFQPVRLEQGNDQTLAILCSSGTTGIPKAVT 207
Cdd:PRK12582 160 VVFAqSGAPFARALAALDLLDVTVVHVTGPGEGiaSIAFADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 208 ITNSRQILNS--SHSLTTNDVQYSHST-LDWI------------TGLLttVTSGVFStkriIADNIFDPEFF---MRLVE 269
Cdd:PRK12582 240 NTQRMMCANIamQEQLRPREPDPPPPVsLDWMpwnhtmggnanfNGLL--WGGGTLY----IDDGKPLPGMFeetIRNLR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 270 EHQITWIIQAPAHMAM----MVNSPSFTTSDLSSLRYYLFGGSR------------ASVETQHRIrsrlskdCLHFAYGF 333
Cdd:PRK12582 314 EISPTVYGNVPAGYAMlaeaMEKDDALRRSFFKNLRLMAYGGATlsddlyermqalAVRTTGHRI-------PFYTGYGA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 334 TELGSMaALNLHFD-EKPNSVGRLVAGLKLKVIcEKGESLgpdevgELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGD 412
Cdd:PRK12582 387 TETAPT-TTGTHWDtERVGLIGLPLPGVELKLA-PVGDKY------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGD 458
|
....*...
gi 21356441 413 LG-YVDDD 419
Cdd:PRK12582 459 AArFVDPD 466
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
58-483 |
2.01e-15 |
|
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: 79.00 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 58 TRAELQANAMHIASYMRSLGLLQMDIVGIIARNT-----THISAVAYACFFNGIAFHSLN--ISYeqstiekLFSITRPN 130
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRpewvwAELAAQAIGALSLGIYQDSMAeeVAY-------LLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 131 IIFCDGDEfekvrsataQLDvKIIT------------------MRNHPSGS-IRIDQVLSTPIEKNFQ-PVRLEQ----G 186
Cdd:cd17641 86 VVIAEDEE---------QVD-KLLEiadripsvryviycdprgMRKYDDPRlISFEDVVALGRALDRRdPGLYERevaaG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 NDQTLAILCS-SGTTGIPKAVTITNSRQILNSSHSLTTN-----DVQYSHSTLDWITGLLTTVTSGVFStkRIIADNIFD 260
Cdd:cd17641 156 KGEDVAVLCTtSGTTGKPKLAMLSHGNFLGHCAAYLAADplgpgDEYVSVLPLPWIGEQMYSVGQALVC--GFIVNFPEE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 261 PEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLF-------------GGSRASVETQHRIRSRLS---- 323
Cdd:cd17641 234 PETMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFelgmklglraldrGKRGRPVSLWLRLASWLAdall 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 324 ----KDCLHFA------------------------------YGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKVicekg 369
Cdd:cd17641 314 frplRDRLGFSrlrsaatggaalgpdtfrffhaigvplkqlYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI----- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 370 eslgpDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQN-IMYYPNEIESVI 448
Cdd:cd17641 389 -----DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDgTRFSPQFIENKL 463
|
490 500 510
....*....|....*....|....*....|....*
gi 21356441 449 SKMPDVVEVCVFGvwneiNGDEATAAVVKKRGSAL 483
Cdd:cd17641 464 KFSPYIAEAVVLG-----AGRPYLTAFICIDYAIV 493
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
30-525 |
3.56e-15 |
|
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: 77.86 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 30 SIGEIIFNEMRRHPQLIAQISatENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFH 109
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVF--EDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 110 SLNISYEQStieklfsitRPNIIFCDgdefekvrsatAQLdvkiitmrnhpsgsiridQVLSTpieknfQPVRLeqgndq 189
Cdd:cd17644 79 PLDPNYPQE---------RLTYILED-----------AQI------------------SVLLT------QPENL------ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 190 tLAILCSSGTTGIPKAVTITNsRQILNSSHSL------TTND--VQYSHSTLD-WITGLLTTVTSGvfSTKRIIADNIF- 259
Cdd:cd17644 109 -AYVIYTSGSTGKPKGVMIEH-QSLVNLSHGLikeygiTSSDrvLQFASIAFDvAAEEIYVTLLSG--ATLVLRPEEMRs 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 260 DPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDL-SSLRYYLFGGSRASVETQHRIRSRLSKD--CLHfAYGFTEl 336
Cdd:cd17644 185 SLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVGNFiqLIN-VYGPTE- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 337 GSMAAL--NLHFDEKPNS----VGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFH- 409
Cdd:cd17644 263 ATIAATvcRLTQLTERNItsvpIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSs 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 410 -------TGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSA 482
Cdd:cd17644 343 eserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEES 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 21356441 483 LTAQDIVDYVETH-----IDAKYKQLnggaiivEDLVRSPNGKTNRMA 525
Cdd:cd17644 423 PSTVELRQFLKAKlpdymIPSAFVVL-------EELPLTPNGKIDRRA 463
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
162-454 |
4.35e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 78.02 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 162 GSIRIDQVLSTPIEKNFQPVRLeqGNDQTLAILCSSGTTGIPKAVTITNsrQILNSSHSLTTNDVQYSHSTLDWIT---- 237
Cdd:PRK09274 150 GGTTLATLLRDGAAAPFPMADL--APDDMAAILFTSGSTGTPKGVVYTH--GMFEAQIEALREDYGIEPGEIDLPTfplf 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 238 ---GLLTTVTSgvfstkrIIADNIF------DPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGS 308
Cdd:PRK09274 226 alfGPALGMTS-------VIPDMDPtrpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 309 RASVETQHRIRSRLSKDCLHFA-YGFTE---LGSMAALNLHFDEKPNS-------VGRLVAGLKLKVI---------CEK 368
Cdd:PRK09274 299 PVPIAVIERFRAMLPPDAEILTpYGATEalpISSIESREILFATRAATdngagicVGRPVDGVEVRIIaisdapipeWDD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 369 GESLGPDEVGELCLWNGQYWAGYYGNPEET--HKMRD-HHNWFH-TGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEI 444
Cdd:PRK09274 379 ALRLATGEIGEIVVAGPMVTRSYYNRPEATrlAKIPDgQGDVWHrMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPC 458
|
330
....*....|
gi 21356441 445 ESVISKMPDV 454
Cdd:PRK09274 459 ERIFNTHPGV 468
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
69-520 |
5.73e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 77.75 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 69 IASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDgDEFEKV------ 142
Cdd:PLN03102 52 LAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD-RSFEPLarevlh 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 143 -----------------------RSATAQLDVKIITMRNHPSGSIRIDQVLstpIEKNFQPVRLEQgndqtlailcSSGT 199
Cdd:PLN03102 131 llssedsnlnlpvifiheidfpkRPSSEELDYECLIQRGEPTPSLVARMFR---IQDEHDPISLNY----------TSGT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 200 TGIPKAVTITNSRQILNSSHSLTTNDVQYSHSTLdWITGLLT----TVTSGVFST--KRIIADNIFDPEFFmRLVEEHQI 273
Cdd:PLN03102 198 TADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYL-WTLPMFHcngwTFTWGTAARggTSVCMRHVTAPEIY-KNIEMHNV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 274 TWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRsRLSKDCLHfAYGFTElgsmAALNLHFDEKPNSV 353
Cdd:PLN03102 276 THMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQ-RLGFQVMH-AYGLTE----ATGPVLFCEWQDEW 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 354 GRLVAGLKLKVICEKGES-LGPDEV------------------GELCLWNGQYWAGYYGNPEETHKMRDHhNWFHTGDLG 414
Cdd:PLN03102 350 NRLPENQQMELKARQGVSiLGLADVdvknketqesvprdgktmGEIVIKGSSIMKGYLKNPKATSEAFKH-GWLNTGDVG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 415 YVDDDGFIYIVERKKDML--KFQNIMYYpnEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQDIVDYV 492
Cdd:PLN03102 429 VIHPDGHVEIKDRSKDIIisGGENISSV--EVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLV 506
|
490 500 510
....*....|....*....|....*....|....*.
gi 21356441 493 ETHID-AKYKQLN-------GGAIIVEDLVRSPNGK 520
Cdd:PLN03102 507 TRERDlIEYCRENlphfmcpRKVVFLQELPKNGNGK 542
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
38-523 |
9.52e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 76.71 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 38 EMRRHPQLIAQISatENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQ 117
Cdd:PRK06164 19 HARARPDAVALID--EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 118 STIEKLFSITRPNII-----FCDGDEFEKVRSA--TAQLDVKIITMRNHPSGSI------RIDQVLSTPIEKNFQPVRLE 184
Cdd:PRK06164 97 HEVAHILGRGRARWLvvwpgFKGIDFAAILAAVppDALPPLRAIAVVDDAADATpapapgARVQLFALPDPAPPAAAGER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 185 QGNDQTLAIL-CSSGTTGIPKAV-----TITNSRQILNSSHSLTTNDVQYSHSTLDWI---TGLLTTVTSGVfstkRIIA 255
Cdd:PRK06164 177 AADPDAGALLfTTSGTTSGPKLVlhrqaTLLRHARAIARAYGYDPGAVLLAALPFCGVfgfSTLLGALAGGA----PLVC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 256 DNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSfTTSDLSSLRYYLFGG-SRASVETQHRIRSRLSKdcLHFAYGFT 334
Cdd:PRK06164 253 EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAG-ERADFPSARLFGFASfAPALGELAALARARGVP--LTGLYGSS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 335 ELGSMAAL---NLHFDEKPNSVGRLVAGLKLKVIC--EKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFH 409
Cdd:PRK06164 330 EVQALVALqpaTDPVSVRIEGGGRPASPEARVRARdpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 410 TGDLGY-VDDDGFIYiVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwnEINGD-EATAAVVKKRGSALTAQD 487
Cdd:PRK06164 410 TGDLGYtRGDGQFVY-QTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTDGASPDEAG 486
|
490 500 510
....*....|....*....|....*....|....*....
