|
Name |
Accession |
Description |
Interval |
E-value |
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1-535 |
0e+00 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 1143.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 1 MRIPFTRWPDEFARRYREKGYWQDVPLTDILTRHADSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQL 80
Cdd:PRK10946 1 MSIPFTRWPEEFARRYREKGYWQDLPLTDILTRHAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 81 GNVPELYITFFALLKLGVAPVLALFSHQRTELNAYAMQIAPTLVIADRQHTLFAGEDFLNTFVAEHRSVRVVLLRNDDGD 160
Cdd:PRK10946 81 GNVAEFYITFFALLKLGVAPVNALFSHQRSELNAYASQIEPALLIADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDDGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 161 HSLDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSS 240
Cdd:PRK10946 161 HSLDDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYPMSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 241 PGALGVFLAKGTVVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARI 320
Cdd:PRK10946 241 PGALGVFLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 321 PAEIGCQLQQVFGMAEGLVNYTRLDDSPERIINTQGRPMCPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLH 400
Cdd:PRK10946 321 PAELGCQLQQVFGMAEGLVNYTRLDDSDERIFTTQGRPMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 401 NASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVV 480
Cdd:PRK10946 401 NASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 677652367 481 KEPLRAVQVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASRSP 535
Cdd:PRK10946 481 KEPLKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1-531 |
0e+00 |
|
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: 929.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 1 MRIPFTRWPDEFARRYREKGYWQDVPLTDILTRHAD--SDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALV 78
Cdd:COG1021 1 MLEGFTPWPEEFAARYREAGYWRGETLGDLLRRRAErhPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 79 QLGNVPELYITFFALLKLGVAPVLALFSHQRTELNAYAMQIAPTLVIADRQHTLFAGEDFLNTFVAEHRSVRVVLLRNDD 158
Cdd:COG1021 81 QLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGFDYRALARELQAEVPSLRHVLVVGDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 159 GD-HSLDAAMRQAAEDFTATPSPaDEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYA 237
Cdd:COG1021 161 GEfTSLDALLAAPADLSEPRPDP-DDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 238 MSSPGALGVFLAKGTVVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQAIqEWGGNApLASLRLLQVGGARLSATLA 317
Cdd:COG1021 240 LSSPGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAA-ERSRYD-LSSLRVLQVGGAKLSPELA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 318 ARIPAEIGCQLQQVFGMAEGLVNYTRLDDSPERIINTQGRPMCPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNS 397
Cdd:COG1021 318 RRVRPALGCTLQQVFGMAEGLVNYTRLDDPEEVILTTQGRPISPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 398 PLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAY 477
Cdd:COG1021 398 PEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAF 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 677652367 478 LVVK-EPLRAVQVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLA 531
Cdd:COG1021 478 VVPRgEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| DHB_AMP_lig |
TIGR02275 |
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme ... |
3-527 |
0e+00 |
|
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme family (pfam00501). Members activate 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate; many are involved in synthesis of siderophores such as enterobactin, vibriobactin, vulnibactin, etc. The most closely related proteine believed to differ in function activates salicylate rather than DHB. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 274063 [Multi-domain] Cd Length: 526 Bit Score: 909.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 3 IPFTRWPDEFARRYREKGYWQDVPLTDILTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQL 80
Cdd:TIGR02275 1 IEFTPWPEELAERYREKGYWQDKPLTDILRDQAARypDAIAIICGNRQWSYRELDQRADNLAAGLTKLGIKQGDTAVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 81 GNVPELYITFFALLKLGVAPVLALFSHQRTELNAYAMQIAPTLVIADRQHTLFAGEDFLNTFVAEHRSVRVVLLRNDDGD 160
Cdd:TIGR02275 81 PNIAEFYIVFFALLKLGVAPVLALFSHRKSELTAYASQIEPALYIIDRAHSLFDYDDFARQLQSKLPTLRNIIVAGQTGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 161 HSLDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSS 240
Cdd:TIGR02275 161 AELFLWLESPAEPVKFPPTKSDEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICWLTQQTRYLCALPAAHNYPLSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 241 PGALGVFLAKGTVVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQAIQEWggNAPLASLRLLQVGGARLSATLAARI 320
Cdd:TIGR02275 241 PGALGVFYAGGCVVLAPDPSPTDCFPLIERHKVTVTALVPPAVALWMQAASKS--RADLSSLKLLQVGGAKFSAAAARRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 321 PAEIGCQLQQVFGMAEGLVNYTRLDDSPERIINTQGRPMCPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLH 400
Cdd:TIGR02275 319 PAVFGCQLQQVFGMAEGLVNYTRLDDPAEIIFTTQGRPMSPDDEVRVVDDHGNPVAPGETGMLLTRGPYTFRGYYKAPEH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 401 NASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVV 480
Cdd:TIGR02275 399 NAAAFDAEGFYYTGDLVRLTPEGYIVVVGRAKDQINRGGEKIAAEEIENLLLAHPAVHDAALVSMPDELLGEKSCAFIVV 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 677652367 481 KEP-LRAVQVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:TIGR02275 479 RDPaLKAAQLRRFLRERGLAEYKLPDRVEFVDSLPLTAVGKVDKKALR 526
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
11-526 |
0e+00 |
|
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: 764.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 11 EFARRYREKGYWQDVPLTDILTRHA--DSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYI 88
Cdd:cd05920 1 EFARRYRAAGYWQDEPLGDLLARSAarHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 89 TFFALLKLGVAPVLALFSHQRTELNAYAMQIAPTLVIADRQHTLFageDFLNTFVAEHRSVRvvllrnddgdhsldaamr 168
Cdd:cd05920 81 LFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAGF---DHRALARELAESIP------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 169 qaaedftatpspadEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSPGALGVFL 248
Cdd:cd05920 140 --------------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACPGVLGTLL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 249 AKGTVVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQAiQEWGGnAPLASLRLLQVGGARLSATLAARIPAEIGCQL 328
Cdd:cd05920 206 AGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDA-AASRR-ADLSSLRLLQVGGARLSPALARRVPPVLGCTL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 329 QQVFGMAEGLVNYTRLDDSPERIINTQGRPMCPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDAN 408
Cdd:cd05920 284 QQVFGMAEGLLNYTRLDDPDEVIIHTQGRPMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 409 GFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE-PLRAV 487
Cdd:cd05920 364 GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDpPPSAA 443
|
490 500 510
....*....|....*....|....*....|....*....
gi 677652367 488 QVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd05920 444 QLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
27-534 |
1.19e-117 |
|
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: 354.89 E-value: 1.19e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLal 104
Cdd:COG0318 1 LADLLRRAAARhpDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 105 fshqrteLNayamqiaPTLVIADRQHtlfagedflntfVAEHRSVRVVLlrnddgdhsldaamrqaaedftatpspadeV 184
Cdd:COG0318 79 -------LN-------PRLTAEELAY------------ILEDSGARALV------------------------------T 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 185 AYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLATDPSATLC 264
Cdd:COG0318 103 ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTV-GLLAPLLAGATLVLLPRFDPERV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 265 FPLIEKHQINATALVPPAVSLWLQAIQEwgGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAE-GLVNYTR 343
Cdd:COG0318 182 LELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTEtSPVVTVN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 344 LDDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDG 423
Cdd:COG0318 260 PEDPGERRPGSVGRPL-PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 424 YITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLRAVQVRRFLREQgVAEF 501
Cdd:COG0318 338 YLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPgaELDAEELRAFLRER-LARY 416
|
490 500 510
....*....|....*....|....*....|...
gi 677652367 502 KLPDRVECVASLPLTPVGKVDKKQLRQRLASRS 534
Cdd:COG0318 417 KVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
183-522 |
2.29e-91 |
|
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: 283.02 E-value: 2.29e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 183 EVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSspGALGVFLAKGTVVLATDPSAT 262
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF--GLLGALLAGGTVVLLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 263 LCFPLIEKHQINATALVPPAVSLWLQAIQEWGgnAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAE--GLVN 340
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAG--YDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTEtgGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 341 YTRLDDSPERIiNTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPlHNASAFDANGFYCSGDLISID 420
Cdd:cd04433 157 TGPPDDDARKP-GSVGRPV-PGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNP-EATAAVDEDGWYRTGDLGRLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 421 QDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAV--QVRRFLREQgV 498
Cdd:cd04433 234 EDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDaeELRAHVRER-L 312
|
330 340
....*....|....*....|....
gi 677652367 499 AEFKLPDRVECVASLPLTPVGKVD 522
Cdd:cd04433 313 APYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
15-535 |
1.24e-89 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 285.41 E-value: 1.24e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 15 RYREKGYWQDVPLTDILTRHADS--DKTAVIE------GERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPEL 86
Cdd:PRK13295 14 ASIAAGHWHDRTINDDLDACVAScpDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 87 YITFFALLKLGVA--PVLALFSHQrtELnAYAMQIAPTLVIADRQHtlFAGEDF---LNTFVAEHRSVRVVLLRNDDGDH 161
Cdd:PRK13295 94 TVLYLACSRIGAVlnPLMPIFRER--EL-SFMLKHAESKVLVVPKT--FRGFDHaamARRLRPELPALRHVVVVGGDGAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 162 SLDAAM----RQAAEDFTAT-----PSPaDEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPA 232
Cdd:PRK13295 169 SFEALLitpaWEQEPDAPAIlarlrPGP-DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 233 AHN----YAMSSPGALGvflakGTVVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQAIQEWGgnAPLASLRLLQVG 308
Cdd:PRK13295 248 AHQtgfmYGLMMPVMLG-----ATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESG--RPVSSLRTFLCA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 309 GARLSATLAARIPAEIGCQLQQVFGMAE-GLVNYTRLDDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRG 387
Cdd:PRK13295 321 GAPIPGALVERARAALGAKIVSAWGMTEnGAVTLTKLDDPDERASTTDGCPL-PGVEVRVVDADGAPLPAGQIGRLQVRG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 388 PYTFRGYFNSPLHNASafDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMED 467
Cdd:PRK13295 400 CSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 468 ELLGEKSCAYLVVK--EPLRAVQVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASRSP 535
Cdd:PRK13295 478 ERLGERACAFVVPRpgQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGEDA 547
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
10-533 |
1.15e-88 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 283.18 E-value: 1.15e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 10 DEFARRYREKGYWQDVPLTDILTRHADS--DKTAVIEGERA-FSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPEL 86
Cdd:PRK06087 8 EQRRAAYRQQGYWGDASLADYWQQTARAmpDKIAVVDNHGAsYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 87 YITFFALLKLG--VAPVLALFSHqrTELnAYAMQ-------IAPTLViADRQHtlfagEDFLNTFVAEHRSVRVVLLRND 157
Cdd:PRK06087 88 TIIYLACLKVGavSVPLLPSWRE--AEL-VWVLNkcqakmfFAPTLF-KQTRP-----VDLILPLQNQLPQLQQIVGVDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 158 DGDHSLDAAMRQAAEDF----TATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAA 233
Cdd:PRK06087 159 LAPATSSLSLSQIIADYepltTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 234 HN----YAMSSPgalgvFLAKGTVVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQAIQEWGgnAPLASLRLLQVGG 309
Cdd:PRK06087 239 HAtgflHGVTAP-----FLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQP--ADLSALRFFLCGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 310 ARLSATLAaRIPAEIGCQLQQVFGMAEGLVN-YTRLDDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGP 388
Cdd:PRK06087 312 TTIPKKVA-RECQQRGIKLLSVYGSTESSPHaVVNLDDPLSRFMHTDGYAA-AGVEIKVVDEARKTLPPGCEGEEASRGP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 389 YTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDE 468
Cdd:PRK06087 390 NVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDE 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 677652367 469 LLGEKSCAYLVVKEP---LRAVQVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASR 533
Cdd:PRK06087 470 RLGERSCAYVVLKAPhhsLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRR 537
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
38-438 |
5.84e-85 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 269.18 E-value: 5.84e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGE-RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlALFSHQRTElnAYA 116
Cdd:pfam00501 10 DKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYV-PLNPRLPAE--ELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 117 MQIA---PTLVIADRQHTLFAGEDFLNTFVAEHRSVRVVLLRNDDGDHSLDAAMRQAAEDFTATPSPADEVAYFQLSGGT 193
Cdd:pfam00501 87 YILEdsgAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 194 TGTPKLIPRTHNDYYYSVRRSNEIC----GFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLA---TDPSATLCFP 266
Cdd:pfam00501 167 TGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSL-GLLGPLLAGATVVLPpgfPALDPAALLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 267 LIEKHQINATALVPPAVSLWLQAIQEWggNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAE--GLVNYTRL 344
Cdd:pfam00501 246 LIERYKVTVLYGVPTLLNMLLEAGAPK--RALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTEttGVVTTPLP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 345 DDSPERIINTQGRPMcPDDEVWVADAD-GNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDG 423
Cdd:pfam00501 324 LDEDLRSLGSVGRPL-PGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDG 402
|
410
....*....|....*
gi 677652367 424 YITVHGREKDQINRG 438
Cdd:pfam00501 403 YLEIVGRKKDQIKLG 417
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-528 |
5.58e-84 |
|
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: 267.32 E-value: 5.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 48 AFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG--VAPVLALFshqrtelnayamqiaptlvi 125
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGavTNPILPFF-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 126 adRQHTLfagedflnTFVAEHRSVRVVLLRNDDGDHsldaamrqaaeDFTATPspaDEVAYFQLSGGTTGTPKLIPRTHN 205
Cdd:cd05903 61 --REHEL--------AFILRRAKAKVFVVPERFRQF-----------DPAAMP---DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 206 DYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLATDPSATLCFPLIEKHQINATALVPPAVSL 285
Cdd:cd05903 117 TLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVY-GFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 286 WLQAIQEWGgnAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEGLVNYTRLDDSPE-RIINTQGRPMcPDDE 364
Cdd:cd05903 196 LLNAVEEAG--EPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEdRRLYTDGRPL-PGVE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 365 VWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPlHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAA 444
Cdd:cd05903 273 IKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRP-DLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 445 EEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEP--LRAVQVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVD 522
Cdd:cd05903 352 LEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGalLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQ 431
|
....*.
gi 677652367 523 KKQLRQ 528
Cdd:cd05903 432 KFRLRE 437
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
23-531 |
6.93e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 267.05 E-value: 6.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 23 QDVPLT--DILTRHAD--SDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGV 98
Cdd:PRK06187 2 QDYPLTigRILRHGARkhPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 99 apVLA-----LFSHQRtelnAYAMQIAptlviADRqhTLFAGEDFLNTF--VAEH-RSVRVVLLRNDDGD-------HSL 163
Cdd:PRK06187 82 --VLHpinirLKPEEI----AYILNDA-----EDR--VVLVDSEFVPLLaaILPQlPTVRTVIVEGDGPAaplapevGEY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 164 DAAMRQAAEDF-TATPSPADEVAYFQLSGgTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSPG 242
Cdd:PRK06187 149 EELLAAASDTFdFPDIDENDAAAMLYTSG-TTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 243 aLGVFL-AKGTVVLATDPSATLcfPLIEKHQINATALVPPAVSLWLQ---AIQEWggnapLASLRLLQVGGARLSATLAA 318
Cdd:PRK06187 228 -LALMAgAKQVIPRRFDPENLL--DLIETERVTFFFAVPTIWQMLLKaprAYFVD-----FSSLRLVIYGGAALPPALLR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 319 RIPAEIGCQLQQVFGMAE--GLVNYTRLDD---SPERIINTQGRPmCPDDEVWVADADGNPLPP--GEIGRLMTRGPYTF 391
Cdd:PRK06187 300 EFKEKFGIDLVQGYGMTEtsPVVSVLPPEDqlpGQWTKRRSAGRP-LPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 392 RGYFNSPLHNASAFDaNGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLG 471
Cdd:PRK06187 379 QGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWG 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 677652367 472 EKSCAYLVVKE--PLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLA 531
Cdd:PRK06187 458 ERPVAVVVLKPgaTLDAKELRAFLRGR-LAKFKLPKRIAFVDELPRTSVGKILKRVLREQYA 518
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
27-527 |
3.18e-82 |
|
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: 263.65 E-value: 3.18e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHADsdKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLalfs 106
Cdd:cd05936 5 LEEAARRFPD--KTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 107 hqrteLNayamqiaPTLVIADRQHTLfagedflntfvaEHRSVRVVLLrnddgDHSLDAAMRQAA-EDFTATPSPADeVA 185
Cdd:cd05936 79 -----LN-------PLYTPRELEHIL------------NDSGAKALIV-----AVSFTDLLAAGApLGERVALTPED-VA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 186 YFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFN--EDTRFLCAIPAAHNYAMSSPGALGVFLAkGTVVLATDPSATL 263
Cdd:cd05936 129 VLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLleGDDVVLAALPLFHVFGLTVALLLPLALG-ATIVLIPRFRPIG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 264 CFPLIEKHQINATALVPPAVSLWLQAiqEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEG--LVNY 341
Cdd:cd05936 208 VLKEIRKHRVTIFPGVPTMYIALLNA--PEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETspVVAV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 342 TRLDDspERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDaNGFYCSGDLISIDQ 421
Cdd:cd05936 286 NPLDG--PRKPGSIGIPL-PGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 422 DGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLRAVQVRRFLREQgVA 499
Cdd:cd05936 362 DGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEgaSLTEEEIIAFCREQ-LA 440
|
490 500
....*....|....*....|....*...
gi 677652367 500 EFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:cd05936 441 GYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
29-535 |
5.06e-79 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 258.12 E-value: 5.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 29 DILTRHADS--DKTAVI-EGE----RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG--VA 99
Cdd:COG0365 13 NCLDRHAEGrgDKVALIwEGEdgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGavHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 100 PVLALFSHQrtELNAYAMQIAPTLVIAD----RQHTLFAGEDFLNTFVAEHRSVRVVLLRND-------DGDHSLDAAMR 168
Cdd:COG0365 93 PVFPGFGAE--ALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDEALEELPSLEHVIVVGRtgadvpmEGDLDWDELLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 169 QAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNE-ICGFNEDTRFLCAipA------AHNYAMSSP 241
Cdd:COG0365 171 AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCT--AdigwatGHSYIVYGP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 242 GALGVflakgTVVL----ATDPSATLCFPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLA 317
Cdd:COG0365 249 LLNGA-----TVVLyegrPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 318 ARIPAEIGCQLQQVFGMAE---GLVNYTRLDD----SPeriintqGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYT 390
Cdd:COG0365 324 EWWYEAVGVPIVDGWGQTEtggIFISNLPGLPvkpgSM-------GKPV-PGYDVAVVDEDGNPVPPGEEGELVIKGPWP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 391 --FRGYFNSPLHNASAF--DANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSME 466
Cdd:COG0365 396 gmFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVP 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 677652367 467 DELLGEKSCAYLVVKEP------LRAvQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASRSP 535
Cdd:COG0365 476 DEIRGQVVKAFVVLKPGvepsdeLAK-ELQAHVREE-LGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPL 548
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
31-523 |
1.26e-75 |
|
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: 245.60 E-value: 1.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 31 LTRHA--DSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQ 108
Cdd:cd17631 1 LRRRArrHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 109 RTELNayamqiaptlviadrqhtlfagedflntFVAEHRSVRVVLlrnddgdhsldaamrqaaedftatpspaDEVAYFQ 188
Cdd:cd17631 81 PPEVA----------------------------YILADSGAKVLF----------------------------DDLALLM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 189 LSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSPGaLGVFLAKGTVVLATDPSATLCFPLI 268
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFT-LPTLLRGGTVVILRKFDPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 269 EKHQINATALVPPAVSLWLQAiQEWGGnAPLASLRLLQVGGARLSATLAARIpAEIGCQLQQVFGMAE--GLVNYTRLDD 346
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQH-PRFAT-TDLSSLRAVIYGGAPMPERLLRAL-QARGVKFVQGYGMTEtsPGVTFLSPED 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 347 SPERIiNTQGRPmCPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYIT 426
Cdd:cd17631 261 HRRKL-GSAGRP-VFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLY 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 427 VHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLRAVQVRRFLREQgVAEFKLP 504
Cdd:cd17631 338 IVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPgaELDEDELIAHCRER-LARYKIP 416
|
490
....*....|....*....
gi 677652367 505 DRVECVASLPLTPVGKVDK 523
Cdd:cd17631 417 KSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
35-528 |
7.39e-71 |
|
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: 234.90 E-value: 7.39e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 35 ADSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG--VAPVLALFshQRTEL 112
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGavVAPLNPAY--KKAEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 113 NAYAMQIAPTLVIADRQHTLFAGEdflntfVAEHRSVRVVLLRNDDGD-------HSLDAAMRQAAEDFTATPSPADEVA 185
Cdd:cd05926 79 EFYLADLGSKLVLTPKGELGPASR------AASKLGLAILELALDVGVlirapsaESLSNLLADKKNAKSEGVPLPDDLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 186 YFQLSGGTTGTPKLIPRTHNDYYYSVR---RSNEIcgfNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLATDPSAT 262
Cdd:cd05926 153 LILHTSGTTGRPKGVPLTHRNLAASATnitNTYKL---TPDDRTLVVMPLFHVHGLVA-SLLSTLAAGGSVVLPPRFSAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 263 LCFPLIEKHQINATALVPPAVSLWLQAIQEWGGNaPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEG--LVN 340
Cdd:cd05926 229 TFWPDVRDYNATWYTAVPTIHQILLNRPEPNPES-PPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAahQMT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 341 YTRLDDSPeRIINTQGRPMCPddEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISID 420
Cdd:cd05926 308 SNPLPPGP-RKPGSVGKPVGV--EVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 421 QDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAV--QVRRFLReQGV 498
Cdd:cd05926 385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTeeELRAFCR-KHL 463
|
490 500 510
....*....|....*....|....*....|
gi 677652367 499 AEFKLPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:cd05926 464 AAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
22-529 |
2.20e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 223.63 E-value: 2.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 22 WQDVPltDILTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG-- 97
Cdd:PRK07656 4 WMTLP--ELLARAARRfgDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGav 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 98 VAPVLALFShqrtelnayAMQIAPTLVIADRQhTLFAGEDFLNTFVAEHRSV----RVVLLRNDDGD------HSLDAAM 167
Cdd:PRK07656 82 VVPLNTRYT---------ADEAAYILARGDAK-ALFVLGLFLGVDYSATTRLpaleHVVICETEEDDphtekmKTFTDFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 168 RQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVF 247
Cdd:PRK07656 152 AAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKA-GVNAPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 248 LAKGTVVLAT--DPSATlcFPLIEKHQINATALVPPAVSLWLQAiqEWGGNAPLASLRLLQVGGARLSATLAARIPAEIG 325
Cdd:PRK07656 231 MRGATILPLPvfDPDEV--FRLIETERITVLPGPPTMYNSLLQH--PDRSAEDLSSLRLAVTGAASMPVALLERFESELG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 326 CQ-LQQVFGMAE--GLVNYTRLDDSPERIINTQGRPmCPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNA 402
Cdd:PRK07656 307 VDiVLTGYGLSEasGVTTFNRLDDDRKTVAGTIGTA-IAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 403 SAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE 482
Cdd:PRK07656 386 AAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKP 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 677652367 483 --PLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQR 529
Cdd:PRK07656 466 gaELTEEELIAYCREH-LAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
24-526 |
1.87e-62 |
|
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: 212.87 E-value: 1.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 24 DVPLTDILTRHADSDKTAVIEGE--RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG--VA 99
Cdd:cd05904 6 PLDSVSFLFASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGavVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 100 PVLALFShqRTELNAYAMQIAPTLVIADRQHTlfagedflnTFVAEHrSVRVVLLRNDDgDHSLDAAMRQAAEDFTATPS 179
Cdd:cd05904 86 TANPLST--PAEIAKQVKDSGAKLAFTTAELA---------EKLASL-ALPVVLLDSAE-FDSLSFSDLLFEADEAEPPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 180 P---ADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVR--RSNEICGFNEDTRFLCAIPAAHNYAMSSPgALGVFLAKGTVV 254
Cdd:cd05904 153 VvikQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAqfVAGEGSNSDSEDVFLCVLPMFHIYGLSSF-ALGLLRLGATVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 255 LATDPSATLCFPLIEKHQINATALVPP-AVSLWLQAIqewGGNAPLASLRLLQVGGARLSATL----AARIPaeiGCQLQ 329
Cdd:cd05904 232 VMPRFDLEELLAAIERYKVTHLPVVPPiVLALVKSPI---VDKYDLSSLRQIMSGAAPLGKELieafRAKFP---NVDLG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 330 QVFGMAE--GLVNYTRLDDSPERIINTQGRPMcPDDEVWVADAD-GNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFD 406
Cdd:cd05904 306 QGYGMTEstGVVAMCFAPEKDRAKYGSVGRLV-PNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 407 ANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYlVVKEP--- 483
Cdd:cd05904 385 KEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAF-VVRKPgss 463
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 677652367 484 LRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd05904 464 LTEDEIMDFVAKQ-VAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
27-536 |
5.52e-62 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 213.10 E-value: 5.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHADSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFS 106
Cdd:PRK12583 24 FDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 107 HQRTELnAYAMQIAP--TLVIADRqhtlFAGEDFLNTFVA-----------EHRSVR------VVLLRNDDGDHSL---- 163
Cdd:PRK12583 104 YRASEL-EYALGQSGvrWVICADA----FKTSDYHAMLQEllpglaegqpgALACERlpelrgVVSLAPAPPPGFLawhe 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 164 -----DAAMRQAAEDFTATPSPADEVAyFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAM 238
Cdd:PRK12583 179 lqargETVSREALAERQASLDRDDPIN-IQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 239 SSpGALGVFLAKGTVVL---ATDPSATLcfPLIEKHQinATAL--VPPAVSLWLQAIQEwgGNAPLASLRLLQVGGARLS 313
Cdd:PRK12583 258 VL-ANLGCMTVGACLVYpneAFDPLATL--QAVEEER--CTALygVPTMFIAELDHPQR--GNFDLSSLRTGIMAGAPCP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 314 ATLAARIPAEIGC-QLQQVFGMAEG--LVNYTRLDDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYT 390
Cdd:PRK12583 331 IEVMRRVMDEMHMaEVQIAYGMTETspVSLQTTAADDLERRVETVGRTQ-PHLEVKVVDPDGATVPRGEIGELCTRGYSV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 391 FRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELL 470
Cdd:PRK12583 410 MKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 677652367 471 GEKSCAYLVVK--EPLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASRSPL 536
Cdd:PRK12583 490 GEEIVAWVRLHpgHAASEEELREFCKAR-IAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEELAL 556
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
46-527 |
2.34e-59 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 202.52 E-value: 2.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 46 ERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlalfshqrtELNAYAMqiaptlvi 125
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLV---------PINTALR-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 126 adrqhtlfagEDFLNTFVAEHRSVRVVllrnddgdhsldaamrqaaedftatpspADEVAYFQLSGgTTGTPKLIPRTHN 205
Cdd:cd05934 64 ----------GDELAYIIDHSGAQLVV----------------------------VDPASILYTSG-TTGPPKGVVITHA 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 206 DYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLATDPSATLCFPLIEKHQINATALVPPAVSL 285
Cdd:cd05934 105 NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAV-SVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 286 WLQAiqewggnAPLAS-----LRLlqVGGARLSATLAARIPAEIGCQLQQVFGMAEGLVNYTRLDDSPeRIINTQGRPMc 360
Cdd:cd05934 184 LLAQ-------PPSPDdrahrLRA--AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEP-RRPGSIGRPA- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 361 PDDEVWVADADGNPLPPGEIGRLMTR---GPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINR 437
Cdd:cd05934 253 PGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRR 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 438 GGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVK--EPLRAVQVRRFLREQgVAEFKLPDRVECVASLPL 515
Cdd:cd05934 332 RGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRpgETLDPEELFAFCEGQ-LAYFKVPRYIRFVDDLPK 410
|
490
....*....|..
gi 677652367 516 TPVGKVDKKQLR 527
Cdd:cd05934 411 TPTEKVAKAQLR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
47-521 |
2.01e-58 |
|
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: 201.67 E-value: 2.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 47 RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvAPVLALfSHQRT--ELnAYAMQIA-PTL 123
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAG-GIFSAA-NPIYTadEL-AHQLKISkPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 124 VIADRQHTlfagEDFLNTFVAEHRSVRVVLLRN-----DDGDHSLDAAMRQAAEDFTATP-SPADEVAYFQLSGGTTGTP 197
Cdd:cd05911 86 IFTDPDGL----EKVKEAAKELGPKDKIIVLDDkpdgvLSIEDLLSPTLGEEDEDLPPPLkDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 198 KLIPRTHNDY---YYSVRRSNEICGFNEDtRFLCAIPAAHNYAMSSpgALGVFLAKGTVVLATDPSATLCFPLIEKHQIN 274
Cdd:cd05911 162 KGVCLSHRNLianLSQVQTFLYGNDGSND-VILGFLPLYHIYGLFT--TLASLLNGATVIIMPKFDSELFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 275 ATALVPPAVsLWLQaiqewggNAP------LASLRLLQVGGARLSATLAARIPAEIG-CQLQQVFGMAE--GLVNYTRL- 344
Cdd:cd05911 239 FLYLVPPIA-AALA-------KSPlldkydLSSLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTEtgGILTVNPDg 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 345 DDSPERIintqGRPMcPDDEVWVADADGNP-LPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDG 423
Cdd:cd05911 311 DDKPGSV----GRLL-PNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 424 YITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYlVVKEP---LRAVQVRRFLREQgVAE 500
Cdd:cd05911 386 YLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAY-VVRKPgekLTEKEVKDYVAKK-VAS 463
|
490 500
....*....|....*....|..
gi 677652367 501 FK-LPDRVECVASLPLTPVGKV 521
Cdd:cd05911 464 YKqLRGGVVFVDEIPKSASGKI 485
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
27-533 |
7.41e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 192.95 E-value: 7.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHA--DSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLAL 104
Cdd:PRK07470 9 LAHFLRQAArrFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 105 FSHQRTELNAYAMQIAPTLVIADRqhtlfageDFlntfvAEH-RSVR--------VVLLRNDDGDHSLDAAMrqaAEDFT 175
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMICHA--------DF-----PEHaAAVRaaspdlthVVAIGGARAGLDYEALV---ARHLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 176 ATPSPA----DEVAYFQLSGGTTGTPKLIPRTHNDYYYSVrrSNEIC----GFNEDTRFLCAIPAAHnyamsspGAlGVF 247
Cdd:PRK07470 153 ARVANAavdhDDPCWFFFTSGTTGRPKAAVLTHGQMAFVI--TNHLAdlmpGTTEQDASLVVAPLSH-------GA-GIH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 248 ----LAKG--TVVLATDP-SATLCFPLIEKHQINATALVPPAVSLWLQaiQEWGGNAPLASLRLLQVGGARLSATLAARI 320
Cdd:PRK07470 223 qlcqVARGaaTVLLPSERfDPAEVWALVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSLRYVIYAGAPMYRADQKRA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 321 PAEIGCQLQQVFGMAEGLVNYTRL-------DDSPERIINTQGRP---McpddEVWVADADGNPLPPGEIGRLMTRGPYT 390
Cdd:PRK07470 301 LAKLGKVLVQYFGLGEVTGNITVLppalhdaEDGPDARIGTCGFErtgM----EVQIQDDEGRELPPGETGEICVIGPAV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 391 FRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELL 470
Cdd:PRK07470 377 FAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVW 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 677652367 471 GEKSCAYLVVKE--PLRAVQVRRFLrEQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASR 533
Cdd:PRK07470 456 GEVGVAVCVARDgaPVDEAELLAWL-DGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEER 519
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
50-526 |
4.76e-53 |
|
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: 186.12 E-value: 4.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 50 SYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVapVLALFSHQRT--ELNAYAMQIAPTLVIAD 127
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGA--EIAMLNTRLTenERTNQLEDLDVQLLLTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 128 rqhTLFAGEDFLNTFVAEhrsvrvvLLRNDDGDHSLDAAMrqaaedftatpsPADEVAYFQLSGGTTGTPKLIPRTHNDY 207
Cdd:TIGR01923 79 ---SLLEEKDFQADSLDR-------IEAAGRYETSLSASF------------NMDQIATLMFTSGTTGKPKAVPHTFRNH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 208 YYSVRRSNEICGFNEDTRFLCAIPAAHnyaMSSPGALGVFLAKGTVVLATDPSATLcFPLIEKHQINATALVPPAVSLWL 287
Cdd:TIGR01923 137 YASAVGSKENLGFTEDDNWLLSLPLYH---ISGLSILFRWLIEGATLRIVDKFNQL-LEMIANERVTHISLVPTQLNRLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 288 QAiqewgGNAPLaSLRLLQVGGARLSATLAaRIPAEIGCQLQQVFGMAEGLVNYT--RLDDSPERIINtqGRPMcPDDEV 365
Cdd:TIGR01923 213 DE-----GGHNE-NLRKILLGGSAIPAPLI-EEAQQYGLPIYLSYGMTETCSQVTtaTPEMLHARPDV--GRPL-AGREI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 366 WVADADgnplpPGEIGRLMTRGPYTFRGYF-NSPLhnASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAA 444
Cdd:TIGR01923 283 KIKVDN-----KEGHGEIMVKGANLMKGYLyQGEL--TPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 445 EEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKK 524
Cdd:TIGR01923 356 EEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEK-LAKYKVPIAFEKLDELPYNASGKILRN 434
|
..
gi 677652367 525 QL 526
Cdd:TIGR01923 435 QL 436
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
38-528 |
6.33e-53 |
|
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: 185.96 E-value: 6.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQG-IKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELnAYa 116
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL-EY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 117 mqiaptlVIADRQHTLFagedflntfvaehrsvrvvllrnddgdhsLDAAMrqaaedftatpspadeVAYfqlSGGTTGT 196
Cdd:cd05941 79 -------VITDSEPSLV-----------------------------LDPAL----------------ILY---TSGTTGR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 197 PKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLATDPSATLCFPLIEKHQINAT 276
Cdd:cd05941 104 PKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVN-ALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 277 ALVPPAVSLWLQAIQ------EWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEGLVNYT-RLDDspE 349
Cdd:cd05941 183 MGVPTIYTRLLQYYEahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSnPLDG--E 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 350 RIINTQGRPMcPDDEVWVADADGN-PLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVH 428
Cdd:cd05941 261 RRPGTVGMPL-PGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 429 GREK-DQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAV---QVRRFLREQgVAEFKLP 504
Cdd:cd05941 340 GRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALsleELKEWAKQR-LAPYKRP 418
|
490 500
....*....|....*....|....