gi 21356441 488 IVDYVETHIdAKYKqLNGGAIIVEDL--VRSPNG-KTNR 523
Cdd:PRK06164 487 LMAACREAL-AGFK-VPARVQVVEAFpvTESANGaKIQK 523
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
40-459 |
9.75e-15 |
|
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: 76.55 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 40 RRHPQLIAQIsaTENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQST 119
Cdd:cd17646 9 ARTPDAPAVV--DEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 120 IEKLFSITRPNIIFCDGDEfekVRSATAQLDVKIITMRNHPSGSIRIDQVLSTPieknfqpvrleqgnDQTLAILCSSGT 199
Cdd:cd17646 87 LAYMLADAGPAVVLTTADL---AARLPAGGDVALLGDEALAAPPATPPLVPPRP--------------DNLAYVIYTSGS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 200 TGIPKAVTITNsRQILN------SSHSLTTNDV--QYSHSTLD---WitGLLTTVTSGvfsTKRIIA--DNIFDPEFFMR 266
Cdd:cd17646 150 TGRPKGVMVTH-AGIVNrllwmqDEYPLGPGDRvlQKTPLSFDvsvW--ELFWPLVAG---ARLVVArpGGHRDPAYLAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 267 LVEEHQITWIIQAPAHMAMMVNSPsfTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDcLHFAYGFTElgsmAALNL-H 345
Cdd:cd17646 224 LIREHGVTTCHFVPSMLRVFLAEP--AAGSCASLRRVFCSGEALPPELAARFLALPGAE-LHNLYGPTE----AAIDVtH 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 346 F------DEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKmRDHHNWF-------HTGD 412
Cdd:cd17646 297 WpvrgpaETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAE-RFVPDPFgpgsrmyRTGD 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 21356441 413 LGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCV 459
Cdd:cd17646 376 LARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVV 422
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
251-523 |
1.02e-14 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 76.57 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 251 KRIIADNIFDPEFFMRLVEEhQITWIIQAPAHMammvnspsfttsdLSSLRYYLFGGSRASVE-----TQHRIRSRLSkd 325
Cdd:PRK07445 197 KSGQELPPNPSDFFLSLVPT-QLQRLLQLRPQW-------------LAQFRTILLGGAPAWPSlleqaRQLQLRLAPT-- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 326 clhfaYGFTELGSM-AALnlhfdeKP-------NSVGRLVAGLKLKVICEKgeslgpdeVGELCLWNGQYWAGYYgnPEe 397
Cdd:PRK07445 261 -----YGMTETASQiATL------KPddflagnNSSGQVLPHAQITIPANQ--------TGNITIQAQSLALGYY--PQ- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 398 thkMRDHHNWFHTGDLGYVDDDGFIYIVERKKDML--KFQNImyYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAV 475
Cdd:PRK07445 319 ---ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIitGGENV--YPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIY 393
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 21356441 476 VKKRGsaltaQDIVDYVETHID---AKYKQLNgGAIIVEDLVRSPNGKTNR 523
Cdd:PRK07445 394 VPKDP-----SISLEELKTAIKdqlSPFKQPK-HWIPVPQLPRNPQGKINR 438
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
31-525 |
1.45e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.30 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 31 IGEIIFNEMRRHPQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHS 110
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVVFGDQH--LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVP 2082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 111 LNISYEQSTIEKLFSITRPNIIFCDgdefekvRSATAQLDVkiitmrnhPSGSIRIDqvLSTPIEKNFQPVR--LEQGND 188
Cdd:PRK12316 2083 LDPNYPAERLAYMLEDSGAALLLTQ-------RHLLERLPL--------PAGVARLP--LDRDAEWADYPDTapAVQLAG 2145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 189 QTLA-ILCSSGTTGIPKAVTITNSR-----QILNSSHSLTTNDVQYSHSTLDW---ITGLLTTVTSGVfstkRIIA--DN 257
Cdd:PRK12316 2146 ENLAyVIYTSGSTGLPKGVAVSHGAlvahcQAAGERYELSPADCELQFMSFSFdgaHEQWFHPLLNGA----RVLIrdDE 2221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 258 IFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSsLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTElg 337
Cdd:PRK12316 2222 LWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPA-VRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTE-- 2298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 338 sMAALNLHFDEKPN--------SVGRLVAGLKLKVICEKGESLGPDEVGELCLwNGQYWA-GYYGNPEETHK--MRDHHN 406
Cdd:PRK12316 2299 -AVVTPLLWKCRPQdpcgaayvPIGRALGNRRAYILDADLNLLAPGMAGELYL-GGEGLArGYLNRPGLTAErfVPDPFS 2376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 407 -----WFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwNEINGDEATAAVVKKRGS 481
Cdd:PRK12316 2377 asgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAA 2455
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 21356441 482 ALTAQDIVDYVETHIDAkyKQLNGGAIIVEDLVRSPNGKTNRMA 525
Cdd:PRK12316 2456 EDLLAELRAWLAARLPA--YMVPAHWVVLERLPLNPNGKLDRKA 2497
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
29-525 |
2.21e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 75.56 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 29 LSIGEIIFNEMRRHPQLIAQISATENTIL--TRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGI 106
Cdd:PRK06018 10 LLCHRIIDHAARIHGNREVVTRSVEGPIVrtTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 107 AFHSLNISYEQSTIEKLFSITRPNIIFCD----------GDEFEKVRSATAQLDVKII---TMRNHPSGSIRIDQVLSTP 173
Cdd:PRK06018 90 ICHTVNPRLFPEQIAWIINHAEDRVVITDltfvpilekiADKLPSVERYVVLTDAAHMpqtTLKNAVAYEEWIAEADGDF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 174 IEKNFqpvrleqgNDQTLAILC-SSGTTGIPKAVTITNSRQILnssHSLTTNDVQY----SHSTLDWITGLLTTVTSGV- 247
Cdd:PRK06018 170 AWKTF--------DENTAAGMCyTSGTTGDPKGVLYSHRSNVL---HALMANNGDAlgtsAADTMLPVVPLFHANSWGIa 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 248 FS-----TKRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSrASVETQHRIRSRL 322
Cdd:PRK06018 239 FSapsmgTKLVMPGAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGS-AMPRSMIKAFEDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 323 SKDCLHfAYGFTE---LGSMAALNLHFDEKPNSV--------GRLVAGLKLKVICEKGESLGPD--EVGELCLWNGQYWA 389
Cdd:PRK06018 318 GVEVRH-AWGMTEmspLGTLAALKPPFSKLPGDArldvlqkqGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 390 GYYGnpeETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGD 469
Cdd:PRK06018 397 AYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDE 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 21356441 470 EATAAVVKKRGSALTAQDIVDYVETHIdAKYkQLNGGAIIVEDLVRSPNGKTNRMA 525
Cdd:PRK06018 474 RPLLIVQLKPGETATREEILKYMDGKI-AKW-WMPDDVAFVDAIPHTATGKILKTA 527
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
183-525 |
3.05e-14 |
|
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: 74.71 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 183 LEQGNDQTLAILCSSGTTGIPKAVTITNSR-----QILNSSHSLTTNDVQYSHSTLDW---ITGLLTTVTSGVfstkRII 254
Cdd:cd17649 89 LTHHPRQLAYVIYTSGSTGTPKGVAVSHGPlaahcQATAERYGLTPGDRELQFASFNFdgaHEQLLPPLICGA----CVV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 255 ---ADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDL-SSLRYYLFGGSRASVETQHRIrsrLSKDCLHF- 329
Cdd:cd17649 165 lrpDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRpPSLRLYIFGGEALSPELLRRW---LKAPVRLFn 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 330 AYGFTElGSMAALNLH----FDEKPNSV--GRLVAGLKLKVICEKGESLGPDEVGELCLwNGQYWA-GYYGNPEETHK-- 400
Cdd:cd17649 242 AYGPTE-ATVTPLVWKceagAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGELYI-GGEGLArGYLGRPELTAErf 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 401 -----MRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwnEINGDEATAAV 475
Cdd:cd17649 320 vpdpfGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL--DGAGGKQLVAY 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 21356441 476 VKKRGSALTAQDiVDYVETHIDAK---YKQlNGGAIIVEDLVRSPNGKTNRMA 525
Cdd:cd17649 398 VVLRAAAAQPEL-RAQLRTALRASlpdYMV-PAHLVFLARLPLTPNGKLDRKA 448
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
300-461 |
4.01e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 75.24 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 300 LRYYLFGGSRASVETQHRIRSrlsKDCLHF--AYGFTElgSMAALNLHFDEKPNSVGRLVAG-----LKLKVICEKG-ES 371
Cdd:PLN02430 385 LRLLISGGAPLSTEIEEFLRV---TSCAFVvqGYGLTE--TLGPTTLGFPDEMCMLGTVGAPavyneLRLEEVPEMGyDP 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 372 LGPDEVGELCLWNGQYWAGYYGNPEETHK-MRDhhNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNE-IESVIS 449
Cdd:PLN02430 460 LGEPPRGEICVRGKCLFSGYYKNPELTEEvMKD--GWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEyLENVYG 537
|
170
....*....|..
gi 21356441 450 KMPDVVEVCVFG 461
Cdd:PLN02430 538 QNPIVEDIWVYG 549
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
31-523 |
4.88e-14 |
|
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: 74.50 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 31 IGEIIFNEMRRHPQLIAqISATENTiLTRAELQANAMHIASYMRSLGLLQMDIVGI---------IArntthISAVAYAc 101
Cdd:cd05918 1 VHDLIEERARSQPDAPA-VCAWDGS-LTYAELDRLSSRLAHHLRSLGVGPGVFVPLcfekskwavVA-----MLAVLKA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 102 ffnGIAFHSLNISYEQSTIEKLFSITRPNIIFCdgdefekvrsataqldvkiitmrnhpsgsiridqvlSTPieknfqpv 181
Cdd:cd05918 73 ---GGAFVPLDPSHPLQRLQEILQDTGAKVVLT------------------------------------SSP-------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 182 rleqgnDQTLAILCSSGTTGIPKAVTITNsRQILNSSHS------LTTND--VQYSHSTLD-WITGLLTTVTSG--VFST 250
Cdd:cd05918 106 ------SDAAYVIFTSGSTGKPKGVVIEH-RALSTSALAhgralgLTSESrvLQFASYTFDvSILEIFTTLAAGgcLCIP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 251 KRiiADNIFDPEFFMRlveEHQITWIIQAPAHMAMMvnSPSfttsDLSSLRYYLFGG---SRASVET-QHRIRsrlskdc 326
Cdd:cd05918 179 SE--EDRLNDLAGFIN---RLRVTWAFLTPSVARLL--DPE----DVPSLRTLVLGGealTQSDVDTwADRVR------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 327 LHFAYGFTELGSMAALNL-HFDEKPNSVGRLVAGLKLKVICEKGESLGP-DEVGELCLWNGQYWAGYYGNPEETHK---- 400
Cdd:cd05918 241 LINAYGPAECTIAATVSPvVPSTDPRNIGRPLGATCWVVDPDNHDRLVPiGAVGELLIEGPILARGYLNDPEKTAAafie 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 401 ----MRDHHNWFH-----TGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISK-MPDVVEVCVfGVWNEINGDE 470
Cdd:cd05918 321 dpawLKQEGSGRGrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVV-EVVKPKDGSS 399
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356441 471 AT--AAVVKKRGSALTAQDIVDyVETHIDAKYKQLNGGA-----------------IIVEDLVRSPNGKTNR 523
Cdd:cd05918 400 SPqlVAFVVLDGSSSGSGDGDS-LFLEPSDEFRALVAELrsklrqrlpsymvpsvfLPLSHLPLTASGKIDR 470
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
58-423 |
5.12e-14 |
|
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: 74.78 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 58 TRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAF------HSLnISYEQSTIEKLFSITRPNI 131
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAapvspaYSL-MSQDLAKLKHLFELLKPGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 132 IFC-DGDEFEKVRSATAQLDVKIITMRNHPSG--SIRIDQVLSTPIEKNFQPVRLEQGNDQTLAILCSSGTTGIPKAVTI 208
Cdd:cd05921 106 VFAqDAAPFARALAAIFPLGTPLVVSRNAVAGrgAISFAELAATPPTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVIN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 209 TNSRQILNSSHSLTTNDVQYSH--STLDWITGLLTTVTSGVFST------KRIIADNIFDPEFF---MRLVEEHQITWII 277
Cdd:cd05921 186 TQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLvlynggTLYIDDGKPMPGGFeetLRNLREISPTVYF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 278 QAPAHMAMMVNS----PSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLH-----FAYGFTELGSmAALNLHFD- 347
Cdd:cd05921 266 NVPAGWEMLVAAlekdEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALAVATVGEripmmAGLGATETAP-TATFTHWPt 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 348 EKPNSVGRLVAGLKLKVICEKGESlgpdevgELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLG-YVDDD----GFI 422
Cdd:cd05921 345 ERSGLIGLPAPGTELKLVPSGGKY-------EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAkLADPDdpakGLV 417
|
.
gi 21356441 423 Y 423
Cdd:cd05921 418 F 418
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
179-525 |
5.72e-14 |
|
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: 73.88 E-value: 5.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 179 QPVRLEQGNDQTLAILCSSGTTGIPKAVTITNS---RQILNSSHSLTTND----VQYSHSTLD---W-ITGLLTTVTSGV 247
Cdd:cd17643 84 GPSLLLTDPDDLAYVIYTSGSTGRPKGVVVSHAnvlALFAATQRWFGFNEddvwTLFHSYAFDfsvWeIWGALLHGGRLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 248 ---FSTKRiiadnifDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSR--ASVETQHRIRSRL 322
Cdd:cd17643 164 vvpYEVAR-------SPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEAleAAMLRPWAGRFGL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 323 SKDCLHFAYGFTE--------LGSMAALNLHfDEKPnsVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGN 394
Cdd:cd17643 237 DRPQLVNMYGITEttvhvtfrPLDAADLPAA-AASP--IGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 395 PEETH-------KMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEIN 467
Cdd:cd17643 314 PELTAerfvanpFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPG 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356441 468 GDEATAAVVKKRGSALTAQDIVDYVETH-----IDAKYkqlnggaIIVEDLVRSPNGKTNRMA 525
Cdd:cd17643 394 DTRLVAYVVADDGAAADIAELRALLKELlpdymVPARY-------VPLDALPLTVNGKLDRAA 449
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
330-529 |
6.66e-14 |
|
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: 74.04 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 330 AYGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKVicekgeslgpDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWFH 409
Cdd:cd05932 305 AYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLR 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 410 TGDLGYVDDDGFIYIVERKKDMLKFQNIMYY-PNEIESVISKMPDVVEVCVFG----------VWNEINGDEATAAVVKK 478
Cdd:cd05932 375 TGDKGELDADGNLTITGRVKDIFKTSKGKYVaPAPIENKLAEHDRVEMVCVIGsglpaplalvVLSEEARLRADAFARAE 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21356441 479 RGSALtaQDIVDYVETHIDaKYKQLNGGAII-----VEDLVRSPNGKTNR-MANKAF 529
Cdd:cd05932 455 LEASL--RAHLARVNSTLD-SHEQLAGIVVVkdpwsIDNGILTPTLKIKRnVLEKAY 508
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
33-525 |
8.78e-14 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 73.78 E-value: 8.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 33 EIIFNEMRRHPQLIAQISATEntILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLN 112
Cdd:PRK04813 6 ETIEEFAQTQPDFPAYDYLGE--KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 113 ISYEQSTIEKLFSITRPNIIFCDGDEfekvrsATAQLDVKIITmrnhpsgsirIDQVLSTPIEKN-FQPVRLEQGNDqTL 191
Cdd:PRK04813 84 VSSPAERIEMIIEVAKPSLIIATEEL------PLEILGIPVIT----------LDELKDIFATGNpYDFDHAVKGDD-NY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 192 AILCSSGTTGIPKAVTIT------------------NSRQILNsshslttndvQ--YSH--STLDWITGLlttvTSG--- 246
Cdd:PRK04813 147 YIIFTSGTTGKPKGVQIShdnlvsftnwmledfalpEGPQFLN----------QapYSFdlSVMDLYPTL----ASGgtl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 247 VFSTKRIIADNIfdpEFFMRLVEEHQITWIiQAP--AHMAMMvnSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSK 324
Cdd:PRK04813 213 VALPKDMTANFK---QLFETLPQLPINVWV-STPsfADMCLL--DPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 325 DCLHFAYGFTElGSMAALNLHFDE------KPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEET 398
Cdd:PRK04813 287 ATIYNTYGPTE-ATVAVTSIEITDemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 399 HK---MRDHHNWFHTGDLGYVdDDGFIYIVERkkdmLKFQnIMYypN-------EIESVISKMPDVVEVCVFGVWNEING 468
Cdd:PRK04813 366 AEaffTFDGQPAYHTGDAGYL-EDGLLFYQGR----IDFQ-IKL--NgyrieleEIEQNLRQSSYVESAVVVPYNKDHKV 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356441 469 DEATAAVVKKRGS-----ALTAQ-------DIVDYVethIDAKYkqlnggaIIVEDLVRSPNGKTNRMA 525
Cdd:PRK04813 438 QYLIAYVVPKEEDferefELTKAikkelkeRLMEYM---IPRKF-------IYRDSLPLTPNGKIDRKA 496
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-462 |
1.27e-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: 72.88 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 188 DQTLAILCSSGTTGIPKAVTITNSR---QI--LNSSHSLTTNDVQYS----HSTLDWITGlLTTVTSGVFSTKRIIAdni 258
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTfaaQIdaLRQLYGIRPGEVDLAtfplFALFGPALG-LTSVIPDMDPTRPARA--- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 259 fDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFA-YGFTE-- 335
Cdd:cd05910 161 -DPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDEAEILTpYGATEal 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 336 ----LGSMAALNLHFDEKPNS----VGRLVAGLKLKVI---------CEKGESLGPDEVGELCLWNGQYWAGYYGNPEET 398
Cdd:cd05910 240 pvssIGSRELLATTTAATSGGagtcVGRPIPGVRVRIIeiddepiaeWDDTLELPRGEIGEITVTGPTVTPTYVNRPVAT 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356441 399 --HKMRDHHN--WFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGV 462
Cdd:cd05910 320 alAKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
42-501 |
2.52e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 72.29 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 42 HPQLIAQISatENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIE 121
Cdd:PRK08162 31 YPDRPAVIH--GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 122 KLFSITRPNIIFCDGDEFEKVRSATAQLDVKIITM---------RNHPSGSIRIDQVLSTPiEKNFQPvRLEQGNDQTLA 192
Cdd:PRK08162 109 FMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVidvddpeypGGRFIGALDYEAFLASG-DPDFAW-TLPADEWDAIA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 193 ILCSSGTTGIPKAVTITNSRQILNS-SHSLTTNDVQysHSTLDWITGLL----------TTVTSGVfstkriiadNI--- 258
Cdd:PRK08162 187 LNYTSGTTGNPKGVVYHHRGAYLNAlSNILAWGMPK--HPVYLWTLPMFhcngwcfpwtVAARAGT---------NVclr 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 259 -FDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGS---RASVETQHRIRSRLskdcLHfAYGFT 334
Cdd:PRK08162 256 kVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAappAAVIAKMEEIGFDL----TH-VYGLT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 335 ELGSMAALN--------LHFDEKPNSVGR------LVAGLK------LKVICEKGESLGpdEV---GELCLwngqywAGY 391
Cdd:PRK08162 331 ETYGPATVCawqpewdaLPLDERAQLKARqgvrypLQEGVTvldpdtMQPVPADGETIG--EImfrGNIVM------KGY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 392 YGNPEETHK-MRDhhNWFHTGDLGYVDDDGFIYIVERKKDML--KFQNIMYYpnEIESVISKMPDVVEVCVFGVWNEING 468
Cdd:PRK08162 403 LKNPKATEEaFAG--GWFHTGDLAVLHPDGYIKIKDRSKDIIisGGENISSI--EVEDVLYRHPAVLVAAVVAKPDPKWG 478
|
490 500 510
....*....|....*....|....*....|...
gi 21356441 469 DEATAAVVKKRGSALTAQDIVDYVETHIdAKYK 501
Cdd:PRK08162 479 EVPCAFVELKDGASATEEEIIAHCREHL-AGFK 510
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
27-459 |
3.40e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.89 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 27 PHLSIGEIIFNEMRRHPQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGI 106
Cdd:PRK05691 1129 AQAWLPELLNEQARQTPERIALVWDGGS--LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGG 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 107 AFHSLNISYEQSTIEKLFSITRPNIIFCDGDEFEKVRSA--TAQLDVKIITMRNHPSgsiridqvlstpieknfQPVRLE 184
Cdd:PRK05691 1207 AYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAegVSAIALDSLHLDSWPS-----------------QAPGLH 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 185 QGNDQTLAILCSSGTTGIPKAVTITNSR-----QILNSSHSLTTNDV--QYSHSTLD---W------ITGLlTTVTSGVF 248
Cdd:PRK05691 1270 LHGDNLAYVIYTSGSTGQPKGVGNTHAAlaerlQWMQATYALDDSDVlmQKAPISFDvsvWecfwplITGC-RLVLAGPG 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 249 STKriiadnifDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSftTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLH 328
Cdd:PRK05691 1349 EHR--------DPQRIAELVQQYGVTTLHFVPPLLQLFIDEPL--AAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLH 1418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 329 FAYGFTElgsmAALNL-HF-----DEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKM- 401
Cdd:PRK05691 1419 NRYGPTE----TAINVtHWqcqaeDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERf 1494
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356441 402 ------RDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCV 459
Cdd:PRK05691 1495 vpdplgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAV 1558
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
191-515 |
3.49e-13 |
|
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: 72.21 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 191 LAILCSSGTTGIPKAVTITNSRQILnssHSLTT---------NDVQYSHSTLDWITG--------LLTTVTSGVFSTkri 253
Cdd:cd05966 234 LFILYTSGSTGKPKGVVHTTGGYLL---YAATTfkyvfdyhpDDIYWCTADIGWITGhsyivygpLANGATTVMFEG--- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 254 iADNIFDPEFFMRLVEEHQITWIIQAP-AHMAMMVNSPSFTT-SDLSSLR----------------YY-LFGGSRAS-VE 313
Cdd:cd05966 308 -TPTYPDPGRYWDIVEKHKVTIFYTAPtAIRALMKFGDEWVKkHDLSSLRvlgsvgepinpeawmwYYeVIGKERCPiVD 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 314 TqhrirsrlskdclhfaYGFTELGS--MAALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCL---WNGQYw 388
Cdd:cd05966 387 T----------------WWQTETGGimITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIkrpWPGMA- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 389 AGYYGNPE--ETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLkfqNI-------MyypnEIESVISKMPDVVEVCV 459
Cdd:cd05966 450 RTIYGDHEryEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVI---NVsghrlgtA----EVESALVAHPAVAEAAV 522
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 21356441 460 FGVWNEINGDEATAAVVKKRG---SALTAQDIVDYVETHIdakykqlngGAIIVEDLVR 515
Cdd:cd05966 523 VGRPHDIKGEAIYAFVTLKDGeepSDELRKELRKHVRKEI---------GPIATPDKIQ 572
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
155-448 |
4.68e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 71.39 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 155 TMRNHPS--GSIRIDQVLSTPIEknfQPVRL----EQGNDQTLAILCSSGTTGIPKAVTITNSRQILNSSHSL-----TT 223
Cdd:PRK06334 147 EVRKELSfwEKCRIGIYMSIPFE---WLMRWfgvsDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLkffspKE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 224 NDVQYSHSTLDWITGL----LTTVTSGVfstKRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSS 299
Cdd:PRK06334 224 DDVMMSFLPPFHAYGFnsctLFPLLSGV---PVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 300 LRYYLFGGSrasvETQHRIRSRLSKDCLHFA----YGFTELGSMAALNLHFDEKPNS-VGRLVAGLKLKVICEkgESLGP 374
Cdd:PRK06334 301 LRFVVIGGD----AFKDSLYQEALKTFPHIQlrqgYGTTECSPVITINTVNSPKHEScVGMPIRGMDVLIVSE--ETKVP 374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356441 375 DEVGE--LCLWNG-QYWAGYYGN-PEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVI 448
Cdd:PRK06334 375 VSSGEtgLVLTRGtSLFSGYLGEdFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
187-524 |
6.46e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 70.89 E-value: 6.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 NDQTLAILC-SSGTTGIPKAVTITNSRQILNS-------SHSLTTND-----VQYSHSTLdWitGLLTTVT-SG---VFS 249