gi 677652367 505 DRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:cd05941 419 RRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
50-533 |
1.29e-51 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 186.31 E-value: 1.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 50 SYRQL----NQAAdNLacsLRRQGIKPGETALVQLGNVPELYITFFALLKLG-VAPVLALFS-HQRTEL--NAYA---MQ 118
Cdd:PRK07529 60 TYAELladvTRTA-NL---LHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGiANPINPLLEpEQIAELlrAAGAkvlVT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 119 IAPTL----------VIADRQHTLFAGEDFLNTFVAEHRSVRVVLLRND--DGDHSLDAAM-RQAAED-FTATPSPADEV 184
Cdd:PRK07529 136 LGPFPgtdiwqkvaeVLAALPELRTVVEVDLARYLPGPKRLAVPLIRRKahARILDFDAELaRQPGDRlFSGRPIGPDDV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 185 A-YFQlSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAH-NYAMssPGALGVFLAKGTVVLAT----- 257
Cdd:PRK07529 216 AaYFH-TGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHvNALL--VTGLAPLARGAHVVLATpqgyr 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 258 DPSATLCF-PLIEKHQINATALVPPAVSLWLQAIQewgGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAE 336
Cdd:PRK07529 293 GPGVIANFwKIVERYRINFLSGVPTVYAALLQVPV---DGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 337 G----LVNYTrldDSPERIiNTQGRPMcPDDEVWVA--DADGN---PLPPGEIGRLMTRGPYTFRGYFNsPLHNASAFDA 407
Cdd:PRK07529 370 AtcvsSVNPP---DGERRI-GSVGLRL-PYQRVRVVilDDAGRylrDCAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 408 NGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLR 485
Cdd:PRK07529 444 DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPgaSAT 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 677652367 486 AVQVRRFLREQgVAE-FKLPDRVECVASLPLTPVGKVDKKQLRQRLASR 533
Cdd:PRK07529 524 EAELLAFARDH-IAErAAVPKHVRILDALPKTAVGKIFKPALRRDAIRR 571
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
31-529 |
3.48e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 182.88 E-value: 3.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 31 LTRHADsdKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlALfsHQRT 110
Cdd:PRK06188 22 LKRYPD--RPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRT-AL--HPLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 111 ELNAYAMQIA----PTLVIADRQHTLFAGEdflntFVAEHRSVRVVLlRNDDGDHSLDAAmrQAAEDFTATP----SPAD 182
Cdd:PRK06188 97 SLDDHAYVLEdagiSTLIVDPAPFVERALA-----LLARVPSLKHVL-TLGPVPDGVDLL--AAAAKFGPAPlvaaALPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 183 EVAYFQLSGGTTGTPKLIPRTHNdyyySVRRSNEIC----GFNEDTRFLCAIPAAHnyamsspgALGVF----LAKG-TV 253
Cdd:PRK06188 169 DIAGLAYTGGTTGKPKGVMGTHR----SIATMAQIQlaewEWPADPRFLMCTPLSH--------AGGAFflptLLRGgTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 254 VLAT--DPSATLcfPLIEKHQINATALVP---------PAVSlwlqaiqewggNAPLASLRLLQVGGARLSATLAARIPA 322
Cdd:PRK06188 237 IVLAkfDPAEVL--RAIEEQRITATFLVPtmiyalldhPDLR-----------TRDLSSLETVYYGASPMSPVRLAEAIE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 323 EIGCQLQQVFGMAEGLVNYTRL------DDSPERIiNTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFN 396
Cdd:PRK06188 304 RFGPIFAQYYGQTEAPMVITYLrkrdhdPDDPKRL-TSCGRPT-PGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 397 SPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCA 476
Cdd:PRK06188 382 RPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTA 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 677652367 477 YLVVK--EPLRAVQVRRFLRE-QGVAEfkLPDRVECVASLPLTPVGKVDKKQLRQR 529
Cdd:PRK06188 461 VVVLRpgAAVDAAELQAHVKErKGSVH--APKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
182-527 |
3.57e-51 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 178.63 E-value: 3.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 182 DEVAYFQLSGGTTGTPKLIPRTH----NDYYYSVRRSneicGFNEDTRFLCAIPAAHNYAMsspgALGVF--LAKG-TVV 254
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHhnivNNGYFIGERL----GLTEQDRLCIPVPLFHCFGS----VLGVLacLTHGaTMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 255 LAT---DPSATLcfPLIEKHQinATAL--VPPAVslwlqaIQEWG----GNAPLASLRLLQVGGARLSATLAARIPAEIG 325
Cdd:cd05917 74 FPSpsfDPLAVL--EAIEKEK--CTALhgVPTMF------IAELEhpdfDKFDLSSLRTGIMAGAPCPPELMKRVIEVMN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 326 C-QLQQVFGMAEG--LVNYTRLDDSPERIINTQGRPMcPDDEVWVADADGNPLPP-GEIGRLMTRGPYTFRGYFNSPLHN 401
Cdd:cd05917 144 MkDVTIAYGMTETspVSTQTRTDDSIEKRVNTVGRIM-PHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 402 ASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVK 481
Cdd:cd05917 223 AEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLK 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 677652367 482 E--PLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:cd05917 303 EgaELTEEDIKAYCKGK-IAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
23-529 |
1.19e-50 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 182.32 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 23 QDVPLT---------DILTRHADSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFAL 93
Cdd:PRK08315 9 TDVPLLeqtigqlldRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 94 LKLGVAPVLALFSHQRTELnAYAMQIA--PTLVIADRqhtlFAGEDF---LNTFVAE--------HRSVRVVLLRN---- 156
Cdd:PRK08315 89 AKIGAILVTINPAYRLSEL-EYALNQSgcKALIAADG----FKDSDYvamLYELAPElatcepgqLQSARLPELRRvifl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 157 ---------------DDGDHSLDAAMRQAAEDFTAtpspaDEVAYFQLSGGTTGTPKLIPRTH----NDYYYSVRRsnei 217
Cdd:PRK08315 164 gdekhpgmlnfdellALGRAVDDAELAARQATLDP-----DDPINIQYTSGTTGFPKGATLTHrnilNNGYFIGEA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 218 CGFNEDTRFLCAIPAAHNYAMSspgaLGVF--LAKG-TVVL---ATDPSATLcfPLIEKHQinATAL--VPPAVslwlqa 289
Cdd:PRK08315 235 MKLTEEDRLCIPVPLYHCFGMV----LGNLacVTHGaTMVYpgeGFDPLATL--AAVEEER--CTALygVPTMF------ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 290 IQEWggNAP------LASLRLLQVGGARLSATLAARIPAEIGC-QLQQVFGMAEG--LVNYTRLDDSPERIINTQGRPMc 360
Cdd:PRK08315 301 IAEL--DHPdfarfdLSSLRTGIMAGSPCPIEVMKRVIDKMHMsEVTIAYGMTETspVSTQTRTDDPLEKRVTTVGRAL- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 361 PDDEVWVADAD-GNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGG 439
Cdd:PRK08315 378 PHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 440 EKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTP 517
Cdd:PRK08315 458 ENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPgaTLTEEDVRDFCRGK-IAHYKIPRYIRFVDEFPMTV 536
|
570
....*....|..
gi 677652367 518 VGKVDKKQLRQR 529
Cdd:PRK08315 537 TGKIQKFKMREM 548
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
27-532 |
1.72e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 181.28 E-value: 1.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHA--DSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLAL 104
Cdd:PRK08316 13 IGDILRRSArrYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 105 FSHQRTELnAYAM-QIAPTLVIADrqhTLFAGEdfLNTFVAEHRSVRVVLLR------NDDGDHSLDAaMRQAAEDFTAT 177
Cdd:PRK08316 93 FMLTGEEL-AYILdHSGARAFLVD---PALAPT--AEAALALLPVDTLILSLvlggreAPGGWLDFAD-WAEAGSVAEPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 178 PSPADE-VAYFQLSGGTTGTPKLIPRTHN----DYYYSVRRsneiCGFNEDTRFLCAIPAAHNYAMSspgalgVFL---- 248
Cdd:PRK08316 166 VELADDdLAQILYTSGTESLPKGAMLTHRaliaEYVSCIVA----GDMSADDIPLHALPLYHCAQLD------VFLgpyl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 249 -AKGTVVLATDPSATLCFPLIEKHQInaTAL-VPPAVslwlqaiqeWGG--NAP------LASLRLLQVGGARLSAT--- 315
Cdd:PRK08316 236 yVGATNVILDAPDPELILRTIEAERI--TSFfAPPTV---------WISllRHPdfdtrdLSSLRKGYYGASIMPVEvlk 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 316 -LAARIPaeiGCQLQQVFGMAE--GLVNYTRLDDSPERIiNTQGRPmCPDDEVWVADADGNPLPPGEIGRLMTRGPYTFR 392
Cdd:PRK08316 305 eLRERLP---GLRFYNCYGQTEiaPLATVLGPEEHLRRP-GSAGRP-VLNVETRVVDDDGNDVAPGEVGEIVHRSPQLML 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 393 GYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGE 472
Cdd:PRK08316 380 GYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIE 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 677652367 473 KSCAYLVVK--EPLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLAS 532
Cdd:PRK08316 459 AVTAVVVPKagATVTEDELIAHCRAR-LAGFKVPKRVIFVDELPRNPSGKILKRELRERYAG 519
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
25-527 |
2.41e-50 |
|
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: 179.80 E-value: 2.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 25 VPLTDI--LTRHAD--SDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFallklGVAP 100
Cdd:cd12118 2 VPLTPLsfLERAAAvyPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHF-----GVPM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 101 VLALFSHQRTELNA--YAMQIA---PTLVIADRQhtlFAGEDFLNTfvaehrsvrvvllrnddGDhsldaamrqaaEDFT 175
Cdd:cd12118 77 AGAVLNALNTRLDAeeIAFILRhseAKVLFVDRE---FEYEDLLAE-----------------GD-----------PDFE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 176 ATPsPADE-----VAYfqlSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHnyAMSSPGALGVFLAK 250
Cdd:cd12118 126 WIP-PADEwdpiaLNY---TSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFH--CNGWCFPWTVAAVG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 251 GTVVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPlASLRLLqVGGARLSATLAARIpAEIGCQLQQ 330
Cdd:cd12118 200 GTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLP-HRVHVM-TAGAPPPAAVLAKM-EELGFDVTH 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 331 VFGMAE--GLV-------NYTRLDDSPE-RIINTQGRPMCPDDEVWVADADGN-PLP-PGE-IGRLMTRGPYTFRGYFNS 397
Cdd:cd12118 277 VYGLTEtyGPAtvcawkpEWDELPTEERaRLKARQGVRYVGLEEVDVLDPETMkPVPrDGKtIGEIVFRGNIVMKGYLKN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 398 PLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAY 477
Cdd:cd12118 357 PEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAF 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 677652367 478 LVVKE--PLRAVQVRRFLREQgVAEFKLPDRVEcVASLPLTPVGKVDKKQLR 527
Cdd:cd12118 436 VELKEgaKVTEEEIIAFCREH-LAGFMVPKTVV-FGELPKTSTGKIQKFVLR 485
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
38-530 |
1.60e-49 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 177.46 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVapvLALFSHQRTELNAYAM 117
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA---VAVLLNTRLSREELLW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAP---TLVIADrqhtlfagedflNTFVAEHRSVRVVLLrnddgdhslDAAMRQAAEDFT-ATPSPADEVAYFQLSGGT 193
Cdd:PRK03640 94 QLDDaevKCLITD------------DDFEAKLIPGISVKF---------AELMNGPKEEAEiQEEFDLDEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 194 TGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSspgalgvFLAKG-----TVVLATDPSATLCFPLI 268
Cdd:PRK03640 153 TGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLS-------ILMRSviygmRVVLVEKFDAEKINKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 269 EKHQINATALVPPAVSLWLQAIQEwgGNAPlASLRLLQVGG-----ARLSATLAARIPaeigcqLQQVFGMAEGLVNYTR 343
Cdd:PRK03640 226 QTGGVTIISVVSTMLQRLLERLGE--GTYP-SSFRCMLLGGgpapkPLLEQCKEKGIP------VYQSYGMTETASQIVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 344 LDdsPERIIN---TQGRPMCPDdEVWVADaDGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDaNGFYCSGDLISID 420
Cdd:PRK03640 297 LS--PEDALTklgSAGKPLFPC-ELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 421 QDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVRRFLREQgVAE 500
Cdd:PRK03640 372 EEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEK-LAK 450
|
490 500 510
....*....|....*....|....*....|
gi 677652367 501 FKLPDRVECVASLPLTPVGKVDKKQLRQRL 530
Cdd:PRK03640 451 YKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
39-527 |
1.60e-49 |
|
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: 176.50 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 39 KTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLAlfshqrtelnayamq 118
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVI--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 119 iaptlviadrqHTLFAGEDFLntFVAEHRSVRVVLLRNDDgdhsldaamrqaaedftatpspadeVAYFQLSGGTTGTPK 198
Cdd:cd05919 66 -----------NPLLHPDDYA--YIARDCEARLVVTSADD-------------------------IAYLLYSSGTTGPPK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 199 LIPRTHNDYYYSVRR-SNEICGFNEDTRFLCAIPAAHNYAMSSPGALGVFLAKGTVVLATDPSATLCFPLIEKHQINATA 277
Cdd:cd05919 108 GVMHAHRDPLLFADAmAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLY 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 278 LVPpavSLWLQAI-QEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEglVNYTRLDDSPERI-INTQ 355
Cdd:cd05919 188 GVP---TFYANLLdSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATE--VGHIFLSNRPGAWrLGST 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 356 GRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQI 435
Cdd:cd05919 263 GRPV-PGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDML 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 436 NRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLR-----AVQVRRFLREQgVAEFKLPDRVECV 510
Cdd:cd05919 341 KVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAApqeslARDIHRHLLER-LSAHKVPRRIAFV 419
|
490
....*....|....*..
gi 677652367 511 ASLPLTPVGKVDKKQLR 527
Cdd:cd05919 420 DELPRTATGKLQRFKLR 436
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
50-528 |
3.62e-49 |
|
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: 174.84 E-value: 3.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 50 SYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlalfshqrtelnayamqiaptlviadrq 129
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAV---------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 130 htlfagedFLNTFVAEHRsvrvvllrnddgdhsLDAAMRQAAEDFtatpspaDEVAYFQLSGGTTGTPKLIPRTHNDYYY 209
Cdd:cd05912 55 --------LLNTRLTPNE---------------LAFQLKDSDVKL-------DDIATIMYTSGTTGKPKGVQQTFGNHWW 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 210 SVRRSNEICGFNEDTRFLCAIPAAHNYAMSspgalgvFLAKG-----TVVLATDPSATLCFPLIEKHQINATALVPPAvs 284
Cdd:cd05912 105 SAIGSALNLGLTEDDNWLCALPLFHISGLS-------ILMRSviygmTVYLVDKFDAEQVLHLINSGKVTIISVVPTM-- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 285 lwLQAIQEWGGNAPLASLRLLQVGGARLSATLAArIPAEIGCQLQQVFGMAEGLVNYTRL--DDSPERIiNTQGRPMcPD 362
Cdd:cd05912 176 --LQRLLEILGEGYPNNLRCILLGGGPAPKPLLE-QCKEKGIPVYQSYGMTETCSQIVTLspEDALNKI-GSAGKPL-FP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 363 DEVWVADADGNPLPPGEIgrlMTRGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKI 442
Cdd:cd05912 251 VELKIEDDGQPPYEVGEI---LLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENI 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 443 AAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVD 522
Cdd:cd05912 327 YPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEK-LAKYKVPKKIYFVDELPRTASGKLL 405
|
....*.
gi 677652367 523 KKQLRQ 528
Cdd:cd05912 406 RHELKQ 411
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
38-526 |
5.65e-49 |
|
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: 175.02 E-value: 5.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPV-LALfSHQRTELNAYA 116
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVpLDP-SYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 117 MQIAPTLVIADrqhtlfagedflntfvaehrsvrvvllrnddgdhsldaamrqaaedftatpspADEVAYFQLSGGTTGT 196
Cdd:cd05930 81 EDSGAKLVLTD-----------------------------------------------------PDDLAYVIYTSGSTGK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 197 PKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCaiPAAHNYAMSSPGALGVFLAKGTVVLA-----TDPSATLcfPLIEKH 271
Cdd:cd05930 108 PKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQ--FTSFSFDVSVWEIFGALLAGATLVVLpeevrKDPEALA--DLLAEE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 272 QINATALVPPAVSLWLQAiqewGGNAPLASLRLLQVGGARLSATLAARI-PAEIGCQLQQVFGMAEGLVNYTRLDDSPER 350
Cdd:cd05930 184 GITVLHLTPSLLRLLLQE----LELAALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVDATYYRVPPDD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 351 IINTQ---GRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------YCSGDLISIDQ 421
Cdd:cd05930 260 EEDGRvpiGRPI-PNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFgpgermYRTGDLVRWLP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 422 DGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLRAVQVRRFLREQgVA 499
Cdd:cd05930 339 DGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAER-LP 417
|
490 500
....*....|....*....|....*..
gi 677652367 500 EFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd05930 418 DYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
180-533 |
1.36e-48 |
|
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: 171.89 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 180 PADEVAYFQlSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAmSSPGALGVFLAKGTVVLAT-- 257
Cdd:cd05944 1 SDDVAAYFH-TGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLTPLASGAHVVLAGpa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 258 ---DPSATLCF-PLIEKHQINATALVPPAVSLWLQAiqewGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFG 333
Cdd:cd05944 79 gyrNPGLFDNFwKLVERYRITSLSTVPTVYAALLQV----PVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 334 MAEGLVNYTRLDDSPERIINTQGRPMcPDDEVWVA--DADGN---PLPPGEIGRLMTRGPYTFRGYFNSpLHNASAFDAN 408
Cdd:cd05944 155 LTEATCLVAVNPPDGPKRPGSVGLRL-PYARVRIKvlDGVGRllrDCAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 409 GFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYL-------VVK 481
Cdd:cd05944 233 GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqlkpgavVEE 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 677652367 482 EPLRAvQVRRFLREQGVaefkLPDRVECVASLPLTPVGKVDKKQLRQRLASR 533
Cdd:cd05944 313 EELLA-WARDHVPERAA----VPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
37-527 |
6.54e-48 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 174.10 E-value: 6.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 37 SDKTAVI----EGE-RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG--VAPVLALFSHQR 109
Cdd:PRK08008 21 GHKTALIfessGGVvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGaiMVPINARLLREE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 110 TelnAYAMQ--IAPTLVIADRQHTLFAGEDFLNTFVAEHRSVRVVLLRNDDGDHSLDAAM-RQAAEDFTATPSPADEVAY 186
Cdd:PRK08008 101 S---AWILQnsQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKaQQPATLCYAPPLSTDDTAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 187 FQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAH-----NYAMSspgalgVFLAKGTVVLATDPSA 261
Cdd:PRK08008 178 ILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHidcqcTAAMA------AFSAGATFVLLEKYSA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 262 TLCFPLIEKHQINATALVPPAV-SLWLQAIQEWGGNAPLAS-LRLLQVGGARLSATLAaripaEIGCQLQQVFGMAEGLV 339
Cdd:PRK08008 252 RAFWGQVCKYRATITECIPMMIrTLMVQPPSANDRQHCLREvMFYLNLSDQEKDAFEE-----RFGVRLLTSYGMTETIV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 340 NYtrLDDSP--ERIINTQGRP-MCPddEVWVADADGNPLPPGEIGRLMTRG---PYTFRGYFNSPLHNASAFDANGFYCS 413
Cdd:PRK08008 327 GI--IGDRPgdKRRWPSIGRPgFCY--EAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 414 GDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRaVQVRRFL 493
Cdd:PRK08008 403 GDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGET-LSEEEFF 481
|
490 500 510
....*....|....*....|....*....|....*.
gi 677652367 494 R--EQGVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:PRK08008 482 AfcEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
38-526 |
8.21e-48 |
|
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: 172.48 E-value: 8.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVA--PVLALFSHQRteLNAY 115
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAyvPLDPDYPADR--LRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 116 AMQIAPTLVIADRqhtlfAGEDFLntfvaeHRSVRVVLLRNDDGDHSLDAAmrqaaedfTATPSPADeVAYFQLSGGTTG 195
Cdd:cd12116 80 LEDAEPALVLTDD-----ALPDRL------PAGLPVLLLALAAAAAAPAAP--------RTPVSPDD-LAYVIYTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 196 TPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAhnYAMSSPGALGVFLAKGTVVLAT-----DPSATLcfPLIEK 270
Cdd:cd12116 140 RPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYA--FDISLLELLLPLLAGARVVIAPretqrDPEALA--RLIEA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 271 HQIN---ATalvpPAvsLW-LQAIQEWGGnapLASLRLLqVGGARLSATLAARIPAEIGCqLQQVFGMAEGLV--NYTRL 344
Cdd:cd12116 216 HSITvmqAT----PA--TWrMLLDAGWQG---RAGLTAL-CGGEALPPDLAARLLSRVGS-LWNLYGPTETTIwsTAARV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 345 DDSPERIinTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF-------YCSGDLI 417
Cdd:cd12116 285 TAAAGPI--PIGRPL-ANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFagpgsrlYRTGDLV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 418 SIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGeKSCAYLVVKE--PLRAVQVRRFLRE 495
Cdd:cd12116 362 RRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDR-RLVAYVVLKAgaAPDAAALRAHLRA 440
|
490 500 510
....*....|....*....|....*....|.
gi 677652367 496 QgVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd12116 441 T-LPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
44-528 |
1.69e-47 |
|
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: 172.82 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 44 EGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVapVL-----ALFSHQRtelnAYAMQ 118
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGA--VLhtinpRLFPEQI----AYIIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 119 IAptlviADRqhTLFAGEDFL---NTFVAEHRSVRVVLLRNDDGDHSLDAAMRQAA-EDFTATPSP------ADE----- 183
Cdd:cd12119 95 HA-----EDR--VVFVDRDFLpllEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAyEELLAAESPeydwpdFDEntaaa 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 184 VAYfqlSGGTTGTPKLIPRTHndyyysvrRSNeicgfnedtrFLcaipaaHNYAMSSPGALGvfLAKGTVVLATDP---- 259
Cdd:cd12119 168 ICY---TSGTTGNPKGVVYSH--------RSL----------VL------HAMAALLTDGLG--LSESDVVLPVVPmfhv 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 260 -------SATLC-----FP-----------LIEKHQINATALVPpavSLWLQAIQEWGGNAP-LASLRLLQVGGARLSAT 315
Cdd:cd12119 219 nawglpyAAAMVgaklvLPgpyldpaslaeLIEREGVTFAAGVP---TVWQGLLDHLEANGRdLSSLRRVVIGGSAVPRS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 316 LAARIpAEIGCQLQQVFGMAE----GLVNYTR---LDDSPERIIN---TQGRPMcPDDEVWVADADGNPLP--PGEIGRL 383
Cdd:cd12119 296 LIEAF-EERGVRVIHAWGMTEtsplGTVARPPsehSNLSEDEQLAlraKQGRPV-PGVELRIVDDDGRELPwdGKAVGEL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 384 MTRGPYTFRGYFNSPlHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALV 463
Cdd:cd12119 374 QVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVI 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 677652367 464 SMEDELLGEKSCAYLVVKEPLRAVQ--VRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:cd12119 453 GVPHPKWGERPLAVVVLKEGATVTAeeLLEFLADK-VAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
31-536 |
2.63e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 172.65 E-value: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 31 LTRHA--DSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQ 108
Cdd:PRK07786 23 LARHAlmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 109 RTELnAYamqiaptlVIADRQHTLFAGEDFLNTFVAEHR-------SVRVVLLRNDDGDHSLDAAMRQAAEDFTATPSPA 181
Cdd:PRK07786 103 PPEI-AF--------LVSDCGAHVVVTEAALAPVATAVRdivpllsTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 182 DEVAYFQLSGGTTGTPKLIPRTHNDYY---YSVRRSNEIcGFNEDTRFlCAIPAAHNYAMSSPGAlGVFLAKGTVVL--- 255
Cdd:PRK07786 174 DSPALIMYTSGTTGRPKGAVLTHANLTgqaMTCLRTNGA-DINSDVGF-VGVPLFHIAGIGSMLP-GLLLGAPTVIYplg 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 256 ATDPSATLcfPLIEKHQINATALVPpavSLWlQAIQEWGGNAPLA-SLRLLQVGGARLSATLAARIPAEI-GCQLQQVFG 333
Cdd:PRK07786 251 AFDPGQLL--DVLEAEKVTGIFLVP---AQW-QAVCAEQQARPRDlALRVLSWGAAPASDTLLRQMAATFpEAQILAAFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 334 MAE-GLVNYTRLDDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFdANGFYC 412
Cdd:PRK07786 325 QTEmSPVTCMLLGEDAIRKLGSVGKVI-PTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFH 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 413 SGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVR-- 490
Cdd:PRK07786 403 SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEdl 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 677652367 491 -RFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASRSPL 536
Cdd:PRK07786 483 aEFLTDR-LARYKHPKALEIVDALPRNPAGKVLKTELRERYGACVNV 528
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
49-527 |
2.62e-46 |
|
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: 167.51 E-value: 2.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 49 FSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvAPVLALFshqrtelnayamqiaptlviadr 128
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLG-AVYVPLT----------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 129 qhTLFAGEDFLNTFvaEHRSVRVVLlrnddgdhsldaamrqaaedftatpSPADEVAYFQLSGGTTGTPKLIPRTHNDYY 208
Cdd:cd05972 57 --TLLGPKDIEYRL--EAAGAKAIV-------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 209 YSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSPGaLGVFLAKGTVVLATDP--SATLCFPLIEKHQINATALVPPAVSLW 286
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSF-FGPWLLGATVFVYEGPrfDAERILELLERYGVTSFCGPPTAYRML 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 287 LQAIQEWGGnapLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAE-GLV--NYTRLDDSPERIintqGRPMcPDD 363
Cdd:cd05972 187 IKQDLSSYK---FSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTEtGLTvgNFPDMPVKPGSM----GRPT-PGY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 364 EVWVADADGNPLPPGEIG----RLMTRGPytFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGG 439
Cdd:cd05972 259 DVAIIDDDGRELPPGEEGdiaiKLPPPGL--FLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 440 EKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVK---EPLR--AVQVRRFLREQgVAEFKLPDRVECVASLP 514
Cdd:cd05972 336 YRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTsgyEPSEelAEELQGHVKKV-LAPYKYPREIEFVEELP 414
|
490
....*....|...
gi 677652367 515 LTPVGKVDKKQLR 527
Cdd:cd05972 415 KTISGKIRRVELR 427
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
50-526 |
6.52e-46 |
|
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: 166.50 E-value: 6.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 50 SYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlalfshqrtelnayamQIAPTLViadrq 129
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVV----------------PINPMLK----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 130 htlfagEDFLNTFVAEHRSVRVVLLrnddgdhsldaamrqaaedftatpSPADEVAYFQLSGGTTGTPKLIPRTHNDYYY 209
Cdd:cd05935 62 ------ERELEYILNDSGAKVAVVG------------------------SELDDLALIPYTSGTTGLPKGCMHTHFSAAA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 210 SVrrSNEICGFN---EDTrFLCAIPAAHNYAMSSPGALGVFlAKGTVVLATDPSATLCFPLIEKHQINATALVPPAVSLW 286
Cdd:cd05935 112 NA--LQSAVWTGltpSDV-ILACLPLFHVTGFVGSLNTAVY-VGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 287 LQA--IQEWGgnapLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEGLVNYTRldDSPERI-INTQGRPMCPDD 363
Cdd:cd05935 188 LATpeFKTRD----LSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHT--NPPLRPkLQCLGIP*FGVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 364 EVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAF---DANGFYCSGDLISIDQDGYITVHGREKDQINRGGE 440
Cdd:cd05935 262 ARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFieiKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 441 KIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAV----QVRRFLREQgVAEFKLPDRVECVASLPLT 516
Cdd:cd05935 342 KVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKvteeDIIEWAREQ-MAAYKYPREVEFVDELPRS 420
|
490
....*....|
gi 677652367 517 PVGKVDKKQL 526
Cdd:cd05935 421 ASGKILWRLL 430
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
24-527 |
1.43e-45 |
|
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: 167.16 E-value: 1.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 24 DVPLTDILTRHADSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLa 103
Cdd:cd05959 5 AATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVP- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 104 lfshqrteLNayamqiapTLVIAD---------RQHTLFAGEDFLNTF-----VAEHRSVRVVLL---RNDDGDHSLDAA 166
Cdd:cd05959 84 --------VN--------TLLTPDdyayyledsRARVVVVSGELAPVLaaaltKSEHTLVVLIVSggaGPEAGALLLAEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 167 MRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRR-SNEICGFNEDTRFLCAIPAAHNY----AMSSP 241
Cdd:cd05959 148 VAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELyARNVLGIREDDVCFSAAKLFFAYglgnSLTFP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 242 GALGvflakGTVVL-ATDPSATLCFPLIEKHQINATALVPpavSLW--LQAIQEWGGNAPLaSLRLLQVGGARLSATLAA 318
Cdd:cd05959 228 LSVG-----ATTVLmPERPTPAAVFKRIRRYRPTVFFGVP---TLYaaMLAAPNLPSRDLS-SLRLCVSAGEALPAEVGE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 319 RIPAEIGCQLQQVFGMAEGLVNYtrLDDSPERI-INTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNS 397
Cdd:cd05959 299 RWKARFGLDILDGIGSTEMLHIF--LSNRPGRVrYGTTGKPV-PGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 398 PLHNASAFDAnGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAY 477
Cdd:cd05959 376 RDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAF 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 677652367 478 LVVKEPLRAVQV-RRFLRE---QGVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:cd05959 455 VVLRPGYEDSEAlEEELKEfvkDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
28-526 |
3.40e-45 |
|
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: 165.91 E-value: 3.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 28 TDILTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVApVLALF 105
Cdd:cd17646 1 HALVAEQAARtpDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAA-YLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 106 SHQRTELNAYamqiaptlVIAD-RQHTLFAGEDFLNTFVAEHrsVRVVLLRNDDGDHSldaamrqaAEDFTATPSPADeV 184
Cdd:cd17646 80 PGYPADRLAY--------MLADaGPAVVLTTADLAARLPAGG--DVALLGDEALAAPP--------ATPPLVPPRPDN-L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 185 AYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpgALGVFLAKGTVVLA-----TDP 259
Cdd:cd17646 141 AYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWE--LFWPLVAGARLVVArpgghRDP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 260 SATLcfPLIEKHQINATALVPpavSLwLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEGLV 339
Cdd:cd17646 219 AYLA--ALIREHGVTTCHFVP---SM-LRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 340 NYT--RLDDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------Y 411
Cdd:cd17646 293 DVThwPVRGPAETPSVPIGRPV-PNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 412 CSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVV---KEPLRAVQ 488
Cdd:cd17646 372 RTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPaagAAGPDTAA 451
|
490 500 510
....*....|....*....|....*....|....*...
gi 677652367 489 VRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd17646 452 LRAHLAER-LPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
38-526 |
4.71e-45 |
|
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: 165.45 E-value: 4.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELNAYAM 117
Cdd:cd12117 12 DAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPTLVIADRQHTLFAGEDflntfvaehrSVRVVLLRNDDgdhsldaamrQAAEDFTATPSPADEVAYFQLSGGTTGTP 197
Cdd:cd12117 92 DAGAKVLLTDRSLAGRAGGL----------EVAVVIDEALD----------AGPAGNPAVPVSPDDLAYVMYTSGSTGRP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 198 KLIPRTHNDYYYSVRRSNEIcGFNEDTRFLCAIPAAHNYAMSSP-GALgvfLAKGTVVLAtdPSATLCFP-----LIEKH 271
Cdd:cd12117 152 KGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIwGAL---LNGARLVLA--PKGTLLDPdalgaLIAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 272 QINATALVPPAVSLWLQAIQEWggnapLASLRLLQVGGARLSATLAARIPAEI-GCQLQQVFGMAEGLVNYT-----RLD 345
Cdd:cd12117 226 GVTVLWLTAALFNQLADEDPEC-----FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTTFTTshvvtELD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 346 DSPERI-IntqGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------YCSGDLIS 418
Cdd:cd12117 301 EVAGSIpI---GRPI-ANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLAR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 419 IDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVRRFLREQgV 498
Cdd:cd12117 377 WLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRER-L 455
|
490 500
....*....|....*....|....*...
gi 677652367 499 AEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd12117 456 PAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
26-532 |
7.83e-45 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 165.05 E-value: 7.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 26 PLTDIL-TRHADSDKTAV-IEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvapvlA 103
Cdd:PRK07514 4 NLFDALrAAFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAG-----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 104 LF-----SHQRTELnAYAMQIA-PTLVIADRqhtlfAGEDFLNTfVAEHRSVRVVLLRNDDGDHSLDAAMRQAAEDFTAT 177
Cdd:PRK07514 79 VFlplntAYTLAEL-DYFIGDAePALVVCDP-----ANFAWLSK-IAAAAGAPHVETLDADGTGSLLEAAAAAPDDFETV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 178 PSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYamsspgalGVFLAKGTVVLAT 257
Cdd:PRK07514 152 PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTH--------GLFVATNVALLAG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 258 dpSATLCFPLIEKHQI-----NATAL--VPpavSLWLQAIQEWGGNAPLAS-LRLLQVGGARLSATLAARIPAEIGCQLQ 329
Cdd:PRK07514 224 --ASMIFLPKFDPDAVlalmpRATVMmgVP---TFYTRLLQEPRLTREAAAhMRLFISGSAPLLAETHREFQERTGHAIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 330 QVFGMAEGLVNYTRLDDSpERIINTQGRPMcPDDEVWVADAD-GNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDAN 408
Cdd:PRK07514 299 ERYGMTETNMNTSNPYDG-ERRAGTVGFPL-PGVSLRVTDPEtGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRAD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 409 GFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAyLVVKEP---LR 485
Cdd:PRK07514 377 GFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTA-VVVPKPgaaLD 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 677652367 486 AVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLAS 532
Cdd:PRK07514 456 EAAILAALKGR-LARFKQPKRVFFVDELPRNTMGKVQKNLLREQYAD 501
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
39-527 |
1.16e-44 |
|
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: 163.42 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 39 KTAVIEGERAFSYRQLNQAADNLACSLRRQ-GIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELNAYAM 117
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPTLVIADRQHTlfagedflntfvaehrsvrvvllrnddgdhsldaamrqaaedftatpsPADEVAYFQLSGGTTGTP 197
Cdd:cd05958 81 KARITVALCAHALT------------------------------------------------ASDDICILAFTSGTTGAP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 198 KLIPRTHNDYYYSVRR-SNEICGFNEDTRFLCAIPAAHNYA-------MSSPGALGVFLAKGTvvlatdpsATLCFPLIE 269
Cdd:cd05958 113 KATMHFHRDPLASADRyAVNVLRLREDDRFVGSPPLAFTFGlggvllfPFGVGASGVLLEEAT--------PDLLLSAIA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 270 KHQINATALVPPAVSLWLQAIQEWGGNapLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEGLVNYtrLDDSPE 349
Cdd:cd05958 185 RYKPTVLFTAPTAYRAMLAHPDAAGPD--LSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIF--ISARPG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 350 RI-INTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSplHNASAFDaNGFYCSGDLISIDQDGYITVH 428
Cdd:cd05958 261 DArPGATGKPV-PGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRYLADK--RQRTYVQ-GGWNITGDTYSRDPDGYFRHQ 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 429 GREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVK-----EPLRAVQVRRFLREQgVAEFKL 503
Cdd:cd05958 337 GRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpgvipGPVLARELQDHAKAH-IAPYKY 415
|
490 500
....*....|....*....|....
gi 677652367 504 PDRVECVASLPLTPVGKVDKKQLR 527
Cdd:cd05958 416 PRAIEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
37-526 |
4.60e-44 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 162.88 E-value: 4.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 37 SDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVA--PVLALFSHQRTElna 114
Cdd:cd17655 11 PDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAylPIDPDYPEERIQ--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 115 YAMQIAPTLVIADrQHTLFAGEDFLNTfvaehrsvrVVLLRNDDGDHsldaamrQAAEDFtATPSPADEVAYFQLSGGTT 194
Cdd:cd17655 88 YILEDSGADILLT-QSHLQPPIAFIGL---------IDLLDEDTIYH-------EESENL-EPVSKSDDLAYVIYTSGST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 195 GTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFlcAIPAAHNYAMSSPGALGVFLAKGTVVL---ATDPSATLCFPLIEKH 271
Cdd:cd17655 150 GKPKGVMIEHRGVVNLVEWANKVIYQGEHLRV--ALFASISFDASVTEIFASLLSGNTLYIvrkETVLDGQALTQYIRQN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 272 QINATALvPPAVslwLQAIQEWGGNAPLaSLRLLQVGGARLSATLAARIPAEIG--CQLQQVFGMAEGLV-----NYTRL 344
Cdd:cd17655 228 RITIIDL-TPAH---LKLLDAADDSEGL-SLKHLIVGGEALSTELAKKIIELFGtnPTITNAYGPTETTVdasiyQYEPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 345 DDSPERI-IntqGRPMCpDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------YCSGDLI 417
Cdd:cd17655 303 TDQQVSVpI---GKPLG-NTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 418 SIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVRRFLREQg 497
Cdd:cd17655 379 RWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARE- 457
|
490 500
....*....|....*....|....*....
gi 677652367 498 VAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd17655 458 LPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
183-530 |
5.20e-44 |
|
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: 158.65 E-value: 5.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 183 EVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAH--NYAMsspgALGVFLAKGTVVLATdps 260
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHvgGLAI----LVRSLLAGAELVLLE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 261 atLCFPLIEKHQINA---TALVPPAvsLWlQAIQEWGGNAPLASLRLLQVGGARLSATLAARIpAEIGCQLQQVFGMAE- 336
Cdd:cd17630 74 --RNQALAEDLAPPGvthVSLVPTQ--LQ-RLLDSGQGPAALKSLRAVLLGGAPIPPELLERA-ADRGIPLYTTYGMTEt 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 337 -GLVNYTRLDDSPERiinTQGRPMcPDDEVWVADAdgnplppgeiGRLMTRGPYTFRGYFNSPLHNAsaFDANGFYCSGD 415
Cdd:cd17630 148 aSQVATKRPDGFGRG---GVGVLL-PGRELRIVED----------GEIWVGGASLAMGYLRGQLVPE--FNEDGWFTTKD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 416 LISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVRRFLRE 495
Cdd:cd17630 212 LGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELRAWLKD 291
|
330 340 350
....*....|....*....|....*....|....*
gi 677652367 496 QgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRL 530
Cdd:cd17630 292 K-LARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
50-461 |
6.45e-44 |
|
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: 160.51 E-value: 6.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 50 SYRQLNQAADNLACSLR-RQGIKPGETALVQLGNVPELYITFFALLKLGVApVLALFSHQRTE-LNAYAMQIAPTLVIAD 127
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAA-YVPLDPAYPAErLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 128 RQHtlfagedflntfvaEHRSVRVVLLRNDDGDHSLDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDY 207
Cdd:TIGR01733 80 SAL--------------ASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 208 YYSVRRSNEICGFNEDTRFLCAipAAHNYAMSSPGALGVFLAKGTVVLATD----PSATLCFPLIEKHQINATALVPPAV 283
Cdd:TIGR01733 146 VNLLAWLARRYGLDPDDRVLQF--ASLSFDASVEEIFGALLAGATLVVPPEdeerDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 284 SLWLQAIQEwggnaPLASLRLLQVGGARLSATLAARIPAEIG-CQLQQVFGMAEGLVN--YTRLDDSPERIINTQ--GRP 358
Cdd:TIGR01733 224 ALLAAALPP-----ALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWstATLVDPDDAPRESPVpiGRP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 359 McPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF--------YCSGDLISIDQDGYITVHGR 430
Cdd:TIGR01733 299 L-ANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlYRTGDLVRYLPDGNLEFLGR 377
|
410 420 430
....*....|....*....|....*....|.