Cdd:PRK07008 174 DENQASSLCyTSGTTGNPKGALYSHRSTVLHAygaalpdAMGLSARDavlpvVPMFHVNA-W--GLPYSAPlTGaklVLP 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 250 TKRIIADNIFDpeffmrLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHf 329
Cdd:PRK07008 251 GPDLDGKSLYE------LIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIH- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 330 AYGFTE---LGSMAALNLHFDEKPNSV--------GRLVAGLKLKVICEKGESLGPDEV--GELCLWNGQYWAGYYGNpe 396
Cdd:PRK07008 324 AWGMTEmspLGTLCKLKWKHSQLPLDEqrkllekqGRVIYGVDMKIVGDDGRELPWDGKafGDLQVRGPWVIDRYFRG-- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 397 ETHKMRDhhNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGV----WNEingdEAT 472
Cdd:PRK07008 402 DASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpkWDE----RPL 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 21356441 473 AAVVKKRGSALTAQDIVDYVETHIdAKYkQLNGGAIIVEDLvrsPNGKTNRM 524
Cdd:PRK07008 476 LVVVKRPGAEVTREELLAFYEGKV-AKW-WIPDDVVFVDAI---PHTATGKL 522
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
36-487 |
7.52e-13 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 71.13 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 36 FNEMRRH-------PQLIAQISAT-ENTILTRAELQANAMHIASYMRSLGLLQMDIVGIiarnttHISAVAYACF----- 102
Cdd:PRK10524 56 HNAVDRHlakrpeqLALIAVSTETdEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLI------YMPMIAEAAFamlac 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 103 ----------FNGIAFHSLNISYEQSTiEKLfsitrpnIIFCD-GDEFEKVRSATAQLDvKIITMRNHPSGSIRIdqvls 171
Cdd:PRK10524 130 arigaihsvvFGGFASHSLAARIDDAK-PVL-------IVSADaGSRGGKVVPYKPLLD-EAIALAQHKPRHVLL----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 172 tpIEKNFQPVRLEQGNDQTLA-----------------------ILCSSGTTGIPK---------AVTITNSRQilnssH 219
Cdd:PRK10524 196 --VDRGLAPMARVAGRDVDYAtlraqhlgarvpvewlesnepsyILYTSGTTGKPKgvqrdtggyAVALATSMD-----T 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 220 SLTTN--DVQYSHSTLDWITG--------LLTTVTSGVFSTKRIIADnifdPEFFMRLVEEHQITWIIQAPAHMAMMVNS 289
Cdd:PRK10524 269 IFGGKagETFFCASDIGWVVGhsyivyapLLAGMATIMYEGLPTRPD----AGIWWRIVEKYKVNRMFSAPTAIRVLKKQ 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 290 PS--FTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTELG-SMAALNLHFDEKPN---SVGRLVAGLKLK 363
Cdd:PRK10524 345 DPalLRKHDLSSLRALFLAGEPLDEPTASWISEALGVPVID-NYWQTETGwPILAIARGVEDRPTrlgSPGVPMYGYNVK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 364 VICEK-GESLGPDEVGEL---------CL---WN------GQYWAGYygnpeethkmrdHHNWFHTGDLGYVDDDGFIYI 424
Cdd:PRK10524 424 LLNEVtGEPCGPNEKGVLviegplppgCMqtvWGdddrfvKTYWSLF------------GRQVYSTFDWGIRDADGYYFI 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356441 425 VERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSALTAQD 487
Cdd:PRK10524 492 LGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRE 554
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
354-531 |
9.73e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 70.42 E-value: 9.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 354 GRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNpEETHKMRDHHNWFHTGDLGYVdDDGFIYIVERKKDM-- 431
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLii 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 432 LKFQNImyYPNEIESVISKMPDVV--EVCVFGVWNEinGDEATAAVVKKRGSALTA-QDIVDyvetHIDAKYKQLNGGAI 508
Cdd:PRK09192 466 INGRNI--WPQDIEWIAEQEPELRsgDAAAFSIAQE--NGEKIVLLVQCRISDEERrGQLIH----ALAALVRSEFGVEA 537
|
170 180
....*....|....*....|....*....
gi 21356441 509 IVEdLV------RSPNGKTNRMANKAFFL 531
Cdd:PRK09192 538 AVE-LVpphslpRTSSGKLSRAKAKKRYL 565
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
183-461 |
3.02e-12 |
|
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: 68.92 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 183 LEQGNDQTLAILCSSGTTGIPKAVTITnsrqilnsshslttndvqysHSTLDW-ITGLLTTVTSGVfsTKRIIAdnIFDP 261
Cdd:cd17640 83 VENDSDDLATIIYTSGTTGNPKGVMLT--------------------HANLLHqIRSLSDIVPPQP--GDRFLS--ILPI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 262 -EFFMRLVEEHQITWiiqapaHMAMMVNSPSFTTSDLSSLR-YY------LFGGSRASVETQHRIRSRLSKDCLHFA--- 330
Cdd:cd17640 139 wHSYERSAEYFIFAC------GCSQAYTSIRTLKDDLKRVKpHYivsvprLWESLYSGIQKQVSKSSPIKQFLFLFFlsg 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 331 -------------------------------YGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKVICEKG-ESLGPDEVG 378
Cdd:cd17640 213 gifkfgisgggalpphvdtffeaigievlngYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGnVVLPPGEKG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 379 ELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKD---MLKFQNIMyyPNEIESVISKMPDVV 455
Cdd:cd17640 293 IVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDtivLSNGENVE--PQPIEEALMRSPFIE 370
|
....*.
gi 21356441 456 EVCVFG 461
Cdd:cd17640 371 QIMVVG 376
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
369-525 |
4.50e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.43 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 369 GESLGPDEVGELclwngqyWA-------GYYGNPEETHKM---RDHHNWFHTGDLGYVDDdGFIYIVERKKDMLKFQNIM 438
Cdd:PRK05691 389 LEVLGDNRVGEI-------WAsgpsiahGYWRNPEASAKTfveHDGRTWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHN 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 439 YYPNEIESVISKMPDVV---EVCVFGVwnEINGDEA---TAAVVKKRGSALTAQDIVDYVETHIDAKYKQ-------LNG 505
Cdd:PRK05691 461 LYPQDIEKTVEREVEVVrkgRVAAFAV--NHQGEEGigiAAEISRSVQKILPPQALIKSIRQAVAEACQEapsvvllLNP 538
|
170 180
....*....|....*....|
gi 21356441 506 GAiivedLVRSPNGKTNRMA 525
Cdd:PRK05691 539 GA-----LPKTSSGKLQRSA 553
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
56-538 |
5.66e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 68.52 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 56 ILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGI-AF------HSLNISYEQSTIEKLFSITr 128
Cdd:PRK06060 30 VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVmAFlanpelHRDDHALAARNTEPALVVT- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 129 pNIIFCDgdefekvrsataqldvkiitmRNHPSGSIRIDQVLSTPIE---KNFQPVrleqGNDQTLAILCSSGTTGIPKA 205
Cdd:PRK06060 109 -SDALRD---------------------RFQPSRVAEAAELMSEAARvapGGYEPM----GGDALAYATYTSGTTGPPKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 206 V------TITNSRQILNSSHSLTTNDVQYSHSTLDWITGL-------LTTVTSGVFSTKRIIAdnifdpEFFMRLVEEHQ 272
Cdd:PRK06060 163 AihrhadPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLgnsvwfpLATGGSAVINSAPVTP------EAAAILSARFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 273 ITWIIQAPAHMAMMVNSPSftTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTELGSMAALNLHFDEKPNS 352
Cdd:PRK06060 237 PSVLYGVPNFFARVIDSCS--PDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 353 VGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEethKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDML 432
Cdd:PRK06060 315 LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 433 KFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRGSAL---TAQDIVDYVETHIDAkYKQLNGGAII 509
Cdd:PRK06060 392 VIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIdgsVMRDLHRGLLNRLSA-FKVPHRFAVV 470
|
490 500
....*....|....*....|....*....
gi 21356441 510 vEDLVRSPNGKTNRMAnkaffLEAKSSAK 538
Cdd:PRK06060 471 -DRLPRTPNGKLVRGA-----LRKQSPTK 493
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-525 |
8.14e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 68.26 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 28 HLSIGEIIFNEMRRHPQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIA 107
Cdd:PRK12467 3094 ERLVHQLIEAQVARTPEAPALVFGDQQ--LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGA 3171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 108 FHSLNISYEQstiEKLFSITrpniifcdGDEFEKVRSATAQLDVKIitMRNHPSGSIRIDQV-LSTPIEKNFQPVRleqg 186
Cdd:PRK12467 3172 YVPLDPEYPR---ERLAYMI--------EDSGVKLLLTQAHLLEQL--PAPAGDTALTLDRLdLNGYSENNPSTRV---- 3234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 NDQTLA-ILCSSGTTGIPKAV-----TITNSRQILNSSHSLTTND--VQYSHSTLD-----WITGLLTtvtsgvfSTKRI 253
Cdd:PRK12467 3235 MGENLAyVIYTSGSTGKPKGVgvrhgALANHLCWIAEAYELDANDrvLLFMSFSFDgaqerFLWTLIC-------GGCLV 3307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 254 IADN-IFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSftTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYG 332
Cdd:PRK12467 3308 VRDNdLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAG--GADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYG 3385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 333 FTElgsMAALNLHFDEKPNSV--------GRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKmRDH 404
Cdd:PRK12467 3386 PTE---AVVTVTLWKCGGDAVceapyapiGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAE-RFV 3461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 405 HNWFH--------TGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwNEINGDEATAAVV 476
Cdd:PRK12467 3462 ADPFSgsggrlyrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVV 3540
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 21356441 477 kkrgSALTAQDIVDYVETHIDAKYKQLNGGAIIV--EDLVRSPNGKTNRMA 525
Cdd:PRK12467 3541 ----PADPQGDWRETLRDHLAASLPDYMVPAQLLvlAAMPLGPNGKVDRKA 3587
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
41-525 |
1.11e-11 |
|
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: 66.97 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 41 RHPQLIAQISatENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNT----THISAVAYAcffnGIAFHSLNISYE 116
Cdd:cd17655 9 KTPDHTAVVF--EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSlemiVGILGILKA----GGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 117 QSTIEKLFSITRPNIIFCDGDEFEKVRSATAQLDVKIITMRNHPSgsiridqvlstpieKNFQPVrleqGNDQTLA-ILC 195
Cdd:cd17655 83 EERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEES--------------ENLEPV----SKSDDLAyVIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 196 SSGTTGIPKAVTITNsRQILNSSHSLTTNDVQYSHSTLdwitGLLT------TVTSgVF----STKRII---ADNIFDPE 262
Cdd:cd17655 145 TSGSTGKPKGVMIEH-RGVVNLVEWANKVIYQGEHLRV----ALFAsisfdaSVTE-IFasllSGNTLYivrKETVLDGQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 263 FFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTsdlSSLRYYLFGGSRASVETQHRIRSRLSKDCLHF-AYGFTE--LGSM 339
Cdd:cd17655 219 ALTQYIRQNRITIIDLTPAHLKLLDAADDSEG---LSLKHLIVGGEALSTELAKKIIELFGTNPTITnAYGPTEttVDAS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 340 AALNLHFDEKPNSV--GRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEET-HKMRDH-----HNWFHTG 411
Cdd:cd17655 296 IYQYEPETDQQVSVpiGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTaEKFVDDpfvpgERMYRTG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 412 DLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRgsALTAQDIVDY 491
Cdd:cd17655 376 DLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK--ELPVAQLREF 453
|
490 500 510
....*....|....*....|....*....|....*....