gi 677652367 431 EKDQINRGGEKIAAEEIENLLLRHPVVIHAA 461
Cdd:TIGR01733 378 IDDQVKIRGYRIELGEIEAALLRHPGVREAV 408
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
183-523 |
1.18e-43 |
|
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: 157.66 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 183 EVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVV--LATDPS 260
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKA-GIVACLLTGATVVpvAVFDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 261 ATLcfPLIEKHQInatALVPPAVSLWLQAIQEWGG-NAPLASLRLLQVGGARLSATLAARIPAEIGCQ-LQQVFGMAE-G 337
Cdd:cd17638 80 AIL--EAIERERI---TVLPGPPTLFQSLLDHPGRkKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEaG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 338 LVNYTRLDDSPERIINTQGRPmCPDDEVWVADadgnplpPGEIgrlMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLI 417
Cdd:cd17638 155 VATMCRPGDDAETVATTCGRA-CPGFEVRIAD-------DGEV---LVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 418 SIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEP--LRAVQVRRFLRE 495
Cdd:cd17638 224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGvtLTEEDVIAWCRE 303
|
330 340
....*....|....*....|....*...
gi 677652367 496 QgVAEFKLPDRVECVASLPLTPVGKVDK 523
Cdd:cd17638 304 R-LANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
38-522 |
1.80e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 161.98 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELnAYAM 117
Cdd:PRK07798 18 DRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDEL-RYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIA-PTLVIADRQhtlFAGEdflntfVAEHR----SVRVVLLRNDDGDHSL--------DAAMRQAAEDFTATPSPADev 184
Cdd:PRK07798 97 DDSdAVALVYERE---FAPR------VAEVLprlpKLRTLVVVEDGSGNDLlpgavdyeDALAAGSPERDFGERSPDD-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 185 AYFQLSGGTTGTPKLIPRTHNDYYYS-------------------VRRSNEicgfNEDTRFLCAIPAAHNYAMSSpgALG 245
Cdd:PRK07798 166 LYLLYTGGTTGMPKGVMWRQEDIFRVllggrdfatgepiedeeelAKRAAA----GPGMRRFPAPPLMHGAGQWA--AFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 246 VFLAKGTVVLATDPS--ATLCFPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAe 323
Cdd:PRK07798 240 ALFSGQTVVLLPDVRfdADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLSSLFAIASGGALFSPSVKEALLE- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 324 igcQLQQV-----FGMAEGLVNYTRLddSPERIINTQGRPMCPDDEVWVADADGNPLPPG--EIGRLmTRGPYTFRGYFN 396
Cdd:PRK07798 319 ---LLPNVvltdsIGSSETGFGGSGT--VAKGAVHTGGPRFTIGPRTVVLDEDGNPVEPGsgEIGWI-ARRGHIPLGYYK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 397 SPLHNASAF-DANG--FYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEK 473
Cdd:PRK07798 393 DPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQE 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 677652367 474 SCAYLVVKEPLRA--VQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVD 522
Cdd:PRK07798 473 VVAVVQLREGARPdlAELRAHCRSS-LAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
3-527 |
2.23e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 162.02 E-value: 2.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 3 IPFTRwPDEFAR------RYREKGywqdvpltdILTRHA---DSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPG 73
Cdd:PRK07788 30 VDLER-PDNGLRlaadirRYGPFA---------GLVAHAarrAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 74 ETALVQLGNVPELYITFFALLKLGVAPVLalfshqrteLNA--YAMQIAPtlVIA-DRQHTLFAGEDFLNTFVAEHRSV- 149
Cdd:PRK07788 100 DGVAVLARNHRGFVLALYAAGKVGARIIL---------LNTgfSGPQLAE--VAArEGVKALVYDDEFTDLLSALPPDLg 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 150 RV-VLLRNDDGDHSLDAAMRQ-----AAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRthndyyysvrrsNEICGFNED 223
Cdd:PRK07788 169 RLrAWGGNPDDDEPSGSTDETlddliAGSSTAPLPKPPKPGGIVILTSGTTGTPKGAPR------------PEPSPLAPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 224 TRFLCAIPAAHN--YAMSSP-------GALGVFLAKG-TVVLAT--DPSATLcfPLIEKHQINATALVPPAVSLWLQAIQ 291
Cdd:PRK07788 237 AGLLSRVPFRAGetTLLPAPmfhatgwAHLTLAMALGsTVVLRRrfDPEATL--EDIAKHKATALVVVPVMLSRILDLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 292 EWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEglVNYTRLDDSPERIIN--TQGRPmCPDDEVWVAD 369
Cdd:PRK07788 315 EVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTE--VAFATIATPEDLAEApgTVGRP-PKGVTVKILD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 370 ADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNAsafdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIEN 449
Cdd:PRK07788 392 ENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVED 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 450 LLLRHPVVIHAALVSMEDELLGEKSCAYlVVKEPLRAV---QVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:PRK07788 468 LLAGHPDVVEAAVIGVDDEEFGQRLRAF-VVKAPGAALdedAIKDYVRDN-LARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
.
gi 677652367 527 R 527
Cdd:PRK07788 546 R 546
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
149-527 |
1.07e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 158.37 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 149 VRVVLLRNDDGDHSLDA-AMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFL 227
Cdd:cd05922 83 LRDALPASPDPGTVLDAdGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRAL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 228 CAIPAAHNYAMSSpgALGVFLAKGTVVLATD--PSATLcFPLIEKHQINATALVPPAVSLWLQAIQEwggNAPLASLRLL 305
Cdd:cd05922 163 TVLPLSYDYGLSV--LNTHLLRGATLVLTNDgvLDDAF-WEDLREHGATGLAGVPSTYAMLTRLGFD---PAKLPSLRYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 306 -QVGGARLSATLAARIPAEIGCQLQQVFGMAEGLVNYTRLDdsPERIIN---TQGRPMcPDDEVWVADADGNPLPPGEIG 381
Cdd:cd05922 237 tQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLP--PERILEkpgSIGLAI-PGGEFEILDDDGTPTPPGEPG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 382 RLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAA 461
Cdd:cd05922 314 EIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAA 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 677652367 462 LVSMEDElLGEKSCAYLVVKEPLRAVQVRRFLREQGvAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:cd05922 394 AVGLPDP-LGEKLALFVTAPDKIDPKDVLRSLAERL-PPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
110-527 |
1.14e-42 |
|
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: 158.69 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 110 TELNAYAMQIAPTLVIAD-RQHTLFAGEDFLNTFVAEH-RSVRVVLLRNDDGDHSLDAAMrQAAEDFTATPSPADEVAY- 186
Cdd:cd05929 50 INSILTVFAAAAAWKCGAcPAYKSSRAPRAEACAIIEIkAAALVCGLFTGGGALDGLEDY-EAAEGGSPETPIEDEAAGw 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 187 -FQLSGGTTGTPKLIPRTH------NDyyySVRRSNEICGFNEDTRFLCAIPAAHNyAMSSPGALGVFLAkGTVVLAT-- 257
Cdd:cd05929 129 kMLYSGGTTGRPKGIKRGLpggppdND---TLMAAALGFGPGADSVYLSPAPLYHA-APFRWSMTALFMG-GTLVLMEkf 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 258 DPSATLcfPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEG 337
Cdd:cd05929 204 DPEEFL--RLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 338 lVNYTrlddsperIINTQ---------GRPMcpDDEVWVADADGNPLPPGEIGRLMTRGPYTFRgYFNSPLHNASAFDAN 408
Cdd:cd05929 282 -QGLT--------IINGEewlthpgsvGRAV--LGKVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 409 GFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAY-----LVVKEP 483
Cdd:cd05929 350 GWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVvqpapGADAGT 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 677652367 484 LRAVQVRRFLReQGVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:cd05929 430 ALAEELIAFLR-DRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
27-529 |
5.21e-42 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 158.00 E-value: 5.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlal 104
Cdd:PRK06155 23 LPAMLARQAERypDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 105 fshqrtELNAYAM--QIAPTLviADRQHTLFAGE----DFLNTFVAEHRSVRVVLLRNDDGDHSLDAAMR-----QAAED 173
Cdd:PRK06155 100 ------PINTALRgpQLEHIL--RNSGARLLVVEaallAALEAADPGDLPLPAVWLLDAPASVSVPAGWStaplpPLDAP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 174 FT-ATPSPADEVAYFQLSgGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpgALGVFLAKGT 252
Cdd:PRK06155 172 APaAAVQPGDTAAILYTS-GTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNA--FFQALLAGAT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 253 VVLATDPSATLCFPLIEKHQINATALVPPAVSLWLqaiqewgGNAPLASLRllqvgGARLSATLAARIPAEIGCQLQQVF 332
Cdd:PRK06155 249 YVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILL-------SQPARESDR-----AHRVRVALGPGVPAALHAAFRERF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 333 GMA--EGL----VNYTRLDDSPERIINTQGRpMCPDDEVWVADADGNPLPPGEIGRLMTRG--PYTF-RGYFNSPLHNAS 403
Cdd:PRK06155 317 GVDllDGYgsteTNFVIAVTHGSQRPGSMGR-LAPGFEARVVDEHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 404 AFDaNGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE- 482
Cdd:PRK06155 396 AWR-NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDg 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 677652367 483 -PLRAVQVRRFLrEQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQR 529
Cdd:PRK06155 475 tALEPVALVRHC-EPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
49-529 |
1.07e-41 |
|
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: 155.35 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 49 FSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvAPVLALFShqrtelnayamQIAPTlVIADR 128
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIG-AVICPLFS-----------AFGPE-AIRDR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 129 qhtlfagedflntfvAEHRSVRVVLlrnddgdhsldaamrqAAEDFTATPSPADEvAYFQLSGGTTGTPKLIPRTHNDYY 208
Cdd:cd05969 68 ---------------LENSEAKVLI----------------TTEELYERTDPEDP-TLLHYTSGTTGTPKGVLHVHDAMI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 209 YSVRRSNEICGFNEDTRFLC-AIPA---AHNYAMSSPGALGVflakGTVVLATDPSATLCFPLIEKHQINATALVPPAVS 284
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCtADPGwvtGTVYGIWAPWLNGV----TNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 285 LWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEG----LVNYTRLDDSPeriiNTQGRPMc 360
Cdd:cd05969 192 MLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgsimIANYPCMPIKP----GSMGKPL- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 361 PDDEVWVADADGNPLPPGEIGRLMTRG--PYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRG 438
Cdd:cd05969 267 PGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 439 GEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRA-----VQVRRFLReQGVAEFKLPDRVECVASL 513
Cdd:cd05969 346 GHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPsdelkEEIINFVR-QKLGAHVAPREIEFVDNL 424
|
490
....*....|....*.
gi 677652367 514 PLTPVGKVDKKQLRQR 529
Cdd:cd05969 425 PKTRSGKIMRRVLKAK 440
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
27-533 |
1.38e-41 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 156.59 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHADSDKTA---VIEGER-AFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVA--- 99
Cdd:PRK05852 18 IADLVEVAATRLPEApalVVTADRiAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVvvp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 100 --PVLALfSHQRTELNAYAMQIaptlVIADRqhtLFAGEDFLNTFVAEHRSVRVvllrndDGDHSLDAAMRQAAEDFTAT 177
Cdd:PRK05852 98 ldPALPI-AEQRVRSQAAGARV----VLIDA---DGPHDRAEPTTRWWPLTVNV------GGDSGPSGGTLSVHLDAATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 178 PSPA--------DEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpgALGVFLA 249
Cdd:PRK05852 164 PTPAtstpeglrPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIA--ALLATLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 250 KGTVVLATDP---SATLCFPLIekHQINAT--ALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEI 324
Cdd:PRK05852 242 SGGAVLLPARgrfSAHTFWDDI--KAVGATwyTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 325 GCQLQQVFGMAEGL--VNYTRLD-----DSPERIINTQGRPMCPDdeVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNS 397
Cdd:PRK05852 320 AAPVVCAFGMTEAThqVTTTQIEgigqtENPVVSTGLVGRSTGAQ--IRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 398 PLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAY 477
Cdd:PRK05852 398 PTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAV 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 677652367 478 LVVKEPLR--AVQVRRFLREqGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASR 533
Cdd:PRK05852 477 IVPRESAPptAEELVQFCRE-RLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQFGHS 533
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
25-535 |
1.46e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 157.03 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 25 VPLT--DILTRHAD--SDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVap 100
Cdd:PRK08162 16 VPLTplSFLERAAEvyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 101 VL-ALfsHQRTELNAYAMQIA---PTLVIADRQHTLFAGEDFlntfvAEHRSVRVVLLRNDD---------GDHSLDAAM 167
Cdd:PRK08162 94 VLnTL--NTRLDAASIAFMLRhgeAKVLIVDTEFAEVAREAL-----ALLPGPKPLVIDVDDpeypggrfiGALDYEAFL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 168 RQAAEDFTATPsPADEVAYFQLS--GGTTGTPKLIPRTHNDYYYSVRrSNEI-CGFNEDTRFLCAIPAAH-N-----YAM 238
Cdd:PRK08162 167 ASGDPDFAWTL-PADEWDAIALNytSGTTGNPKGVVYHHRGAYLNAL-SNILaWGMPKHPVYLWTLPMFHcNgwcfpWTV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 239 SSPGALGVFLAKgtvvlaTDPsaTLCFPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPlASLRLLQVGGARLSATLAA 318
Cdd:PRK08162 245 AARAGTNVCLRK------VDP--KLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGID-HPVHAMVAGAAPPAAVIAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 319 RipAEIGCQLQQVFGMAE----GLVN-----YTRLDDSPERIINT-QGRPMCPDDEVWVADAD-GNPLP-PGE-IGRLMT 385
Cdd:PRK08162 316 M--EEIGFDLTHVYGLTEtygpATVCawqpeWDALPLDERAQLKArQGVRYPLQEGVTVLDPDtMQPVPaDGEtIGEIMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 386 RGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSM 465
Cdd:PRK08162 394 RGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAK 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 677652367 466 EDELLGEKSCAYLVVKE--PLRAVQVRRFLREQgVAEFKLPDRVEcVASLPLTPVGKVDKKQLRQRLASRSP 535
Cdd:PRK08162 473 PDPKWGEVPCAFVELKDgaSATEEEIIAHCREH-LAGFKVPKAVV-FGELPKTSTGKIQKFVLREQAKSLKA 542
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
47-535 |
1.62e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 155.74 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 47 RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELNAYAMQIAPTLVIA 126
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 127 DRQhtlfagedflntfvaehrsvrVVLLRNDDGDHSLDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHND 206
Cdd:PRK09088 101 DDA---------------------VAAGRTDVEDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 207 YYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpgALGVFLAKGTVVLATD---PSATLCFPLIEKHQINATALVPPAv 283
Cdd:PRK09088 160 LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLIT--SVRPVLAVGGSILVSNgfePKRTLGRLGDPALGITHYFCVPQM- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 284 slwLQAIQEWGGNAP--LASLRLLQVGGARLSAT-----LAARIPAEIGcqlqqvFGMAE-GLVNYTRLDdsPERIIN-- 353
Cdd:PRK09088 237 ---AQAFRAQPGFDAaaLRHLTALFTGGAPHAAEdilgwLDDGIPMVDG------FGMSEaGTVFGMSVD--CDVIRAka 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 354 -TQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREK 432
Cdd:PRK09088 306 gAAGIPT-PTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 433 DQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLRAVQVRRFLREQgVAEFKLPDRVECV 510
Cdd:PRK09088 385 DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADgaPLDLERIRSHLSTR-LAKYKVPKHLRLV 463
|
490 500
....*....|....*....|....*
gi 677652367 511 ASLPLTPVGKVDKKQLRQRLASRSP 535
Cdd:PRK09088 464 DALPRTASGKLQKARLRDALAAGRK 488
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
38-526 |
1.69e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 156.31 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLAlfshqRTELNAYAM 117
Cdd:PRK13383 50 GRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPI-----STEFRSDAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAptlVIADRQHTLFAGEDFLNTFVAEHRSVRVVllrnddgdhslDAAMrQAAEDFTATPSPADEVAYFQLSGGTTGTP 197
Cdd:PRK13383 125 AAA---LRAHHISTVVADNEFAERIAGADDAVAVI-----------DPAT-AGAEESGGRPAVAAPGRIVLLTSGTTGKP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 198 KLIPRTHN------DYYYSVRRSNEICGfnedTRFLCAIPAAHNYAMsspGALGVFLAKGTVVLAT---DPSATLCFPLI 268
Cdd:PRK13383 190 KGVPRAPQlrsavgVWVTILDRTRLRTG----SRISVAMPMFHGLGL---GMLMLTIALGGTVLTHrhfDAEAALAQASL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 269 ekHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAE----GLVNYTRL 344
Cdd:PRK13383 263 --HRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEvgigALATPADL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 345 DDSPEriinTQGRPM--CPddeVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSplhnASAFDANGFYCSGDLISIDQD 422
Cdd:PRK13383 341 RDAPE----TVGKPVagCP---VRILDRNNRPVGPRVTGRIFVGGELAGTRYTDG----GGKAVVDGMTSTGDMGYLDNA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 423 GYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLRAVQVRRFLREQgVAE 500
Cdd:PRK13383 410 GRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPgsGVDAAQLRDYLKDR-VSR 488
|
490 500
....*....|....*....|....*.
gi 677652367 501 FKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:PRK13383 489 FEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
25-532 |
2.67e-41 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 155.91 E-value: 2.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 25 VPLTD-ILTRHAD-SDKTAVIEGE--RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAP 100
Cdd:PLN02246 23 LPLHDyCFERLSEfSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 101 VLALFSHQRTELNAYAMQIAPTLVIadrqhTLFAGEDFLNTFVAEhRSVRVVLLrNDDGDHSLD-AAMRQAAEDFTATP- 178
Cdd:PLN02246 103 TTANPFYTPAEIAKQAKASGAKLII-----TQSCYVDKLKGLAED-DGVTVVTI-DDPPEGCLHfSELTQADENELPEVe 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 179 -SPADEVAyFQLSGGTTGTPKLIPRTHNDYYYSVRR----SNEICGFNEDTRFLCAIPAAHNYAMSSpgalgVFL----A 249
Cdd:PLN02246 176 iSPDDVVA-LPYSSGTTGLPKGVMLTHKGLVTSVAQqvdgENPNLYFHSDDVILCVLPMFHIYSLNS-----VLLcglrV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 250 KGTVVLATDPSATLCFPLIEKHQINATALVPPAVsLWLqAIQEWGGNAPLASLRLLQVGGA----RLSATLAARIPAEIg 325
Cdd:PLN02246 250 GAAILIMPKFEIGALLELIQRHKVTIAPFVPPIV-LAI-AKSPVVEKYDLSSIRMVLSGAAplgkELEDAFRAKLPNAV- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 326 cqLQQVFGMAE-GLVnytrlddsperiintqgRPMCP-------------------DDEVWVADAD-GNPLPPGEIGRLM 384
Cdd:PLN02246 327 --LGQGYGMTEaGPV-----------------LAMCLafakepfpvksgscgtvvrNAELKIVDPEtGASLPRNQPGEIC 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 385 TRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVS 464
Cdd:PLN02246 388 IRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVP 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 677652367 465 MEDELLGEKSCAYlVVKEP---LRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLAS 532
Cdd:PLN02246 468 MKDEVAGEVPVAF-VVRSNgseITEDEIKQFVAKQ-VVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKLAA 536
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
31-527 |
3.05e-41 |
|
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: 154.81 E-value: 3.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 31 LTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQ 108
Cdd:cd17651 1 FERQAARtpDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 109 RTELNAYAMQIAPTLVIADRQHtlfagedflnTFVAEHRSVRVVLLrnddgdhsLDAAMRQAAEDFTATPSPADEVAYFQ 188
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPAL----------AGELAVELVAVTLL--------DQPGAAAGADAEPDPALDADDLAYVI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 189 LSGGTTGTPKLIPRTHndyyysvRRSNEICGFNedTRFLCAIPAAHNYAMSSPG-------ALGVFLAKGTVVLA----- 256
Cdd:cd17651 143 YTSGSTGRPKGVVMPH-------RSLANLVAWQ--ARASSLGPGARTLQFAGLGfdvsvqeIFSTLCAGATLVLPpeevr 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 257 TDPSATLCFplIEKHQINATALVPPAVSLWLQAIqeWGGNAPLASLRLLQVGGARLSATLAARIP--AEIGCQLQQVFGM 334
Cdd:cd17651 214 TDPPALAAW--LDEQRISRVFLPTVALRALAEHG--RPLGVRLAALRYLLTGGEQLVLTEDLREFcaGLPGLRLHNHYGP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 335 AEG-LVNYTRLDDSPER--IINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF- 410
Cdd:cd17651 290 TEThVVTALSLPGDPAAwpAPPPIGRPI-DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFv 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 411 -----YCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVK--EP 483
Cdd:cd17651 369 pgarmYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDpeAP 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 677652367 484 LRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:cd17651 449 VDAAELRAALATH-LPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
38-533 |
3.09e-41 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 155.02 E-value: 3.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLR-RQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELNaYA 116
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELI-FQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 117 MQIAPTLViadrqhtLFAGEDFLNTfVAEHRSVRVV--LLRNDDGDHSLDAamrqaaEDFTATPSPADEVAYFQLSGGTT 194
Cdd:PRK06839 96 LKDSGTTV-------LFVEKTFQNM-ALSMQKVSYVqrVISITSLKEIEDR------KIDNFVEKNESASFIICYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 195 GTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHnyamssPGALGVF-----LAKGTVVLATDPSATLCFPLIE 269
Cdd:PRK06839 162 GKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFH------IGGIGLFafptlFAGGVIIVPRKFEPTKALSMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 270 KHQINATALVPPAVSLWLQAIQEWGGNapLASLRLLQVGGARLSATLAaRIPAEIGCQLQQVFGMAE-GLVNYTRLDDSP 348
Cdd:PRK06839 236 KHKVTVVMGVPTIHQALINCSKFETTN--LQSVRWFYNGGAPCPEELM-REFIDRGFLFGQGFGMTEtSPTVFMLSEEDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 349 ERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDaNGFYCSGDLISIDQDGYITVH 428
Cdd:PRK06839 313 RRKVGSIGKPV-LFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQ-DGWLCTGDLARVDEDGFVYIV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 429 GREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYlVVKEPlRAVQVRRFLRE---QGVAEFKLPD 505
Cdd:PRK06839 391 GRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAF-IVKKS-SSVLIEKDVIEhcrLFLAKYKIPK 468
|
490 500
....*....|....*....|....*...
gi 677652367 506 RVECVASLPLTPVGKVDKKQLRQRLASR 533
Cdd:PRK06839 469 EIVFLKELPKNATGKIQKAQLVNQLKSR 496
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
7-531 |
7.63e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 155.20 E-value: 7.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 7 RWPdefARRYREKGY-WQDVPLTDILTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNV 83
Cdd:PRK06178 17 AWP---AGIPREPEYpHGERPLTEYLRAWARErpQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNC 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 84 PELYITFFALLKLGV--APVLALFshQRTELnAYAMQIA-PTLVIAdrqhtlfagEDFLNTFVAEHR---SVRVVLL--- 154
Cdd:PRK06178 94 PQFHIVFFGILKLGAvhVPVSPLF--REHEL-SYELNDAgAEVLLA---------LDQLAPVVEQVRaetSLRHVIVtsl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 155 --------------------RNDDGDHSLDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRS 214
Cdd:PRK06178 162 advlpaeptlplpdslraprLAAAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 215 NEICG-FNEDTRFLCAIP----AAHNYAMSSPGALGvflakGTVVLAT--DPSATLcfPLIEKHQINATA-LVPPAVSLW 286
Cdd:PRK06178 242 YAVAVvGGEDSVFLSFLPefwiAGENFGLLFPLFSG-----ATLVLLArwDAVAFM--AAVERYRVTRTVmLVDNAVELM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 287 lqaiqewggNAPLAS---LRLLQVGGA-----RLSATLAARIPAEIGCQLQQV-FGMAEGLVNYT-----RLDDsperiI 352
Cdd:PRK06178 315 ---------DHPRFAeydLSSLRQVRVvsfvkKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTftagfQDDD-----F 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 353 NTQGRPM-----CPDDEVWVADAD-GNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYIT 426
Cdd:PRK06178 381 DLLSQPVfvglpVPGTEFKICDFEtGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLH 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 427 VHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLRAVQVRRFLREQgVAEFKLP 504
Cdd:PRK06178 460 YLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPgaDLTAAALQAWCREN-MAVYKVP 538
|
570 580
....*....|....*....|....*..
gi 677652367 505 DrVECVASLPLTPVGKVDKKQLRQRLA 531
Cdd:PRK06178 539 E-IRIVDALPMTATGKVRKQDLQALAE 564
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
23-533 |
7.04e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 152.46 E-value: 7.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 23 QDVPLTDILTRHAD--SDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAP 100
Cdd:PRK05605 30 GDTTLVDLYDNAVArfGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 101 VL--ALFSHQrtELNAYAMQIAPTLVI-----ADRQHTLfAGEDFLNTFVAEH--------------------RSVRVVL 153
Cdd:PRK05605 110 VEhnPLYTAH--ELEHPFEDHGARVAIvwdkvAPTVERL-RRTTPLETIVSVNmiaampllqrlalrlpipalRKARAAL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 154 LRNDDGD---HSLDAAMRQAAEDFTATPSP-ADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNE-ICGFNE-DTRFL 227
Cdd:PRK05605 187 TGPAPGTvpwETLVDAAIGGDGSDVSHPRPtPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwVPGLGDgPERVL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 228 CAIPAAHNYAMSSPGALGVFLAkGTVVLATDPSATLCFPLIEKHQinATAL--VPPAVSLWLQAIQEWGgnAPLASLRLL 305
Cdd:PRK05605 267 AALPMFHAYGLTLCLTLAVSIG-GELVLLPAPDIDLILDAMKKHP--PTWLpgVPPLYEKIAEAAEERG--VDLSGVRNA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 306 QVGGARLSATLAARIPAEIGCQLQQVFGMAEG----LVNYTrlddSPERIINTQGRPMcPDDEVWVADADgNP---LPPG 378
Cdd:PRK05605 342 FSGAMALPVSTVELWEKLTGGLLVEGYGLTETspiiVGNPM----SDDRRPGYVGVPF-PDTEVRIVDPE-DPdetMPDG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 379 EIGRLMTRGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVI 458
Cdd:PRK05605 416 EEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVE 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 677652367 459 HAALVSMEDELLGEKSCAyLVVKEPLRAVQ---VRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASR 533
Cdd:PRK05605 495 DAAVVGLPREDGSEEVVA-AVVLEPGAALDpegLRAYCREH-LTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEK 570
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
22-530 |
1.06e-39 |
|
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: 151.67 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 22 WQDVPLT--DILTRHADSDKTAVI------EGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFAL 93
Cdd:cd05906 5 PEGAPRTllELLLRAAERGPTKGItyidadGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 94 LKLGVAPVLALFSHQRTELNAYAMQIAPTLVIADRQHTLFAGEdflntFVAEHRSVRVVLLRNDDGDHSLDAAMRQAAeD 173
Cdd:cd05906 85 VLAGFVPAPLTVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAE-----LVAEFAGLETLSGLPGIRVLSIEELLDTAA-D 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 174 FTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSPGALGVFLAKGTV 253
Cdd:cd05906 159 HDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 254 VLATdpSATLCFP-----LIEKHQINATALVPPAVSLWLQAIQEW-GGNAPLASLRLLQVGGARLSATLAARIPAEIG-C 326
Cdd:cd05906 239 HVPT--EEILADPlrwldLIDRYRVTITWAPNFAFALLNDLLEEIeDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEpY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 327 QLQQ-----VFGMAE---GlVNYTRLDDSPERIINTQ----GRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGY 394
Cdd:cd05906 317 GLPPdairpAFGMTEtcsG-VIYSRSFPTYDHSQALEfvslGRPI-PGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 395 FNSPLHNASAFDANGFYCSGDLISIDqDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIH--AALVSMEDELLGE 472
Cdd:cd05906 395 YNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAET 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 677652367 473 KSCA--YLVVKEPL-RAVQVRRFLREQGVAEFKL-PDRVECVA--SLPLTPVGKVDKKQLRQRL 530
Cdd:cd05906 474 EELAifFVPEYDLQdALSETLRAIRSVVSREVGVsPAYLIPLPkeEIPKTSLGKIQRSKLKAAF 537
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
38-536 |
4.08e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 150.11 E-value: 4.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQ-GIKPGETALVQLGNVPELYITFFALLKLG--VAPVLAL-----FSHQR 109
Cdd:PRK08314 25 DKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANavVVPVNPMnreeeLAHYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 110 TELNA--------YAMQIAPTLVIADRQHTLFA---------GEDFLNTFVAEHRSVRVVllrNDDGDHSLDAAMRQAAE 172
Cdd:PRK08314 105 TDSGArvaivgseLAPKVAPAVGNLRLRHVIVAqysdylpaePEIAVPAWLRAEPPLQAL---APGGVVAWKEALAAGLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 173 DFTATPSPaDEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAH----NYAMSSPGALGvfl 248
Cdd:PRK08314 182 PPPHTAGP-DDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHvtgmVHSMNAPIYAG--- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 249 akGTVVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQ--AIQEwggnAPLASLRLLQVGGARLSATLAARIPAEIGC 326
Cdd:PRK08314 258 --ATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLAspGLAE----RDLSSLRYIGGGGAAMPEAVAERLKELTGL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 327 QLQQVFGMAEGLvnytrlddSPErIINTQGRP--MC---PDDEV--WVADAD-GNPLPPGEIGRLMTRGPYTFRGYFNSP 398
Cdd:PRK08314 332 DYVEGYGLTETM--------AQT-HSNPPDRPklQClgiPTFGVdaRVIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 399 LHNASAF---DANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSC 475
Cdd:PRK08314 403 EATAEAFieiDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVK 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 677652367 476 AYLVVKEPLRAV----QVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASRSPL 536
Cdd:PRK08314 483 AVVVLRPEARGKtteeEIIAWAREH-MAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAAK 546
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
37-527 |
5.82e-39 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 149.79 E-value: 5.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 37 SDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG--VAPVLALFS-----HQR 109
Cdd:PRK07059 37 ADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGyvVVNVNPLYTpreleHQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 110 TELNAYAMQI----APTL--VIA--DRQHTLFAGE-DFLN------TFVAehRSVR-VVLLRNDDGDHSLDAAMRQ-AAE 172
Cdd:PRK07059 117 KDSGAEAIVVlenfATTVqqVLAktAVKHVVVASMgDLLGfkghivNFVV--RRVKkMVPAWSLPGHVRFNDALAEgARQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 173 DFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSV-----------RRSNEICGFNedtrFLCAIPAAHNYAMSSP 241
Cdd:PRK07059 195 TFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqpafEKKPRPDQLN----FVCALPLYHIFALTVC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 242 GALGVFLAkGTVVLATDPSATLCF-PLIEKHQINatalVPPAVSLWLQAIQewggNAP------LASLRLLQVGGARLSA 314
Cdd:PRK07059 271 GLLGMRTG-GRNILIPNPRDIPGFiKELKKYQVH----IFPAVNTLYNALL----NNPdfdkldFSKLIVANGGGMAVQR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 315 TLAARIPAEIGCQLQQVFGMAEglvnytrldDSPERIIN---------TQGRPMcPDDEVWVADADGNPLPPGEIGRLMT 385
Cdd:PRK07059 342 PVAERWLEMTGCPITEGYGLSE---------TSPVATCNpvdatefsgTIGLPL-PSTEVSIRDDDGNDLPLGEPGEICI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 386 RGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSM 465
Cdd:PRK07059 412 RGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGV 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 677652367 466 EDELLGEKSCAYLVVKEP-LRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:PRK07059 492 PDEHSGEAVKLFVVKKDPaLTEEDVKAFCKER-LTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
38-527 |
6.96e-39 |
|
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: 147.51 E-value: 6.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlalfshqrtelnayam 117
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYV---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPtlviadrqhtlfagedflntfvaEHRSVRVVLLRNDDGDHSLDaamrqaaedfTATPspaDEVAYFQLSGGTTGTP 197
Cdd:cd17649 66 PLDP-----------------------EYPAERLRYMLEDSGAGLLL----------THHP---RQLAYVIYTSGSTGTP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 198 KLIPRTHNDYYYSVRRSNEICGFNEDTRFLcaipaaHNYAMSSPGA----LGVFLAKGTVVLATDP----SATLCfPLIE 269
Cdd:cd17649 110 KGVAVSHGPLAAHCQATAERYGLTPGDREL------QFASFNFDGAheqlLPPLICGACVVLRPDElwasADELA-EMVR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 270 KHQINATALVPPAVSLWLQAIQEWGGNAPlASLRLLQVGGARLSATLAARIpAEIGCQLQQVFGMAEGLVNYT------R 343
Cdd:cd17649 183 ELGVTVLDLPPAYLQQLAEEADRTGDGRP-PSLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEATVTPLvwkceaG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 344 LDDSPERI-IntqGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF-------YCSGD 415
Cdd:cd17649 261 AARAGASMpI---GRPL-GGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgapgsrlYRTGD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 416 LISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSmEDELLGEKSCAYLVVKEPLR----AVQVRR 491
Cdd:cd17649 337 LARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVA-LDGAGGKQLVAYVVLRAAAAqpelRAQLRT 415
|
490 500 510
....*....|....*....|....*....|....*.
gi 677652367 492 FLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:cd17649 416 ALRAS-LPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
38-526 |
8.87e-39 |
|
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: 147.08 E-value: 8.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVA--PVLALFSHQRtelnay 115
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAyvPLDPAYPPER------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 116 amqiaptlviadrqhtlfagedflNTFVAEHRSVRVVLLRNDDgdhsldaamrqaaedftatpspadeVAYFQLSGGTTG 195
Cdd:cd12115 88 ------------------------LRFILEDAQARLVLTDPDD-------------------------LAYVIYTSGSTG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 196 TPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHN---YAMSSPGALGvflakGTVVLATDPSATLCFP-LIEKH 271
Cdd:cd12115 119 RPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDlsvFELFGPLATG-----GKVVLADNVLALPDLPaAAEVT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 272 QINAtalVPPAVSLWLQAiqewggNAPLASLRLLQVGGARLSATLAARIPAEIgcQLQQVF---GMAEGLV--NYTRLDD 346
Cdd:cd12115 194 LINT---VPSAAAELLRH------DALPASVRVVNLAGEPLPRDLVQRLYARL--QVERVVnlyGPSEDTTysTVAPVPP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 347 SPERIInTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------YCSGDLISID 420
Cdd:cd12115 263 GASGEV-SIGRPL-ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWR 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 421 QDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDElLGEKSCAYLVVKEPLRAVQV---RRFLReQG 497
Cdd:cd12115 341 PDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDA-AGERRLVAYIVAEPGAAGLVedlRRHLG-TR 418
|
490 500
....*....|....*....|....*....
gi 677652367 498 VAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd12115 419 LPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
44-500 |
2.04e-38 |
|
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: 146.20 E-value: 2.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 44 EGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQrtelnayAMQIAptl 123
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSS-------AEQIA--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 124 viadrqhtlfagedflntFVAEHRSVRVVLLrnDDGDHsldaamrqaaedfTATpspadeVAYfqlSGGTTGTPKLIPRT 203
Cdd:cd05907 71 ------------------YILNDSEAKALFV--EDPDD-------------LAT------IIY---TSGTTGRPKGVMLS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 204 HNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLATD------------PSATLCFPLI-EK 270
Cdd:cd05907 109 HRNILSNALALAERLPATEGDRHLSFLPLAHVFERRA-GLYVPLLAGARIYFASSaetllddlsevrPTVFLAVPRVwEK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 271 HQiNATALVppAVSLWLQAIQEWggnAPLASLRLLQVGGARLSATLAaRIPAEIGCQLQQVFGMAE--GLVNYTRLDDsp 348
Cdd:cd05907 188 VY-AAIKVK--AVPGLKRKLFDL---AVGGRLRFAASGGAPLPAELL-HFFRALGIPVYEGYGLTEtsAVVTLNPPGD-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 349 eRIINTQGRPMcPDDEVWVADAdgnplppGEIgrlMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVH 428
Cdd:cd05907 259 -NRIGTVGKPL-PGVEVRIADD-------GEI---LVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHIT 326
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 677652367 429 GREKD-QINRGGEKIAAEEIENLLLRHPVVIHAALVSmeDellGEKSCAYLVVkepLRAVQVRRFLREQGVAE 500
Cdd:cd05907 327 GRKKDlIITSGGKNISPEPIENALKASPLISQAVVIG--D---GRPFLVALIV---PDPEALEAWAEEHGIAY 391
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
35-528 |
2.16e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 147.97 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 35 ADSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvAPVLALFSHQRTELNA 114
Cdd:PRK06164 22 ARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLG-ATVIAVNTRYRSHEVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 115 YAMQI--APTLVIADRQHTL-FAG--EDFLNTFVAEHRSVRVVllrnDDGDHSLDAAMRQAAEDFTATPSPA-------- 181
Cdd:PRK06164 101 HILGRgrARWLVVWPGFKGIdFAAilAAVPPDALPPLRAIAVV----DDAADATPAPAPGARVQLFALPDPAppaaager 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 182 ----DEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSspGALGVFLAKGTVVL-- 255
Cdd:PRK06164 177 aadpDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFS--TLLGALAGGAPLVCep 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 256 ATDPSATLcfPLIEKHQINATAlvpPAVSLWLQAIQEWGGNAPLASLRLLQVGG-ARLSATLAARIPAEiGCQLQQVFGM 334
Cdd:PRK06164 255 VFDAARTA--RALRRHRVTHTF---GNDEMLRRILDTAGERADFPSARLFGFASfAPALGELAALARAR-GVPLTGLYGS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 335 AE--GLVNYTRLDDSPERIINTQGRPMCPDDEVWVAD-ADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGFY 411
Cdd:PRK06164 329 SEvqALVALQPATDPVSVRIEGGGRPASPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 412 CSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDEllGEKSCAYLVVKE---PLRAVQ 488
Cdd:PRK06164 409 RTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKTVPVAFVIPTdgaSPDEAG 486
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 677652367 489 VRRFLREQgVAEFKLPDRVECVASLPLTPVG---KVDKKQLRQ 528
Cdd:PRK06164 487 LMAACREA-LAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
32-526 |
6.29e-38 |
|
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: 145.73 E-value: 6.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 32 TRHADSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTE 111
Cdd:cd05923 12 SRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 112 LNayamqiapTLVIADRQHTLFAGEDFLNTFVAEHRSVRVVLLRNDDGDHSLDAAmRQAAEDftATPSPADEVAYFQLSG 191
Cdd:cd05923 92 LA--------ELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESA-GPLIED--PPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 192 gTTGTPK--LIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYamsspGALGVFLAK----GTVVLATDPSATLCF 265
Cdd:cd05923 161 -TTGLPKgaVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVI-----GFFAVLVAAlaldGTYVVVEEFDPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 266 PLIEKHQINATALVPPAVSLWLQAIQEWGGNapLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEGLvNYTRLD 345
Cdd:cd05923 235 KLIEQERVTSLFATPTHLDALAAAAEFAGLK--LSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM-NSLYMR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 346 DSperiinTQGRPMCP--DDEVWVADADGNP---LPPGEIGRLMTR--GPYTFRGYFNSPLHNASAFdANGFYCSGDLIS 418
Cdd:cd05923 312 DA------RTGTEMRPgfFSEVRIVRIGGSPdeaLANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 419 IDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE-PLRAVQVRRFLREQG 497
Cdd:cd05923 385 VDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREgTLSADELDQFCRASE 464
|
490 500
....*....|....*....|....*....
gi 677652367 498 VAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd05923 465 LADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
38-526 |
9.48e-38 |
|
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: 144.37 E-value: 9.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlalfshqrtelnayam 117
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYV---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPTLVIADRQHTLfagedflntfvaEHRSVRVVLLRNDDgdhsldaamrqaaedftatpspadeVAYFQLSGGTTGTP 197
Cdd:cd17643 66 PIDPAYPVERIAFIL------------ADSGPSLLLTDPDD-------------------------LAYVIYTSGSTGRP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 198 KLIPRTHNDYYYSVRRSNEICGFNEDTRFLcaipAAHNYAM--SSPGALGVFLAKGTVVL-----ATDPSAtlcFPLIEK 270
Cdd:cd17643 109 KGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAFdfSVWEIWGALLHGGRLVVvpyevARSPED---FARLLR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 271 HQ----INATalvPPAVSLWLQAIQEWGGNAPlaSLRLLQVGGARLSATL----AARIPAEiGCQLQQVFGMAEG--LVN 340
Cdd:cd17643 182 DEgvtvLNQT---PSAFYQLVEAADRDGRDPL--ALRYVIFGGEALEAAMlrpwAGRFGLD-RPQLVNMYGITETtvHVT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 341 YTRLD--DSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF-------Y 411
Cdd:cd17643 256 FRPLDaaDLPAAAASPIGRPL-PGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmY 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 412 CSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLRAVQV 489
Cdd:cd17643 335 RTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDgaAADIAEL 414
|
490 500 510
....*....|....*....|....*....|....*..
gi 677652367 490 RRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd17643 415 RALLKEL-LPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
299-528 |
1.03e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 144.75 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 299 LASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEGLVNY-TRLDDspERIINTQGRPMcPDDEVWVADADGNPLPP 377
Cdd:PRK07787 240 LRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLsTRADG--ERRPGWVGLPL-AGVETRLVDEDGGPVPH 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 378 -GE-IGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREK-DQINRGGEKIAAEEIENLLLRH 454
Cdd:PRK07787 317 dGEtVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGH 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 677652367 455 PVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:PRK07787 397 PGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQ-LSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
33-529 |
2.44e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 145.04 E-value: 2.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 33 RHADS---DKTAVI----EGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG--VAPvla 103
Cdd:PRK04319 51 RHADGgrkDKVALRyldaSRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGaiVGP--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 104 LFS-------HQRTELNAYAMQI-APTL---VIADR----QHTLFAGEDflntfvaehrsvrvvlLRNDDGDHSLDAAMR 168
Cdd:PRK04319 128 LFEafmeeavRDRLEDSEAKVLItTPALlerKPADDlpslKHVLLVGED----------------VEEGPGTLDFNALME 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 169 QAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHN---DYYYSVRRsneICGFNEDTRFLC-AIP---AAHNYAMSSP 241
Cdd:PRK04319 192 QASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNamlQHYQTGKY---VLDLHEDDVYWCtADPgwvTGTSYGIFAP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 242 GALGVflakGTVVLATDPSATLCFPLIEKHQINA--TAlvPPAVSLWLQAIQEWGGNAPLASLR-LLQVG---------- 308
Cdd:PRK04319 269 WLNGA----TNVIDGGRFSPERWYRILEDYKVTVwyTA--PTAIRMLMGAGDDLVKKYDLSSLRhILSVGeplnpevvrw 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 309 GARlsaTLAARI-----PAEIGCQLqqvfgmaegLVNYTRLDDSPeriiNTQGRPMcPDDEVWVADADGNPLPPGEIGRL 383
Cdd:PRK04319 343 GMK---VFGLPIhdnwwMTETGGIM---------IANYPAMDIKP----GSMGKPL-PGIEAAIVDDQGNELPPNRMGNL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 384 -MTRG-PYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAA 461
Cdd:PRK04319 406 aIKKGwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAG 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 677652367 462 LVSMEDELLGEKSCAYLVVK---EP---LRAvQVRRFLREqGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQR 529
Cdd:PRK04319 485 VIGKPDPVRGEIIKAFVALRpgyEPseeLKE-EIRGFVKK-GLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAW 556
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
38-526 |
3.25e-37 |
|
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: 142.77 E-value: 3.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvAPVLALFSHQRTELNAYAM 117
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAG-HAYVPLDASSPAERIREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIA-PTLVIADrqhtlfagedflntfvaehrsvrvvllrnddgdhsldaamrqaaedftatpspADEVAYFQLSGGTTGT 196
Cdd:cd05945 85 DAAkPALLIAD-----------------------------------------------------GDDNAYIIFTSGSTGR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 197 PKLIPRTHN--DYYYSVRRSNEIcgFNEDTRFLCAipAAHNYAMSSPGALGVFLAKGTVVL----ATDPSATLcFPLIEK 270
Cdd:cd05945 112 PKGVQISHDnlVSFTNWMLSDFP--LGPGDVFLNQ--APFSFDLSVMDLYPALASGATLVPvprdATADPKQL-FRFLAE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 271 HQINATALVPpavSLWLQAIQEWGGNAP-LASLRLLQVGG----ARLSATLAARIPaeiGCQLQQVFGMAE--GLVNYTR 343
Cdd:cd05945 187 HGITVWVSTP---SFAAMCLLSPTFTPEsLPSLRHFLFCGevlpHKTARALQQRFP---DARIYNTYGPTEatVAVTYIE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 344 LDDSP----ERIinTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAF---DANGFYCSGDL 416
Cdd:cd05945 261 VTPEVldgyDRL--PIGYAK-PGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfpdEGQRAYRTGDL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 417 ISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVK---EPLRAVQVRRFL 493
Cdd:cd05945 338 VRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKpgaEAGLTKAIKAEL 417
|
490 500 510
....*....|....*....|....*....|...
gi 677652367 494 REQgVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd05945 418 AER-LPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
31-521 |
4.74e-37 |
|
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: 144.64 E-value: 4.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 31 LTRHA--DSDKTAVI-EGE-----RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGV--AP 100
Cdd:cd17634 59 LDRHLreNGDRTAIIyEGDdtsqsRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAvhSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 101 VLALFSHQrtelnAYAMQIA---PTLVI-------ADRQHTLFAGEDflNTFVAEHRSVRVVLLRNDDG---------DH 161
Cdd:cd17634 139 IFGGFAPE-----AVAGRIIdssSRLLItadggvrAGRSVPLKKNVD--DALNPNVTSVEHVIVLKRTGsdidwqegrDL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 162 SLDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDY-YYSVRRSNEICGFNEDTRFLCAIP----AAHNY 236
Cdd:cd17634 212 WWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYlVYAATTMKYVFDYGPGDIYWCTADvgwvTGHSY 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 237 AMSSPGALG--VFLAKGTVVlatDPSATLCFPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSA 314
Cdd:cd17634 292 LLYGPLACGatTLLYEGVPN---WPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 315 ---TLAARIPAEIGCQLQQVFGMAE-GLVNYTRLDDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPY- 389
Cdd:cd17634 369 eayEWYWKKIGKEKCPVVDTWWQTEtGGFMITPLPGAIELKAGSATRPV-FGVQPAVVDNEGHPQPGGTEGNLVITDPWp 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 390 --TFRGYFNSPLHNASAFDA-NGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSME 466
Cdd:cd17634 448 gqTRTLFGDHERFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIP 527
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 467 DELLGEKSCAYLVVKE-----PLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKV 521
Cdd:cd17634 528 HAIKGQAPYAYVVLNHgvepsPELYAELRNWVRKE-IGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-528 |
4.90e-37 |
|
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: 142.19 E-value: 4.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 49 FSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGV--APVLALFshqrtelnayamqiaptlvia 126
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAiaVPLFALF--------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 127 drqhtlfaGEDFLNtFVAEHRSVRVVLlrnDDGdhsldaamrqaaedftatpspADEVAYFQLSGGTTGTPKLIPRTHnd 206
Cdd:cd05971 66 --------GPEALE-YRLSNSGASALV---TDG---------------------SDDPALIIYTSGTTGPPKGALHAH-- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 207 yyysvrrsneicgfnedtRFLCA-IPA---AHNYA------MSSP-------GALGVFLAK---GTVVLAT-----DPSA 261
Cdd:cd05971 111 ------------------RVLLGhLPGvqfPFNLFprdgdlYWTPadwawigGLLDVLLPSlyfGVPVLAHrmtkfDPKA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 262 TlcFPLIEKHQINaTALVPPAVslwLQAIQEWGGNAPLASLRLLQV--GGARLSATLAARIPAEIGCQLQQVFGMAEG-L 338
Cdd:cd05971 173 A--LDLMSRYGVT-TAFLPPTA---LKMMRQQGEQLKHAQVKLRAIatGGESLGEELLGWAREQFGVEVNEFYGQTECnL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 339 VNYTRLDDSPERIiNTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTR--GPYTFRGYFNSPLHNASAFdANGFYCSGDL 416
Cdd:cd05971 247 VIGNCSALFPIKP-GSMGKPI-PGHRVAIVDDNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 417 ISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVK---EPLRAV--QVRR 491
Cdd:cd05971 324 GRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNpgeTPSDALarEIQE 403
|
490 500 510
....*....|....*....|....*....|....*..
gi 677652367 492 FLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:cd05971 404 LVKTR-LAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
30-531 |
8.05e-37 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 143.83 E-value: 8.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 30 ILTRHADSDKTAVIEGERAF--SYRQLNQAADNLACSLRRQ-GIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFS 106
Cdd:PLN02574 46 IFSHHNHNGDTALIDSSTGFsiSYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 107 HQRTELNAYAMQIAPTLVIADRQHtlfagedflntfVAEHRSVRV-VLLRNDDGDHSlDAAMRQAA------EDFTATPS 179
Cdd:PLN02574 126 SSLGEIKKRVVDCSVGLAFTSPEN------------VEKLSPLGVpVIGVPENYDFD-SKRIEFPKfyelikEDFDFVPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 180 PA---DEVAYFQLSGGTTGTPKLIPRTHNDYYYSVR-----RSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKG 251
Cdd:PLN02574 193 PVikqDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrfEASQYEYPGSDNVYLAALPMFHIYGLSL-FVVGLLSLGS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 252 TVVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQAIQEWGGNaPLASLRLLQVGGARLSA-TLAARIPAEIGCQLQQ 330
Cdd:PLN02574 272 TIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGE-VLKSLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 331 VFGMAEGLVNYTR-LDDSPERIINTQGRpMCPDDEVWVAD-ADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDAN 408
Cdd:PLN02574 351 GYGMTESTAVGTRgFNTEKLSKYSSVGL-LAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 409 GFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYlVVKEP---LR 485
Cdd:PLN02574 430 GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAF-VVRRQgstLS 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 677652367 486 AVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLA 531
Cdd:PLN02574 509 QEAVINYVAKQ-VAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLT 553
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
27-533 |
2.27e-36 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 142.25 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHADSdkTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGE-TALVQLGNvpELYIT-FFALLKLG--VAPVL 102
Cdd:PLN02860 13 LTRLATLRGNA--VVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDvVAIAALNS--DLYLEwLLAVACAGgiVAPLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 103 ALFSHQrtELNAYAMQIAPTLVIADRQhTLFAGEDFLNTfvaEHRSVRVVLLRNDDGDH---------SLDAAMRQAAED 173
Cdd:PLN02860 89 YRWSFE--EAKSAMLLVRPVMLVTDET-CSSWYEELQND---RLPSLMWQVFLESPSSSvfiflnsflTTEMLKQRALGT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 174 FTATPSPA-DEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpgALGVFLAKGT 252
Cdd:PLN02860 163 TELDYAWApDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSS--ALAMLMVGAC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 253 VVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGC-QLQQV 331
Cdd:PLN02860 241 HVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNaKLFSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 332 FGMAEGLVNYT--RLDD----SPERIINTQGRPMCPDDEVWVADADGNPLPPGEI----------GRLMTRGPYTFRGYF 395
Cdd:PLN02860 321 YGMTEACSSLTfmTLHDptleSPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELkigldessrvGRILTRGPHVMLGYW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 396 NSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSC 475
Cdd:PLN02860 401 GQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVV 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 677652367 476 AYLVVKE----------------PLRAVQVRRFLREQGVAEFKLPDR-VECVASLPLTPVGKVDKKQLRQRLASR 533
Cdd:PLN02860 481 ACVRLRDgwiwsdnekenakknlTLSSETLRHHCREKNLSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRREVLSH 555
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
34-529 |
5.35e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 140.60 E-value: 5.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 34 HADSDKTAVIEGE--RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLaLFSHQRTE 111
Cdd:PRK13391 8 QTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTC-VNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 112 LNAYAM-QIAPTLVIADRQHTLFAGEDFLNTFVAEHRsvrVVLLRNDDGDHSLDAAmrQAAEDFTATPSPaDEV--AYFQ 188
Cdd:PRK13391 87 EAAYIVdDSGARALITSAAKLDVARALLKQCPGVRHR---LVLDGDGELEGFVGYA--EAVAGLPATPIA-DESlgTDML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 189 LSGGTTGTPKLI-------PRTHNDYYYSVrrSNEICGFNEDTRFLCAIPAAHNYAMSSPG---ALGvflakGTVVL--A 256
Cdd:PRK13391 161 YSSGTTGRPKGIkrplpeqPPDTPLPLTAF--LQRLWGFRSDMVYLSPAPLYHSAPQRAVMlviRLG-----GTVIVmeH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 257 TDPSATLcfPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAE 336
Cdd:PRK13391 234 FDAEQYL--ALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 337 GLvNYTRLDdSPERIIN--TQGRPMCPDdeVWVADADGNPLPPGEIGRLMTRGPYTFRgYFNSPLHNASAFDANG-FYCS 413
Cdd:PRK13391 312 GL-GFTACD-SEEWLAHpgTVGRAMFGD--LHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 414 GDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYL-----VVKEPLRAVQ 488
Cdd:PRK13391 387 GDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVqpvdgVDPGPALAAE 466
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 677652367 489 VRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQR 529
Cdd:PRK13391 467 LIAFCRQR-LSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
38-526 |
1.84e-35 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 137.77 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVA--PVLALFSHQRtelNAY 115
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAylPLDPAYPAER---IAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 116 AMQIA-PTLVIADrqhtlfagedflntfvaehrsvrvvllrnddgdhsldaamrqaaedftatpspADEVAYFQLSGGTT 194
Cdd:cd17652 79 MLADArPALLLTT-----------------------------------------------------PDNLAYVIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 195 GTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLcaipaahnyAMSSPG-------ALGVFLAKGTVVLATDPSATLCFPL 267
Cdd:cd17652 106 GRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVL---------QFASPSfdasvweLLMALLAGATLVLAPAEELLPGEPL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 268 IE---KHQINATALvPPAVSLWLQAiqewggnAPLASLRLLQVGGARLSATLAARIPAeiGCQLQQVFGMAEGLVNYTRL 344
Cdd:cd17652 177 ADllrEHRITHVTL-PPAALAALPP-------DDLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGPTETTVCATMA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 345 DDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF-------YCSGDLI 417
Cdd:cd17652 247 GPLPGGGVPPIGRPV-PGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 418 SIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLR--AVQVRRFLRE 495
Cdd:cd17652 326 RWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAptAAELRAHLAE 405
|
490 500 510
....*....|....*....|....*....|.
gi 677652367 496 QgVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd17652 406 R-LPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
27-499 |
1.98e-35 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 140.24 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHAD--SDKTAVIE----GERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAP 100
Cdd:COG1022 13 LPDLLRRRAArfPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 101 VlALFSHQRTELNAYAMQIA-PTLVIADRQHTLfageDFLNTFVAEHRSVR-VVLL-----RNDDGDHSLDAAMRQAAED 173
Cdd:COG1022 93 V-PIYPTSSAEEVAYILNDSgAKVLFVEDQEQL----DKLLEVRDELPSLRhIVVLdprglRDDPRLLSLDELLALGREV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 174 FT--------ATPSPADeVA---YfqlSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAmsspG 242
Cdd:COG1022 168 ADpaelearrAAVKPDD-LAtiiY---TSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFE----R 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 243 ALGVF-LAKGTVV--------LATD-----PSATLCFP-LIEK----HQINATALVPPAVSLWLQAI---QEWG-----G 295
Cdd:COG1022 240 TVSYYaLAAGATVafaespdtLAEDlrevkPTFMLAVPrVWEKvyagIQAKAEEAGGLKRKLFRWALavgRRYArarlaG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 296 NAPLASLRLL--------------QVGG-ARLSATLAARIPAE-------IGCQLQQVFGMAE--GLVNYTRLDDspeRI 351
Cdd:COG1022 320 KSPSLLLRLKhaladklvfsklreALGGrLRFAVSGGAALGPElarffraLGIPVLEGYGLTEtsPVITVNRPGD---NR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 352 INTQGRPMcPDDEVWVADadgnplpPGEIgrlMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGRE 431
Cdd:COG1022 397 IGTVGPPL-PGVEVKIAE-------DGEI---LVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRK 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 677652367 432 KDQI-NRGGEKIAAEEIENLLLRHPVVIHAALVsmedellGE--KSCAYLVVkepLRAVQVRRFLREQGVA 499
Cdd:COG1022 466 KDLIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrPFLAALIV---PDFEALGEWAEENGLP 526
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
19-526 |
2.28e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 139.40 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 19 KGYWQDVPLT---DILTRHADSDKTAVIEGERA--------FSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELY 87
Cdd:PRK06710 9 KSYPEEIPSTisyDIQPLHKYVEQMASRYPEKKalhflgkdITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 88 ITFFALLKLG--VAPVLALFSHQRTELNAY------------------AMQIAPTL--VIADRQHTLFA-GEDFLNTFVA 144
Cdd:PRK06710 89 IGYYGTLLAGgiVVQTNPLYTERELEYQLHdsgakvilcldlvfprvtNVQSATKIehVIVTRIADFLPfPKNLLYPFVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 145 EHRSVRVVLLRNDDGDHSLDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHND----------YYYSVRRS 214
Cdd:PRK06710 169 KKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNlvsntlmgvqWLYNCKEG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 215 NEICgfnedtrfLCAIPAAHNYAMSSPGALGVfLAKGTVVLATDPSATLCFPLIEKHQINataLVPPAVSLWLQAIqewg 294
Cdd:PRK06710 249 EEVV--------LGVLPFFHVYGMTAVMNLSI-MQGYKMVLIPKFDMKMVFEAIKKHKVT---LFPGAPTIYIALL---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 295 gNAPLasLRLLQVGGARLSATLAARIPAEIGCQLQQVFG--MAEGlvnYTRLDDSP---------ERIINTQGRPMcPDD 363
Cdd:PRK06710 313 -NSPL--LKEYDISSIRACISGSAPLPVEVQEKFETVTGgkLVEG---YGLTESSPvthsnflweKRVPGSIGVPW-PDT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 364 EVWVADAD-GNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDaNGFYCSGDLISIDQDGYITVHGREKDQINRGGEKI 442
Cdd:PRK06710 386 EAMIMSLEtGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 443 AAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAV--QVRRFLREQgVAEFKLPDRVECVASLPLTPVGK 520
Cdd:PRK06710 465 YPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSeeELNQFARKY-LAAYKVPKVYEFRDELPKTTVGK 543
|
....*.
gi 677652367 521 VDKKQL 526
Cdd:PRK06710 544 ILRRVL 549
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
38-526 |
4.07e-35 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 137.40 E-value: 4.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlalfshqrtelnayam 117
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYV---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPTLVIADRQHTLFAGEdfLNTFVAEHRSVRVVLLRNDDGDHSLDAAmrQAAEDFTATPSPADEVAYFQLSGGTTGTP 197
Cdd:cd12114 66 PVDIDQPAARREAILADAG--ARLVLTDGPDAQLDVAVFDVLILDLDAL--AAPAPPPPVDVAPDDLAYVIFTSGSTGTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 198 KLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAipAAHNYAMSSPGALGVFLAKGTVVL-----ATDPSATLcfPLIEKHQ 272
Cdd:cd12114 142 KGVMISHRAALNTILDINRRFAVGPDDRVLAL--SSLSFDLSVYDIFGALSAGATLVLpdearRRDPAHWA--ELIERHG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 273 INATALVPPavslWLQAIQEWGG--NAPLASLRLLQVGGARLSATLAARI-PAEIGCQLQQVFGMAEGLV--NYTRLDDS 347
Cdd:cd12114 218 VTLWNSVPA----LLEMLLDVLEaaQALLPSLRLVLLSGDWIPLDLPARLrALAPDARLISLGGATEASIwsIYHPIDEV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 348 PE--RIInTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAF----DANGFYCSGDLISIDQ 421
Cdd:cd12114 294 PPdwRSI-PYGRPL-ANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvthpDGERLYRTGDLGRYRP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 422 DGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDEllGEKS-CAYLVVKEPLRAV---QVRRFLrEQG 497
Cdd:cd12114 372 DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP--GGKRlAAFVVPDNDGTPIapdALRAFL-AQT 448
|
490 500
....*....|....*....|....*....
gi 677652367 498 VAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd12114 449 LPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
38-527 |
5.69e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 137.45 E-value: 5.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGE--RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVapVLALFSHQRTELNAy 115
Cdd:PRK13390 12 DRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGL--YITAINHHLTAPEA- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 116 amqiapTLVIADRQHTLFAGEDFLNTFVAE---HRSVRVVLLRNDDGDHSLDAAMRQAAEDFTATPSPAdeVAYFqlSGG 192
Cdd:PRK13390 89 ------DYIVGDSGARVLVASAALDGLAAKvgaDLPLRLSFGGEIDGFGSFEAALAGAGPRLTEQPCGA--VMLY--SSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 193 TTGTPKLI----PRTHNDYYYS--VRRSNEICGFNEDTRFLCAIPAAHNYAMSSPG---ALGvflakGTVVLAT--DPSA 261
Cdd:PRK13390 159 TTGFPKGIqpdlPGRDVDAPGDpiVAIARAFYDISESDIYYSSAPIYHAAPLRWCSmvhALG-----GTVVLAKrfDAQA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 262 TLCFplIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEglVNY 341
Cdd:PRK13390 234 TLGH--VERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE--AHG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 342 TRLDDSPERIIN--TQGRPMCPDdeVWVADADGNPLPPGEIGRL-MTRGPYTFRgYFNSPLHNASA-FDANGFYCS-GDL 416
Cdd:PRK13390 310 MTFIDSPDWLAHpgSVGRSVLGD--LHICDDDGNELPAGRIGTVyFERDRLPFR-YLNDPEKTAAAqHPAHPFWTTvGDL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 417 ISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLR-----AVQVRR 491
Cdd:PRK13390 387 GSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRgsdelARELID 466
|
490 500 510
....*....|....*....|....*....|....*.
gi 677652367 492 FLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:PRK13390 467 YTRSR-IAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
27-533 |
7.92e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 136.83 E-value: 7.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHAD--SDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVqLGNVPELYITFFALLKLGVAPVLAL 104
Cdd:PRK07638 3 ITKEYKKHASlqPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAIL-LENRIEFLQLFAGAAMAGWTCVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 105 FSHQRTELnAYAMQIA-PTLVIADRQhtlfagedFLNTFVAEhrSVRVVLLRNDDGDhsldaaMRQAAEDFTATPSPADE 183
Cdd:PRK07638 82 IKWKQDEL-KERLAISnADMIVTERY--------KLNDLPDE--EGRVIEIDEWKRM------IEKYLPTYAPIENVQNA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 184 VAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLcaIPAAHNYAMSSPGALGVFLAKGTVVLATDPSATL 263
Cdd:PRK07638 145 PFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVL--IAGTLVHSLFLYGAISTLYVGQTVHLMRKFIPNQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 264 CFPLIEKHQINATALVPPAVSLWLQAiqewggNAPLASLRLLQVGGARLSAT----LAARIPAeigCQLQQVFGMAE-GL 338
Cdd:PRK07638 223 VLDKLETENISVMYTVPTMLESLYKE------NRVIENKMKIISSGAKWEAEakekIKNIFPY---AKLYEFYGASElSF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 339 VNYTRLDDSpERIINTQGRPmCPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLhNASAFDANGFYCSGDLIS 418
Cdd:PRK07638 294 VTALVDEES-ERRPNSVGRP-FHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGV-LARELNADGWMTVRDVGY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 419 IDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYlvVKEPLRAVQVRRFLREQgV 498
Cdd:PRK07638 371 EDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAI--IKGSATKQQLKSFCLQR-L 447
|
490 500 510
....*....|....*....|....*....|....*
gi 677652367 499 AEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASR 533
Cdd:PRK07638 448 SSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQ 482
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
50-529 |
9.25e-35 |
|
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: 136.69 E-value: 9.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 50 SYRQLNQAADNLACSLRRqGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELNAYAMQIAPTLVIADRQ 129
Cdd:cd05909 9 TYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 130 HTLFAGEDFLNTFVAEHRSVRVVLLRNDDGDHS-----LDAAMRQAAED--FTATPSPADEVAYFQLSGGTTGTPKLIPR 202
Cdd:cd05909 88 FIEKLKLHHLFDVEYDARIVYLEDLRAKISKADkckafLAGKFPPKWLLriFGVAPVQPDDPAVILFTSGSEGLPKGVVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 203 THNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLATDPSATLCFP-LIekHQINATALVpp 281
Cdd:cd05909 168 SHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTG-CLWLPLLSGIKVVFHPNPLDYKKIPeLI--YDKKATILL-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 282 AVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEG----LVNYTRLDDSPEriinTQGR 357
Cdd:cd05909 243 GTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECspviSVNTPQSPNKEG----TVGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 358 PMcPDDEVWVADADGN-PLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQIN 436
Cdd:cd05909 319 PL-PGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 437 RGGEKIAAEEIENLLLRH-PVVIHAALVSMEDELLGEKSCAYLVVKEPLRAvQVRRFLREQGVAEFKLPDRVECVASLPL 515
Cdd:cd05909 397 IAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPS-SLNDILKNAGISNLAKPSYIHQVEEIPL 475
|
490
....*....|....
gi 677652367 516 TPVGKVDKKQLRQR 529
Cdd:cd05909 476 LGTGKPDYVTLKAL 489
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
25-530 |
2.33e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 135.78 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 25 VPLTDILTRHA--DSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVL 102
Cdd:PRK06145 2 FNLSASIAFHArrTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 103 ALFSHQRTELnAYAMQIAPTLViadrqhtLFAGEDFLNTFVAEHRsvRVVLlrnddGDHSLDAAMRQAAEDFTATPSPA- 181
Cdd:PRK06145 82 INYRLAADEV-AYILGDAGAKL-------LLVDEEFDAIVALETP--KIVI-----DAAAQADSRRLAQGGLEIPPQAAv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 182 --DEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSPGaLGVFLAKGTVVLATDP 259
Cdd:PRK06145 147 apTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPG-IAVLWVGGTLRIHREF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 260 SATLCFPLIEKHQINATALVPPAVSLWLQAIQEWggNAPLASLRLLQVGGARlsaTLAARIPAE----IGCQLQQVFGMA 335
Cdd:PRK06145 226 DPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGGGEK---TPESRIRDFtrvfTRARYIDAYGLT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 336 EGLVNYTRLDDSPE-RIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFdANGFYCSG 414
Cdd:PRK06145 301 ETCSGDTLMEAGREiEKIGSTGRAL-AHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 415 DLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLRAVQVRRF 492
Cdd:PRK06145 379 DVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgaTLTLEALDRH 458
|
490 500 510
....*....|....*....|....*....|....*...
gi 677652367 493 LReQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRL 530
Cdd:PRK06145 459 CR-QRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
38-536 |
5.41e-34 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 135.74 E-value: 5.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFAL-----------LKLGVAPVLALFS 106
Cdd:PLN02479 35 TRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVpmagavvncvnIRLNAPTIAFLLE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 107 HQRTELnayamqiaptlVIADRQHTLFAGEDF-------LNTFvaehRSVRVVLLRNDDGDH-SLDAAMRQAA---EDFT 175
Cdd:PLN02479 115 HSKSEV-----------VMVDQEFFTLAEEALkilaekkKSSF----KPPLLIVIGDPTCDPkSLQYALGKGAieyEKFL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 176 AT--PS-----PADEVAYFQL--SGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSPGALGV 246
Cdd:PLN02479 180 ETgdPEfawkpPADEWQSIALgyTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 247 FLakGTVVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQAIQEwGGNAPLASLRLLQVGGARLSATLAARIpAEIGC 326
Cdd:PLN02479 260 LC--GTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKS-ETILPLPRVVHVMTAGAAPPPSVLFAM-SEKGF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 327 QLQQVFGMAEGLVNYTRLDDSPE----------RIINTQGRPMCPDDEVWVADA-DGNPLPP--GEIGRLMTRGPYTFRG 393
Cdd:PLN02479 336 RVTHTYGLSETYGPSTVCAWKPEwdslppeeqaRLNARQGVRYIGLEGLDVVDTkTMKPVPAdgKTMGEIVMRGNMVMKG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 394 YFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEK 473
Cdd:PLN02479 416 YLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGES 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 474 SCAYLVVK-------EPLRAVQVRRFLREQgVAEFKLPDRVeCVASLPLTPVGKVDKKQLRQRLASRSPL 536
Cdd:PLN02479 495 PCAFVTLKpgvdksdEAALAEDIMKFCRER-LPAYWVPKSV-VFGPLPKTATGKIQKHVLRAKAKEMGPV 562
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
4-528 |
9.27e-34 |
|
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: 135.52 E-value: 9.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 4 PFTRWpdeFARRYREKGYwqdvpltDILTRHADS---DKTAVI------EGERAFSYRQLNQAADNLACSLRRQGIKPGE 74
Cdd:cd05967 39 PFTRW---FVGGRLNTCY-------NALDRHVEAgrgDQIALIydspvtGTERTYTYAELLDEVSRLAGVLRKLGVVKGD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 75 TALVQLGNVPELYITFFALLKLG---------------------VAPVLALFSHQRTELNayamQIAPTLVIADRQHTLf 133
Cdd:cd05967 109 RVIIYMPMIPEAAIAMLACARIGaihsvvfggfaakelasriddAKPKLIVTASCGIEPG----KVVPYKPLLDKALEL- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 134 agedflntfvAEHRSVRVVLLRNDD-----GDHSLD---AAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHN 205
Cdd:cd05967 184 ----------SGHKPHHVLVLNRPQvpadlTKPGRDldwSELLAKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 206 DY----YYSVRrsnEICGFNEDTRFLCAIP----AAHNYAMSSPGALGV--FLAKGTVVLATDPSATlcFPLIEKHQINA 275
Cdd:cd05967 254 GHavalNWSMR---NIYGIKPGDVWWAASDvgwvVGHSYIVYGPLLHGAttVLYEGKPVGTPDPGAF--WRVIEKYQVNA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 276 TALVPPAvslwLQAIQ------EWGGNAPLASLRLLQVGGARL-SATLAaripaeigcQLQQVFG--------------- 333
Cdd:cd05967 329 LFTAPTA----IRAIRkedpdgKYIKKYDLSSLRTLFLAGERLdPPTLE---------WAENTLGvpvidhwwqtetgwp 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 334 -MAeglvNYTRLDDSPERIiNTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTfRGYFNSPLHNASAF------D 406
Cdd:cd05967 396 iTA----NPVGLEPLPIKA-GSPGKPV-PGYQVQVLDEDGEPVGPNELGNIVIKLPLP-PGCLLTLWKNDERFkklylsK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 407 ANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PL 484
Cdd:cd05967 469 FPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEgvKI 548
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 677652367 485 RAVQVRRFL----REQ--GVAEFKLpdrVECVASLPLTPVGKVDKKQLRQ 528
Cdd:cd05967 549 TAEELEKELvalvREQigPVAAFRL---VIFVKRLPKTRSGKILRRTLRK 595
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
23-531 |
9.99e-34 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 134.91 E-value: 9.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 23 QDVPL--TDILTR----HADSDKTAVIEGERA-FSYRQLNQAADNLACSLRRQ-GIKPGETALVQLGNVPELYITFFALL 94
Cdd:PRK05620 6 QDVPLslTRILEYgstvHGDTTVTTWGGAEQEqTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 95 KLGvapvlALFShqrtELNAYAM--QI-------APTLVIADRqhtlfAGEDFLNTFVAEHRSVRVVLLRnddGDHSLDA 165
Cdd:PRK05620 86 CMG-----AVFN----PLNKQLMndQIvhiinhaEDEVIVADP-----RLAEQLGEILKECPCVRAVVFI---GPSDADS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 166 AMRQAAEDFTAT---------------PS-PADEVAYFQLSGGTTGTPKLIPRTHNDYYY---SVRRSNEICGFNeDTRF 226
Cdd:PRK05620 149 AAAHMPEGIKVYsyealldgrstvydwPElDETTAAAICYSTGTTGAPKGVVYSHRSLYLqslSLRTTDSLAVTH-GESF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 227 LCAIPAAHNYAMSSPgaLGVFLAKGTVVLatdPSATLCFPLIEKhqINATAL------VPpavSLWLQAIQEWGGNAP-L 299
Cdd:PRK05620 228 LCCVPIYHVLSWGVP--LAAFMSGTPLVF---PGPDLSAPTLAK--IIATAMprvahgVP---TLWIQLMVHYLKNPPeR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 300 ASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAE------------GLVNYTRLDdspERIinTQGR-------PMC 360
Cdd:PRK05620 298 MSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTEtspvgtvarppsGVSGEARWA---YRV--SQGRfpasleyRIV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 361 PDDEVwVADADGNPlppgeiGRLMTRGPYTFRGYFNSPLHN----------------ASAFDANGFYCSGDLISIDQDGY 424
Cdd:PRK05620 373 NDGQV-MESTDRNE------GEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVGSVTRDGF 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 425 ITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVK---EPLR--AVQVRRFLREQgVA 499
Cdd:PRK05620 446 LTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLApgiEPTRetAERLRDQLRDR-LP 524
|
570 580 590
....*....|....*....|....*....|..