gi 21356441 492 VETH-----IDAKYKQLnggaiivEDLVRSPNGKTNRMA 525
Cdd:cd17655 454 LARElpdymIPSYFIKL-------DEIPLTPNGKVDRKA 485
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
259-524 |
3.71e-11 |
|
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: 65.28 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 259 FDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPsfTTSDLSSLRYYLFGGSRASVETQHRIRsRLSKDCLHFAYGFTELGS 338
Cdd:cd05974 163 FDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD--LASFDVKLREVVGAGEPLNPEVIEQVR-RAWGLTIRDGYGQTETTA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 339 MAALNLHFDEKPNSVGRLVAGLKLKVICEKGeslGPDEVGELCLWNGQY-----WAGYYGNPEET-HKMRDHHnwFHTGD 412
Cdd:cd05974 240 LVGNSPGQPVKAGSMGRPLPGYRVALLDPDG---APATEGEVALDLGDTrpvglMKGYAGDPDKTaHAMRGGY--YRTGD 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 413 LGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKKRG---SALTAQDIV 489
Cdd:cd05974 315 IAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGyepSPETALEIF 394
|
250 260 270
....*....|....*....|....*....|....*
gi 21356441 490 DYVETHIdAKYKQLNGGAIIveDLVRSPNGKTNRM 524
Cdd:cd05974 395 RFSRERL-APYKRIRRLEFA--ELPKTISGKIRRV 426
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
13-525 |
5.49e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.75 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 13 RKIWSGDQLEYYFDPHLSIGEIIFNEMRRHPQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTT 92
Cdd:PRK12316 4535 RIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEK--LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSA 4612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 93 HISAVAYACFFNGIAFHSLNISYEQSTIEKLFSITRPNIIFCDgdefekvRSATAQLDVkiitmrnhPSG--SIRIDQVL 170
Cdd:PRK12316 4613 EMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQ-------SHLLQRLPI--------PDGlaSLALDRDE 4677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 171 STPIEKNFQPVRLEQGndQTLA-ILCSSGTTGIPKAVTITNsRQILNSSHS------LTTND--VQYSHSTLD-WITGLL 240
Cdd:PRK12316 4678 DWEGFPAHDPAVRLHP--DNLAyVIYTSGSTGRPKGVAVSH-GSLVNHLHAtgeryeLTPDDrvLQFMSFSFDgSHEGLY 4754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 241 TTVTSGvfSTKRIIADNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSfTTSDLSSLRYYLFGGSRASVETQHRIRS 320
Cdd:PRK12316 4755 HPLING--ASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASYDLAWR 4831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 321 RLSKDCLHFAYGFTElgsMAALNLHFDEKPNS--------VGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYY 392
Cdd:PRK12316 4832 ALKPVYLFNGYGPTE---TTVTVLLWKARDGDacgaaympIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYL 4908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 393 GNPEET-----------HKMRdhhnWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFG 461
Cdd:PRK12316 4909 ERPALTaerfvpdpfgaPGGR----LYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA 4984
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 462 VWNE----------------INGDEATAAVVKKRGSALtAQDIVDY-VETHIdakykqlnggaIIVEDLVRSPNGKTNRM 524
Cdd:PRK12316 4985 QEGAvgkqlvgyvvpqdpalADADEAQAELRDELKAAL-RERLPEYmVPAHL-----------VFLARMPLTPNGKLDRK 5052
|
.
gi 21356441 525 A 525
Cdd:PRK12316 5053 A 5053
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
393-528 |
5.86e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 64.29 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 393 GNPEEThKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEAT 472
Cdd:PRK08308 279 NAPEEI-VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVK 357
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 21356441 473 AAVVKKrgSALTAQDIVDYVETHIdAKYkQLNGGAIIVEDLVRSPNGKTNRMANKA 528
Cdd:PRK08308 358 AKVISH--EEIDPVQLREWCIQHL-APY-QVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-525 |
6.97e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 65.57 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 25 FDPHLSIGEIIFNEMRRHPQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFN 104
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGEQE--LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKA 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 105 GIAFHSLNISYEQSTIEKLFSITRPNIIFCDgdefekvRSATAQLDVkiitmrnhPSG--SIRIDQV---LSTPIEKNFQ 179
Cdd:PRK12467 1648 GGAYVPLDPEYPRERLAYMIEDSGIELLLTQ-------SHLQARLPL--------PDGlrSLVLDQEddwLEGYSDSNPA 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 180 pVRLeqgNDQTLA-ILCSSGTTGIPKAVTITNSRQI-----LNSSHSLTTNDV-------QYSHSTLDWITGLLT--TVT 244
Cdd:PRK12467 1713 -VNL---APQNLAyVIYTSGSTGRPKGAGNRHGALVnrlcaTQEAYQLSAADVvlqftsfAFDVSVWELFWPLINgaRLV 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 245 SGVFSTKRiiadnifDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSsLRYYLFGGSRASVETQHRIRSRLSK 324
Cdd:PRK12467 1789 IAPPGAHR-------DPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS-LRRVVCGGEALEVEALRPWLERLPD 1860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 325 DCLHFAYGFTELG---SMAALNLHFDEKPNSV--GRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETH 399
Cdd:PRK12467 1861 TGLFNLYGPTETAvdvTHWTCRRKDLEGRDSVpiGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTA 1940
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 400 KM-------RDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwNEINGDEAT 472
Cdd:PRK12467 1941 ERfvadpfgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLV 2019
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 473 AAVVKKrGSALTAQD--IVDYVETHIDAKYKQL-----NGGAIIVEDLVRSPNGKTNRMA 525
Cdd:PRK12467 2020 AYVVPT-DPGLVDDDeaQVALRAILKNHLKASLpeymvPAHLVFLARMPLTPNGKLDRKA 2078
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
173-525 |
1.17e-10 |
|
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: 63.73 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 173 PIEKNFQPVRLE-QGNDQTLAILCS-----------SGTTGIPKAVTITNSRQI-----LNSSHSLTTND--VQYSHSTL 233
Cdd:cd17645 77 PIDPDYPGERIAyMLADSSAKILLTnpddlayviytSGSTGLPKGVMIEHHNLVnlcewHRPYFGVTPADksLVYASFSF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 234 D-WITGLLTTVTSGvfSTKRIIADNI-FDPEFFMRLVEEHQITwIIQAPAHMAmmvnsPSFTTSDLSSLRYYLFGGSRAS 311
Cdd:cd17645 157 DaSAWEIFPHLTAG--AALHVVPSERrLDLDALNDYFNQEGIT-ISFLPTGAA-----EQFMQLDNQSLRVLLTGGDKLK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 312 VETQHRIRsrlskdcLHFAYGFTELGSMA-ALNLHFDEKPNSVGRLVAGLKLkVICEKGESLGPDEV-GELCLWNGQYWA 389
Cdd:cd17645 229 KIERKGYK-------LVNNYGPTENTVVAtSFEIDKPYANIPIGKPIDNTRV-YILDEALQLQPIGVaGELCIAGEGLAR 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 390 GYYGNPEET------HKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVw 463
Cdd:cd17645 301 GYLNRPELTaekfivHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAK- 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356441 464 NEINGDEATAA--VVKKRGS-----ALTAQDIVDYVethIDAKYKQLNGGAIIVedlvrspNGKTNRMA 525
Cdd:cd17645 380 EDADGRKYLVAyvTAPEEIPheelrEWLKNDLPDYM---IPTYFVHLKALPLTA-------NGKVDRKA 438
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
196-492 |
1.58e-10 |
|
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: 63.46 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 196 SSGTTGIPKAVTITNSR----QILNSSHSLTTNDVQYSHSTLDWITGLL-----------TTVTSGVFSTKRIIADnifd 260
Cdd:cd05938 152 TSGTTGLPKAARISHLRvlqcSGFLSLCGVTADDVIYITLPLYHSSGFLlgiggcielgaTCVLKPKFSASQFWDD---- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 261 peffmrlVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRAsvETQHRIRSRLSKDCLHFAYGFTElGSMA 340
Cdd:cd05938 228 -------CRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRA--DVWREFLRRFGPIRIREFYGSTE-GNIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 341 ALNlhFDEKPNSVGRlvAGLKLKVIC---------EKGESL----------GPDEVGELC--LWNGQYWAGYYGNPEETH 399
Cdd:cd05938 298 FFN--YTGKIGAVGR--VSYLYKLLFpfelikfdvEKEEPVrdaqgfcipvAKGEPGLLVakITQQSPFLGYAGDKEQTE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 400 K--MRDHHN----WFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwnEINGDE--- 470
Cdd:cd05938 374 KklLRDVFKkgdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV--TVPGHEgri 451
|
330 340
....*....|....*....|..
gi 21356441 471 ATAAVVKKRGSALTAQDIVDYV 492
Cdd:cd05938 452 GMAAVKLKPGHEFDGKKLYQHV 473
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
300-459 |
2.44e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 63.07 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 300 LRYYLFGGSRASVETQHRIRSRLSkdCLHFAYGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKV--ICEKGESLGPDEV 377
Cdd:PTZ00216 430 VRAMLSGGGPLSAATQEFVNVVFG--MVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLldTEEYKHTDTPEPR 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 378 GELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNE-IESVISKMPDVVE 456
Cdd:PTZ00216 508 GEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEaLEALYGQNELVVP 587
|
....*
gi 21356441 457 --VCV 459
Cdd:PTZ00216 588 ngVCV 592
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
392-533 |
4.10e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 61.60 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 392 YGNPEETHKMRDHhNWFHTGDLGYVDDdGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEA 471
Cdd:PRK07824 221 YRNPVDPDPFAEP-GWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRV 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356441 472 TAAVVKKRGSALTAQDIVDYVETHID--AKYKQLNggaiIVEDLVRSPNGKTNRMANKAFFLEA 533
Cdd:PRK07824 299 VAAVVGDGGPAPTLEALRAHVARTLDrtAAPRELH----VVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
179-525 |
5.26e-10 |
|
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: 61.72 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 179 QPVRLEQGNDQTLAILCSSGTTGIPKAVTITNsRQILN-------SSHSLTTNDV-QYSHSTLD-WITGLLTTVTSGvfS 249
Cdd:cd17656 119 SNIDYINNSDDLLYIIYTSGTTGKPKGVQLEH-KNMVNllhfereKTNINFSDKVlQFATCSFDvCYQEIFSTLLSG--G 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 250 TKRIIADNI-FDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVeTQHRIRSRLSKDC-L 327
Cdd:cd17656 196 TLYIIREETkRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLVI-TNEFKEMLHEHNVhL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 328 HFAYGFTE--LGSMAALNlHFDEKPN--SVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK--- 400
Cdd:cd17656 275 HNHYGPSEthVVTTYTIN-PEAEIPElpPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEkff 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 401 ---MRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFgVWNEINGD-EATAAVV 476
Cdd:cd17656 354 pdpFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVL-DKADDKGEkYLCAYFV 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 21356441 477 KKRgsALTAQDIVDYV-----ETHIDAKYKQLnggaiivEDLVRSPNGKTNRMA 525
Cdd:cd17656 433 MEQ--ELNISQLREYLakqlpEYMIPSFFVPL-------DQLPLTPNGKVDRKA 477
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
43-492 |
1.42e-09 |
|
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: 60.11 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 43 PQLIAQISATENtiLTRAELQANAMHIASYMRSLGLLQMD-IVGIIARNTTHISAVAYACFFNGIAFHSLNISYEQSTIE 121
Cdd:cd17648 1 PDRVAVVYGDKR--LTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 122 KLFSITRpniifcdgdefekvrsatAQLdvkiitmrnhpsgsiridqVLSTPIEknfqpvrleqgndqtLA-ILCSSGTT 200
Cdd:cd17648 79 FILEDTG------------------ARV-------------------VITNSTD---------------LAyAIYTSGTT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 201 GIPKAV-----TITNSRQILNSSHSLTTNDVQ----YSHSTLD-WITGLLTTVTSGvfsTKRIIADN--IFDPEFFMRLV 268
Cdd:cd17648 107 GKPKGVlvehgSVVNLRTSLSERYFGRDNGDEavlfFSNYVFDfFVEQMTLALLNG---QKLVVPPDemRFDPDRFYAYI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 269 EEHQITWIIQAPAHMAMmvnspsFTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTELgSMAALNLHF-- 346
Cdd:cd17648 184 NREKVTYLSGTPSVLQQ------YDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIIN-AYGPTET-TVTNHKRFFpg 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 347 -DEKPNSVGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYG-----------NPEETHKMRDHHNW---FHTG 411
Cdd:cd17648 256 dQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNrpeltaerflpNPFQTEQERARGRNarlYKTG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 412 DLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEvcvfgvwneingdeatAAVVKKRGSALTAQDIVDY 491
Cdd:cd17648 336 DLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRE----------------CAVVAKEDASQAQSRIQKY 399
|
.