gi 677652367 500 EFKLPDRVECVASLPLTPVGKVDKKQLRQRLA 531
Cdd:PRK05620 525 NWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLA 556
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
40-529 |
1.76e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 133.11 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 40 TAVIEGE-RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGV--APVlalfSHQRTelnayA 116
Cdd:PRK08276 2 AVIMAPSgEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLyyTPI----NWHLT-----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 117 MQIAptLVIADRQ-HTLFAGEDFLNTF--VAEHRSVRVVLLRNDDGDHSLDAAMRQAAEDFTATPsPADEVA--YFQLSG 191
Cdd:PRK08276 73 AEIA--YIVDDSGaKVLIVSAALADTAaeLAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTP-IADETAgaDMLYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 192 GTTGTPKLI--PRTHNDYYYSVRRSNEICGF----NEDTRFLCAIPAAH----NYAMSSPgALGvflakGTVVLAT--DP 259
Cdd:PRK08276 150 GTTGRPKGIkrPLPGLDPDEAPGMMLALLGFgmygGPDSVYLSPAPLYHtaplRFGMSAL-ALG-----GTVVVMEkfDA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 260 SATLcfPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLqvggarLSAtlAARIPAEI--------GCQLQQV 331
Cdd:PRK08276 224 EEAL--ALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVA------IHA--AAPCPVEVkramidwwGPIIHEY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 332 FGMAEGlvNYTRLDDSPERIIN--TQGRPMcpDDEVWVADADGNPLPPGEIGRL-MTRGPYTFRgYFNSPLHNASAFDAN 408
Cdd:PRK08276 294 YASSEG--GGVTVITSEDWLAHpgSVGKAV--LGEVRILDEDGNELPPGEIGTVyFEMDGYPFE-YHNDPEKTAAARNPH 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 409 GFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAylVVK------- 481
Cdd:PRK08276 369 GWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQpadgada 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 677652367 482 EPLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQR 529
Cdd:PRK08276 447 GDALAAELIAWLRGR-LAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
219-523 |
3.13e-33 |
|
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: 129.31 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 219 GFNEDTRFLCAIPAAHNYAMSSpgALGVFLAKGTVVLAT--DPSATLcfPLIEKHQINATALVPPAVSLWLQAIQEwgGN 296
Cdd:cd17637 37 GLTEADVYLNMLPLFHIAGLNL--ALATFHAGGANVVMEkfDPAEAL--ELIEEEKVTLMGSFPPILSNLLDAAEK--SG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 297 APLASLRllQVGGARLSATLAaRIPAEIGCQLQQVFGMAE--GLVNYTRLDDSPeriiNTQGRPMcPDDEVWVADADGNP 374
Cdd:cd17637 111 VDLSSLR--HVLGLDAPETIQ-RFEETTGATFWSLYGQTEtsGLVTLSPYRERP----GSAGRPG-PLVRVRIVDDNDRP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 375 LPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDaNGFYCSGDLISIDQDGYITVHGR--EKDQINRGGEKIAAEEIENLLL 452
Cdd:cd17637 183 VPAGETGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVIL 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 677652367 453 RHPVVIHAALVSMEDELLGE--KSCAYLVVKEPLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDK 523
Cdd:cd17637 262 EHPAIAEVCVIGVPDPKWGEgiKAVCVLKPGATLTADELIEFVGSR-IARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
38-526 |
3.41e-33 |
|
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: 131.44 E-value: 3.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvapvlalfshqrtelNAYaM 117
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAG---------------GAY-V 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPTLViADRQHtlfagedflntFVAEHRSVRVVLLRNDDgdhsldaamrqaaedftatpspadeVAYFQLSGGTTGTP 197
Cdd:cd17650 66 PIDPDYP-AERLQ-----------YMLEDSGAKLLLTQPED-------------------------LAYVIYTSGTTGKP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 198 KLIPRTHNDY---YYSVRRSNEICGFNedTRFLCAipAAHNYAMSSPGALGVFLAKGTVVLATDP---SATLCFPLIEKH 271
Cdd:cd17650 109 KGVMVEHRNVahaAHAWRREYELDSFP--VRLLQM--ASFSFDVFAGDFARSLLNGGTLVICPDEvklDPAALYDLILKS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 272 QINATALVPpAVSLWLQAIQEWGGnAPLASLRLLQVGG----ARLSATLAARIPAeiGCQLQQVFGMAEGLVNYTRLDDS 347
Cdd:cd17650 185 RITLMESTP-ALIRPVMAYVYRNG-LDLSAMRLLIVGSdgckAQDFKTLAARFGQ--GMRIINSYGVTEATIDSTYYEEG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 348 PERIINTQ----GRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------YCSGDLI 417
Cdd:cd17650 261 RDPLGDSAnvpiGRPL-PNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 418 SIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDElLGEKS-CAYLVVKEPLRAVQVRRFLREQ 496
Cdd:cd17650 340 RWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEARlCAYVVAAATLNTAELRAFLAKE 418
|
490 500 510
....*....|....*....|....*....|
gi 677652367 497 gVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd17650 419 -LPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
37-532 |
3.82e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 135.29 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 37 SDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVApVLALFSHQRTELNAYa 116
Cdd:PRK12467 526 PERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGA-YVPLDPEYPQDRLAY- 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 117 mqiaptlVIADRQHTLFAGEDFLNTFVAEHRSVRVVLLrNDDGDhsldaAMRQAAEDFTATPSPADEVAYFQLSGGTTGT 196
Cdd:PRK12467 604 -------MLDDSGVRLLLTQSHLLAQLPVPAGLRSLCL-DEPAD-----LLCGYSGHNPEVALDPDNLAYVIYTSGSTGQ 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 197 PKLIPRTHNDYyysvrrSNEICGFNEDTRFLcaipAAHNYAMSSPGALGVF-------LAKG-TVVLAT-----DPSATL 263
Cdd:PRK12467 671 PKGVAISHGAL------ANYVCVIAERLQLA----ADDSMLMVSTFAFDLGvtelfgaLASGaTLHLLPpdcarDAEAFA 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 264 CfpLIEKHQINATALVPPAVSLWLQAIQEwggnAPLASLRLLQVGGARLSATLAARIPA-EIGCQLQQVFGMAEGLVNYT 342
Cdd:PRK12467 741 A--LMADQGVTVLKIVPSHLQALLQASRV----ALPRPQRALVCGGEALQVDLLARVRAlGPGARLINHYGPTETTVGVS 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 343 RLDDSPERIINTQ---GRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF-------YC 412
Cdd:PRK12467 815 TYELSDEERDFGNvpiGQPL-ANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYR 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 413 SGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMeDELLGEKSCAYLVVKEPLRAVQ---- 488
Cdd:PRK12467 894 TGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ-PGDAGLQLVAYLVPAAVADGAEhqat 972
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 677652367 489 ---VRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLAS 532
Cdd:PRK12467 973 rdeLKAQLRQV-LPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAS 1018
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
29-529 |
5.91e-33 |
|
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: 132.23 E-value: 5.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 29 DILTRHADS--DKTAVI-----EGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPV 101
Cdd:cd05970 21 DVVDAMAKEypDKLALVwcddaGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 102 LAlfSHQRTELN-AYAMQIAPT-LVIADrqhtlfAGEDFLNTFVAEHRSVRVVLLRNDDGDH------SLDAAMRQAAED 173
Cdd:cd05970 101 PA--THQLTAKDiVYRIESADIkMIVAI------AEDNIPEEIEKAAPECPSKPKLVWVGDPvpegwiDFRKLIKNASPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 174 FTATPSPA----DEVAYFQLSGGTTGTPKLIPRTHN---------DYYYSVRrsneicgfnEDTRFLCAipAAHNYAMSS 240
Cdd:cd05970 173 FERPTANSypcgEDILLVYFSSGTTGMPKMVEHDFTyplghivtaKYWQNVR---------EGGLHLTV--ADTGWGKAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 241 PGAL-GVFLAkGTVVLATD-----PSATLcfPLIEKHQINaTALVPPAVSLWLqaIQEWGGNAPLASLRLLQVGGARLSA 314
Cdd:cd05970 242 WGKIyGQWIA-GAAVFVYDydkfdPKALL--EKLSKYGVT-TFCAPPTIYRFL--IREDLSRYDLSSLRYCTTAGEALNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 315 TLAARIPAEIGCQLQQVFGMAEGLV---NYTRLDDSPERIintqGRPMcPDDEVWVADADGNPLPPGEIG----RLMTRG 387
Cdd:cd05970 316 EVFNTFKEKTGIKLMEGFGQTETTLtiaTFPWMEPKPGSM----GKPA-PGYEIDLIDREGRSCEAGEEGeiviRTSKGK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 388 PY-TFRGYFNSPLHNASAFDaNGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSME 466
Cdd:cd05970 391 PVgLFGGYYKDAEKTAEVWH-DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVP 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 677652367 467 DELLGEKSCAYLVVKEPLRAVQVR----RFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQR 529
Cdd:cd05970 470 DPIRGQVVKATIVLAKGYEPSEELkkelQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
38-526 |
1.33e-32 |
|
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: 130.29 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVApVLALFSHQRTELNAYAM 117
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGA-FVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPT-LVIADRQHTLFAGEDFLntfvaehrsvrVVLLRNDDGDHSLDAAMRQAAEdftatpspADEVAYFQLSGGTTGT 196
Cdd:cd17656 82 LDSGVrVVLTQRHLKSKLSFNKS-----------TILLEDPSISQEDTSNIDYINN--------SDDLLYIIYTSGTTGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 197 PKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAipAAHNYAMSSPGALGVFLAKGTVVLA---TDPSATLCFPLIEKHQI 273
Cdd:cd17656 143 PKGVQLEHKNMVNLLHFEREKTNINFSDKVLQF--ATCSFDVCYQEIFSTLLSGGTLYIIreeTKRDVEQLFDLVKRHNI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 274 NaTALVPpaVSLWLQAIQEWGGNAPLAS-LRLLQVGGARLSAT-LAARIPAEIGCQLQQVFGMAEG-LVNYTRLDDSPE- 349
Cdd:cd17656 221 E-VVFLP--VAFLKFIFSEREFINRFPTcVKHIITAGEQLVITnEFKEMLHEHNVHLHNHYGPSEThVVTTYTINPEAEi 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 350 RIINTQGRPMCpDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------YCSGDLISIDQDG 423
Cdd:cd17656 298 PELPPIGKPIS-NTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 424 YITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVRRFLREQgVAEFKL 503
Cdd:cd17656 377 NIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQ-LPEYMI 455
|
490 500
....*....|....*....|...
gi 677652367 504 PDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd17656 456 PSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
41-528 |
1.56e-32 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 130.59 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 41 AVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlALFSHQRTELNAYAMQIA 120
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAV-PVNWHFKPEEIAYILEDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 121 PTLViadrqhtLFAGEDFLNTfVAEH--RSVRVVLL----------RNDDGDHSLDAAMR------QAAEDFTATPSPAD 182
Cdd:PRK12406 83 GARV-------LIAHADLLHG-LASAlpAGVTVLSVptppeiaaayRISPALLTPPAGAIdwegwlAQQEPYDGPPVPQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 183 EVAYFqlSGGTTGTPKLIPR---THNDYYYSVRRSNEICGFNEDTRFLCAIPAAHnyamSSPGALGVFLAK--GTVVLAT 257
Cdd:PRK12406 155 QSMIY--TSGTTGHPKGVRRaapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYH----SAPNAYGLRAGRlgGVLVLQP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 258 --DPSATLcfPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGgarlsatlAARIPAEI--------GCQ 327
Cdd:PRK12406 229 rfDPEELL--QLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHA--------AAPCPADVkramiewwGPV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 328 LQQVFGMAE-GLVNYTRLDDSPERIiNTQGRPmCPDDEVWVADADGNPLPPGEIGRLMTRGP-YTFRGYFNSPLHNASAf 405
Cdd:PRK12406 299 IYEYYGSTEsGAVTFATSEDALSHP-GTVGKA-APGAELRFVDEDGRPLPQGEIGEIYSRIAgNPDFTYHNKPEKRAEI- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 406 DANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLvvkEP-- 483
Cdd:PRK12406 376 DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV---EPqp 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 677652367 484 ---LRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:PRK12406 453 gatLDEADIRAQLKAR-LAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
36-529 |
2.79e-32 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 130.26 E-value: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 36 DSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLalfshqrteLNAY 115
Cdd:PRK13382 56 CPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILL---------LNTS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 116 AMQIAPTLVIADRQ-HTLFAGEDFLNT----FVAEHRSVRVVLLRNDDGDHSLDAAMRQAAEDftaTPSPADEVA-YFQL 189
Cdd:PRK13382 127 FAGPALAEVVTREGvDTVIYDEEFSATvdraLADCPQATRIVAWTDEDHDLTVEVLIAAHAGQ---RPEPTGRKGrVILL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 190 SGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSPgALGVFLAkGTVVLAT--DPSATLcfPL 267
Cdd:PRK13382 204 TSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQL-VLAASLA-CTIVTRRrfDPEATL--DL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 268 IEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEGLVNYTRLDDS 347
Cdd:PRK13382 280 IDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPAD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 348 PERIINTQGRPmcPD-DEVWVADADGNPLPPGEIGRLMTRGPYTFRGYfnSPLHNASAFDanGFYCSGDLISIDQDGYIT 426
Cdd:PRK13382 360 LRAAPDTAGRP--AEgTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHD--GFMASGDVGYLDENGRLF 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 427 VHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQ--VRRFLREQgVAEFKLP 504
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPetLKQHVRDN-LANYKVP 512
|
490 500
....*....|....*....|....*
gi 677652367 505 DRVECVASLPLTPVGKVDKKQLRQR 529
Cdd:PRK13382 513 RDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
38-526 |
6.35e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 131.44 E-value: 6.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELnAYAM 117
Cdd:PRK12467 3110 EAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERL-AYMI 3188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPTLVIADRQHTLfagedflntfvaEH----RSVRVVLLrnDDGDhsldaaMRQAAEDFTATPSPADEVAYFQLSGGT 193
Cdd:PRK12467 3189 EDSGVKLLLTQAHLL------------EQlpapAGDTALTL--DRLD------LNGYSENNPSTRVMGENLAYVIYTSGS 3248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 194 TGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPaaHNYAMSSPGALGVFLAKGTVVLAT----DPSATlcFPLIE 269
Cdd:PRK12467 3249 TGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMS--FSFDGAQERFLWTLICGGCLVVRDndlwDPEEL--WQAIH 3324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 270 KHQINaTALVPPAvslWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIG-CQLQQVFGMAEGLVNYTRL---- 344
Cdd:PRK12467 3325 AHRIS-IACFPPA---YLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLWkcgg 3400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 345 DDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF-------YCSGDLI 417
Cdd:PRK12467 3401 DAVCEAPYAPIGRPV-AGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLA 3479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 418 SIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMeDELLGEKSCAYLVVKEPLRAV--QVRRFLRE 495
Cdd:PRK12467 3480 RYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWreTLRDHLAA 3558
|
490 500 510
....*....|....*....|....*....|.
gi 677652367 496 QgVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:PRK12467 3559 S-LPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-526 |
7.29e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 131.23 E-value: 7.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 40 TAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlALFSHQRTELNAYamqi 119
Cdd:PRK12316 528 PALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYV-PLDPEYPAERLAY---- 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 120 aptlVIADRQHTLFAGEDFLNTFVAEHRSVRVVLLrnDDGDHSLDAAMRQAAEdftaTPSPADEVAYFQLSGGTTGTPKL 199
Cdd:PRK12316 603 ----MLEDSGVQLLLSQSHLGRKLPLAAGVQVLDL--DRPAAWLEGYSEENPG----TELNPENLAYVIYTSGSTGKPKG 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 200 IPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYA--------MSspGALGVFLAKGtvvLATDPSATLcfPLIEKH 271
Cdd:PRK12316 673 AGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSvweffwplMS--GARLVVAAPG---DHRDPAKLV--ELINRE 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 272 QINATALVPPAvslwLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEI-GCQLQQVFGMAE---GLVNYTRLDDS 347
Cdd:PRK12316 746 GVDTLHFVPSM----LQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLpQAGLYNLYGPTEaaiDVTHWTCVEEG 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 348 PERIinTQGRPMCpDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------YCSGDLISIDQ 421
Cdd:PRK12316 822 GDSV--PIGRPIA-NLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRA 898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 422 DGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEdellGEKSCAYLVVKEPlrAVQVRRFLR---EQGV 498
Cdd:PRK12316 899 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESE--GGDWREALKahlAASL 972
|
490 500
....*....|....*....|....*...
gi 677652367 499 AEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:PRK12316 973 PEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-526 |
7.56e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 131.23 E-value: 7.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlALFSHQRTELNAYAM 117
Cdd:PRK12316 3072 DAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYV-PLDPEYPEERLAYML 3150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPTLVIADRQHTLFAGEDflntfvaehrSVRVVLLrnddgdhslDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTP 197
Cdd:PRK12316 3151 EDSGAQLLLSQSHLRLPLAQ----------GVQVLDL---------DRGDENYAEANPAIRTMPENLAYVIYTSGSTGKP 3211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 198 KLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpgaLGVFLAKGTVVLATDPSATLCFPLIEKHQINATA 277
Cdd:PRK12316 3212 KGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEE---LFWPLMSGARVVLAGPEDWRDPALLVELINSEGV 3288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 278 LVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAeiGCQLQQVFGMAEGLVNYTRLDDSPERIINTQ-G 356
Cdd:PRK12316 3289 DVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEATITVTHWQCVEEGKDAVPiG 3366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 357 RPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------YCSGDLISIDQDGYITVHGR 430
Cdd:PRK12316 3367 RPI-ANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGR 3445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 431 EKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEdellGEKSCAYLVVKEPlrAVQVRRFLRE---QGVAEFKLPDRV 507
Cdd:PRK12316 3446 VDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDE--AGDLREALKAhlkASLPEYMVPAHL 3519
|
490
....*....|....*....
gi 677652367 508 ECVASLPLTPVGKVDKKQL 526
Cdd:PRK12316 3520 LFLERMPLTPNGKLDRKAL 3538
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
23-535 |
9.06e-32 |
|
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: 130.75 E-value: 9.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 23 QDVPLTDILTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVA- 99
Cdd:COG1020 474 ADATLHELFEAQAARtpDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAy 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 100 -PVLALFSHQRTelnAYAMQIA-PTLVIADRQHTLFAGEDflntfvaehrSVRVVLLrnddgDhslDAAMRQAAEDFTAT 177
Cdd:COG1020 554 vPLDPAYPAERL---AYMLEDAgARLVLTQSALAARLPEL----------GVPVLAL-----D---ALALAAEPATNPPV 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 178 PSPADEVAYFQLSGGTTGTPK--LIP--------RTHNDYYysvrrsneicGFNEDTRFLcaipaahnyAMSSPGA---- 243
Cdd:COG1020 613 PVTPDDLAYVIYTSGSTGRPKgvMVEhralvnllAWMQRRY----------GLGPGDRVL---------QFASLSFdasv 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 244 ---LGVFLAKGTVVLAT-----DPSATLcfPLIEKHQINATALVPPAVSLWLQAiqewgGNAPLASLRLLQVGGARLSAT 315
Cdd:COG1020 674 weiFGALLSGATLVLAPpearrDPAALA--ELLARHRVTVLNLTPSLLRALLDA-----APEALPSLRLVLVGGEALPPE 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 316 LAARI-PAEIGCQLQQVFGMAEGLV--NYTRLDDSPER-----IintqGRPMcPDDEVWVADADGNPLPPGEIGRLMTRG 387
Cdd:COG1020 747 LVRRWrARLPGARLVNLYGPTETTVdsTYYEVTPPDADggsvpI----GRPI-ANTRVYVLDAHLQPVPVGVPGELYIGG 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 388 PYTFRGYFNSPLHNASAFDANGF-------YCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHA 460
Cdd:COG1020 822 AGLARGYLNRPELTAERFVADPFgfpgarlYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREA 901
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 677652367 461 ALVSMEDElLGEKSCAYLVVKEPLRAV--QVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASRSP 535
Cdd:COG1020 902 VVVAREDA-PGDKRLVAYVVPEAGAAAaaALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA 977
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
186-523 |
1.20e-31 |
|
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: 124.44 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 186 YFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSspGALGVFLAKGTVVLATDPSATLCF 265
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLY--GAISALYLGGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 266 PLIEKHQINATALVPPAVSLWLQAiqewggNAPLASLRLLQVGGARLSATLAARIPAEI-GCQLQQVFGMAE-GLVNYTR 343
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALART------LEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSElSFITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 344 LDDSPERiiNTQGRPmCPDDEVWVADADGnplppGEIGRLMTRGPYTFRGYFNSPLHNAsafdaNGFYCSGDLISIDQDG 423
Cdd:cd17633 156 NQESRPP--NSVGRP-FPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 424 YITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAyLVVKEPLRAVQVRRFLReQGVAEFKL 503
Cdd:cd17633 223 YLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA-LYSGDKLTYKQLKRFLK-QKLSRYEI 300
|
330 340
....*....|....*....|
gi 677652367 504 PDRVECVASLPLTPVGKVDK 523
Cdd:cd17633 301 PKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
37-527 |
1.24e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 128.73 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 37 SDKTAVIEGERAFSYRQLNQAADNLACSLRRQ-GIKPGETALVQLGNVPELYITFFALLKLGVAPVLA--LFS-----HQ 108
Cdd:PRK05677 38 ADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTnpLYTaremeHQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 109 RTELNAYAM-----------------QIAPTLV--IADRQHTLfagEDFLNTFVAEHRSvRVVLLRNDDGDHSLDAAMRQ 169
Cdd:PRK05677 118 FNDSGAKALvclanmahlaekvlpktGVKHVIVteVADMLPPL---KRLLINAVVKHVK-KMVPAYHLPQAVKFNDALAK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 170 AA-EDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICG--FNEDTRFLCA-IPAAHNYAMSSpGALG 245
Cdd:PRK05677 194 GAgQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGsnLNEGCEILIApLPLYHIYAFTF-HCMA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 246 VFLAKGTVVLATDPSATLCFpLIEKHQINATALVppAVSLWLQAI--QEWGGNAPLASLRLLQVGGARLSATLAARIPAE 323
Cdd:PRK05677 273 MMLIGNHNILISNPRDLPAM-VKELGKWKFSGFV--GLNTLFVALcnNEAFRKLDFSALKLTLSGGMALQLATAERWKEV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 324 IGCQLQQVFGMAEglvnytrldDSPERIIN--------TQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYF 395
Cdd:PRK05677 350 TGCAICEGYGMTE---------TSPVVSVNpsqaiqvgTIGIPV-PSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYW 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 396 NSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSC 475
Cdd:PRK05677 420 QRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIK 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 677652367 476 AYLVVK--EPLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:PRK05677 500 VFVVVKpgETLTKEQVMEHMRAN-LTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
162-527 |
2.45e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 127.63 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 162 SLDAAMRQ-AAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICG---------FNEDTRFLCA-I 230
Cdd:PRK12492 186 PFKQALRQgRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgpdgqplMKEGQEVMIApL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 231 PAAHNYAMSSpGALGVFLAKGTVVLATDPSATLCFpLIEKHQINATALVppAVSLWLQAIQEWGG--NAPLASLRLLQVG 308
Cdd:PRK12492 266 PLYHIYAFTA-NCMCMMVSGNHNVLITNPRDIPGF-IKELGKWRFSALL--GLNTLFVALMDHPGfkDLDFSALKLTNSG 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 309 GARLSATLAARIPAEIGCQLQQVFGMAE-GLVNYTRLDDSPERIiNTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRG 387
Cdd:PRK12492 342 GTALVKATAERWEQLTGCTIVEGYGLTEtSPVASTNPYGELARL-GTVGIPV-PGTALKVIDDDGNELPLGERGELCIKG 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 388 PYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMED 467
Cdd:PRK12492 420 PQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPD 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 677652367 468 ELLGEKSCAYLVVKEP-LRAVQVRRFLREQGVAeFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:PRK12492 500 ERSGEAVKLFVVARDPgLSVEELKAYCKENFTG-YKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
30-528 |
1.81e-30 |
|
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: 124.95 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 30 ILTRHAD-SDKTAVIEG--ERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG--VAPVLAL 104
Cdd:cd17642 23 AMKRYASvPGTIAFTDAhtGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGvgVAPTNDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 105 FSHQrtELNaYAMQIA-PTLVIADRQhTL--FAGEDFLNTFVAehrsvRVVLLrnddgDHSLDAAMRQAAEDFTATPSPA 181
Cdd:cd17642 103 YNER--ELD-HSLNISkPTIVFCSKK-GLqkVLNVQKKLKIIK-----TIIIL-----DSKEDYKGYQCLYTFITQNLPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 182 ---------------DEVAYFQLSGGTTGTPKLIPRTHNDY---YYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpgA 243
Cdd:cd17642 169 gfneydfkppsfdrdEQVALIMNSSGSTGLPKGVQLTHKNIvarFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFT--T 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 244 LGVFLAKGTVVLATDPSATLCFPLIEKHQINATALVPPAVSLWlqAIQEWGGNAPLASLRLLQVGGARLSAtlaaripaE 323
Cdd:cd17642 247 LGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFF--AKSTLVDKYDLSNLHEIASGGAPLSK--------E 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 324 IGCQLQQVFGMAEGLVNYTRLDDSPERIINTQG--RP-----MCPDDEVWVADAD-GNPLPPGEIGRLMTRGPYTFRGYF 395
Cdd:cd17642 317 VGEAVAKRFKLPGIRQGYGLTETTSAILITPEGddKPgavgkVVPFFYAKVVDLDtGKTLGPNERGELCVKGPMIMKGYV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 396 NSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSC 475
Cdd:cd17642 397 NNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 677652367 476 AYLVVKE--PLRAVQVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:cd17642 477 AVVVLEAgkTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
190-523 |
2.34e-30 |
|
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: 121.21 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 190 SGGTTGTPKLIPRTHNDYYYSVR--RSNEICGFNEDTRFLcAIPAAHNYAMSSpGALGVFLAKGTVVLATDPSATLCFPL 267
Cdd:cd17635 9 TSGTTGEPKAVLLANKTFFAVPDilQKEGLNWVVGDVTYL-PLPATHIGGLWW-ILTCLIHGGLCVTGGENTTYKSLFKI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 268 IEKHQINATALVPPA----VSLWLQAIQEwggnapLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAE-GLVNYT 342
Cdd:cd17635 87 LTTNAVTTTCLVPTLlsklVSELKSANAT------VPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSEtGTALCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 343 RLDDSPERIiNTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQD 422
Cdd:cd17635 161 PTDDDSIEI-NAVGRPY-PGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERRED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 423 GYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPL---RAVQVRRFLREQgVA 499
Cdd:cd17635 238 GFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELdenAIRALKHTIRRE-LE 316
|
330 340
....*....|....*....|....
gi 677652367 500 EFKLPDRVECVASLPLTPVGKVDK 523
Cdd:cd17635 317 PYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
29-528 |
8.81e-30 |
|
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: 121.65 E-value: 8.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 29 DILTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlalfs 106
Cdd:cd17653 1 DAFERIAAAhpDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYV----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 107 hqrtelnayamQIAPTLVIADRQHTLfagedflntfvaehrsvrvvllrnddgdhsldaamRQAAEDFTATPSPADEVAY 186
Cdd:cd17653 76 -----------PLDAKLPSARIQAIL-----------------------------------RTSGATLLLTTDSPDDLAY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 187 FQLSGGTTGTPKLIPRTHNdyyySVRRSNEICGFNEDTRflcaiPAAHNYAMSSPG---ALGVFLAK----GTVVLAtDP 259
Cdd:cd17653 110 IIFTSGSTGIPKGVMVPHR----GVLNYVSQPPARLDVG-----PGSRVAQVLSIAfdaCIGEIFSTlcngGTLVLA-DP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 260 SATLcFPLIEKhqINATALVPPAVSLwLQAiqewggnAPLASLRLLQVGGARLSATLAARI-----------PAEIGCql 328
Cdd:cd17653 180 SDPF-AHVART--VDALMSTPSILST-LSP-------QDFPNLKTIFLGGEAVPPSLLDRWspgrrlynaygPTECTI-- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 329 qqvfgmaegLVNYTRLddSPERIInTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDAN 408
Cdd:cd17653 247 ---------SSTMTEL--LPGQPV-TIGKPI-PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 409 GF------YCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLR-HPVVIHAALVSMEDELLGekscayLVVK 481
Cdd:cd17653 314 PFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIVVNGRLVA------FVTP 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 677652367 482 EPLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:cd17653 388 ETVDVDGLRSELAKH-LPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
27-527 |
1.24e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 122.48 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHADSDKTAVIEGERAFSYRQLNQAADNLACSLRRQgIKPGETALVQ--LGNVPELYITFFALLKLGVAPVlAL 104
Cdd:PRK07867 7 VAELLLPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRAR-LDPTRPPHVGvlLDNTPEFSLLLGAAALSGIVPV-GL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 105 FSHQRTElnAYAMQIAPT---LVIADRQH-TLFAGEDflntfvaehRSVRVVLLRNDDGDHSLdAAMRQAAEDFtATPSP 180
Cdd:PRK07867 85 NPTRRGA--ALARDIAHAdcqLVLTESAHaELLDGLD---------PGVRVINVDSPAWADEL-AAHRDAEPPF-RVADP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 181 ADEVA-YFqlSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSPGALGVfLAKGTVVLATDP 259
Cdd:PRK07867 152 DDLFMlIF--TSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVAL-AAGASIALRRKF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 260 SATLCFPLIEKHQINATALVPPAVSlWLQAIQEWGGNAPlASLRLlqVGGARLSATLAARIPAEIGCQLQQVFGMAEGLV 339
Cdd:PRK07867 229 SASGFLPDVRRYGATYANYVGKPLS-YVLATPERPDDAD-NPLRI--VYGNEGAPGDIARFARRFGCVVVDGFGSTEGGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 340 NYTRLDDSPERIIntqGRPmcPDDeVWVADAD-GNPLPPGE------------IGRLM-TRGPYTFRGYFNSPLHNASAF 405
Cdd:PRK07867 305 AITRTPDTPPGAL---GPL--PPG-VAIVDPDtGTECPPAEdadgrllnadeaIGELVnTAGPGGFEGYYNDPEADAERM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 406 dANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--P 483
Cdd:PRK07867 379 -RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPgaK 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 677652367 484 LRAVQVRRFLREQG-VAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:PRK07867 458 FDPDAFAEFLAAQPdLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
178-522 |
1.45e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 119.41 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 178 PSPADevAYFQLSGGTTGTPKLIPRTHNDYYYS----------VRRSNEICGF----NEDTRFLCAIPAAHNYAMSSpgA 243
Cdd:cd05924 1 RSADD--LYILYTGGTTGMPKGVMWRQEDIFRMlmggadfgtgEFTPSEDAHKaaaaAAGTVMFPAPPLMHGTGSWT--A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 244 LGVFLAKGTVVLAT---DPSATLcfPLIEKHQINATALVPPAVSL-WLQAIQEwGGNAPLASLRLLQVGGARLSATLAAR 319
Cdd:cd05924 77 FGGLLGGQTVVLPDdrfDPEEVW--RTIEKHKVTSMTIVGDAMARpLIDALRD-AGPYDLSSLFAISSGGALLSPEVKQG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 320 IPAEI-GCQLQQVFGMAEGLVNYTRLddSPERIINTQGRpMCPDDEVWVADADGNPLPPGE--IGRLMTRGpYTFRGYFN 396
Cdd:cd05924 154 LLELVpNITLVDAFGSSETGFTGSGH--SAGSGPETGPF-TRANPDTVVLDDDGRVVPPGSggVGWIARRG-HIPLGYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 397 SPLHNASAF-DANG--FYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEK 473
Cdd:cd05924 230 DEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 677652367 474 SCAYLVVKEPLRAV--QVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVD 522
Cdd:cd05924 310 VVAVVQLREGAGVDleELREHCRTR-IARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-528 |
2.01e-29 |
|
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: 120.70 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 49 FSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvAPVLALFShqrtelnAYAMQiaptlVIADR 128
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLG-AVYQPLFT-------AFGPK-----AIEHR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 129 qhtlFAGEDflntfvaehrsVRVVLLrNDDGDHSLDAAMrqAAEDFTAtpspadevayfqlsgGTTGTPKLIPRTHNDYY 208
Cdd:cd05973 68 ----LRTSG-----------ARLVVT-DAANRHKLDSDP--FVMMFTS---------------GTTGLPKGVPVPLRALA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 209 YSVRRSNEICGFNEDTRFLC-AIPA-AHN--YAMSSPGALGVflakGTVVLATDPSATLCFPLIEKHQINATALVPPAVS 284
Cdd:cd05973 115 AFGAYLRDAVDLRPEDSFWNaADPGwAYGlyYAITGPLALGH----PTILLEGGFSVESTWRVIERLGVTNLAGSPTAYR 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 285 LWLQAIQEwGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAE-GLVNYTRLDDSPERIINTQGRPMcPDD 363
Cdd:cd05973 191 LLMAAGAE-VPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTElGMVLANHHALEHPVHAGSAGRAM-PGW 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 364 EVWVADADGNPLPPGEIGRL---MTRGP-YTFRGYFNSPlhnASAFDAnGFYCSGDLISIDQDGYITVHGREKDQINRGG 439
Cdd:cd05973 269 RVAVLDDDGDELGPGEPGRLaidIANSPlMWFRGYQLPD---TPAIDG-GYYLTGDTVEFDPDGSFSFIGRADDVITMSG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 440 EKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE-----PLRAVQVRRFLREQgVAEFKLPDRVECVASLP 514
Cdd:cd05973 345 YRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGghegtPALADELQLHVKKR-LSAHAYPRTIHFVDELP 423
|
490
....*....|....
gi 677652367 515 LTPVGKVDKKQLRQ 528
Cdd:cd05973 424 KTPSGKIQRFLLRR 437
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-529 |
3.81e-29 |
|
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: 119.59 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 49 FSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALfshqrtelnayamqiaptlviadr 128
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPAT------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 129 qhTLFAGEDFLNtfvaehrsvrvvllRNDDGDHSldaamRQAAEDFTATPSPAdeVAYFqlSGGTTGTPKLIPRTHNDYy 208
Cdd:cd05974 57 --TLLTPDDLRD--------------RVDRGGAV-----YAAVDENTHADDPM--LLYF--TSGTTSKPKLVEHTHRSY- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 209 ysvrrsneICGFNEDTRFLCAIPAAHNYAMSSPG----ALGVFLA----KGTVVLATDP--SATLCFPLIEKHQINaTAL 278
Cdd:cd05974 111 --------PVGHLSTMYWIGLKPGDVHWNISSPGwakhAWSCFFApwnaGATVFLFNYArfDAKRVLAALVRYGVT-TLC 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 279 VPPAVslWLQAIQEwggnaPLASLR--LLQVGGA--RLSATLAARIPAEIGCQLQQVFGMAEGLVnytRLDDSPERIINT 354
Cdd:cd05974 182 APPTV--WRMLIQQ-----DLASFDvkLREVVGAgePLNPEVIEQVRRAWGLTIRDGYGQTETTA---LVGNSPGQPVKA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 355 --QGRPMcPDDEVWVADADGNPLPPGEIGRLM--TRGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGR 430
Cdd:cd05974 252 gsMGRPL-PGYRVALLDPDGAPATEGEVALDLgdTRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGR 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 431 EKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE-----PLRAVQVRRFLREQgVAEFKLPD 505
Cdd:cd05974 330 ADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAgyepsPETALEIFRFSRER-LAPYKRIR 408
|
490 500
....*....|....*....|....