gi 21356441 492 V 492
Cdd:cd17648 400 L 400
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
193-525 |
2.86e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.36 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 193 ILCSSGTTGIPKAVTItnsrqilnsSHSLTTNDVQYSHST--LDWITGLL--TTVTSGV---------FSTKRII---AD 256
Cdd:PRK12316 660 VIYTSGSTGKPKGAGN---------RHRALSNRLCWMQQAygLGVGDTVLqkTPFSFDVsvweffwplMSGARLVvaaPG 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 257 NIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSftTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTEl 336
Cdd:PRK12316 731 DHRDPAKLVELINREGVDTLHFVPSMLQAFLQDED--VASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTE- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 337 gsmAALNL-HF---DEKPNSV--GRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK------MRDH 404
Cdd:PRK12316 808 ---AAIDVtHWtcvEEGGDSVpiGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAErfvpspFVAG 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 405 HNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwneiNGDEATAAVVKKRGSALT 484
Cdd:PRK12316 885 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGYVVLESEGGDW 960
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 21356441 485 --------AQDIVDY-VETHIdakykqlnggaIIVEDLVRSPNGKTNRMA 525
Cdd:PRK12316 961 realkahlAASLPEYmVPAQW-----------LALERLPLTPNGKLDRKA 999
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
193-525 |
7.20e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.82 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 193 ILCSSGTTGIPKAVTI-----TNSRQILNSSHSLTTNDVQYSHSTLDW---ITGLLTTVTSGVFSTKRIIADNIfDPEFF 264
Cdd:PRK12316 3201 VIYTSGSTGKPKGVGIrhsalSNHLCWMQQAYGLGVGDRVLQFTTFSFdvfVEELFWPLMSGARVVLAGPEDWR-DPALL 3279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 265 MRLVEEHQITWIIQAPAHMAMMVNSPSftTSDLSSLRYYLFGGSRASVETQHRIrsrLSKDCLHFAYGFTELGSMAALNL 344
Cdd:PRK12316 3280 VELINSEGVDVLHAYPSMLQAFLEEED--AHRCTSLKRIVCGGEALPADLQQQV---FAGLPLYNLYGPTEATITVTHWQ 3354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 345 HFDEKPNS--VGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEETHK------MRDHHNWFHTGDLGYV 416
Cdd:PRK12316 3355 CVEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAErfvpdpFVPGERLYRTGDLARY 3434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 417 DDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwneiNGDEATAAVVKKRGS--------ALTAQDI 488
Cdd:PRK12316 3435 RADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV----DGRQLVAYVVPEDEAgdlrealkAHLKASL 3510
|
330 340 350
....*....|....*....|....*....|....*...
gi 21356441 489 VDY-VETHIdakykqlnggaIIVEDLVRSPNGKTNRMA 525
Cdd:PRK12316 3511 PEYmVPAHL-----------LFLERMPLTPNGKLDRKA 3537
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
296-462 |
8.05e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 58.24 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 296 DLSSLRYYLFGGSRASVETQHRIRSRLSK-----DCLHFAYGFTElgSMAALN-------LHFDE----------KPNSV 353
Cdd:PRK05851 270 DLGALRVALNGGEPVDCDGFERFATAMAPfgfdaGAAAPSYGLAE--STCAVTvpvpgigLRVDEvttddgsgarRHAVL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 354 GRLVAGLKLKVICEKGES-LGPDEVGELCLWNGQYWAGYYGNPEethkmRDHHNWFHTGDLGYVDDDGFIyIVERKKDML 432
Cdd:PRK05851 348 GNPIPGMEVRISPGDGAAgVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYLVDGGLV-VCGRAKELI 421
|
170 180 190
....*....|....*....|....*....|..
gi 21356441 433 KF--QNImyYPNEIESVISKMPDVVEVCVFGV 462
Cdd:PRK05851 422 TVagRNI--FPTEIERVAAQVRGVREGAVVAV 451
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
188-525 |
8.16e-09 |
|
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: 57.86 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 188 DQTLAILCSSGTTGIPKAVTITNsRQILNSSH---------SLTTNDVQYSHSTLDWITG-LLTTVTSGvfSTKRIIADN 257
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEH-RNVAHAAHawrreyeldSFPVRLLQMASFSFDVFAGdFARSLLNG--GTLVICPDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 258 I-FDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETQHRIRSRL-SKDCLHFAYGFTE 335
Cdd:cd17650 170 VkLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFgQGMRIINSYGVTE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 336 lgsmAALNLHF-----DEKPNS----VGRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGNPEEThKMRDHHN 406
Cdd:cd17650 250 ----ATIDSTYyeegrDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELT-AERFVEN 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 407 WF-------HTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVfGVWNEINGDEATAAVVKKR 479
Cdd:cd17650 325 PFapgermyRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVV-AVREDKGGEARLCAYVVAA 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 21356441 480 GS-------ALTAQDIVDYVethIDAKYKQLNGgaiivedLVRSPNGKTNRMA 525
Cdd:cd17650 404 ATlntaelrAFLAKELPSYM---IPSYYVQLDA-------LPLTPNGKVDRRA 446
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
188-490 |
1.35e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 57.49 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 188 DQTLAILC-SSGTTGIPKAVTITNSRQILNSSHSLTTNDVQYSHST-----------LDWitGL-LTTVTSGvfsTKRII 254
Cdd:PRK05620 180 ETTAAAICySTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHGEsflccvpiyhvLSW--GVpLAAFMSG---TPLVF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 255 ADNIFDPEFFMRLVEE------HQI-TWIIQAPAHMamMVNSPsfttsDLSSLRYYLFGGSRASVETQHRIRSRLSKDCL 327
Cdd:PRK05620 255 PGPDLSAPTLAKIIATamprvaHGVpTLWIQLMVHY--LKNPP-----ERMSLQEIYVGGSAVPPILIKAWEERYGVDVV 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 328 HfAYGFTELGSMAALNlhfdEKPNSV------------GRLVAGLKLKVIcEKGESLGPDE--VGELCLWNGQYWAGYYG 393
Cdd:PRK05620 328 H-VWGMTETSPVGTVA----RPPSGVsgearwayrvsqGRFPASLEYRIV-NDGQVMESTDrnEGEIQVRGNWVTASYYH 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 394 NPEET-----HKMRDHH-----------NWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEV 457
Cdd:PRK05620 402 SPTEEgggaaSTFRGEDvedandrftadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVEC 481
|
330 340 350
....*....|....*....|....*....|....*.
gi 21356441 458 CVFGVWNEINGDEATAAVVKKRG---SALTAQDIVD 490
Cdd:PRK05620 482 AVIGYPDDKWGERPLAVTVLAPGiepTRETAERLRD 517
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
369-534 |
1.55e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 57.44 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 369 GESLGPDEVGELCLWNGQYWAGYYGNPEETH-----KMR-------------DHHNWFHTGDLG-YVddDGFIYIVERKK 429
Cdd:PRK12476 421 GAELPDGEVGEIWLHGDNIGRGYWGRPEETErtfgaKLQsrlaegshadgaaDDGTWLRTGDLGvYL--DGELYITGRIA 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 430 DMLKFQNIMYYPNEIESVISKMPDVVE---VCVFGVWNEingDEATAAVVKKRGSALTAQD---IVDYVETHIDAKY--- 500
Cdd:PRK12476 499 DLIVIDGRNHYPQDIEATVAEASPMVRrgyVTAFTVPAE---DNERLVIVAERAAGTSRADpapAIDAIRAAVSRRHgla 575
|
170 180 190
....*....|....*....|....*....|....*...
gi 21356441 501 ----KQLNGGAIivedlVRSPNGKTNRMANKAFFLEAK 534
Cdd:PRK12476 576 vadvRLVPAGAI-----PRTTSGKLARRACRAQYLDGR 608
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
299-454 |
2.25e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 57.05 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 299 SLRYYLFGGSRASVETQhrirsRLSKDCLHF----AYGFTELGSMAALNlHFDEkpNSVGRLVAGL-----KLkVICEKG 369
Cdd:PLN02387 421 RIRFMLSGGAPLSGDTQ-----RFINICLGApigqGYGLTETCAGATFS-EWDD--TSVGRVGPPLpccyvKL-VSWEEG 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 370 ESLGPDEV---GELCLWNGQYWAGYYGNPEETHK--------MRdhhnWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIM 438
Cdd:PLN02387 492 GYLISDKPmprGEIVIGGPSVTLGYFKNQEKTDEvykvdergMR----WFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGE 567
|
170
....*....|....*..
gi 21356441 439 YYP-NEIESVISKMPDV 454
Cdd:PLN02387 568 YVSlGKVEAALSVSPYV 584
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
50-460 |
4.88e-08 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 55.82 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 50 SATENTILTRAELQANAMHIASYMR-SLGLLQMDIVGIIARNTTHISAVAYACFFNGIafhsLNISYEQSTIEKLFSITR 128
Cdd:cd05905 8 KGKEATTLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGV----VPIPIEPPDISQQLGFLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 129 PNIifcdgdEFEKVRSATAQLDVKIITMRNHPSGSIRID-------QVLSTPIEKNFQPVRLEQG----NDQTLAIL--- 194
Cdd:cd05905 84 GTC------KVRVALTVEACLKGLPKKLLKSKTAAEIAKkkgwpkiLDFVKIPKSKRSKLKKWGPhpptRDGDTAYIeys 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 195 -CSSGTTgIPKAVTitnSRQILNSSHSLTTNDVQYSHSTLdwIT--------GLLTTVTSGVFS--TKRIIADNIF--DP 261
Cdd:cd05905 158 fSSDGSL-SGVAVS---HSSLLAHCRALKEACELYESRPL--VTvldfksglGLWHGCLLSVYSghHTILIPPELMktNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 262 EFFMRLVEEHQI--TWIIQAPAHMAMMVNSPSFTTSD-----LSSLR------------YY------LFG--GSRA---S 311
Cdd:cd05905 232 LLWLQTLSQYKVrdAYVKLRTLHWCLKDLSSTLASLKnrdvnLSSLRmcmvpcenrpriSScdsflkLFQtlGLSPravS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 312 VETQHRIRSRLskdCLHfAYGFTELG----SMAAL-----NLHFDEKPNS-----VGRLVAGLKLKVICEKGESL-GPDE 376
Cdd:cd05905 312 TEFGTRVNPFI---CWQ-GTSGPEPSrvylDMRALrhgvvRLDERDKPNSlplqdSGKVLPGAQVAIVNPETKGLcKDGE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 377 VGELCLWNGQYWAGYYGNPEETHKMRDHHN------------WFHTGDLGYV----------DDDGFIYIVERKKDMLKF 434
Cdd:cd05905 388 IGEIWVNSPANASGYFLLDGETNDTFKVFPstrlstgitnnsYARTGLLGFLrptkctdlnvEEHDLLFVVGSIDETLEV 467
|
490 500
....*....|....*....|....*..