gi 677652367 506 RVEcVASLPLTPVGKVDKKQLRQR 529
Cdd:cd05974 409 RLE-FAELPKTISGKIRRVELRRR 431
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
182-527 |
4.79e-29 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 120.75 E-value: 4.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 182 DEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNE---ICGFNEDTR--FLCAIPAAHNYAMSSPGAlgVFLAKGTVV-L 255
Cdd:PRK08751 208 DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlaGTGKLEEGCevVITALPLYHIFALTANGL--VFMKIGGCNhL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 256 ATDPSATLCFpLIEKHQINATALVppAVSLWLQAIQEWGGNAPL--ASLRLLQVGGARLSATLAARIPAEIGCQLQQVFG 333
Cdd:PRK08751 286 ISNPRDMPGF-VKELKKTRFTAFT--GVNTLFNGLLNTPGFDQIdfSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 334 MAEGlvnytrlddSPERIIN---------TQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASA 404
Cdd:PRK08751 363 LTET---------SPAACINpltlkeyngSIGLPI-PSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKV 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 405 FDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEP- 483
Cdd:PRK08751 433 MDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPa 512
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 677652367 484 LRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:PRK08751 513 LTAEDVKAHARAN-LTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
192-530 |
1.32e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 119.43 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 192 GTTGTPKLIPRTHndyyysvrRSNEIcgfnedtrflcaipaaHNYAMSSPGALGvfLAKGTVVLATDP------------ 259
Cdd:PRK07008 186 GTTGNPKGALYSH--------RSTVL----------------HAYGAALPDAMG--LSARDAVLPVVPmfhvnawglpys 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 260 ----SATLCFP-----------LIEKHQINATALVPpavSLWLQAIQEW-GGNAPLASLRLLQVGGarlSATLAARIPA- 322
Cdd:PRK07008 240 apltGAKLVLPgpdldgkslyeLIEAERVTFSAGVP---TVWLGLLNHMrEAGLRFSTLRRTVIGG---SACPPAMIRTf 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 323 --EIGCQLQQVFGMAE----GLV---NYTRLDDSPE---RIINTQGRPMCPDDeVWVADADGNPLP-PGE-IGRLMTRGP 388
Cdd:PRK07008 314 edEYGVEVIHAWGMTEmsplGTLcklKWKHSQLPLDeqrKLLEKQGRVIYGVD-MKIVGDDGRELPwDGKaFGDLQVRGP 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 389 YTFRGYF---NSPLHNasafdanGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSM 465
Cdd:PRK07008 393 WVIDRYFrgdASPLVD-------GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIAC 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 677652367 466 ------EDELLgekscayLVVKEPLRAVQVRRFLR--EQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRL 530
Cdd:PRK07008 466 ahpkwdERPLL-------VVVKRPGAEVTREELLAfyEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
29-527 |
1.46e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 119.36 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 29 DILTRHADSDKTAVIEGERAFSYRQ-LNQAADN--LACSLRRQGIKPGETALvqLGNVPElYITFFALLKLGVAPVLALF 105
Cdd:PRK13388 7 QLLRDRAGDDTIAVRYGDRTWTWREvLAEAAARaaALIALADPDRPLHVGVL--LGNTPE-MLFWLAAAALGGYVLVGLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 106 SHQRTElnAYAMQIAPT---LVIADRQH-TLFAGEDFlntfvaehrsVRVVLLRNDDGDHsldAAMRQAAEDFTATPSPA 181
Cdd:PRK13388 84 TTRRGA--ALAADIRRAdcqLLVTDAEHrPLLDGLDL----------PGVRVLDVDTPAY---AELVAAAGALTPHREVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 182 DEVAYFQL-SGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpgALGVFLAKG-TVVLATDP 259
Cdd:PRK13388 149 AMDPFMLIfTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMA--GWAPAVASGaAVALPAKF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 260 SATLCFPLIEKHQINATALVPPAVSlWLQAIQEwggnAPLASLRLLQVG-GARLSATLAARIPAEIGCQLQQVFGMAEGL 338
Cdd:PRK13388 227 SASGFLDDVRRYGATYFNYVGKPLA-YILATPE----RPDDADNPLRVAfGNEASPRDIAEFSRRFGCQVEDGYGSSEGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 339 VNYTRLDDSPE----------RIINTQGRPMCPddeVWVADADGNPLPPGE-IGRLM-TRGPYTFRGYFNSPLHNASAFd 406
Cdd:PRK13388 302 VIVVREPGTPPgsigrgapgvAIYNPETLTECA---VARFDAHGALLNADEaIGELVnTAGAGFFEGYYNNPEATAERM- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 407 ANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEP--L 484
Cdd:PRK13388 378 RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGatF 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 677652367 485 RAVQVRRFLREQGVAEFK-LPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:PRK13388 458 DPDAFAAFLAAQPDLGTKaWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
192-531 |
2.78e-28 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 118.32 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 192 GTTGTPKLIPRTHndyyysvrRSN----------EICGFNEDTRFLCAIPAAH----NYAMSSPgalgvflAKGTVVLAt 257
Cdd:PRK06018 187 GTTGDPKGVLYSH--------RSNvlhalmanngDALGTSAADTMLPVVPLFHanswGIAFSAP-------SMGTKLVM- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 258 dPSATL----CFPLIEKHQINATALVPPAVSLWLQAIQEWGgnAPLASLRLLQVGGarlSATLAARIPA--EIGCQLQQV 331
Cdd:PRK06018 251 -PGAKLdgasVYELLDTEKVTFTAGVPTVWLMLLQYMEKEG--LKLPHLKMVVCGG---SAMPRSMIKAfeDMGVEVRHA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 332 FGMAE----GLVN-----YTRL-DDSPERIINTQGRPmcP-DDEVWVADADGNPLP-PGE-IGRLMTRGPYTFRGYFNSp 398
Cdd:PRK06018 325 WGMTEmsplGTLAalkppFSKLpGDARLDVLQKQGYP--PfGVEMKITDDAGKELPwDGKtFGRLKVRGPAVAAAYYRV- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 399 lhNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYL 478
Cdd:PRK06018 402 --DGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIV 479
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 677652367 479 VVKE---PLRAvQVRRFLrEQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLA 531
Cdd:PRK06018 480 QLKPgetATRE-EILKYM-DGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFK 533
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-536 |
4.04e-28 |
|
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: 118.43 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 31 LTRHA--DSDKTAVI-EGE-----RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvAP-- 100
Cdd:cd05966 59 LDRHLkeRGDKVAIIwEGDepdqsRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIG-AVhs 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 101 -VLALFSHQrtelnAYAMQIA---PTLVI-ADRQhtlFAGEDFLNT-----------------FVAEHRSVRVVLlrNDD 158
Cdd:cd05966 138 vVFAGFSAE-----SLADRINdaqCKLVItADGG---YRGGKVIPLkeivdealekcpsvekvLVVKRTGGEVPM--TEG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 159 GDHSLDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDY----YYSVRRSneicgFN--EDTRFLCA--- 229
Cdd:cd05966 208 RDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYllyaATTFKYV-----FDyhPDDIYWCTadi 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 230 --IpAAHNYAMSSPGALGVflakgTVVL----ATDPSATLCFPLIEKHQINA--TAlvPPAVSLWLQAIQEWGGNAPLAS 301
Cdd:cd05966 283 gwI-TGHSYIVYGPLANGA-----TTVMfegtPTYPDPGRYWDIVEKHKVTIfyTA--PTAIRALMKFGDEWVKKHDLSS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 302 LRLL-----------------QVGGARLS---------------ATLAARIPAEIGCQLQQVFGMAEGLVnytrlddspe 349
Cdd:cd05966 355 LRVLgsvgepinpeawmwyyeVIGKERCPivdtwwqtetggimiTPLPGATPLKPGSATRPFFGIEPAIL---------- 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 350 riintqgrpmcpddevwvaDADGNPLPPGEIGRLMTRGPY--TFRG-----------YFnsplhnaSAFdaNGFYCSGDL 416
Cdd:cd05966 425 -------------------DEEGNEVEGEVEGYLVIKRPWpgMARTiygdheryedtYF-------SKF--PGYYFTGDG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 417 ISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE------PLRAvQVR 490
Cdd:cd05966 477 ARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDgeepsdELRK-ELR 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 677652367 491 RFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASRSPL 536
Cdd:cd05966 556 KHVRKE-IGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEEL 600
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
24-535 |
1.48e-27 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 117.84 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 24 DVPLTDILTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVApV 101
Cdd:PRK10252 457 ETTLSALVAQQAAKtpDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAA-W 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 102 LALFSHQRTELNAYAMQIA-PTLVIADrqhtlfagEDFLNTFVAEhrsvrvvllrndDGDHSLDAAMRQAAEDFTATPSP 180
Cdd:PRK10252 536 LPLDTGYPDDRLKMMLEDArPSLLITT--------ADQLPRFADV------------PDLTSLCYNAPLAPQGAAPLQLS 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 181 A-DEVAYFQLSGGTTGTPKLIPRTH----------NDYYysvrrsneicGFNEDTRFLCAIPAAHNYAMSS---Pgalgv 246
Cdd:PRK10252 596 QpHHTAYIIFTSGSTGRPKGVMVGQtaivnrllwmQNHY----------PLTADDVVLQKTPCSFDVSVWEffwP----- 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 247 FLAKGTVVLAT-----DPSATLcfPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIP 321
Cdd:PRK10252 661 FIAGAKLVMAEpeahrDPLAMQ--QFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPADLCREWQ 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 322 AEIGCQLQQVFGMAEGLVNYTRLDDSPERIINTQGRPMCPDDEVW-----VADADGNPLPPGEIGRLMTRGPYTFRGYFN 396
Cdd:PRK10252 739 QLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSVPIGYPVWntglrILDARMRPVPPGVAGDLYLTGIQLAQGYLG 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 397 SPLHNASAFDANGF------YCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHP----VVIHAALVSME 466
Cdd:PRK10252 819 RPDLTASRFIADPFapgermYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQA 898
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 677652367 467 DELLGEKS--CAYLVVK--EPLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKK-----QLRQRLASRSP 535
Cdd:PRK10252 899 AATGGDARqlVGYLVSQsgLPLDTSALQAQLRER-LPPHMVPVVLLQLDQLPLSANGKLDRKalplpELKAQVPGRAP 975
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
24-527 |
1.93e-27 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 116.27 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 24 DVPLTDI--LTRHAD--SDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGva 99
Cdd:PLN03102 11 NVPLTPItfLKRASEcyPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAG-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 100 pvlALFSHQRTELNAYAMQI-----APTLVIADRQHTLFAGEdFLNTFVAEHRSV--RVVLLrnddgdHSLDAAMRQAAE 172
Cdd:PLN03102 89 ---AVLNPINTRLDATSIAAilrhaKPKILFVDRSFEPLARE-VLHLLSSEDSNLnlPVIFI------HEIDFPKRPSSE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 173 DF-------TATPSPADEVAYFQL-----------SGGTTGTPKLIPRTHNDYYYSVRRSneICGFNEDT--RFLCAIPA 232
Cdd:PLN03102 159 ELdyecliqRGEPTPSLVARMFRIqdehdpislnyTSGTTADPKGVVISHRGAYLSTLSA--IIGWEMGTcpVYLWTLPM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 233 AHNYAMSSPgaLGVFLAKGTVVLATDPSATLCFPLIEKHQINATALVPPAVSLWLQaiqewgGN----APLASLRLLQVG 308
Cdd:PLN03102 237 FHCNGWTFT--WGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK------GNsldlSPRSGPVHVLTG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 309 GARLSATLAARIpAEIGCQLQQVFGMAE--GLVNYTRLDDSPERIINTQGRPMCPDDEV---WVADAD--------GNPL 375
Cdd:PLN03102 309 GSPPPAALVKKV-QRLGFQVMHAYGLTEatGPVLFCEWQDEWNRLPENQQMELKARQGVsilGLADVDvknketqeSVPR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 376 PPGEIGRLMTRGPYTFRGYFNSPLHNASAFDaNGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHP 455
Cdd:PLN03102 388 DGKTMGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 456 VVIHAALVSMEDELLGEKSCAYLVVK--EPLRAVQVRRFLREQG---------VAEFKLPDRVECVASLPLTPVGKVDKK 524
Cdd:PLN03102 467 KVLETAVVAMPHPTWGETPCAFVVLEkgETTKEDRVDKLVTRERdlieycrenLPHFMCPRKVVFLQELPKNGNGKILKP 546
|
...
gi 677652367 525 QLR 527
Cdd:PLN03102 547 KLR 549
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
38-534 |
2.08e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 117.57 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELnAYAM 117
Cdd:PRK12467 1589 EAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERL-AYMI 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 Q---IAPTLVIADRQHTLFAGEdflntfvaehrSVRVVLLrnDDGDHSLDAamrQAAEDFTATPSPaDEVAYFQLSGGTT 194
Cdd:PRK12467 1668 EdsgIELLLTQSHLQARLPLPD-----------GLRSLVL--DQEDDWLEG---YSDSNPAVNLAP-QNLAYVIYTSGST 1730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 195 GTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAhnYAMSSPGALGVFLAKGTVVLAT-----DPSATLcfPLIE 269
Cdd:PRK12467 1731 GRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFWPLINGARLVIAPpgahrDPEQLI--QLIE 1806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 270 KHQINATALVPPAVSLWLQAIQEWGGnaPLaSLRLLQVGGARLSATLA----ARIPAEigcQLQQVFGMAEGLVNYT--- 342
Cdd:PRK12467 1807 RQQVTTLHFVPSMLQQLLQMDEQVEH--PL-SLRRVVCGGEALEVEALrpwlERLPDT---GLFNLYGPTETAVDVThwt 1880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 343 -RLDDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF-------YCSG 414
Cdd:PRK12467 1881 cRRKDLEGRDSVPIGQPI-ANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTG 1959
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 415 DLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSmEDELLGEKSCAYLVVKEPL------RAVQ 488
Cdd:PRK12467 1960 DLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYVVPTDPGlvdddeAQVA 2038
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 677652367 489 VRRFLRE---QGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLASRS 534
Cdd:PRK12467 2039 LRAILKNhlkASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASEL 2087
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
23-534 |
4.00e-27 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 115.08 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 23 QDVPLTDILTRHAD--SDKTAVIEGE--RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPElyitfFALLKLGV 98
Cdd:PLN02330 26 DKLTLPDFVLQDAElyADKVAFVEAVtgKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAE-----YGIVALGI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 99 APVLALFSHQR-----TELNAYAMQIAPTLVIADRQH----------TLFAGEDFLNTFVAEHRsvrvvLLRNDD--GDH 161
Cdd:PLN02330 101 MAAGGVFSGANptaleSEIKKQAEAAGAKLIVTNDTNygkvkglglpVIVLGEEKIEGAVNWKE-----LLEAADraGDT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 162 SLDAAMRQAaeDFTATPspadevayfqLSGGTTGTPKLIPRTHNDY-------YYSVRrsNEICGfneDTRFLCAIPAAH 234
Cdd:PLN02330 176 SDNEEILQT--DLCALP----------FSSGTTGISKGVMLTHRNLvanlcssLFSVG--PEMIG---QVVTLGLIPFFH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 235 NYamsspGALGVFLA----KGTVVLATDPSATLCFPLIEKHQINATALVPPAV---------------SLWLQAIQEwgG 295
Cdd:PLN02330 239 IY-----GITGICCAtlrnKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIIlnlvknpiveefdlsKLKLQAIMT--A 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 296 NAPLASlrllqvggaRLSATLAARIPaeiGCQLQQVFGMAE-GLVNYTRLDDSPERII---NTQGRpMCPDDEVWVADAD 371
Cdd:PLN02330 312 AAPLAP---------ELLTAFEAKFP---GVQVQEAYGLTEhSCITLTHGDPEKGHGIakkNSVGF-ILPNLEVKFIDPD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 372 -GNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENL 450
Cdd:PLN02330 379 tGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 451 LLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQ--VRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:PLN02330 459 LLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEedILNFVAAN-VAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
....*.
gi 677652367 529 RLASRS 534
Cdd:PLN02330 538 KMLSIN 543
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
45-533 |
4.52e-27 |
|
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: 113.99 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 45 GERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLalfshqrtelnayamqiaptlv 124
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVV---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 125 iadRQHTlfAGEDFLNTFVAEHRSVrVVLLRNDDGDhsldaamrqaaedfTATpspadeVAYfqlSGGTTGTPKLIPRTH 204
Cdd:cd17640 60 ---RGSD--SSVEELLYILNHSESV-ALVVENDSDD--------------LAT------IIY---TSGTTGNPKGVMLTH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 205 NDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSspgALGVFLAKGTVVLATDPsatlcfplieKHQINATALVPPAV- 283
Cdd:cd17640 111 ANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERS---AEYFIFACGCSQAYTSI----------RTLKDDLKRVKPHYi 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 284 ----SLW---LQAIQEWGGNAPLASLRLLQ--VGGARLSATL--AARIPAE-------IGCQLQQVFGMAE--GLVNYTR 343
Cdd:cd17640 178 vsvpRLWeslYSGIQKQVSKSSPIKQFLFLffLSGGIFKFGIsgGGALPPHvdtffeaIGIEVLNGYGLTEtsPVVSARR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 344 LddsPERIINTQGRPMcPDDEVWVADADGN-PLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQD 422
Cdd:cd17640 258 L---KCNVRGSVGRPL-PGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 423 GYITVHGREKDQIN-RGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEkscayLVV--KEplravQVRRFLREQGVa 499
Cdd:cd17640 334 GELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGA-----LIVpnFE-----ELEKWAKESGV- 402
|
490 500 510
....*....|....*....|....*....|....
gi 677652367 500 eFKLPDRVECVASLPLTpvgKVDKKQLRQRLASR 533
Cdd:cd17640 403 -KLANDRSQLLASKKVL---KLYKNEIKDEISNR 432
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-532 |
1.05e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 115.44 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELnAYAM 117
Cdd:PRK12316 4566 DAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERL-AYMM 4644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPTLVIADRQHTLFAgedflntfvaehrsvrvvlLRNDDGDHSLDAAMRQAAEDFTAT----PSPADEVAYFQLSGGT 193
Cdd:PRK12316 4645 EDSGAALLLTQSHLLQR-------------------LPIPDGLASLALDRDEDWEGFPAHdpavRLHPDNLAYVIYTSGS 4705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 194 TGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPaaHNYAMSSPGALGVFLAKGTVVLA----TDPSATLcfPLIE 269
Cdd:PRK12316 4706 TGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMS--FSFDGSHEGLYHPLINGASVVIRddslWDPERLY--AEIH 4781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 270 KHQINATALVPpavSLWLQAIQEWGGNAPLASLRLLQVGGARL---SATLAARIPAEIGcqLQQVFGMAEGLVNYT---- 342
Cdd:PRK12316 4782 EHRVTVLVFPP---VYLQQLAEHAERDGEPPSLRVYCFGGEAVaqaSYDLAWRALKPVY--LFNGYGPTETTVTVLlwka 4856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 343 RLDDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNA-----SAFDANG--FYCSGD 415
Cdd:PRK12316 4857 RDGDACGAAYMPIGTPL-GNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAerfvpDPFGAPGgrLYRTGD 4935
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 416 LISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDElLGEKSCAYLVVKEP-----------L 484
Cdd:PRK12316 4936 LARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGA-VGKQLVGYVVPQDPaladadeaqaeL 5014
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 677652367 485 RAvQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRQRLAS 532
Cdd:PRK12316 5015 RD-ELKAALRER-LPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDAS 5060
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
42-469 |
5.75e-26 |
|
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: 110.61 E-value: 5.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 42 VIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG--VAPVLALFShqrtelnayAMQI 119
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGaiAVPILAEFT---------ADEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 120 aptlviadrqhtlfagedflnTFVAEHRSVRVVllrnddgdhsldaamrqaaedFTATPspaDEVAYFQLSGGTTGTPKL 199
Cdd:cd05914 72 ---------------------HHILNHSEAKAI---------------------FVSDE---DDVALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 200 IPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSPGALGvFLAKGTVVLATDPSATL---------------C 264
Cdd:cd05914 107 VMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLP-LLNGAHVVFLDKIPSAKiialafaqvtptlgvP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 265 FPLIEKHqINATALVPPAVSLWL-------------------QAIQEWGGNaplasLRLLQVGGARLSATLAARIpAEIG 325
Cdd:cd05914 186 VPLVIEK-IFKMDIIPKLTLKKFkfklakkinnrkirklafkKVHEAFGGN-----IKEFVIGGAKINPDVEEFL-RTIG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 326 CQLQQVFGMAEG--LVNYTRlddsPERIINTQGRPMCPDDEVWVADADgnplPPGEIGRLMTRGPYTFRGYFNSPLHNAS 403
Cdd:cd05914 259 FPYTIGYGMTETapIISYSP----PNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAE 330
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 677652367 404 AFDANGFYCSGDLISIDQDGYITVHGREKDQINRG-GEKIAAEEIENLLLRHPVVIHAALVSMEDEL 469
Cdd:cd05914 331 AFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVVQEKKL 397
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
38-528 |
1.14e-25 |
|
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: 110.21 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAF-----SYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvAPVLALFSHQRTEL 112
Cdd:cd05915 9 GRKEVVSRLHTGevhrtTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMG-AVLHTANPRLSPKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 113 NAYAMQiaptlviADRQHTLFAGEDFLNtfVAEHRsvrVVLLRNDDgDHSLDAAMRQAAEDFTATPSP----------AD 182
Cdd:cd05915 88 IAYILN-------HAEDKVLLFDPNLLP--LVEAI---RGELKTVQ-HFVVMDEKAPEGYLAYEEALGeeadpvrvpeRA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 183 EVAyFQLSGGTTGTPKLIPRTHNDYYY---SVRRSNEIcGFNEDTRFLCAIPAAHNYAMSSPGALGVFlaKGTVV-LATD 258
Cdd:cd05915 155 ACG-MAYTTGTTGLPKGVVYSHRALVLhslAASLVDGT-ALSEKDVVLPVVPMFHVNAWCLPYAATLV--GAKQVlPGPR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 259 PSATLCFPLIEKHQINATALVPPAVSL-------------WLQAIQEWGGNAPLASLRLLQVGGARLSATLaaripaeiG 325
Cdd:cd05915 231 LDPASLVELFDGEGVTFTAGVPTVWLAladylestghrlkTLRRLVVGGSAAPRSLIARFERMGVEVRQGY--------G 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 326 CQlqQVFGMAEGLVNYTRLDDSPE----RIINTQGRPMCPDdEVWVADADGNPLP-PGEIGRLMT-RGPYTFRGYF-NSP 398
Cdd:cd05915 303 LT--ETSPVVVQNFVKSHLESLSEeeklTLKAKTGLPIPLV-RLRVADEEGRPVPkDGKALGEVQlKGPWITGGYYgNEE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 399 LHNASAFDAnGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYL 478
Cdd:cd05915 380 ATRSALTPD-GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVV 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 677652367 479 VVKEP-LRAVQVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:cd05915 459 VPRGEkPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
46-529 |
1.39e-25 |
|
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: 110.25 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 46 ERAFSYRQLNQAADNLACSLRRQ-GIKPGETALVQLGNVPELYITFFALLKLGVapvlaLFSHQRTELNA----YAMQia 120
Cdd:cd05928 39 EVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGL-----VFIPGTIQLTAkdilYRLQ-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 121 ptlviADRQHTLFAGEDF---LNTFVAEHRSVRVVLLRND---DGDHSLDAAMRQAAEDFTATPSPADEVAYFQLSGGTT 194
Cdd:cd05928 112 -----ASKAKCIVTSDELapeVDSVASECPSLKTKLLVSEksrDGWLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 195 GTPKLIPRTHNDY---------YYSVRRSNEICGFNEDTRFLCAIPAAhnyaMSSPGALG--VF---LAK--GTVVLATd 258
Cdd:cd05928 187 GSPKMAEHSHSSLglglkvngrYWLDLTASDIMWNTSDTGWIKSAWSS----LFEPWIQGacVFvhhLPRfdPLVILKT- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 259 psatlcfplIEKHQINATALVPPAVSLWLQ----AIQewggnapLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGM 334
Cdd:cd05928 262 ---------LSSYPITTFCGAPTVYRMLVQqdlsSYK-------FPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 335 AE-GLV--NYTRLDDSPeriiNTQGRPMCPDDeVWVADADGNPLPPGEIGRLMTR-GP----YTFRGYFNSPLHNASAFD 406
Cdd:cd05928 326 TEtGLIcaNFKGMKIKP----GSMGKASPPYD-VQIIDDNGNVLPPGTEGDIGIRvKPirpfGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 407 ANgFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRA 486
Cdd:cd05928 401 GD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLS 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 677652367 487 VQVRRFLRE--QGV----AEFKLPDRVECVASLPLTPVGKVDKKQLRQR 529
Cdd:cd05928 480 HDPEQLTKElqQHVksvtAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
182-527 |
1.87e-25 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 110.14 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 182 DEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICG--FNEDTRF-LCAIPAAHNYAMSSPGALgvFLAKG-TVVLAT 257
Cdd:PRK08974 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGKELvVTALPLYHIFALTVNCLL--FIELGgQNLLIT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 258 DPSATLCF-PLIEKHQINATALVPPAVSLWLqaiqewggNAP------LASLRLLQVGGARLSATLAARIPAEIGCQLQQ 330
Cdd:PRK08974 284 NPRDIPGFvKELKKYPFTAITGVNTLFNALL--------NNEefqeldFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 331 VFGMAEG--LV--NYTRLDDSPERIintqGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFD 406
Cdd:PRK08974 356 GYGLTECspLVsvNPYDLDYYSGSI----GLPV-PSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 407 aNGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEP-LR 485
Cdd:PRK08974 431 -DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPsLT 509
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 677652367 486 AVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:PRK08974 510 EEELITHCRRH-LTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-526 |
4.94e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.43 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELnAYAM 117
Cdd:PRK12316 2018 EAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERL-AYML 2096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAptlviadRQHTLFAGEDFLNTFVAEHRSVRVVLLRnddgdhslDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTP 197
Cdd:PRK12316 2097 EDS-------GAALLLTQRHLLERLPLPAGVARLPLDR--------DAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 198 KLIPRTHN---------DYYYSVRRSNEICGFnedTRFlcAIPAAHNYAMSSpgalgvfLAKGTVVLATDPSATLCFPLI 268
Cdd:PRK12316 2162 KGVAVSHGalvahcqaaGERYELSPADCELQF---MSF--SFDGAHEQWFHP-------LLNGARVLIRDDELWDPEQLY 2229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 269 -EKHQINATALVPPAVSLWLQA-IQEWGGNAPlaSLRLLQVGGARLSATLAARIPAEIGCQ-LQQVFGMAEGLVNYTRLD 345
Cdd:PRK12316 2230 dEMERHGVTILDFPPVYLQQLAeHAERDGRPP--AVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWK 2307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 346 DSPERIINTQGRPM---CPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF-------YCSGD 415
Cdd:PRK12316 2308 CRPQDPCGAAYVPIgraLGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGD 2387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 416 LISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSmEDELLGEKSCAYLVVKEP--LRAVQVRRFL 493
Cdd:PRK12316 2388 LARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA-QDGASGKQLVAYVVPDDAaeDLLAELRAWL 2466
|
490 500 510
....*....|....*....|....*....|...
gi 677652367 494 ReQGVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:PRK12316 2467 A-ARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
44-526 |
1.39e-24 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 107.40 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 44 EGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELNAYAMQIAPTL 123
Cdd:PRK05857 37 DGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 124 VIADRQHTLfaGEDFLNTFVAEHRSVRV-VLLRNDDGDHSLDAAMRQAAEDftatpSPADEVAYFQLSGGTTGTPK--LI 200
Cdd:PRK05857 117 ALVAPGSKM--ASSAVPEALHSIPVIAVdIAAVTRESEHSLDAASLAGNAD-----QGSEDPLAMIFTSGTTGEPKavLL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 201 PrthNDYYYSV------RRSNEICGFNEDTRFlCAIPAAHNYAMSspGALGVFLAKGTVVLATDPSATLcFPLIEKHQIN 274
Cdd:PRK05857 190 A---NRTFFAVpdilqkEGLNWVTWVVGETTY-SPLPATHIGGLW--WILTCLMHGGLCVTGGENTTSL-LEILTTNAVA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 275 ATALVPPAVSLWLQAIQEWGGNAPlaSLRLLQVGGARLSATLAARIPAEiGCQLQQVFGMAEGLVNYTRLDDSPERIINT 354
Cdd:PRK05857 263 TTCLVPTLLSKLVSELKSANATVP--SLRLVGYGGSRAIAADVRFIEAT-GVRTAQVYGLSETGCTALCLPTDDGSIVKI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 355 Q----GRPMcPDDEVWVADADG-NPLPPG-----EIGRLMTRGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGY 424
Cdd:PRK05857 340 EagavGRPY-PGVDVYLAATDGiGPTAPGagpsaSFGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 425 ITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVR--------RFLRE- 495
Cdd:PRK05857 418 FYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARalkhtiaaRFRREs 497
|
490 500 510
....*....|....*....|....*....|.
gi 677652367 496 QGVAEfklPDRVECVASLPLTPVGKVDKKQL 526
Cdd:PRK05857 498 EPMAR---PSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
27-460 |
2.03e-24 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 107.27 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLaL 104
Cdd:PRK08279 39 LGDVFEEAAARhpDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL-L 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 105 FSHQRTELNAYAMQIA-PTLVIadrqhtlfAGEDFLNTF--VAEH--RSVRVVLLRNDDGDHS--LDAAMRQAAEDFTAT 177
Cdd:PRK08279 118 NTQQRGAVLAHSLNLVdAKHLI--------VGEELVEAFeeARADlaRPPRLWVAGGDTLDDPegYEDLAAAAAGAPTTN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 178 PS-----PADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYA-MSSPGAlgVFLAKG 251
Cdd:PRK08279 190 PAsrsgvTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGgTVAWSS--VLAAGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 252 TVVLATDPSATLCFPLIEKHqiNATAlvppavslwLQAIQEWGG---NAPLA------SLRLLqVG-GARlsatlaarip 321
Cdd:PRK08279 268 TLALRRKFSASRFWDDVRRY--RATA---------FQYIGELCRyllNQPPKptdrdhRLRLM-IGnGLR---------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 322 AEIGCQLQQVFGMA---------EGLVNYTRLDDsperIINTQGR-PMC-----------PDDEVWVADADGN--PLPPG 378
Cdd:PRK08279 326 PDIWDEFQQRFGIPrilefyaasEGNVGFINVFN----FDGTVGRvPLWlahpyaivkydVDTGEPVRDADGRciKVKPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 379 E----IGRLMTRGPytFRGYfNSP-------LHNasAF---DAngFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAA 444
Cdd:PRK08279 402 EvgllIGRITDRGP--FDGY-TDPeasekkiLRD--VFkkgDA--WFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVAT 474
|
490
....*....|....*.
gi 677652367 445 EEIENLLLRHPVVIHA 460
Cdd:PRK08279 475 TEVENALSGFPGVEEA 490
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
27-532 |
3.95e-23 |
|
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: 102.24 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 27 LTDILTRHADS--DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLAL 104
Cdd:cd05918 1 VHDLIEERARSqpDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 105 FSHQRTELNAYAMQIAPTLVIAdrqhtlfagedflntfvaehrsvrvvllrnddgdhsldaamrqaaedftatpSPADEV 184
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLT----------------------------------------------------SSPSDA 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 185 AYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAipAAHNYAMSSPGALGVFLAKGTVVLatdPSATLC 264
Cdd:cd05918 109 AYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQF--ASYTFDVSILEIFTTLAAGGCLCI---PSEEDR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 265 FP----LIEKHQINaTALVPPAVSLWLQAIQewggnapLASLRLLQVGGARLSATL----AARI-------PAE--IGCQ 327
Cdd:cd05918 184 LNdlagFINRLRVT-WAFLTPSVARLLDPED-------VPSLRTLVLGGEALTQSDvdtwADRVrlinaygPAEctIAAT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 328 LQQVfgmaeglvnytrLDDSPERIIntqGRPM---CpddevWVADADGN--PLPPGEIGRLMTRGPYTFRGYFNSPLHNA 402
Cdd:cd05918 256 VSPV------------VPSTDPRNI---GRPLgatC-----WVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 403 SAF-------------DANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIH---AALVSME 466
Cdd:cd05918 316 AAFiedpawlkqegsgRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevvVEVVKPK 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 467 DELLGEKSCAYLVVKEPLR-------------------AVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQLR 527
Cdd:cd05918 396 DGSSSPQLVAFVVLDGSSSgsgdgdslflepsdefralVAELRSKLRQR-LPSYMVPSVFLPLSHLPLTASGKIDRRALR 474
|
....*
gi 677652367 528 QRLAS 532
Cdd:cd05918 475 ELAES 479
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
38-527 |
4.73e-23 |
|
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: 102.95 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVI-EGE----RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvAPVLALFShqrtel 112
Cdd:cd05968 76 TRPALRwEGEdgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIG-GIVVPIFS------ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 113 nAYAMQIAPTLVIADRQHTLFAGEDFLntfvaeHRSVRVVLLRNDDGDHSLDAAM------RQAAEDFTATP----SPAD 182
Cdd:cd05968 149 -GFGKEAAATRLQDAEAKALITADGFT------RRGREVNLKEEADKACAQCPTVekvvvvRHLGNDFTPAKgrdlSYDE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 183 EVAY-------------FQL--SGGTTGTPKLIPRTHndyyysvrrsneiCGFnedtrflcAIPAAHNYA---------- 237
Cdd:cd05968 222 EKETagdgaertesedpLMIiyTSGTTGKPKGTVHVH-------------AGF--------PLKAAQDMYfqfdlkpgdl 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 238 ---------MSSPGAL-GVFLAKGTVVL---ATD-PSATLCFPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLR 303
Cdd:cd05968 281 ltwftdlgwMMGPWLIfGGLILGATMVLydgAPDhPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 304 LLQVGGARLSatlaariPAEIGCQLQQVFGMAEGLVNYTRLDDSPERII-NTQGRPM--------CPDDEVWVADADGNP 374
Cdd:cd05968 361 VLGSTGEPWN-------PEPWNWLFETVGKGRNPIINYSGGTEISGGILgNVLIKPIkpssfngpVPGMKADVLDESGKP 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 375 LPPgEIGRLMTRGPY--TFRGYFNSP--LHNA--SAFDanGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIE 448
Cdd:cd05968 434 ARP-EVGELVLLAPWpgMTRGFWRDEdrYLETywSRFD--NVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 449 NLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE-----PLRAVQVRRFLREQGVAEFKlPDRVECVASLPLTPVGKVDK 523
Cdd:cd05968 511 SVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPgvtptEALAEELMERVADELGKPLS-PERILFVKDLPKTRNAKVMR 589
|
....
gi 677652367 524 KQLR 527
Cdd:cd05968 590 RVIR 593
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
38-526 |
1.41e-22 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 100.59 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELNaYAM 117
Cdd:cd17644 15 DAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLT-YIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPTLVIADRQHTLfagedflntfvaehrsvrvvllrnddgdhsldaamrqaaedftatpspadevAYFQLSGGTTGTP 197
Cdd:cd17644 94 EDAQISVLLTQPENL----------------------------------------------------AYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 198 KLIPRTHNDYYYSVRRSNEICGFNEDTRFLcaIPAAHNYAMSSPGALGVFLAKGTVVLATD---PSATLCFPLIEKHQIN 274
Cdd:cd17644 122 KGVMIEHQSLVNLSHGLIKEYGITSSDRVL--QFASIAFDVAAEEIYVTLLSGATLVLRPEemrSSLEDFVQYIQQWQLT 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 275 ATALVPPAVSLWLQAIQEWGGNAPlASLRLLQVGGARLSATLAARIPAEIG--CQLQQVFGMAEGLVNYT--RLDDSPER 350
Cdd:cd17644 200 VLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATvcRLTQLTER 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 351 IIN--TQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF--------YCSGDLISID 420
Cdd:cd17644 279 NITsvPIGRPI-ANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 421 QDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLV--VKEPLRAVQVRRFLReQGV 498
Cdd:cd17644 358 PDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVphYEESPSTVELRQFLK-AKL 436
|
490 500
....*....|....*....|....*...
gi 677652367 499 AEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd17644 437 PDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
38-526 |
1.88e-21 |
|
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: 96.85 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVA--PVLALFSHQRTElnay 115
Cdd:cd17645 13 DHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAyvPIDPDYPGERIA---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 116 amqiaptlviadrqhtlfagedflntFVAEHRSVRVVLlrnddgdhsldaamrqaaedftatpSPADEVAYFQLSGGTTG 195
Cdd:cd17645 89 --------------------------YMLADSSAKILL-------------------------TNPDDLAYVIYTSGSTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 196 TPKLIPRTHNDYYysvrrsnEICGFNEDTRFLCAIPAAHNYAMSS--PGALGVF--LAKGTVVLATDPSATLCFPLI--- 268
Cdd:cd17645 118 LPKGVMIEHHNLV-------NLCEWHRPYFGVTPADKSLVYASFSfdASAWEIFphLTAGAALHVVPSERRLDLDALndy 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 269 -EKHQINATALVPPAVSLWLQAIQEwggnaplaSLRLLQVGGARLsatlaaRIPAEIGCQLQQVFGMAEGLVNYTRLDDS 347
Cdd:cd17645 191 fNQEGITISFLPTGAAEQFMQLDNQ--------SLRVLLTGGDKL------KKIERKGYKLVNNYGPTENTVVATSFEID 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 348 PERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------YCSGDLISIDQ 421
Cdd:cd17645 257 KPYANIPIGKPI-DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFLP 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 422 DGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVRRFLREQgVAEF 501
Cdd:cd17645 336 DGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKND-LPDY 414
|
490 500
....*....|....*....|....*
gi 677652367 502 KLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd17645 415 MIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
13-536 |
2.24e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.09 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 13 ARRYREKGYWQDVP-------LTDILTRHA--DSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNV 83
Cdd:PRK05691 1112 AAERAQLAQWGQAPcapaqawLPELLNEQArqTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERS 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 84 PELYITFFALLKLGVAPVLALFSHQRTELnAYamqiaptlVIADRQHTLFAGEDFLNTFVAEHRSVRVVllrnddgdhsl 163
Cdd:PRK05691 1192 PQLLVGLLAILKAGGAYVPLDPDYPAERL-AY--------MLADSGVELLLTQSHLLERLPQAEGVSAI----------- 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 164 daAMRQAAEDFTATPSPA-----DEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAhnYAM 238
Cdd:PRK05691 1252 --ALDSLHLDSWPSQAPGlhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPIS--FDV 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 239 SSPGALGVFLAKGTVVLAT-----DPSATLcfPLIEKHQINATALVPPAVSLWlqaIQEwggnaPLA----SLRLLQVGG 309
Cdd:PRK05691 1328 SVWECFWPLITGCRLVLAGpgehrDPQRIA--ELVQQYGVTTLHFVPPLLQLF---IDE-----PLAaactSLRRLFSGG 1397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 310 ARLSATLAARIPAEI-GCQLQQVFGMAEGLVNYT----RLDDSPERIIntqGRPM----CPddevwVADADGNPLPPGEI 380
Cdd:PRK05691 1398 EALPAELRNRVLQRLpQVQLHNRYGPTETAINVThwqcQAEDGERSPI---GRPLgnvlCR-----VLDAELNLLPPGVA 1469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 381 GRLMTRGPYTFRGYFNSPLHNASAF--DANG-----FYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLR 453
Cdd:PRK05691 1470 GELCIGGAGLARGYLGRPALTAERFvpDPLGedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA 1549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 454 HPVVIHAAlVSMEDELLGEKSCAYLVVkEPLRAVQVRRFLR--EQGVAEFKLPDRVECVASLPLTPVGKVDKK------- 524
Cdd:PRK05691 1550 QPGVAQAA-VLVREGAAGAQLVGYYTG-EAGQEAEAERLKAalAAELPEYMVPAQLIRLDQMPLGPSGKLDRRalpepvw 1627
|
570
....*....|..