gi 21356441 435 QNIMYYPNEIESVISKM-PDVVEVCVF 460
Cdd:cd05905 468 RGLRHHPSDIEATVMRVhPYRGRCAVF 494
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
378-461 |
6.00e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 55.62 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 378 GELCLWNGQYWAGYYGNPEETHKMRDHhNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNE-IESVISKMPDVVE 456
Cdd:PLN02861 466 GEICLRGNTLFSGYHKRQDLTEEVLID-GWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVEnLENTYSRCPLIAS 544
|
....*
gi 21356441 457 VCVFG 461
Cdd:PLN02861 545 IWVYG 549
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
193-461 |
6.12e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 55.41 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 193 ILCSSGTTGIPKAVTITNS----------RQILNSSHSLTTNDVQYSHSTLDWI-------------------------- 236
Cdd:PLN02614 228 IMYTSGTTGDPKGVMISNEsivtliagviRLLKSANAALTVKDVYLSYLPLAHIfdrvieecfiqhgaaigfwrgdvkll 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 237 -----------------------TGLLTTVTSGVFSTKRIiadniFDPEFfmrlveEHQITWIIQAPAHMAMmvnSPSFT 293
Cdd:PLN02614 308 iedlgelkptifcavprvldrvySGLQKKLSDGGFLKKFV-----FDSAF------SYKFGNMKKGQSHVEA---SPLCD 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 294 TSDLSSLRYYLFGGSRASVETQHRIRSRLSK-----DCLHF--AYGFTE--LGSMAALNLHFDeKPNSVGRLVAG--LKL 362
Cdd:PLN02614 374 KLVFNKVKQGLGGNVRIILSGAAPLASHVESflrvvACCHVlqGYGLTEscAGTFVSLPDELD-MLGTVGPPVPNvdIRL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 363 KVICEKG-ESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHhNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYP 441
Cdd:PLN02614 453 ESVPEMEyDALASTPRGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVA 531
|
330 340
....*....|....*....|.
gi 21356441 442 NE-IESVISKMPDVVEVCVFG 461
Cdd:PLN02614 532 VEnIENIYGEVQAVDSVWVYG 552
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
187-488 |
6.75e-08 |
|
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: 55.13 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 NDQTLAILCS-SGTTGIPKAVTITNSR-----QILNSSHSLTTNDVQYS-----HSTlDWITGLLTTVTSGvfSTkrIIA 255
Cdd:cd05937 85 DPDDPAILIYtSGTTGLPKAAAISWRRtlvtsNLLSHDLNLKNGDRTYTcmplyHGT-AAFLGACNCLMSG--GT--LAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 256 DNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRYYLFGGSRASVETqhRIRSRLSKDCLHFAYGFTE 335
Cdd:cd05937 160 SRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWE--RFRERFNVPEIGEFYAATE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 336 lGSMAALNLHF-DEKPNSVGR--LVAGLKL-------KVICEKGESLGPD-----------EVGELC----LWNGQYWAG 390
Cdd:cd05937 238 -GVFALTNHNVgDFGAGAIGHhgLIRRWKFenqvvlvKMDPETDDPIRDPktgfcvrapvgEPGEMLgrvpFKNREAFQG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 391 YYGNPEETHK--MRDHHN----WFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWN 464
Cdd:cd05937 317 YLHNEDATESklVRDVFRkgdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKV 396
|
330 340
....*....|....*....|....
gi 21356441 465 EINGDEATAAVVKKRGSALTAQDI 488
Cdd:cd05937 397 PGHDGRAGCAAITLEESSAVPTEF 420
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
191-496 |
1.05e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 54.76 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 191 LAILCSSGTTGIPKAVtitnsrqiLNSS-----HSLTT---------NDVQYShsTLD--WITG--------LLTTVTSG 246
Cdd:PRK00174 248 LFILYTSGSTGKPKGV--------LHTTggylvYAAMTmkyvfdykdGDVYWC--TADvgWVTGhsyivygpLANGATTL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 247 VFSTkriiADNIFDPEFFMRLVEEHQITWIIQAP----AHMAMMVNSPsfTTSDLSSLR----------------YY-LF 305
Cdd:PRK00174 318 MFEG----VPNYPDPGRFWEVIDKHKVTIFYTAPtairALMKEGDEHP--KKYDLSSLRllgsvgepinpeawewYYkVV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 306 GGSRAS-VET--QhrirsrlskdclhfaygfTELGSM--AALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGPDEVGEL 380
Cdd:PRK00174 392 GGERCPiVDTwwQ------------------TETGGImiTPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 381 CL---WNGQYwAGYYGNPE---ETHKMRDHHNWFhTGDLGYVDDDGFIYIVERKKDMLkfqNI-------MyypnEIESV 447
Cdd:PRK00174 454 VIkdpWPGMM-RTIYGDHErfvKTYFSTFKGMYF-TGDGARRDEDGYYWITGRVDDVL---NVsghrlgtA----EIESA 524
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 21356441 448 ISKMPDVVEVCVFGVWNEINGDEATAAVVKKRG---SALTAQDIVDYVETHI 496
Cdd:PRK00174 525 LVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGeepSDELRKELRNWVRKEI 576
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
378-461 |
1.07e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 54.72 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 378 GELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYY-PNEIESVISKMPDVVE 456
Cdd:PLN02736 459 GEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIaPEKIENVYAKCKFVAQ 538
|
....*
gi 21356441 457 VCVFG 461
Cdd:PLN02736 539 CFVYG 543
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
193-459 |
1.09e-07 |
|
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: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 193 ILCSSGTTGIPKAV---------TITNSRQILNSSHS---LTTNDVQYSHSTLDWITGL-----LTTVTSGVFSTKRIIA 255
Cdd:cd17654 123 VIHTSGTTGTPKIVavphkcilpNIQHFRSLFNITSEdilFLTSPLTFDPSVVEIFLSLssgatLLIVPTSVKVLPSKLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 256 DNIFdpeffmrlvEEHQITwIIQAPAHMAMMVNS---PSFTTSDLSSLRYYLFGG----------SRASVETQHRIRSrl 322
Cdd:cd17654 203 DILF---------KRHRIT-VLQATPTLFRRFGSqsiKSTVLSATSSLRVLALGGepfpslvilsSWRGKGNRTRIFN-- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 323 skdclhfAYGFTELGSMAALN-LHFDEKPNSVGRLVAGLKLKVICEKG-ESLGPDEVGELCLwnGQYWAGYYGNPEEThk 400
Cdd:cd17654 271 -------IYGITEVSCWALAYkVPEEDSPVQLGSPLLGTVIEVRDQNGsEGTGQVFLGGLNR--VCILDDEVTVPKGT-- 339
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 21356441 401 mrdhhnWFHTGDLGYVdDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCV 459
Cdd:cd17654 340 ------MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV 391
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
57-426 |
2.08e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 53.73 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 57 LTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGIAFHSLNISYeqSTI----EKL---FSITRP 129
Cdd:PRK08180 70 LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAY--SLVsqdfGKLrhvLELLTP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 130 NIIFC-DGDEFEKVRSATAQLDVKIITMRNHPSGS--IRIDQVLSTP----IEKNFQPVRLEqgndqTLA-ILCSSGTTG 201
Cdd:PRK08180 148 GLVFAdDGAAFARALAAVVPADVEVVAVRGAVPGRaaTPFAALLATPptaaVDAAHAAVGPD-----TIAkFLFTSGSTG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 202 IPKAVTIT------NSRQILNSSHSLTTNDVQYshstLDWITgllttvTSGVFSTKRIIADNIFD------------PEF 263
Cdd:PRK08180 223 LPKAVINThrmlcaNQQMLAQTFPFLAEEPPVL----VDWLP------WNHTFGGNHNLGIVLYNggtlyiddgkptPGG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 264 FMRLVE---EHQITWIIQAPAHMAMMVNS----PSFTTSDLSSLRYYLFGG-----------SRASVETQ-HRIRsrlsk 324
Cdd:PRK08180 293 FDETLRnlrEISPTVYFNVPKGWEMLVPAlerdAALRRRFFSRLKLLFYAGaalsqdvwdrlDRVAEATCgERIR----- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 325 dcLHFAYGFTELGSMaALNLHF-DEKPNSVGRLVAGLKLKV--------ICEKGESLGPdevgelclwngqywaGYYGNP 395
Cdd:PRK08180 368 --MMTGLGMTETAPS-ATFTTGpLSRAGNIGLPAPGCEVKLvpvggkleVRVKGPNVTP---------------GYWRAP 429
|
410 420 430
....*....|....*....|....*....|....*....
gi 21356441 396 EETHKMRDHHNWFHTGDLG-YVDDD----GFIY---IVE 426
Cdd:PRK08180 430 ELTAEAFDEEGYYRSGDAVrFVDPAdperGLMFdgrIAE 468
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
267-478 |
2.09e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 53.46 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 267 LVEEHQIT-----------WI--IQAPAHMAMmvnspsfttsdLSSLRYYLFGGSRASVETQHRIRSRLSkdC-LHFAYG 332
Cdd:PRK10946 267 LIEKHQVNvtalvppavslWLqaIAEGGSRAQ-----------LASLKLLQVGGARLSETLARRIPAELG--CqLQQVFG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 333 FTE-LGSMAALNLHFDEKPNSVGRLVAGL-KLKVICEKGESLGPDEVGELcLWNGQY-WAGYYGNPEETHKMRDHHNWFH 409
Cdd:PRK10946 334 MAEgLVNYTRLDDSDERIFTTQGRPMSPDdEVWVADADGNPLPQGEVGRL-MTRGPYtFRGYYKSPQHNASAFDANGFYC 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356441 410 TGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNEINGDEATAAVVKK 478
Cdd:PRK10946 413 SGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK 481
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
192-429 |
3.98e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.05 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 192 AILCSSGTTGIPKAVTIT------NSRQILnSSHSLTTNDVQYS-----HStLDWITGLLTTVTSGVfstkriiadnifd 260
Cdd:PRK06814 797 VILFTSGSEGTPKGVVLShrnllaNRAQVA-ARIDFSPEDKVFNalpvfHS-FGLTGGLVLPLLSGV------------- 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 261 PEFF------MRLVEEhqitWIIQAPAhmAMMVNSPSFTTS--------DLSSLRYYLFGGSRASVETQH----RIRSRL 322
Cdd:PRK06814 862 KVFLypsplhYRIIPE----LIYDTNA--TILFGTDTFLNGyaryahpyDFRSLRYVFAGAEKVKEETRQtwmeKFGIRI 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 323 SKdclhfAYGFTELGSMAALN--LHFdeKPNSVGRLVAGLKLKVicEKGEslGPDEVGELCLWNGQYWAGYY--GNPEET 398
Cdd:PRK06814 936 LE-----GYGVTETAPVIALNtpMHN--KAGTVGRLLPGIEYRL--EPVP--GIDEGGRLFVRGPNVMLGYLraENPGVL 1004
|
250 260 270
....*....|....*....|....*....|.