gi 677652367 525 QLRQRLASRSPL 536
Cdd:PRK05691 1628 QQREHVEPRTEL 1639
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
221-522 |
3.48e-21 |
|
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: 94.68 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 221 NEDTRFLCAIPAAHNYAMSspGALGVFLAKGTVVLA--TDPSATLcfPLIEKHQINATALVPPAVSLWLQAIQewGGNAP 298
Cdd:cd17636 39 DEGTVFLNSGPLFHIGTLM--FTLATFHAGGTNVFVrrVDAEEVL--ELIEAERCTHAFLLPPTIDQIVELNA--DGLYD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 299 LASLRllQVGGARLSATLAARIPAEIGCQLQQvFGMAE--GLVNYTRLDDSPeriINTQGRPmCPDDEVWVADADGNPLP 376
Cdd:cd17636 113 LSSLR--SSPAAPEWNDMATVDTSPWGRKPGG-YGQTEvmGLATFAALGGGA---IGGAGRP-SPLVQVRILDEDGREVP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 377 PGEIGRLMTRGPYTFRGYFNSPLHNASAFdANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPV 456
Cdd:cd17636 186 DGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPA 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 677652367 457 VIHAALVSMEDELLGEKSCAyLVVKEP---LRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVD 522
Cdd:cd17636 265 VADAAVIGVPDPRWAQSVKA-IVVLKPgasVTEAELIEHCRAR-IASYKKPKSVEFADALPRTAGGADD 331
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
33-521 |
4.22e-20 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 93.86 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 33 RHADS--DKTAVI------EGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGV--APVL 102
Cdd:PRK10524 61 RHLAKrpEQLALIavstetDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAihSVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 103 ALF-SHqrtelnAYAMQI---APTLVI-AD---RQHTLFAGEDFLNTFV--AEHRSVRVVLL--------RNDDGDHSLd 164
Cdd:PRK10524 141 GGFaSH------SLAARIddaKPVLIVsADagsRGGKVVPYKPLLDEAIalAQHKPRHVLLVdrglapmaRVAGRDVDY- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 165 AAMRQAAEDfTATPS---PADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEI--CGFNEDTrFLCAIP----AAHN 235
Cdd:PRK10524 214 ATLRAQHLG-ARVPVewlESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTifGGKAGET-FFCASDigwvVGHS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 236 YAMSSPgalgvFLAKGTVV----LATDPSATLCFPLIEKHQINATALVPPAVSLWLQAIQEWGGNAPLASLRLLQVGGAR 311
Cdd:PRK10524 292 YIVYAP-----LLAGMATImyegLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 312 LSATLAARIPAEIGCQLQQVFGMAEG----LVNYTRLDDSPERIiNTQGRPMCPDDEVWVADADGNPLPPGEIGRLMTRG 387
Cdd:PRK10524 367 LDEPTASWISEALGVPVIDNYWQTETgwpiLAIARGVEDRPTRL-GSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 388 PY------TFRG--------YFnsplhnaSAFDANgFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLR 453
Cdd:PRK10524 446 PLppgcmqTVWGdddrfvktYW-------SLFGRQ-VYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISS 517
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 677652367 454 HPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAVQVRRFLREQG----VAEFKL-----PDRVECVASLPLTPVGKV 521
Cdd:PRK10524 518 HPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREARLALEKeimaLVDSQLgavarPARVWFVSALPKTRSGKL 594
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
44-534 |
6.66e-20 |
|
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: 93.07 E-value: 6.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 44 EGERAFSYRQLNQAADNLACSLRRQGiKPGETALVQLGNVPELYITFFALLKLGVAPVLA----LFSHQRTELNAYAmQI 119
Cdd:cd05931 20 GREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppptPGRHAERLAAILA-DA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 120 APTLVIADRQHTLFAGEDFLNTFVAEHRSVRVVllrnddgdhslDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKL 199
Cdd:cd05931 98 GPRVVLTTAAALAAVRAFAASRPAAGTPRLLVV-----------DLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 200 IPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLaTDPSATLCFPLiekhqinatalv 279
Cdd:cd05931 167 VVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIG-GLLTPLYSGGPSVL-MSPAAFLRRPL------------ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 280 ppavsLWLQAIQEWGGN---AP--------------------LASLRLLQVGGARLSA-TLAARIPAEIGCQL-QQVF-- 332
Cdd:cd05931 233 -----RWLRLISRYRATisaAPnfaydlcvrrvrdedlegldLSSWRVALNGAEPVRPaTLRRFAEAFAPFGFrPEAFrp 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 333 --GMAE--GLVNYTRLDDSP-----ERIINTQ------------------GRPMcPDDEVWVADADGN-PLPPGEIGRLM 384
Cdd:cd05931 308 syGLAEatLFVSGGPPGTGPvvlrvDRDALAGravavaaddpaarelvscGRPL-PDQEVRIVDPETGrELPDGEVGEIW 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 385 TRGPYTFRGYFNSPLHNASAF------DANGFYCSGDLISIdQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVI 458
Cdd:cd05931 387 VRGPSVASGYWGRPEATAETFgalaatDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPAL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 459 H---AALVSMEDELLGEkscayLVV-------KEPLRAVQVRRFLREQGVAEFKL-PDRVECVA--SLPLTPVGKVdkkq 525
Cdd:cd05931 466 RpgcVAAFSVPDDGEER-----LVVvaevergADPADLAAIAAAIRAAVAREHGVaPADVVLVRpgSIPRTSSGKI---- 536
|
....*....
gi 677652367 526 lrQRLASRS 534
Cdd:cd05931 537 --QRRACRA 543
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
49-457 |
1.05e-19 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 92.15 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 49 FSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlALFSHQRTELNAYAMQIAPTLViadr 128
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISV-PLYPTLNPDTIRYVLEHSESKA---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 129 qhtLFAG--EDFLNT--FVAEhRSVRVVLLRNDDG--DHSLDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPR 202
Cdd:cd05932 82 ---LFVGklDDWKAMapGVPE-GLISISLPPPSAAncQYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 203 THNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYA-----MSS-PGALGVFLAKGTVVLATD-----PSATLCFP-LIEK 270
Cdd:cd05932 158 TFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTErvfveGGSlYGGVLVAFAESLDTFVEDvqrarPTLFFSVPrLWTK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 271 HQINATALVPPA---VSLWLQAIQEWGGNAPLASLRLLQVggaRLSATLAARIPA-------EIGCQLQQVFGMAEGLVn 340
Cdd:cd05932 238 FQQGVQDKIPQQklnLLLKIPVVNSLVKRKVLKGLGLDQC---RLAGCGSAPVPPallewyrSLGLNILEAYGMTENFA- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 341 YTRLDDSPERIINTQGRPMcPDDEVWVADAdgnplppgeiGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISID 420
Cdd:cd05932 314 YSHLNYPGRDKIGTVGNAG-PGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELD 382
|
410 420 430
....*....|....*....|....*....|....*...
gi 677652367 421 QDGYITVHGREKDQINRG-GEKIAAEEIENLLLRHPVV 457
Cdd:cd05932 383 ADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRV 420
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
38-526 |
1.17e-18 |
|
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: 88.61 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 38 DKTAVIEGERAFSYRQLNQAADNLACSLRRQG-IKPGETALVQLGNVPELYITFFALLKLGVA--PVLALFSHQRTElna 114
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAyvPIDPSYPDERIQ--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 115 yamqiaptlviadrqhtlfagedflntFVAEHRSVRVVLlrnddgdhsldaamrqaaedftATPSpadEVAYFQLSGGTT 194
Cdd:cd17648 79 ---------------------------FILEDTGARVVI----------------------TNST---DLAYAIYTSGTT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 195 GTPKLIPRTHNdyyySVRRS-NEICGfnedtRFLCAIPAAHNYAMSSPGALGVFLAKGTVVL-------------ATDPS 260
Cdd:cd17648 107 GKPKGVLVEHG----SVVNLrTSLSE-----RYFGRDNGDEAVLFFSNYVFDFFVEQMTLALlngqklvvppdemRFDPD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 261 ATlcFPLIEKHQ---INATalvpPAVslwLQAIQEwggnAPLASLRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEG 337
Cdd:cd17648 178 RF--YAYINREKvtyLSGT----PSV---LQQYDL----ARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTET 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 338 LV-NYTRLDDSPERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------ 410
Cdd:cd17648 245 TVtNHKRFFPGDQRFDKSLGRPV-RNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqer 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 411 --------YCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKS------CA 476
Cdd:cd17648 324 argrnarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRiqkylvGY 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 677652367 477 YLVVKEPLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd17648 404 YLPEPGHVPESDLLSFLRAK-LPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
26-448 |
7.97e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 86.59 E-value: 7.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 26 PLTDILTRHADSDKTAVIEGE----RAFSYRQLNQAADNLACSLRRQGIKPGETALVqLGNVPELYITFFALLKLGVAPV 101
Cdd:PRK07768 3 RFTEKMYANARTSPRGMVTGEpdapVRHTWGEVHERARRIAGGLAAAGVGPGDAVAV-LAGAPVEIAPTAQGLWMRGASL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 102 LALfsHQ---RTELNAYA--------MQIAPTLVIadrqhtlfaGEDFLNTF-VAEHRSVRVVLLrnddgdhsldAAMRq 169
Cdd:PRK07768 82 TML--HQptpRTDLAVWAedtlrvigMIGAKAVVV---------GEPFLAAApVLEEKGIRVLTV----------ADLL- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 170 AAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDT-RFLCAIPAAHNYAM----SSPGAL 244
Cdd:PRK07768 140 AADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETdVMVSWLPLFHDMGMvgflTVPMYF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 245 GVFLAKGTVV--LATdpsaTLCFP-LIEKHQINATALVPPAVSLW--LQAIQEWGGNAPLASLRLLQVGG--------AR 311
Cdd:PRK07768 220 GAELVKVTPMdfLRD----PLLWAeLISKYRGTMTAAPNFAYALLarRLRRQAKPGAFDLSSLRFALNGAepidpadvED 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 312 LsATLAARI---PAEIGCqlqqVFGMAE------------GLV----------NYTR---LDDSPERIINTQGRPMcPDD 363
Cdd:PRK07768 296 L-LDAGARFglrPEAILP----AYGMAEatlavsfspcgaGLVvdevdadllaALRRavpATKGNTRRLATLGPPL-PGL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 364 EVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHnASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIA 443
Cdd:PRK07768 370 EVRVVDEDGQVLPPRGVGVIELRGESVTPGYLTMDGF-IPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIY 448
|
....*
gi 677652367 444 AEEIE 448
Cdd:PRK07768 449 PTDIE 453
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
276-533 |
8.38e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 85.10 E-value: 8.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 276 TALVPpaVSLwLQAIQEWGGNAPLASLRLLQVGGARLSATLAARiPAEIGCQLQQVFGMAEglvnytrlddsperiinTQ 355
Cdd:PRK07824 130 TSLVP--MQL-AKALDDPAATAALAELDAVLVGGGPAPAPVLDA-AAAAGINVVRTYGMSE-----------------TS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 356 GRpmCpddeVWvadaDGNPLPPGEI----GRLMTRGPYTFRGYFNSPLHNAsaFDANGFYCSGDLISIDqDGYITVHGRE 431
Cdd:PRK07824 189 GG--C----VY----DGVPLDGVRVrvedGRIALGGPTLAKGYRNPVDPDP--FAEPGWFRTDDLGALD-DGVLTVLGRA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 432 KDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEK-SCAYLVVKEPLRAVQVRRFLREQGVAEFKLPDRVECV 510
Cdd:PRK07824 256 DDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRvVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVV 335
|
250 260
....*....|....*....|...
gi 677652367 511 ASLPLTPVGKVDKKQLRQRLASR 533
Cdd:PRK07824 336 DELPRRGIGKVDRRALVRRFAGE 358
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
12-535 |
9.85e-18 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 86.62 E-value: 9.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 12 FARRYREKGyWQDVPL---TDILTrhadsdktaviegerafsYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYI 88
Cdd:PRK06060 10 LAEQASEAG-WYDRPAfyaADVVT------------------HGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 89 TFFALLKLGVapvLALFSHQRTELNAYAMQ---IAPTLVIADrqhtlfagedflNTFVAEHRSVRVVllrndDGDHSLDA 165
Cdd:PRK06060 71 LLLACLARGV---MAFLANPELHRDDHALAarnTEPALVVTS------------DALRDRFQPSRVA-----EAAELMSE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 166 AMRQAAEDFTatPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVrrsNEICgfnedtrflcaipaaHNYAMSSPGALG 245
Cdd:PRK06060 131 AARVAPGGYE--PMGGDALAYATYTSGTTGPPKAAIHRHADPLTFV---DAMC---------------RKALRLTPEDTG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 246 VFLAK-------GTVV---LATDPSATLC-FPLIEKHQINATALVPPAV-----SLWLQAIQEWGGNApLASLRLLQVGG 309
Cdd:PRK06060 191 LCSARmyfayglGNSVwfpLATGGSAVINsAPVTPEAAAILSARFGPSVlygvpNFFARVIDSCSPDS-FRSLRCVVSAG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 310 ARLSATLAARIPAEIGcQLQQVFGMAEGLVNYTRLDDS-PERIINTQGRPMcPDDEVWVADADGNPLPPGEIGRLMTRGP 388
Cdd:PRK06060 270 EALELGLAERLMEFFG-GIPILDGIGSTEVGQTFVSNRvDEWRLGTLGRVL-PPYEIRVVAPDGTTAGPGVEGDLWVRGP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 389 YTFRGYFNSPlhnASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDE 468
Cdd:PRK06060 348 AIAKGYWNRP---DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRES 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 677652367 469 LLGEKSCAYLV------VKEP-LRAVQvRRFLREqgVAEFKLPDRVECVASLPLTPVGKVdkkqLRQRLASRSP 535
Cdd:PRK06060 425 TGASTLQAFLVatsgatIDGSvMRDLH-RGLLNR--LSAFKVPHRFAVVDRLPRTPNGKL----VRGALRKQSP 491
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
31-520 |
1.43e-17 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 85.79 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 31 LTRHADSDKTAVI----EGERA-FSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG-----VAP 100
Cdd:cd05943 76 LLRHADADDPAAIyaaeDGERTeVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGaiwssCSP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 101 ------VLALFShqrtelnayamQIAPTLVIADRQHTlFAGEDF-----LNTFVAEHRSVR-VVLLRNDDGDHSLDAAMR 168
Cdd:cd05943 156 dfgvpgVLDRFG-----------QIEPKVLFAVDAYT-YNGKRHdvrekVAELVKGLPSLLaVVVVPYTVAAGQPDLSKI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 169 QAA---EDFTATPS---------PADEVAYFQLSGGTTGTPKLIP--------------RTHND-------YYYSVrrsn 215
Cdd:cd05943 224 AKAltlEDFLATGAagelefeplPFDHPLYILYSSGTTGLPKCIVhgaggtllqhlkehILHCDlrpgdrlFYYTT---- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 216 eiCGFnedtrflcaipAAHNYAMSSpgalgvfLAKGTVVLATD-----PSATLCFPLIEKHQINATALVPPAVSLWLQAI 290
Cdd:cd05943 300 --CGW-----------MMWNWLVSG-------LAVGATIVLYDgspfyPDTNALWDLADEEGITVFGTSAKYLDALEKAG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 291 QEWGGNAPLASLRLLQVGGARLSATLAARIPAEIG--CQLQQVFG---MAEGLVNYTRLDdsPERIINTQGRPMCPDDEV 365
Cdd:cd05943 360 LKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKpdVLLASISGgtdIISCFVGGNPLL--PVYRGEIQCRGLGMAVEA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 366 WvaDADGNPLpPGEIGRLMTRGPytfrgyFNS-PLH----------NASAFDAN-GFYCSGDLISIDQDGYITVHGREKD 433
Cdd:cd05943 438 F--DEEGKPV-WGEKGELVCTKP------FPSmPVGfwndpdgsryRAAYFAKYpGVWAHGDWIEITPRGGVVILGRSDG 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 434 QINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE------PLRAvQVRRFLREQGVAEFkLPDRV 507
Cdd:cd05943 509 TLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREgvelddELRK-RIRSTIRSALSPRH-VPAKI 586
|
570
....*....|...
gi 677652367 508 ECVASLPLTPVGK 520
Cdd:cd05943 587 IAVPDIPRTLSGK 599
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
50-457 |
4.41e-17 |
|
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: 84.19 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 50 SYRQLNQAADNLACSLRRQGIKPGETALVQL--GNVPELYITFFALlklgvapvlalfshqrtelNAYAMQIAPTLviad 127
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPAPASFVGIysINRPEWIISELAC-------------------YAYSLVTVPLY---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 128 rqHTLfaGEDFLnTFVAEHRSVRVVLLRNDDGDHSLDAAMRQAAED-FTATPSPADEVAYFQLSGGTTGTPKLIPRTHND 206
Cdd:cd05927 64 --DTL--GPEAI-EYILNHAEISIVFCDAGVKVYSLEEFEKLGKKNkVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 207 YYYSVRRSNEI----CGFNEDTRFLCAIPAAH-------NYAMSSPGALGVFlaKGTVVLATDPSATL---CFPLI---- 268
Cdd:cd05927 139 IVSNVAGVFKIleilNKINPTDVYISYLPLAHifervveALFLYHGAKIGFY--SGDIRLLLDDIKALkptVFPGVprvl 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 269 ----EKHQINATALVPPAVSL----------WLQA----------------IQE-WGGNaplasLRLLQVGGARLSATLA 317
Cdd:cd05927 217 nriyDKIFNKVQAKGPLKRKLfnfalnyklaELRSgvvraspfwdklvfnkIKQaLGGN-----VRLMLTGSAPLSPEVL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 318 ARIPAEIGCQLQQVFGMAE--GLVNYTRLDDspeRIINTQGRPMcPDDEVWVAD-------ADGNPlPPGEIgrlMTRGP 388
Cdd:cd05927 292 EFLRVALGCPVLEGYGQTEctAGATLTLPGD---TSVGHVGGPL-PCAEVKLVDvpemnydAKDPN-PRGEV---CIRGP 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 677652367 389 YTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKD-----QinrgGEKIAAEEIENLLLRHPVV 457
Cdd:cd05927 364 NVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNifklsQ----GEYVAPEKIENIYARSPFV 433
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
31-528 |
1.03e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 83.27 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 31 LTRHADS--DKTAVI-EGE-----RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvAP-- 100
Cdd:PRK00174 73 LDRHLKTrgDKVAIIwEGDdpgdsRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIG-AVhs 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 101 -VLALFSHQrtelnAYAMQI---APTLVI-AD------RQHTLFAGEDflnTFVAEHRSVR--VVLLRN------DDG-D 160
Cdd:PRK00174 152 vVFGGFSAE-----ALADRIidaGAKLVItADegvrggKPIPLKANVD---EALANCPSVEkvIVVRRTggdvdwVEGrD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 161 HSLDAAMRQAAEDFTATPSPAdEVAYFQL-SGGTTGTPKLIPRTHNDY----YYSVR-----RSNEIcgfnedtrFLCAi 230
Cdd:PRK00174 224 LWWHELVAGASDECEPEPMDA-EDPLFILyTSGSTGKPKGVLHTTGGYlvyaAMTMKyvfdyKDGDV--------YWCT- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 231 paA-------HNYAMSSPGALGVflakgTVVL----ATDPSATLCFPLIEKHQINA--TAlvPPAVslwlQAIQEWGGNA 297
Cdd:PRK00174 294 --AdvgwvtgHSYIVYGPLANGA-----TTLMfegvPNYPDPGRFWEVIDKHKVTIfyTA--PTAI----RALMKEGDEH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 298 P----LASLRLL-----------------QVGGAR---------------LSATLAARIPAEIGCQLQQVFG-MAEglvn 340
Cdd:PRK00174 361 PkkydLSSLRLLgsvgepinpeawewyykVVGGERcpivdtwwqtetggiMITPLPGATPLKPGSATRPLPGiQPA---- 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 341 ytrlddsperiintqgrpmcpddevwVADADGNPLPPGEIGRL--------MTRGPYT-----FRGYFnsplhnaSAFDa 407
Cdd:PRK00174 437 --------------------------VVDEEGNPLEGGEGGNLvikdpwpgMMRTIYGdherfVKTYF-------STFK- 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 408 nGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVK------ 481
Cdd:PRK00174 483 -GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKggeeps 561
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 677652367 482 EPLRAvQVRRFLREQ-G-VAEfklPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:PRK00174 562 DELRK-ELRNWVRKEiGpIAK---PDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
34-526 |
2.12e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 83.29 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 34 HADSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELN 113
Cdd:PRK05691 2199 ARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLH 2278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 114 AYAMQIAPTLVIADRqhTLFAGEDFLNTFVAehrsvRVVLlrndDGDHSLDAAMRQAAEDFTATPspaDEVAYFQLSGGT 193
Cdd:PRK05691 2279 YMIEDSGIGLLLSDR--ALFEALGELPAGVA-----RWCL----EDDAAALAAYSDAPLPFLSLP---QHQAYLIYTSGS 2344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 194 TGTPKLIPRTHNDYYYSVRRSNEICGFNEDTrflCAIpaaHNYAMSSPGA----LGVFLAKGTVVLATD---PSATLCfP 266
Cdd:PRK05691 2345 TGKPKGVVVSHGEIAMHCQAVIERFGMRADD---CEL---HFYSINFDAAserlLVPLLCGARVVLRAQgqwGAEEIC-Q 2417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 267 LIEKHQINATALVPPAVSlwlQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIgcQLQQVF---GMAEGLVnYTR 343
Cdd:PRK05691 2418 LIREQQVSILGFTPSYGS---QLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAF--APQLFFnayGPTETVV-MPL 2491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 344 LDDSPERIinTQGRPMCPDDEV------WVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF------- 410
Cdd:PRK05691 2492 ACLAPEQL--EEGAASVPIGRVvgarvaYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFaadggrl 2569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 411 YCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMeDELLGEKSCAYLVVKEPLRAVQVR 490
Cdd:PRK05691 2570 YRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAVAGQDDEAQ 2648
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 677652367 491 RFLREQGVAEFK--LPD-----RVECVASLPLTPVGKVDKKQL 526
Cdd:PRK05691 2649 AALREALKAHLKqqLPDymvpaHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
361-536 |
6.85e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 80.04 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 361 PDDEVWVADADGNPLP-------PGEIGRLMTRGPYTFRGYFnsPLHnasaFDANGFYCSGDLISIDQDGYITVHGREKD 433
Cdd:PRK07445 275 PDDFLAGNNSSGQVLPhaqitipANQTGNITIQAQSLALGYY--PQI----LDSQGIFETDDLGYLDAQGYLHILGRNSQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 434 QINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPLRAV-QVRRFLREQgVAEFKLPDRVECVAS 512
Cdd:PRK07445 349 KIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLeELKTAIKDQ-LSPFKQPKHWIPVPQ 427
|
170 180
....*....|....*....|....
gi 677652367 513 LPLTPVGKVDKKQLRQRLASRSPL 536
Cdd:PRK07445 428 LPRNPQGKINRQQLQQIAVQRLGL 451
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
174-531 |
1.19e-15 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 80.35 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 174 FTATPSPaDEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSspGALGVFLAKG-T 252
Cdd:PRK08633 775 YGPTFKP-DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLT--VTLWLPLLEGiK 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 253 VVLATDPS-ATLCFPLIEKHqiNATALVppAVSLWLQAIQEWGGNAPL--ASLRLLQVGgarlsatlAARIPAEIGCQLQ 329
Cdd:PRK08633 852 VVYHPDPTdALGIAKLVAKH--RATILL--GTPTFLRLYLRNKKLHPLmfASLRLVVAG--------AEKLKPEVADAFE 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 330 QVFGMA--EGL----------VNY--TRLDDSPERIIN---TQGRPMcPDDEVWVADAD-GNPLPPGEIGRLMTRGPYTF 391
Cdd:PRK08633 920 EKFGIRilEGYgatetspvasVNLpdVLAADFKRQTGSkegSVGMPL-PGVAVRIVDPEtFEELPPGEDGLILIGGPQVM 998
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 392 RGYFNSPLHNASA---FDANGFYCSGDLISIDQDGYITVHGRekdqINR----GGEKIA----AEEIENLLLRHPVVIha 460
Cdd:PRK08633 999 KGYLGDPEKTAEVikdIDGIGWYVTGDKGHLDEDGFLTITDR----YSRfakiGGEMVPlgavEEELAKALGGEEVVF-- 1072
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 677652367 461 ALVSMEDELLGEKsCAYLVVKEPLRAVQVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRqRLA 531
Cdd:PRK08633 1073 AVTAVPDEKKGEK-LVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLK-ELA 1141
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
361-526 |
3.55e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 78.01 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 361 PDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAF---DANGFYCSGDLISIDqDGYITVHGREKDQINR 437
Cdd:PRK04813 325 PDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFftfDGQPAYHTGDAGYLE-DGLLFYQGRIDFQIKL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 438 GGEKIAAEEIENLLLRHPVVIHAALVSMEDE-----LLgekscAYLVVKEPL--RAVQVRRFLRE---QGVAEFKLPDRV 507
Cdd:PRK04813 404 NGYRIELEEIEQNLRQSSYVESAVVVPYNKDhkvqyLI-----AYVVPKEEDfeREFELTKAIKKelkERLMEYMIPRKF 478
|
170
....*....|....*....
gi 677652367 508 ECVASLPLTPVGKVDKKQL 526
Cdd:PRK04813 479 IYRDSLPLTPNGKIDRKAL 497
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
25-535 |
3.78e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 77.60 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 25 VPLTDILTRH---ADSDKTAVIEGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGvAPV 101
Cdd:PRK09029 2 MIFSDWPWRHwaqVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCG-ARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 102 LALfshqrtelnayamqiAPTLvIADRQHTLfagedflntfvAEHRSVRVVLLRNDDGD-HSLDAAMRQAAEDFTATPSP 180
Cdd:PRK09029 81 LPL---------------NPQL-PQPLLEEL-----------LPSLTLDFALVLEGENTfSALTSLHLQLVEGAHAVAWQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 181 ADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHnyaMSSPGALGVFLAKGtvvlatdps 260
Cdd:PRK09029 134 PQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFH---VSGQGIVWRWLYAG--------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 261 ATLCFPliEKHQINAT-------ALVPPAVSLWLQAIQEwggnaPLASLRLLqVGGARlsatlaarIPAEIGCQLQQV-- 331
Cdd:PRK09029 202 ATLVVR--DKQPLEQAlagcthaSLVPTQLWRLLDNRSE-----PLSLKAVL-LGGAA--------IPVELTEQAEQQgi 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 332 -----FGMAE--GLVNYTRLDDSPeriintqgrpmcpddevwvaDAdGNPLPPGEI----GRLMTRGPYTFRGYFNS--- 397
Cdd:PRK09029 266 rcwcgYGLTEmaSTVCAKRADGLA--------------------GV-GSPLPGREVklvdGEIWLRGASLALGYWRQgql 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 398 -PLHNAsafdaNGFYCSGDLiSIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCA 476
Cdd:PRK09029 325 vPLVND-----EGWFATRDR-GEWQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 677652367 477 YLVVKEPLRAVQVRRFLREQgVAEFKLPdrvecVASLPLTPV----G-KVDKKQLRQRLASRSP 535
Cdd:PRK09029 399 VVESDSEAAVVNLAEWLQDK-LARFQQP-----VAYYLLPPElkngGiKISRQALKEWVAQQLG 456
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-531 |
7.69e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 76.73 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 50 SYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELNAYAMQIAPtlviadrq 129
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEP-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 130 htlfagedflNTFVAEHRsvrvvllrnddgdhsldaamrqaaedftatpspADEVAYFQLSGGTTGTPKLIPRTHNDYYY 209
Cdd:cd05910 76 ----------DAFIGIPK---------------------------------ADEPAAILFTSGSTGTPKGVVYRHGTFAA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 210 SVRRSNEICGFNEDTRFLCAIPAahnYAMSSPgALGVflakGTVVLATDPSA------TLCFPLIEKHQINaTALVPPAV 283
Cdd:cd05910 113 QIDALRQLYGIRPGEVDLATFPL---FALFGP-ALGL----TSVIPDMDPTRparadpQKLVGAIRQYGVS-IVFGSPAL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 284 slwLQAIQEWGG--NAPLASLRLLQVGGARLSATLAARIPAEI--GCQLQQVFGMAEGL---------VNYTRlDDSPER 350
Cdd:cd05910 184 ---LERVARYCAqhGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALpvssigsreLLATT-TAATSG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 351 IINT-QGRPMCP--------DDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASA---FDANGF-YCSGDLI 417
Cdd:cd05910 260 GAGTcVGRPIPGvrvriieiDDEPIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAkidDNSEGFwHRMGDLG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 418 SIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSmedelLGEKSCAY--LVVK-EPLRAVQVRRFLR 494
Cdd:cd05910 340 YLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG-----VGKPGCQLpvLCVEpLPGTITPRARLEQ 414
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 677652367 495 EQGVAEFKLPDRVECVASL--PLTPVG-KVDKKQLRQRLA 531
Cdd:cd05910 415 ELRALAKDYPHTQRIGRFLihPSFPVDiRHNAKIFREKLA 454
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
46-497 |
8.01e-15 |
|
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: 76.62 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 46 ERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVLaLFSHQRTELNAYAMQIA-PTLV 124
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAAL-INYNLRGESLAHCLNVSsAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 125 IADRqhtlfagedflntfvaehrsvrvvllrnddgdhsldaamrqaaedftatpspadevAYFQLSGGTTGTPKLIPRTH 204
Cdd:cd05940 80 VVDA--------------------------------------------------------ALYIYTSGTTGLPKAAIISH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 205 NDYYYSVRRSNEICG-FNEDTRFLCaIPAAHNYA-MSSPGAlgVFLAKGTVVLATDPSATLCFPLIEKHQinATALVppa 282
Cdd:cd05940 104 RRAWRGGAFFAGSGGaLPSDVLYTC-LPLYHSTAlIVGWSA--CLASGATLVIRKKFSASNFWDDIRKYQ--ATIFQ--- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 283 vslWLQAIQEWGGNAPLA------SLRLLQVGGARlsatlaaripAEIGCQLQQVFGMAE------------GLVNYTRL 344
Cdd:cd05940 176 ---YIGELCRYLLNQPPKpterkhKVRMIFGNGLR----------PDIWEEFKERFGVPRiaefyaategnsGFINFFGK 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 345 DDSPERIINTQGRPMC-------PDDEVWVADADG--NPLPPGEIGRLMTR--GPYTFRGYFNSPLHNAS----AF-DAN 408
Cdd:cd05940 243 PGAIGRNPSLLRKVAPlalvkydLESGEPIRDAEGrcIKVPRGEPGLLISRinPLEPFDGYTDPAATEKKilrdVFkKGD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 409 GFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAAL--VSMEDeLLGEKSCAYLVVKEP--- 483
Cdd:cd05940 323 AWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAAIVLQPNeef 401
|
490 500
....*....|....*....|....*.
gi 677652367 484 ------------LRAVQVRRFLREQG 497
Cdd:cd05940 402 dlsalaahleknLPGYARPLFLRLQP 427
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
186-521 |
1.10e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 77.09 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 186 YFQLSGGTTGTPKLIPRTHND------YYYSVRRSNeicgfNEDTRFLCAIPAA----HN--YAMSSPGALGVFLAKGtv 253
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSNGPhlvglkYYWRSIIEK-----DIPTVVFSHSSIGwvsfHGflYGSLSLGNTFVMFEGG-- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 254 VLATDPSATLCFPLIEKHQINaTALVPPAVSLWLQAIQEWGGNAP----LASLRLLQVGGARLSATLAARIPAEIGCQLQ 329
Cdd:PTZ00237 331 IIKNKHIEDDLWNTIEKHKVT-HTLTLPKTIRYLIKTDPEATIIRskydLSNLKEIWCGGEVIEESIPEYIENKLKIKSS 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 330 QVFGMAEGLVNYTRLDDSPERIINTQGRPmCPDDEVWVADADGNPLPPGEIGRLMTRGPY------TFrgYFNSPLHNAS 403
Cdd:PTZ00237 410 RGYGQTEIGITYLYCYGHINIPYNATGVP-SIFIKPSILSEDGKELNVNEIGEVAFKLPMppsfatTF--YKNDEKFKQL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 404 AFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEP 483
Cdd:PTZ00237 487 FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQD 566
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 677652367 484 LRAVQVR--------RFLREQGVAEFKLPDRVECVASLPLTPVGKV 521
Cdd:PTZ00237 567 QSNQSIDlnklkneiNNIITQDIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
50-454 |
1.59e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.01 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 50 SYRQLNQAADNLACSLRRQgikPGETALVQLGNVPELYITFFALLKLGVAPVLALFSHQRTELNAYAMQIAPTLVIADRQ 129
Cdd:PRK06334 47 SYNQVRKAVIALATKVSKY---PDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 130 --------HTLFAGEDFLNTFVAEHRSvRVVLLRNDDGDHSLDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIP 201
Cdd:PRK06334 124 lmqhlaqtHGEDAEYPFSLIYMEEVRK-ELSFWEKCRIGIYMSIPFEWLMRWFGVSDKDPEDVAVILFTSGTEKLPKGVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 202 RTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLATDP-SATLCFPLIEKHQINATALVP 280
Cdd:PRK06334 203 LTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNS-CTLFPLLSGVPVVFAYNPlYPKKIVEMIDEAKVTFLGSTP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 281 PAVSLWLQAIQEwgGNAPLASLRLLQVGGARLSATL---AARIPAEIgcQLQQVFGMAEGlvnytrlddSPERIINTQ-- 355
Cdd:PRK06334 282 VFFDYILKTAKK--QESCLPSLRFVVIGGDAFKDSLyqeALKTFPHI--QLRQGYGTTEC---------SPVITINTVns 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 356 -------GRPMCPDDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYF-NSPLHNASAFDANGFYCSGDLISIDQDGYITV 427
Cdd:PRK06334 349 pkhescvGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFL 428
|
410 420
....*....|....*....|....*..