gi 21356441 399 HKMRDhhNWFHTGDLGYVDDDGFIYIVERKK 429
Cdd:PRK06814 1005 EPPAD--GWYDTGDIVTIDEEGFITIKGRAK 1033
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
372-519 |
6.28e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 52.25 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 372 LGPDEVGELCLWNGQYWAGYYGNPEETH-----KMRD------HHNWFHTGDLGYVDDDGFiYIVERKKDMLkfqnIMY- 439
Cdd:PRK05850 392 CPAGTVGEIWVHGDNVAAGYWQKPEETErtfgaTLVDpspgtpEGPWLRTGDLGFISEGEL-FIVGRIKDLL----IVDg 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 440 ---YPNEIESVISKMPD--VVEVCVfgvwnEINGDE--ATAAVVKKRG-SALTAQDIVDYVETHIDAKYKQLNGgaIIVE 511
Cdd:PRK05850 467 rnhYPDDIEATIQEITGgrVAAISV-----PDDGTEklVAIIELKKRGdSDEEAMDRLRTVKREVTSAISKSHG--LSVA 539
|
....*...
gi 21356441 512 DLVRSPNG 519
Cdd:PRK05850 540 DLVLVAPG 547
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
377-491 |
1.25e-06 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 51.00 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 377 VGELCLWNGQYWAGYYGNPEETHKMRDHhNWFHTGDLGYVDDDGFIYIVERKKDML--KFQNIMYYpnEIESVISKMPDV 454
Cdd:PLN02479 402 MGEIVMRGNMVMKGYLKNPKANEEAFAN-GWFHSGDLGVKHPDGYIEIKDRSKDIIisGGENISSL--EVENVVYTHPAV 478
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 21356441 455 VEVCVFGVWNEINGDEATAAVVKKRGS-----ALTAQDIVDY 491
Cdd:PLN02479 479 LEASVVARPDERWGESPCAFVTLKPGVdksdeAALAEDIMKF 520
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
27-525 |
1.31e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 51.58 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 27 PHLSIGEIIFNEMRRHPQliAQISATENTILTRAELQANAMHIASYMRSLGLLQMDIVGIIARNTTHISAVAYACFFNGI 106
Cdd:PRK10252 456 PETTLSALVAQQAAKTPD--APALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGA 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 107 AFHSLNISYEQSTIEKLFSITRPNIIFcdgdefekvrSATAQLDvkiiTMRNHPSGSIRIDQVLSTPIEKnfQPVRLEQG 186
Cdd:PRK10252 534 AWLPLDTGYPDDRLKMMLEDARPSLLI----------TTADQLP----RFADVPDLTSLCYNAPLAPQGA--APLQLSQP 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 187 NDqTLAILCSSGTTGIPKAVTITNsRQILN------SSHSLTTNDV--QYSHSTLD---W------ITGllttvtsgvfs 249
Cdd:PRK10252 598 HH-TAYIIFTSGSTGRPKGVMVGQ-TAIVNrllwmqNHYPLTADDVvlQKTPCSFDvsvWeffwpfIAG----------- 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 250 TKRIIA--DNIFDPEFFMRLVEEHQITWIIQAPAHMAMMVNSPS--FTTSDLSSLRYYLFGGSRASVEtQHRIRSRLSKD 325
Cdd:PRK10252 665 AKLVMAepEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTpeGARQSCASLRQVFCSGEALPAD-LCREWQQLTGA 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 326 CLHFAYGFTElgsmAALNLHF---------DEKPNSV--GRLVAGLKLKVICEKGESLGPDEVGELCLWNGQYWAGYYGN 394
Cdd:PRK10252 744 PLHNLYGPTE----AAVDVSWypafgeelaAVRGSSVpiGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGR 819
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 395 PEETHK------MRDHHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEV----CVFGVWN 464
Cdd:PRK10252 820 PDLTASrfiadpFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthaCVINQAA 899
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356441 465 EINGDEA--TAAVVKKRGSALTAQDIVDYVET----HIDAKYkqlnggAIIVEDLVRSPNGKTNRMA 525
Cdd:PRK10252 900 ATGGDARqlVGYLVSQSGLPLDTSALQAQLRErlppHMVPVV------LLQLDQLPLSANGKLDRKA 960
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
347-445 |
3.25e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 49.73 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 347 DEKPNSVGRLVAGL----KLKVIC--EKGESLGPDEVGELCLWNGQYWAGYYGNPEET---------HKMRDHH------ 405
Cdd:PRK07769 382 ADAPNAVAQVSAGKvgvsEWAVIVdpETASELPDGQIGEIWLHGNNIGTGYWGKPEETaatfqnilkSRLSESHaegapd 461
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 21356441 406 --NWFHTGDLG-YVDDDgfIYIVERKKDMLKFQNIMYYPNEIE 445
Cdd:PRK07769 462 daLWVRTGDYGvYFDGE--LYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
191-490 |
6.61e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 48.95 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 191 LAILCSSGTTGIPKAVTITNSRQILN-----SSHSLTTNDVQYSHSTLDWITGLLTTVTSGVFSTKRIIADNIFDPEFFM 265
Cdd:PRK07868 608 LAFIAFSTAGGELVAKQITNYRWALSafgtaSAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 266 RLVEEHQITWIIQAPAHMAMMVNSPSFTTSDLSSLRyyLFGGSRASVETQHRIRSRLSK-DCLHFaYGFTElGSMAALNL 344
Cdd:PRK07868 688 QEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVR--LFIGSGMPTGLWERVVEAFAPaHVVEF-FATTD-GQAVLANV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 345 HFDeKPNSVGRLVAGL------------KLKVICEKG--ESLGPDEVGELClwngqywaGYYGNPEETHK--MRD----H 404
Cdd:PRK07868 764 SGA-KIGSKGRPLPGAgrvelaaydpehDLILEDDRGfvRRAEVNEVGVLL--------ARARGPIDPTAsvKRGvfapA 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 405 HNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVwnEINGDE-ATAAVVKKRGSAL 483
Cdd:PRK07868 835 DTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGV--EVGGRQlAVAAVTLRPGAAI 912
|
....*..
gi 21356441 484 TAQDIVD 490
Cdd:PRK07868 913 TAADLTE 919
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
196-454 |
9.61e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 48.22 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 196 SSGTTGIPKAVTIT-NSRQILNSSHS-------LTTND-VQ--YSHSTldWITGLL----------TTVTSGVFSTKRII 254
Cdd:COG1541 91 SSGTTGKPTVVGYTrKDLDRWAELFArslraagVRPGDrVQnaFGYGL--FTGGLGlhygaerlgaTVIPAGGGNTERQL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 255 adnifdpeffmRLVEEHQITWIIQAP---AHMAMMVNSPSFTTSDLSsLRYYLFGGSRASVETQHRIRSRLskDC-LHFA 330
Cdd:COG1541 169 -----------RLMQDFGPTVLVGTPsylLYLAEVAEEEGIDPRDLS-LKKGIFGGEPWSEEMRKEIEERW--GIkAYDI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 331 YGFTELGSMAAL------NLHFDEkpnsvgrlvaglkLKVICE-----KGESLGPDEVGEL---CLwngqywagyygNPE 396
Cdd:COG1541 235 YGLTEVGPGVAYeceaqdGLHIWE-------------DHFLVEiidpeTGEPVPEGEEGELvvtTL-----------TKE 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356441 397 ETHKMRdhhnwFHTGDLGYVDDD----G-----FIYIVERKKDMLKF--QNImyYPNEIESVISKMPDV 454
Cdd:COG1541 291 AMPLIR-----YRTGDLTRLLPEpcpcGrthprIGRILGRADDMLIIrgVNV--FPSQIEEVLLRIPEV 352
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
196-525 |
1.79e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 196 SSGTTGIPKAVTITNSRQILNSSHSLTTNDVQYSHSTLDWIT--------GLLTTVTSGVFSTKRiiADNIFDPEFFMRL 267
Cdd:PRK05691 2341 TSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSinfdaaseRLLVPLLCGARVVLR--AQGQWGAEEICQL 2418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 268 VEEHQITWIIQAPAHMAMMVNSPSfTTSDLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHFAYGFTE-----LGSMAAL 342
Cdd:PRK05691 2419 IREQQVSILGFTPSYGSQLAQWLA-GQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTEtvvmpLACLAPE 2497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 343 NLHFDEKPNSVGRLVaGLKLKVICEKGESLGPD-EVGELCLWNGQYWAGYYGNPEETHK-------MRDHHNWFHTGDLG 414
Cdd:PRK05691 2498 QLEEGAASVPIGRVV-GARVAYILDADLALVPQgATGELYVGGAGLAQGYHDRPGLTAErfvadpfAADGGRLYRTGDLV 2576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 415 YVDDDGFIYIVERKKDMLKFQNIMYYPNEIESVISKMPDVVEVCVFGVWNE-------------INGDEATAAVVKKRGS 481
Cdd:PRK05691 2577 RLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPsgkqlagylvsavAGQDDEAQAALREALK 2656
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 21356441 482 ALTAQDIVDY-VETHIdakykqlnggaIIVEDLVRSPNGKTNRMA 525
Cdd:PRK05691 2657 AHLKQQLPDYmVPAHL-----------ILLDSLPLTANGKLDRRA 2690
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
299-459 |
1.99e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 47.17 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 299 SLRYYLFGGSRASVE-----TQHRIRSRLSkdclhfaYGFTELGSM--AALNlhfDEKPNsVGRLVAGLKLKVICE---- 367
Cdd:PRK09029 241 SLKAVLLGGAAIPVElteqaEQQGIRCWCG-------YGLTEMASTvcAKRA---DGLAG-VGSPLPGREVKLVDGeiwl 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 368 KGESLGpdevgelclwngqywAGYYGNpEETHKMRDHHNWFHTGDLGYVDDdGFIYIVERKKDMlkF----QNImyYPNE 443
Cdd:PRK09029 310 RGASLA---------------LGYWRQ-GQLVPLVNDEGWFATRDRGEWQN-GELTILGRLDNL--FfsggEGI--QPEE 368
|
170
....*....|....*.
gi 21356441 444 IESVISKMPDVVEVCV 459
Cdd:PRK09029 369 IERVINQHPLVQQVFV 384
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
331-433 |
1.71e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 44.32 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 331 YGFTELGSMAALNLHFDEKPNSVGRLVA-GLKLKVIC-EKGESLGPDEVGELCLWNGQYWAGYYGNPEETHKMRDHHNWF 408
Cdd:PTZ00342 493 YGLTETTGPIFVQHADDNNTESIGGPISpNTKYKVRTwETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYF 572
|
90 100
....*....|....*....|....*
gi 21356441 409 HTGDLGYVDDDGFIYIVERKKDMLK 433
Cdd:PTZ00342 573 KTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
296-438 |
2.12e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 43.93 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356441 296 DLSSLRYYLFGGSRASVETQHRIRSRLSKDCLHfAYGFTELGSMAALNLHFDEKPNSVGRLVAGLKLKVICEKGESLGpd 375
Cdd:PRK08043 477 DFARLRYVVAGAEKLQESTKQLWQDKFGLRILE-GYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEQG-- 553
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356441 376 evGELCLWNGQYWAGYY--GNP--------EETHKMRDhHNWFHTGDLGYVDDDGFIYIVERKKDMLKFQNIM 438
Cdd:PRK08043 554 --GRLQLKGPNIMNGYLrvEKPgvlevptaENARGEME-RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEM 623
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
378-461 |
5.88e-04 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 42.44 E-value: 5.88e-04
10 20 30 40 50 60 70 80
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gi 21356441 378 GELCLWNGQYWAGYYGNPEETHKMRDHHNWFHTGD-LGYVDDDGFIYiVERKKDMLKFQNIMYYP-NEIESVISKMPDVV 455
Cdd:cd17632 436 GELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDvMAELGPDRLVY-VDRRNNVLKLSQGEFVTvARLEAVFAASPLVR 514
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....*.
gi 21356441 456 EVCVFG 461
Cdd:cd17632 515 QIFVYG 520
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