gi 677652367 428 HGREKDQINRGGEKIAAEEIENLLLRH 454
Cdd:PRK06334 429 KGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
46-533 |
5.09e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 74.66 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 46 ERAFSYRQLNQAADNLACSLRRQGIKPGET-ALVQlGNVPELYITFFALLKLGVAPV-LALFSH--QRtelNAYAMQIAP 121
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRvALIA-ETDGDFVEAFFACQYAGLVPVpLPLPMGfgGR---ESYIAQLRG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 122 TLVIAdrQHTLFAGEDFLNTFVAEhrsvrvvLLRNDDGDHSLDAAM---RQAAEDFTATPSPaDEVAYFQLSGGTTGTPK 198
Cdd:PRK09192 123 MLASA--QPAAIITPDELLPWVNE-------ATHGNPLLHVLSHAWfkaLPEADVALPRPTP-DDIAYLQYSSGSTRFPR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 199 LIPRTHNDYYYSVRrSNEICGFN--EDTRFLCAIPAAHNyaMsspGALGVFLAKGTVVLATDPSATLCF---PLiekhqi 273
Cdd:PRK09192 193 GVIITHRALMANLR-AISHDGLKvrPGDRCVSWLPFYHD--M---GLVGFLLTPVATQLSVDYLPTRDFarrPL------ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 274 natalvppavsLWLQAIQEWGGN---AP-----LASLRLLQVGGAR--LSATLAARIPAE-IGCQLQQVF---------- 332
Cdd:PRK09192 261 -----------QWLDLISRNRGTisySPpfgyeLCARRVNSKDLAEldLSCWRVAGIGADmIRPDVLHQFaeafapagfd 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 333 --------GMAEG----------------LVNYTRL---------DDSPER---IINTqGRPMcPDDEVWVADADGNPLP 376
Cdd:PRK09192 330 dkafmpsyGLAEAtlavsfsplgsgivveEVDRDRLeyqgkavapGAETRRvrtFVNC-GKAL-PGHEIEIRNEAGMPLP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 377 PGEIGRLMTRGPYTFRGYFNSPlHNASAFDANGFYCSGDLiSIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPV 456
Cdd:PRK09192 408 ERVVGHICVRGPSLMSGYFRDE-ESQDVLAADGWLDTGDL-GYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 457 VIH--AALVSMEDEllGEKSCAYLV---VKEPLRAVQVRRFLREQGVAEFKLPDRVECVA--SLPLTPVGKVDKKQLRQR 529
Cdd:PRK09192 486 LRSgdAAAFSIAQE--NGEKIVLLVqcrISDEERRGQLIHALAALVRSEFGVEAAVELVPphSLPRTSSGKLSRAKAKKR 563
|
....
gi 677652367 530 LASR 533
Cdd:PRK09192 564 YLSG 567
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
409-533 |
5.80e-14 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 74.55 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 409 GFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAY--LVVKEPLRA 486
Cdd:PLN02654 513 GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFvtLVEGVPYSE 592
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 677652367 487 vQVRRFL----REQgVAEFKLPDRVECVASLPLTPVGKVDKKQLRqRLASR 533
Cdd:PLN02654 593 -ELRKSLiltvRNQ-IGAFAAPDKIHWAPGLPKTRSGKIMRRILR-KIASR 640
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
188-526 |
5.86e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 73.92 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 188 QLSGGTTGTPKLIPRThndyYYSVRRsnEICGFNE------DTRFLCAIPAAHNYAMSSpGALgVFLAKGTV-VLATDPS 260
Cdd:PRK08308 107 QYSSGTTGEPKLIRRS----WTEIDR--EIEAYNEalnceqDETPIVACPVTHSYGLIC-GVL-AALTRGSKpVIITNKN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 261 ATLCFPLI---EKHQINATALVPPAVSLWLQAIQEwggnaplasLRLLQVGGARLSATLAARIPAEIGCQLQQvFGMAE- 336
Cdd:PRK08308 179 PKFALNILrntPQHILYAVPLMLHILGRLLPGTFQ---------FHAVMTSGTPLPEAWFYKLRERTTYMMQQ-YGCSEa 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 337 GLVNytrlddsperiintqgrpMCPDdeVWVADADGNPLP------------PGEIgrLMTRGPYTFRgyfnsplhnasa 404
Cdd:PRK08308 249 GCVS------------------ICPD--MKSHLDLGNPLPhvsvsagsdenaPEEI--VVKMGDKEIF------------ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 405 fdangfycSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKEPL 484
Cdd:PRK08308 295 --------TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEI 366
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 677652367 485 RAVQVRRFLReQGVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:PRK08308 367 DPVQLREWCI-QHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
50-532 |
1.37e-13 |
|
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: 72.91 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 50 SYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVlalfshqrtelnayamqiaPTLVIADRQ 129
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAV-------------------PVSIGSNEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 130 HTLfagedflNTFVAEHRSVRVVLLRNDDGDHSLdaamrqaaedftatpspADEVAYFQLSGGTTGTPKLIPRTHNDYYY 209
Cdd:cd05908 78 HKL-------KLNKVWNTLKNPYLITEEEVLCEL-----------------ADELAFIQFSSGSTGDPKGVMLTHENLVH 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 210 SVRRSNEICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLAtdPSA------TLCFPLIEKHQINATALVPPAV 283
Cdd:cd05908 134 NMFAILNSTEWKTKDRILSWMPLTHDMGLIA-FHLAPLIAGMNQYLM--PTRlfirrpILWLKKASEHKATIVSSPNFGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 284 SLWLQAIQ-EWGGNAPLASLRLLQVGGARLSATLAARIPAEIG-------CQLQqVFGMAEGLVNYTRLD-DSPERIIN- 353
Cdd:cd05908 211 KYFLKTLKpEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSkyglkrnAILP-VYGLAEASVGASLPKaQSPFKTITl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 354 -----TQGRPMCPDD-------------------EVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANG 409
Cdd:cd05908 290 grrhvTHGEPEPEVDkkdsecltfvevgkpidetDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 410 FYCSGDLISIdQDGYITVHGREKDQINRGGEKIAAEEIENLLlrhpvvihaalVSMEDELLGeKSCAYLVVKEPLRAVQV 489
Cdd:cd05908 370 WLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIA-----------EELEGVELG-RVVACGVNNSNTRNEEI 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 490 RRF-LREQGVAEF-KLPDRVEC---------------VASLPLTPVGKVDKKQLRQRLAS 532
Cdd:cd05908 437 FCFiEHRKSEDDFyPLGKKIKKhlnkrggwqinevlpIRRIPKTTSGKVKRYELAQRYQS 496
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
47-463 |
3.82e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 71.85 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 47 RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVAPVL-----------ALFSHQRTElnAY 115
Cdd:PRK09274 40 DELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLvdpgmgiknlkQCLAEAQPD--AF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 116 ----AMQIAPTLviadrqhtlfagedFLNTFvaehRSVRVVLL---RNDDGDHSLDAAMR-QAAEDFTATPSPADEVAYF 187
Cdd:PRK09274 118 igipKAHLARRL--------------FGWGK----PSVRRLVTvggRLLWGGTTLATLLRdGAAAPFPMADLAPDDMAAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 188 QLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAahnYAMSSPgALGVflakGTVVLATDPS--ATL-- 263
Cdd:PRK09274 180 LFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL---FALFGP-ALGM----TSVIPDMDPTrpATVdp 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 264 --CFPLIEKHQINaTALVPPAVslwLQAIQEWG--GNAPLASLRLLQVGGARLSATLAARipaeigcqLQQVFG-MAEGL 338
Cdd:PRK09274 252 akLFAAIERYGVT-NLFGSPAL---LERLGRYGeaNGIKLPSLRRVISAGAPVPIAVIER--------FRAMLPpDAEIL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 339 VNY--------------TRLDDSPERiinTQ-------GRPMCP--------DDEVWVADADGNPLPPGEIGRLMTRGPY 389
Cdd:PRK09274 320 TPYgatealpissiesrEILFATRAA---TDngagicvGRPVDGvevriiaiSDAPIPEWDDALRLATGEIGEIVVAGPM 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 677652367 390 TFRGYFNSPLHNASA--FDANG--FYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAALV 463
Cdd:PRK09274 397 VTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALV 474
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
446-520 |
4.24e-13 |
|
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: 64.49 E-value: 4.24e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 677652367 446 EIENLLLRHPVVIHAALVSMEDELLGEKSCAYLVVKE--PLRAVQVRRFLREQgVAEFKLPDRVECVASLPLTPVGK 520
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPgvELLEEELVAHVREE-LGPYAVPKEVVFVDELPKTRSGK 76
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
50-457 |
9.33e-13 |
|
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: 70.32 E-value: 9.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 50 SYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFfallklgvapvLALFSHQRTELNAYAmqiaptlviadrq 129
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITA-----------LGCWSQNIPIVTVYA------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 130 hTLfaGEDFLNTFVAEHRSVRVVllrnddgdhsldaamrqaaedftaTPSPADEVAYFQLSGGTTGTPKLIPRTHndyyy 209
Cdd:cd17639 63 -TL--GEDALIHSLNETECSAIF------------------------TDGKPDDLACIMYTSGSTGNPKGVMLTH----- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 210 svrrSNEICG-----------FNEDTRFLCAIPAAH-------NYAMsspgALGVFLAKGTVVLATD------------- 258
Cdd:cd17639 111 ----GNLVAGiaglgdrvpelLGPDDRYLAYLPLAHifelaaeNVCL----YRGGTIGYGSPRTLTDkskrgckgdltef 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 259 -PSATLCFPLI-EKHQINATALVPPAVSL-----WL-----QAIQEWGGNAPLAS--------------LRLLQVGGARL 312
Cdd:cd17639 183 kPTLMVGVPAIwDTIRKGVLAKLNPMGGLkrtlfWTayqskLKALKEGPGTPLLDelvfkkvraalggrLRYMLSGGAPL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 313 SATlAARIPAEIGCQLQQVFGMAEGLVNYTRLDdSPERIINTQGRPMCPDDEVWVADADG-----NPLPPGEIgrlMTRG 387
Cdd:cd17639 263 SAD-TQEFLNIVLCPVIQGYGLTETCAGGTVQD-PGDLETGRVGPPLPCCEIKLVDWEEGgystdKPPPRGEI---LIRG 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 677652367 388 PYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQI-NRGGEKIAAEEIENLLLRHPVV 457
Cdd:cd17639 338 PNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSNPLV 408
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
377-535 |
5.62e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 68.84 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 377 PG--EIGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRGGEKI---AAEEIENLL 451
Cdd:PRK06814 976 PGidEGGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMIslaAVEELAAEL 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 452 lrHPVVIHAAlVSMEDELLGEKsCAYLVVKEPLRAVQVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVD----KKQLR 527
Cdd:PRK06814 1056 --WPDALHAA-VSIPDARKGER-IILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDyvavTKLAE 1131
|
....*...
gi 677652367 528 QRLASRSP 535
Cdd:PRK06814 1132 EAAAKPEA 1139
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
179-526 |
2.60e-11 |
|
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: 65.57 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 179 SPADE-VAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICG-FNEDTRFLCAIP-----------AAHNYA--MSSPGA 243
Cdd:cd17654 114 IRTDEcLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNiTSEDILFLTSPLtfdpsvveiflSLSSGAtlLIVPTS 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 244 LGVFLAKGTVVLATDPSATLCfpliekhQINATALVP-PAVSLWLQAIqewggnAPLASLRLLQVGGARL--SATLAARI 320
Cdd:cd17654 194 VKVLPSKLADILFKRHRITVL-------QATPTLFRRfGSQSIKSTVL------SATSSLRVLALGGEPFpsLVILSSWR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 321 PAEIGCQLQQVFGMAE----GLVNYTRLDDSPERIintqGRPMCpDDEVWVADADGNPLPPGEIGRLMTRGPYTfRGYFN 396
Cdd:cd17654 261 GKGNRTRIFNIYGITEvscwALAYKVPEEDSPVQL----GSPLL-GTVIEVRDQNGSEGTGQVFLGGLNRVCIL-DDEVT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 397 SPLHNasafdangFYCSGDLISIdQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHPVVIHAAlVSMEDEllgEKSCA 476
Cdd:cd17654 335 VPKGT--------MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCA-VTLSDQ---QRLIA 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 677652367 477 YLVVKEPLRAVQVRRFLREqgVAEFKLPDRVECVASLPLTPVGKVDKKQL 526
Cdd:cd17654 402 FIVGESSSSRIHKELQLTL--LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
381-528 |
2.72e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 63.19 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 381 GRLMTRGPYTFRGYF--NSP--LHNASAFDANG-----FYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLL 451
Cdd:PRK08043 554 GRLQLKGPNIMNGYLrvEKPgvLEVPTAENARGemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLA 633
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 677652367 452 LR-HPVVIHAAlVSMEDELLGEKSCAYLVVKEPLRAvQVRRFLREQGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:PRK08043 634 LGvSPDKQHAT-AIKSDASKGEALVLFTTDSELTRE-KLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKS 709
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
176-457 |
4.38e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 62.30 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 176 ATPSPADEVAYFQLSGGTTGTPKLIPRTHNDYYYSV----RRSNEICG-FNEDTRFLCAIPAAHNYAMsspGALGVFLAK 250
Cdd:PTZ00216 258 NIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGIlaleDRLNDLIGpPEEDETYCSYLPLAHIMEF---GVTNIFLAR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 251 GTVV------LATDPSATLC-----------------FPLIEKhqiNATALVPPAVSL-----------WLQAIQE---- 292
Cdd:PTZ00216 335 GALIgfgsprTLTDTFARPHgdltefrpvfligvpriFDTIKK---AVEAKLPPVGSLkrrvfdhayqsRLRALKEgkdt 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 293 --W------------GGNaplasLRLLQVGGARLSATLAARIPAEIGCqLQQVFGMAEGLVNYT--RLDD-SPERIintq 355
Cdd:PTZ00216 412 pyWnekvfsapravlGGR-----VRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETVCCGGiqRTGDlEPNAV---- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 356 GRPMcPDDEVWVADADG-----NPLPPGEIgrlMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGR 430
Cdd:PTZ00216 482 GQLL-KGVEMKLLDTEEykhtdTPEPRGEI---LLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGR 557
|
330 340
....*....|....*....|....*...
gi 677652367 431 EKDQI-NRGGEKIAAEEIENLLLRHPVV 457
Cdd:PTZ00216 558 VKALAkNCLGEYIALEALEALYGQNELV 585
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
362-526 |
1.52e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.95 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 362 DDEVWVADADGNPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDANGF-------YCSGDLISIDQDGYITVHGREKDQ 434
Cdd:PRK05691 4048 NNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQ 4127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 435 INRGGEKIAAEEIENLLLRHPVVIHAAlVSMEDELLGEKSCAYLVVKEPLRAV-----QVRRFLREQgVAEFKLPDRVEC 509
Cdd:PRK05691 4128 VKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQgalleRIKQRLRAE-LPDYMVPLHWLW 4205
|
170
....*....|....*..
gi 677652367 510 VASLPLTPVGKVDKKQL 526
Cdd:PRK05691 4206 LDRLPLNANGKLDRKAL 4222
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
44-417 |
1.83e-09 |
|
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: 60.14 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 44 EGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGVA-----PVLALFSHQRTELNAYAMQ 118
Cdd:cd05921 21 GGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPaapvsPAYSLMSQDLAKLKHLFEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 119 IAPTLVIADRQHTLfagEDFLNTFVAEHRSVrVVLLRNDDGDHSLDAAMRQAAEDFTATPSPA-----DEVAYFQLSGGT 193
Cdd:cd05921 101 LKPGLVFAQDAAPF---ARALAAIFPLGTPL-VVSRNAVAGRGAISFAELAATPPTAAVDAAFaavgpDTVAKFLFTSGS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 194 TGTPKLIPRTHNDYYYSVRRSNEICGF--NEDTRFLCAIPAAHNYAMSSpgALGVFLAK-GTVVL-ATDPSATLCFPLIE 269
Cdd:cd05921 177 TGLPKAVINTQRMLCANQAMLEQTYPFfgEEPPVLVDWLPWNHTFGGNH--NFNLVLYNgGTLYIdDGKPMPGGFEETLR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 270 K-HQINATAL--VPPAVSLWLQAIQewgGNAPL-----ASLRLLQVGGARLSATLAARipaeigcqLQQVfgmAEGLVNy 341
Cdd:cd05921 255 NlREISPTVYfnVPAGWEMLVAALE---KDEALrrrffKRLKLMFYAGAGLSQDVWDR--------LQAL---AVATVG- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 342 trlddspERII------NTQGRPMCPdDEVWVADADGN---PLPPGEI------GRLMTR--GPYTFRGYFNSPLHNASA 404
Cdd:cd05921 320 -------ERIPmmaglgATETAPTAT-FTHWPTERSGLiglPAPGTELklvpsgGKYEVRvkGPNVTPGYWRQPELTAQA 391
|
410
....*....|...
gi 677652367 405 FDANGFYCSGDLI 417
Cdd:cd05921 392 FDEEGFYCLGDAA 404
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
324-460 |
2.33e-09 |
|
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: 59.74 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 324 IGCQLQQVFGMAEGLVNYT--RLDDSPEriiNTQGRPMcPDDEVWVAdadgnplppgEIGRLMTRGPYTFRGYFNSPLHN 401
Cdd:cd17641 347 IGVPLKQLYGQTELAGAYTvhRDGDVDP---DTVGVPF-PGTEVRID----------EVGEILVRSPGVFVGYYKNPEAT 412
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 402 ASAFDANGFYCSGDLISIDQDGYITVHGREKD-QINRGGEKIAAEEIENLLLRHPVVIHA 460
Cdd:cd17641 413 AEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDvGTTSDGTRFSPQFIENKLKFSPYIAEA 472
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
178-470 |
7.05e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 58.57 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 178 PSPADeVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSNEICGFNEDTRFLCAIPAAHNY------AMSSPG-ALGVFlaK 250
Cdd:PLN02736 218 PKPED-VATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYervnqiVMLHYGvAVGFY--Q 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 251 GTVVLATDPSATLcfplieKHQINATalVPpavSLW-------LQAIQEWGG----------NAPLASL----------- 302
Cdd:PLN02736 295 GDNLKLMDDLAAL------RPTIFCS--VP---RLYnriydgiTNAVKESGGlkerlfnaayNAKKQALengknpspmwd 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 303 RLL------QVGG-ARLSATLAARIPAEI--------GCQLQQVFGMAEG--LVNYTRLDDspeRIINTQGRPMcPDDEV 365
Cdd:PLN02736 364 RLVfnkikaKLGGrVRFMSSGASPLSPDVmeflricfGGRVLEGYGMTETscVISGMDEGD---NLSGHVGSPN-PACEV 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 366 WVAD-------ADGNPLPPGEIgrlMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRG 438
Cdd:PLN02736 440 KLVDvpemnytSEDQPYPRGEI---CVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLA 516
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 677652367 439 -GEKIAAEEIENLLLRHPVV----IHA--------ALVSMEDELL 470
Cdd:PLN02736 517 qGEYIAPEKIENVYAKCKFVaqcfVYGdslnsslvAVVVVDPEVL 561
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
33-200 |
1.27e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 57.50 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 33 RHADSDKTAVI-EGE----RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLG-----VAP-- 100
Cdd:PRK03584 94 RHRRDDRPAIIfRGEdgprRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGaiwssCSPdf 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 101 ----VLALFShqrtelnayamQIAPTLVIADRQHTlFAGEDF-----LNTFVAEHRSVR-VVLLRNDDGDHSLDAAMRQA 170
Cdd:PRK03584 174 gvqgVLDRFG-----------QIEPKVLIAVDGYR-YGGKAFdrrakVAELRAALPSLEhVVVVPYLGPAAAAAALPGAL 241
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 677652367 171 A-EDFTAtPSPADEVAYFQL----------SGGTTGTPKLI 200
Cdd:PRK03584 242 LwEDFLA-PAEAAELEFEPVpfdhplwilySSGTTGLPKCI 281
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
47-415 |
2.67e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 56.59 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 47 RAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALLKLGV--APV---LALFSHQRTELNAYAMQIAP 121
Cdd:PRK12582 79 RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVpaAPVspaYSLMSHDHAKLKHLFDLVKP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 122 TLVIADrqhtlfAGEDFLNTFVA-EHRSVRVVLLRND-DGDHSL----------DAAMRQAAEdfTATPspaDEVAYFQL 189
Cdd:PRK12582 159 RVVFAQ------SGAPFARALAAlDLLDVTVVHVTGPgEGIASIafadlaatppTAAVAAAIA--AITP---DTVAKYLF 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 190 SGGTTGTPKLIPRTHndyyysvrrsneicgfnedtRFLCAIPAAH---------------------NYAMSSPGAL-GVF 247
Cdd:PRK12582 228 TSGSTGMPKAVINTQ--------------------RMMCANIAMQeqlrprepdppppvsldwmpwNHTMGGNANFnGLL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 248 LAKGTVVL-ATDPSATLCFPLIEK-HQINATAL--VPPAVSLWLQAIQEwgGNAPLAS----LRLLQVGGARLSATLAAR 319
Cdd:PRK12582 288 WGGGTLYIdDGKPLPGMFEETIRNlREISPTVYgnVPAGYAMLAEAMEK--DDALRRSffknLRLMAYGGATLSDDLYER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 320 IPA----EIGCQ--LQQVFGMAE--GLVNYTRLDdsPERiINTQGRPMcPDDEVWVAdadgnplPPGEIGRLMTRGPYTF 391
Cdd:PRK12582 366 MQAlavrTTGHRipFYTGYGATEtaPTTTGTHWD--TER-VGLIGLPL-PGVELKLA-------PVGDKYEVRVKGPNVT 434
|
410 420
....*....|....*....|....
gi 677652367 392 RGYFNSPLHNASAFDANGFYCSGD 415
Cdd:PRK12582 435 PGYHKDPELTAAAFDEEGFYRLGD 458
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
369-463 |
4.73e-08 |
|
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: 55.83 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 369 DADGnplppgeIGRLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQI-NRGGEKIAAEEI 447
Cdd:cd05933 388 DADG-------IGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIiTAGGENVPPVPI 460
|
90
....*....|....*..
gi 677652367 448 ENLL-LRHPVVIHAALV 463
Cdd:cd05933 461 EDAVkKELPIISNAMLI 477
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
308-450 |
7.66e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 55.11 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 308 GGARLSATLAARIPAEIGCQLQQVFGMAEG----LVNYTRlDDSPERIintqGRPMCPDDEVWVA-----DADGNpLPPG 378
Cdd:PTZ00342 469 GGGKLSPKIAEELSVLLNVNYYQGYGLTETtgpiFVQHAD-DNNTESI----GGPISPNTKYKVRtwetyKATDT-LPKG 542
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 677652367 379 EigrLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLISIDQDGYITVHGREKDQINRG-GEKIAAEEIENL 450
Cdd:PTZ00342 543 E---LLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSqGEYIETDMLNNL 612
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
44-451 |
1.08e-07 |
|
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: 54.60 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 44 EGERaFSYRQLNQAADNLACSLRRQ-GIKPGETALVQLGNVPELYITFFALLKLGVaPVLALFSHQRTE--LNAYAMQIA 120
Cdd:cd05938 2 EGET-YTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGC-PVAFLNTNIRSKslLHCFRCCGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 121 PTLVIA-DRQHTLfagEDFLNTFVAEhrSVRVVLLR---NDDGDHSLDAAMRQAA-----EDFTATPSPADEVAYFQLSg 191
Cdd:cd05938 80 KVLVVApELQEAV---EEVLPALRAD--GVSVWYLShtsNTEGVISLLDKVDAASdepvpASLRAHVTIKSPALYIYTS- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 192 GTTGTPKLIPRTHNDYYYSvrrSN--EICGFNEDTRFLCAIPAAHNYAMSSpGALGVFLAKGTVVLATDPSATLCFPLIE 269
Cdd:cd05938 154 GTTGLPKAARISHLRVLQC---SGflSLCGVTADDVIYITLPLYHSSGFLL-GIGGCIELGATCVLKPKFSASQFWDDCR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 270 KHQINAtalvppavslwLQAIQEwggnaplaSLRLL---------QVGGARLSATLAARipAEIGCQLQQVFG------- 333
Cdd:cd05938 230 KHNVTV-----------IQYIGE--------LLRYLcnqpqspndRDHKVRLAIGNGLR--ADVWREFLRRFGpiriref 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 334 --MAEG---LVNYTRLddsperiINTQGRPMC--------------PDDEVWVADADGN--PLPPGEIGRLMTRGPYT-- 390
Cdd:cd05938 289 ygSTEGnigFFNYTGK-------IGAVGRVSYlykllfpfelikfdVEKEEPVRDAQGFciPVAKGEPGLLVAKITQQsp 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 677652367 391 FRGYFNSPLHNASAFDANGF------YCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLL 451
Cdd:cd05938 362 FLGYAGDKEQTEKKLLRDVFkkgdvyFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVL 428
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
44-534 |
1.30e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.79 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 44 EGERAFSYRQLNQAADNLACSLRRQGiKPGETALVQLGNVPELYITFFALLKLGVAPVLAL------FSHQRTELNAYAm 117
Cdd:PRK05691 36 GEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYppesarRHHQERLLSIIA- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 118 QIAPTLVI--ADRQHTLFAGEDFLNTFVAEhrsvrvvLLRNDdgdhSLDAAMrqaAEDFTATPSPADEVAYFQLSGGTTG 195
Cdd:PRK05691 114 DAEPRLLLtvADLRDSLLQMEELAAANAPE-------LLCVD----TLDPAL---AEAWQEPALQPDDIAFLQYTSGSTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 196 TPKLIPRTHNDYYysvrrSNEI---CGF----NEDTRFLCAIPAAHNyaMSSPGALGVFLAKGTVVLATDPSATLCFPLi 268
Cdd:PRK05691 180 LPKGVQVSHGNLV-----ANEQlirHGFgidlNPDDVIVSWLPLYHD--MGLIGGLLQPIFSGVPCVLMSPAYFLERPL- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 269 ekhqinatalvppavsLWLQAIQEWGGN---AP-----LASLRLLQVGGARLSA----------------TLAARIPAEI 324
Cdd:PRK05691 252 ----------------RWLEAISEYGGTisgGPdfayrLCSERVSESALERLDLsrwrvaysgsepirqdSLERFAEKFA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 325 GCQLQQ-----VFGMAEGLVNYT-----------RLDD---SPERIINTQGRPM--C----PDDEVWVAD-ADGNPLPPG 378
Cdd:PRK05691 316 ACGFDPdsffaSYGLAEATLFVSggrrgqgipalELDAealARNRAEPGTGSVLmsCgrsqPGHAVLIVDpQSLEVLGDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 379 EIGRLMTRGPYTFRGYFNSPLHNASAF---DANGFYCSGDLiSIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHP 455
Cdd:PRK05691 396 RVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 456 VVIH---AALVSMEDEllGEKSCAylVVKEPLRAVQ-------VRRFLReQGVAEF--KLPDRVECV--ASLPLTPVGKV 521
Cdd:PRK05691 475 EVVRkgrVAAFAVNHQ--GEEGIG--IAAEISRSVQkilppqaLIKSIR-QAVAEAcqEAPSVVLLLnpGALPKTSSGKL 549
|
570
....*....|...
gi 677652367 522 DKKQLRQRLASRS 534
Cdd:PRK05691 550 QRSACRLRLADGS 562
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
180-455 |
1.61e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.53 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 180 PADEVAYFQLSGGTTGTPKLIPRTHND---YYYSVRRSNEICGFNEDTRFLCAIPaahnYAMSsPGALGVFLA----KGT 252
Cdd:COG1541 81 PLEEIVRIHASSGTTGKPTVVGYTRKDldrWAELFARSLRAAGVRPGDRVQNAFG----YGLF-TGGLGLHYGaerlGAT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 253 VVLATDPSATLCFPLIEKHQinATALV--PP-AVSLwLQAIQEWGGNAPLASLRLLQVGGARLSATLAARIPAEIGCQLQ 329
Cdd:COG1541 156 VIPAGGGNTERQLRLMQDFG--PTVLVgtPSyLLYL-AEVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAY 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 330 QVFGMAE---GLVNytrldDSPERiintQGRPMCPDD---EVwVADADGNPLPPGEIGRLMtrgpYTfrgyfnsplhnas 403
Cdd:COG1541 233 DIYGLTEvgpGVAY-----ECEAQ----DGLHIWEDHflvEI-IDPETGEPVPEGEEGELV----VT------------- 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 677652367 404 AFDANGF----YCSGDLISIDQD-----------GYITvhGREKDQINRGGEKIAAEEIENLLLRHP 455
Cdd:COG1541 286 TLTKEAMplirYRTGDLTRLLPEpcpcgrthpriGRIL--GRADDMLIIRGVNVFPSQIEEVLLRIP 350
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
369-536 |
3.94e-06 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 49.69 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 369 DADGNPLPP-----GEIG--RLMTRGPYT------FRGYFNS-PLHNASAFDANGfycsgDLISIDQDGYITVHGREKDQ 434
Cdd:PLN03052 540 DDSGNPYPDdapctGELAlfPLMFGASSTllnadhYKVYFKGmPVFNGKILRRHG-----DIFERTSGGYYRAHGRADDT 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 435 INRGGEKIAAEEIENLLLR-HPVVIHAALVSMEDELLG-EKSCAYLVVKEPLRAVQVRRFLREQGVAE--------FKLp 504
Cdd:PLN03052 615 MNLGGIKVSSVEIERVCNAaDESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDLNELKKIFNSAiqkklnplFKV- 693
|
170 180 190
....*....|....*....|....*....|....*
gi 677652367 505 DRVECVASLPLTPVGKVDKKQLRQRLA---SRSPL 536
Cdd:PLN03052 694 SAVVIVPSFPRTASNKVMRRVLRQQLAqelSRSKL 728
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
45-528 |
1.78e-05 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 47.43 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 45 GERAFSYRQLNQAADNLACSLRRQ-GIKPGETALVQLGNVPELYITFFALLKLGVAPVlalfshqrtelnayamqiaptl 123
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPA---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 124 viadrqhtlfagedFLNTFvaehrsvrvvlLRNDDGDHSLD-AAMRQAAEDftatpsPADEVAYFQLSgGTTGTPKLIP- 201
Cdd:cd05937 60 --------------FINYN-----------LSGDPLIHCLKlSGSRFVIVD------PDDPAILIYTS-GTTGLPKAAAi 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 202 RTHNDYYYSVRRSNEICGFNEDTRFLCaIPAAHNYAmSSPGALGVFLAKGTVVLATDPSATLCFPliEKHQINATAlvpp 281
Cdd:cd05937 108 SWRRTLVTSNLLSHDLNLKNGDRTYTC-MPLYHGTA-AFLGACNCLMSGGTLALSRKFSASQFWK--DVRDSGATI---- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 282 avslwLQAIQEWGG---NAPLA------SLRLLQVGGARLSATLAAR----IPaEIGcqlqQVFGMAEGLVNYTRLDDSP 348
Cdd:cd05937 180 -----IQYVGELCRyllSTPPSpydrdhKVRVAWGNGLRPDIWERFRerfnVP-EIG----EFYAATEGVFALTNHNVGD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 349 -------------ERIINTQGRP--MCPD-DEVWVADADG--NPLPPGEIGRLMTRGPYTFRGYFNSPLHNASAFDA--- 407
Cdd:cd05937 250 fgagaighhglirRWKFENQVVLvkMDPEtDDPIRDPKTGfcVRAPVGEPGEMLGRVPFKNREAFQGYLHNEDATESklv 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 408 -------NGFYCSGDLISIDQDGYITVHGREKDQINRGGEKIAAEEIENLLLRHP----VVIHAALVSMEDellGEKSCA 476
Cdd:cd05937 330 rdvfrkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPdiaeANVYGVKVPGHD---GRAGCA 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 677652367 477 YLVVKE------PLRAVQVRRFLREqGVAEFKLPDRVECVASLPLTPVGKVDKKQLRQ 528
Cdd:cd05937 407 AITLEEssavptEFTKSLLASLARK-NLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
44-415 |
2.01e-05 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 47.18 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 44 EGERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPElyitfFALLKLG----------VAPVLALFSHQRTELN 113
Cdd:PRK08180 65 GGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIE-----HALLALAamyagvpyapVSPAYSLVSQDFGKLR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 114 AYAMQIAPTLVIADrQHTLFAgeDFLNTFVAEHrsVRVVLLRNDDGDHS-------LDAAMRQAAEDFTATPSPaDEVAY 186
Cdd:PRK08180 140 HVLELLTPGLVFAD-DGAAFA--RALAAVVPAD--VEVVAVRGAVPGRAatpfaalLATPPTAAVDAAHAAVGP-DTIAK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 187 FQLSGGTTGTPKLIPRTHndyyysvrrsneicgfnedtRFLCAIPAAHNYAMsspgalgVFLAKGTVVLaTD--P-SATL 263
Cdd:PRK08180 214 FLFTSGSTGLPKAVINTH--------------------RMLCANQQMLAQTF-------PFLAEEPPVL-VDwlPwNHTF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 264 ----CFPLIEKH--------------QINAT----ALVPPAVSL-----WLQAIQEWGGNAPLAS-----LRLLQVGGAR 311
Cdd:PRK08180 266 ggnhNLGIVLYNggtlyiddgkptpgGFDETlrnlREISPTVYFnvpkgWEMLVPALERDAALRRrffsrLKLLFYAGAA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 312 LSATLAARIPAeigcqlqqvfgMAEGLVNytrlddspERIINTQG------RPMCPDDEvWVADADGN---PLPPGEI-- 380
Cdd:PRK08180 346 LSQDVWDRLDR-----------VAEATCG--------ERIRMMTGlgmtetAPSATFTT-GPLSRAGNiglPAPGCEVkl 405
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 677652367 381 ----GRLMTR--GPYTFRGYFNSPLHNASAFDANGFYCSGD 415
Cdd:PRK08180 406 vpvgGKLEVRvkGPNVTPGYWRAPELTAEAFDEEGYYRSGD 446
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
302-457 |
8.43e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 45.19 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 302 LRLLQVGGARLSATLAARIPAEIGCQLQQVFGMAE--GLVNYTRLDDSPerIINTQGRPMCPDD----EVWVADAD--GN 373
Cdd:PLN02430 385 LRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTEtlGPTTLGFPDEMC--MLGTVGAPAVYNElrleEVPEMGYDplGE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 374 PlPPGEIgrlMTRGPYTFRGYFNSP-LHNASAFDanGFYCSGDLISIDQDGYITVHGREKDQINRG-GEKIAAEEIENLL 451
Cdd:PLN02430 463 P-PRGEI---CVRGKCLFSGYYKNPeLTEEVMKD--GWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEYLENVY 536
|
....*.
gi 677652367 452 LRHPVV 457
Cdd:PLN02430 537 GQNPIV 542
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
26-106 |
8.44e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 45.44 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 26 PLTDILTRHADS--DKTAVIE---------GERAFSYRQLNQAADNLACSLRRQGIKPGETALVQLGNVPELYITFFALL 94
Cdd:TIGR03443 237 AIHDIFADNAEKhpDRTCVVEtpsfldpssKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVL 316
|
90
....*....|..
gi 677652367 95 KLGvapvlALFS 106
Cdd:TIGR03443 317 KAG-----ATFS 323
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
5-418 |
5.09e-03 |
|
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: 39.75 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 5 FTRWPDEFARRYREKGywqdvPLTDILTRHAdsdKTAVIEGERAFSYRQLNQAADNLACSLR-RQGIKPGEtALVQLGNV 83
Cdd:cd17632 32 MTGYADRPALGQRATE-----LVTDPATGRT---TLRLLPRFETITYAELWERVGAVAAAHDpEQPVRPGD-FVAVLGFT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 84 PELYITF-FALLKLGVAPVLALFSHQRTELNAYAMQIAPTLVIADRQHTLFAGEdflntFVAEHRSVRVVLL---RNDDG 159
Cdd:cd17632 103 SPDYATVdLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVE-----AVLEGGTPPRLVVfdhRPEVD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 160 DH--SLDAAMRQAAE--------------DFTATPSPA-------DEVAYFQLSGGTTGTPKLIPRTHNdyyySVRRSNE 216
Cdd:cd17632 178 AHraALESARERLAAvgipvttltliavrGRDLPPAPLfrpepddDPLALLIYTSGSTGTPKGAMYTER----LVATFWL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 217 ICGFNEDTRFLCAI-----PAAHnyaMSSPGALGVFLAKGTV---VLATDPSaTLcFPLIEKHQINATALVPPAVSLWLQ 288
Cdd:cd17632 254 KVSSIQDIRPPASItlnfmPMSH---IAGRISLYGTLARGGTayfAAASDMS-TL-FDDLALVRPTELFLVPRVCDMLFQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 289 AIQ---EWGGNAPL----------ASLRLLQVGG---------ARLSATLAARIPAEIGCQLQQVFGMAE-GLVNytrLD 345
Cdd:cd17632 329 RYQaelDRRSVAGAdaetlaervkAELRERVLGGrllaavcgsAPLSAEMKAFMESLLDLDLHDGYGSTEaGAVI---LD 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 677652367 346 DspeRIIntqgRPMCPDDE-VWVAD----ADGNPLPPGEigrLMTRGPYTFRGYFNSPLHNASAFDANGFYCSGDLIS 418
Cdd:cd17632 406 G---VIV----RPPVLDYKlVDVPElgyfRTDRPHPRGE---LLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMA 473
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
88-204 |
8.05e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 38.95 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677652367 88 ITFFALLKLGVAPVlALFShqrTELNAYAMQIAptLVIADRQHTLF--------AGEDFLNTFVAEHRSvRVVLLrnddg 159
Cdd:PRK12476 107 AGFFAAIKAGTIAV-PLFA---PELPGHAERLD--TALRDAEPTVVltttaaaeAVEGFLRNLPRLRRP-RVIAI----- 174
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 677652367 160 dhslDAAMRQAAEDFTATPSPADEVAYFQLSGGTTGTPKLIPRTH 204
Cdd:PRK12476 175 ----DAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITH 215
|
|
| |
